9 hits
XFF4834R_chr19710 | hisS | XFF4834R_chr19710 | histidyl tRNA synthetase |
XFF4834R_chr19730 | hisG | XFF4834R_chr19730 | ATP phosphoribosyltransferase |
XFF4834R_chr19740 | hisD | XFF4834R_chr19740 | histidinol dehydrogenase |
XFF4834R_chr19750 | hisC | XFF4834R_chr19750 | histidinol-phosphate aminotransferase |
XFF4834R_chr19760 | hisB | XFF4834R_chr19760 | bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase protein |
XFF4834R_chr19770 | hisH | XFF4834R_chr19770 | imidazole glycerol phosphate synthase, glutamine amidotransferase subunit with HisF |
XFF4834R_chr19780 | hisA | XFF4834R_chr19780 | N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase |
XFF4834R_chr19790 | hisF | XFF4834R_chr19790 | imidazole glycerol phosphate synthase, catalytic subunit with HisH |
XFF4834R_chr19800 | hisIE | XFF4834R_chr19800 | bifunctional phosphoribosyl-AMP cyclohydrolase-phosphoribosyl-ATP pyrophosphatase |
![]() XFF4834R_chr19700 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr_2102 |
ID | hisS |
AC | XFF4834R_chr19710 |
LT | XFF4834R_chr19710 |
OR | XFF4834R_chr from 2263682 to 2265094 on strand + |
DE | histidyl tRNA synthetase |
IP | Histidyl-tRNA synthetase, class IIa |
CL | 1.5.1.16 Histidine GO:0000105 |
EC | |
GO |
InterPro Biological Process: histidyl-tRNA aminoacylation (GO:0006427) Biological Process: tRNA aminoacylation for protein translation (GO:0006418) Biological Process: translation (GO:0006412) Cellular Component: cytoplasm (GO:0005737) Molecular Function: nucleotide binding (GO:0000166) Molecular Function: ATP binding (GO:0005524) Molecular Function: aminoacyl-tRNA ligase activity (GO:0004812) Molecular Function: histidine-tRNA ligase activity (GO:0004821) Curated |
PM | |
AN | |
CC | COG: [J] Translation, ribosomal structure and biogenesis; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by jacques (20110309) |
MW | 51882.8 Da |
SQ | 470 aa |
........10........20........30........40........50 |
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NP_642152.1 lcl|hisS-XAC1826 |
1 |
469 |
S=2281 I=94 E=0 |
histidyl-tRNA synthetase |
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NP_637171.1 lcl|hisS-XCC1806 |
1 |
469 |
S=2224 I=92 E=0 |
histidyl-tRNA synthetase |
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1 |
469 |
S=2100 I=87 E=0 |
probable histidyl-trna synthetase (histidine--trna ligase)(hisrs) protein |
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YP_363603.1 lcl|hisS-XCV1872 |
1 |
469 |
S=2025 I=84 E=0 |
histidyl-tRNA synthetase |
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1 |
447 |
S=850 I=39 E=3.75738e-94 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
Pubmed 18263572 |
|
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1 |
424 |
S=651 I=39 E=4.91061e-70 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
Pubmed 19033196 |
|
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1 |
447 |
S=648 I=38 E=1.27018e-69 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
Pubmed 19011029 |
|
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1 |
457 |
S=598 I=32 E=1.55799e-63 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
Pubmed 19008447 |
|
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2 |
423 |
S=586 I=35 E=3.95693e-62 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
Pubmed 18482458 |
|
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1 |
469 |
S=2281 I=94 E=0 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
||
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1 |
470 |
S=2274 I=94 E=0 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
||
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1 |
470 |
S=2274 I=94 E=0 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
||
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1 |
467 |
S=2254 I=94 E=0 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
||
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1 |
469 |
S=2227 I=92 E=0 |
Histidyl-tRNA synthetase EC=6.1.1.21 ; Aminoacyl-tRNA ATP-binding Cytoplasm Ligase Nucleotide-binding Protein biosynthesis |
||
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[G3DSA:3.30.930.10] | 2 |
364 |
- |
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IPR004154 [G3DSA:3.40.50.800] | 368 |
459 |
Anticodon-binding |
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IPR015807 [MF_00127] | 2 |
465 |
Histidyl-tRNA synthetase, class IIa, subgroup |
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IPR004516 [PIRSF001549] | 1 |
463 |
Histidyl-tRNA synthetase, class IIa |
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IPR004516 [PTHR11476] | 1 |
464 |
Histidyl-tRNA synthetase, class IIa |
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IPR002314 [PF00587] | 22 |
184 |
Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain |
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IPR004154 [PF03129] | 372 |
459 |
Anticodon-binding |
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IPR015807 [TIGR00442] | 5 |
452 |
Histidyl-tRNA synthetase, class IIa, subgroup |
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IPR006195 [PS50862] | 22 |
470 |
Aminoacyl-tRNA synthetase, class II, conserved domain |
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[seg] | 70 |
88 |
- |
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[SignalP-NN(euk)] | 1 |
3 |
- |
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91 |
181 |
S=184 I=46 E=8.45976e-15 |
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93 |
292 |
S=171 I=26 E=3.35168e-13 |
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321 |
412 |
S=125 I=38 E=1.5216e-07 |
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182 |
244 |
S=115 I=42 E=2.49902e-06 |
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1 |
67 |
S=112 I=40 E=4.93307e-06 |
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245 |
269 |
S=107 I=92 E=1.79275e-05 |
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[SSF55681] | 3 |
366 |
- |
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IPR004154 [SSF52954] | 368 |
464 |
Anticodon-binding |
Access unfiltered results
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Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
78 hits |
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Swiss-Prot ncbi-blastp |
0 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
0 hits |
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HAMAP scan |
0 hits |
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IprScan |
13 hits |
Miscellaneous analyses
![]() XFF4834R_chr19720 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr19740 |
ID | hisG |
AC | XFF4834R_chr19730 |
LT | XFF4834R_chr19730 |
OR | XFF4834R_chr from 2266046 to 2266960 on strand + |
DE | ATP phosphoribosyltransferase |
IP | Histidine biosynthesis HisG, C-terminal; ATP phosphoribosyltransferase, catalytic region; ATP phosphoribosyltransferase, conserved site; |
CL | 1.5.1.16 Histidine GO:0000105 |
EC | |
GO |
InterPro Biological Process: histidine biosynthetic process (GO:0000105) Cellular Component: cytoplasm (GO:0005737) Molecular Function: ATP phosphoribosyltransferase activity (GO:0003879) Molecular Function: magnesium ion binding (GO:0000287) Curated |
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by jacques (20110309) |
MW | 32743.4 Da |
SQ | 304 aa |
........10........20........30........40........50 |
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HIS1_MF_00079 | raw_score=4976 norm_score=31.245 | ATP phosphoribosyltransferase [hisG]. |
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YP_363605.1 lcl|hisG-XCV1874 |
1 |
304 |
S=1342 I=88 E=1.40455e-155 |
ATP phosphoribosyltransferase |
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NP_642154.1 lcl|hisG-XAC1828 |
1 |
304 |
S=1330 I=88 E=4.55357e-154 |
ATP phosphoribosyltransferase |
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NP_637173.1 lcl|hisG-XCC1808 |
1 |
304 |
S=1314 I=87 E=3.09757e-152 |
ATP phosphoribosyltransferase |
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1 |
304 |
S=1133 I=75 E=3.20451e-130 |
probable atp phosphoribosyltransferase (atp-prt) protein |
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12 |
303 |
S=501 I=40 E=4.74038e-52 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nu |
||
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12 |
303 |
S=496 I=40 E=1.84717e-51 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nuc |
||
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11 |
303 |
S=461 I=36 E=3.419e-47 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
Pubmed 10555290 |
|
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11 |
303 |
S=456 I=36 E=1.06205e-46 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding N |
Pubmed 9767718 |
|
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11 |
303 |
S=452 I=34 E=3.72736e-46 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
Pubmed 10555290 |
|
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11 |
303 |
S=436 I=33 E=3.68884e-44 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
Pubmed 10555290 |
|
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13 |
303 |
S=396 I=31 E=2.2544e-39 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
Pubmed 19008447 |
|
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13 |
301 |
S=298 I=28 E=1.63067e-27 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
Pubmed 16857943 |
|
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13 |
301 |
S=262 I=26 E=4.46837e-23 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
Pubmed 16820047 |
|
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12 |
203 |
S=255 I=32 E=2.91238e-22 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding N |
||
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1 |
304 |
S=1342 I=88 E=3.65013e-154 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
||
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1 |
304 |
S=1330 I=88 E=1.18338e-152 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
||
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1 |
304 |
S=1323 I=87 E=7.84866e-152 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
||
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1 |
304 |
S=1320 I=87 E=1.92666e-151 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
||
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1 |
304 |
S=1320 I=87 E=1.92666e-151 |
ATP phosphoribosyltransferase EC=2.4.2.17 ; Amino-acid biosynthesis ATP-binding Cytoplasm Glycosyltransferase Histidine Magnesium Metal-binding Nucleotid |
||
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[G3DSA:3.40.190.10] | 7 |
141 |
- |
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IPR015867 [G3DSA:3.30.70.120] | 232 |
304 |
Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal |
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IPR020621 [MF_00079] | 12 |
304 |
Histidine biosynthesis HisG, ATP phosphoribosyltransferase, subgroup |
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IPR013820 [PF01634] | 59 |
227 |
ATP phosphoribosyltransferase, catalytic region |
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IPR013115 [PF08029] | 228 |
302 |
Histidine biosynthesis HisG, C-terminal |
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IPR013820 [TIGR00070] | 13 |
203 |
ATP phosphoribosyltransferase, catalytic region |
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IPR013115 [TIGR03455] | 204 |
303 |
Histidine biosynthesis HisG, C-terminal |
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IPR018198 [PS01316] | 162 |
183 |
ATP phosphoribosyltransferase, conserved site |
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[seg] | 52 |
63 |
- |
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[seg] | 209 |
225 |
- |
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202 |
304 |
S=379 I=77 E=2.01739e-38 |
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96 |
201 |
S=279 I=50 E=2.29626e-26 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr19730 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr19750 |
ID | hisD |
AC | XFF4834R_chr19740 |
LT | XFF4834R_chr19740 |
OR | XFF4834R_chr from 2266957 to 2268252 on strand + |
DE | histidinol dehydrogenase |
IP | Histidinol dehydrogenase, conserved site |
CL | 1.5.1.16 Histidine GO:0000105 |
EC | |
GO |
InterPro Biological Process: histidine biosynthetic process (GO:0000105) Molecular Function: NAD or NADH binding (GO:0051287) Molecular Function: zinc ion binding (GO:0008270) Molecular Function: histidinol dehydrogenase activity (GO:0004399) Curated |
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by jacques (20110309) |
MW | 44741.4 Da |
SQ | 431 aa |
........10........20........30........40........50 |
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HISX_MF_01024 | raw_score=9990 norm_score=41.075 | Histidinol dehydrogenase [hisD]. |
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YP_363606.1 lcl|hisD-XCV1875 |
1 |
431 |
S=1872 I=88 E=0 |
histidinol dehydrogenase |
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NP_642155.1 lcl|hisD-XAC1829 |
1 |
431 |
S=1857 I=89 E=0 |
histidinol dehydrogenase |
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NP_637174.1 lcl|hisD-XCC1809 |
1 |
431 |
S=1826 I=84 E=0 |
histidinol dehydrogenase |
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1 |
427 |
S=1488 I=75 E=4.48512e-173 |
probable histidinol dehydrogenase (hdh) protein |
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3 |
429 |
S=1039 I=50 E=4.16562e-117 |
Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Manganese Metal-binding NAD Oxidoreductase Zinc |
Pubmed 3062174 |
|
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3 |
429 |
S=1025 I=50 E=1.96478e-115 |
Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc |
Pubmed 10222209 |
|
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3 |
429 |
S=1024 I=49 E=3.1462e-115 |
Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc |
||
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4 |
427 |
S=1002 I=47 E=1.39493e-112 |
Histidine biosynthesis trifunctional protein EC=3.5.4.19 EC=3.6.1.31 EC=1.1.1.23 ; Amino-acid ATP-binding Hydrolase Metal-binding Multifunctional enzyme N |
Pubmed 7874737 |
|
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1 |
427 |
S=991 I=49 E=3.19086e-111 |
HIS4 |
Pubmed 12723033 |
|
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10 |
427 |
S=979 I=48 E=8.17501e-110 |
Histidine biosynthesis trifunctional protein EC=3.5.4.19 EC=3.6.1.31 EC=1.1.1.23 ; Amino-acid ATP-binding Hydrolase Metal-binding Multifunctional |
Pubmed 9639316 |
|
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10 |
427 |
S=934 I=46 E=2.50688e-104 |
Histidine biosynthesis trifunctional protein EC=3.5.4.19 EC=3.6.1.31 EC=1.1.1.23 ; Amino-acid ATP-binding Hydrolase Metal-binding Multifunctional e |
||
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36 |
427 |
S=923 I=49 E=5.07549e-103 |
Histidinol dehydrogenase, chloroplastic EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Plastid Transit peptide Zinc |
Pubmed 2034659 |
|
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10 |
427 |
S=919 I=46 E=1.6905e-102 |
Histidine biosynthesis trifunctional protein EC=3.5.4.19 EC=3.6.1.31 EC=1.1.1.23 ; Amino-acid ATP-binding Hydrolase Metal-binding Multifunctional enzyme N |
Pubmed 9778800 |
|
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1 |
427 |
S=917 I=46 E=2.80306e-102 |
Histidinol dehydrogenase, chloroplastic EC=1.1.1.23 ; Alternative splicing Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Pla |
Pubmed 9501997 |
|
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1 |
431 |
S=1872 I=88 E=0 |
Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc |
||
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1 |
431 |
S=1857 I=89 E=0 |
Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc |
||
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1 |
431 |
S=1826 I=84 E=0 |
Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc |
||
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1 |
431 |
S=1821 I=85 E=0 |
Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc |
||
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1 |
431 |
S=1777 I=87 E=0 |
Histidinol dehydrogenase EC=1.1.1.23 ; Amino-acid biosynthesis Histidine Metal-binding NAD Oxidoreductase Zinc |
||
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[G3DSA:3.40.50.10270] | 25 |
237 |
- |
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[G3DSA:3.40.50.1980] | 236 |
397 |
- |
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IPR012131 [MF_01024] | 4 |
427 |
Histidinol dehydrogenase, prokaryotic-type |
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IPR012131 [PF00815] | 14 |
428 |
Histidinol dehydrogenase, prokaryotic-type |
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IPR012131 [TIGR00069] | 33 |
426 |
Histidinol dehydrogenase, prokaryotic-type |
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IPR001692 [PS00611] | 230 |
262 |
Histidinol dehydrogenase, conserved site |
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[seg] | 24 |
35 |
- |
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[seg] | 269 |
292 |
- |
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6 |
429 |
S=973 I=48 E=1.9207e-110 |
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53 |
197 |
S=185 I=39 E=5.96114e-15 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr19740 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr19760 |
ID | hisC |
AC | XFF4834R_chr19750 |
LT | XFF4834R_chr19750 |
OR | XFF4834R_chr from 2268249 to 2269340 on strand + |
DE | histidinol-phosphate aminotransferase |
IP | Aminotransferase, class I/II; Pyridoxal phosphate-dependent transferase, major region, subdomain 1 |
CL | 1.5.1.16 Histidine GO:0000105 |
EC | |
GO |
InterPro Biological Process: biosynthetic process (GO:0009058) Biological Process: histidine biosynthetic process (GO:0000105) Molecular Function: histidinol-phosphate transaminase activity (GO:0004400) Molecular Function: catalytic activity (GO:0003824) Molecular Function: pyridoxal phosphate binding (GO:0030170) transferring nitrogenous groups (GO:0016769) Curated |
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by jacques (20110309) |
MW | 38594.6 Da |
SQ | 363 aa |
........10........20........30........40........50 |
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HIS8_MF_01023 | raw_score=5199 norm_score=33.849 | Histidinol-phosphate aminotransferase [hisC]. |
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XFF4834R_chr28800 lcl|XFF4834R_chr31420498_3321556_f2_XFF4834R-XFF4834R_chr28800 |
26 |
359 |
S=207 I=29 E=1.68896e-18 |
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XFF4834R_chr12240 lcl|XFF4834R_chr12890671_1386873_f1_XFF4834R-XFF4834R_chr12240 |
62 |
266 |
S=192 I=32 E=1.06221e-16 |
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XFF4834R_chr06390 lcl|XFF4834R_chr06650106_0729290_r2_XFF4834R-XFF4834R_chr06390 |
131 |
305 |
S=131 I=29 E=2.27448e-09 |
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XFF4834R_chr11530 lcl|XFF4834R_chr11990091_1285446_r1_XFF4834R-XFF4834R_chr11530 |
75 |
325 |
S=120 I=28 E=5.24837e-08 |
predicted aminotransferase |
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XFF4834R_chr23260 lcl|XFF4834R_chr25460880_2695028_r2_XFF4834R-XFF4834R_chr23260 |
73 |
244 |
S=95 I=25 E=5.81265e-05 |
methionine aminotransferase, PLP-dependent |
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NP_642156.1 lcl|hisC-XAC1830 |
1 |
363 |
S=1817 I=98 E=0 |
histidinol-phosphate aminotransferase |
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YP_363607.1 lcl|hisC2-XCV1876 |
1 |
363 |
S=1774 I=96 E=0 |
histidinol-phosphate aminotransferase |
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NP_637175.1 lcl|hisC-XCC1810 |
1 |
362 |
S=1638 I=87 E=0 |
histidinol-phosphate aminotransferase |
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3 |
362 |
S=1276 I=71 E=1.77574e-147 |
probable histidinol-phosphate aminotransferase (ihpat) protein |
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NP_636940.1 lcl|hisC-XCC1569 |
30 |
360 |
S=244 I=30 E=2.04206e-22 |
putative aminotransferase |
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53 |
360 |
S=211 I=29 E=2.07105e-18 |
putative histidinol-phosphate aminotransferase protein |
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YP_363398.1 lcl|hisC-XCV1667 |
30 |
359 |
S=206 I=29 E=7.20543e-18 |
putative aminotransferase |
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NP_641958.1 lcl|hisC-XAC1626 |
26 |
359 |
S=203 I=29 E=2.01589e-17 |
putative aminotransferase |
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YP_365269.1 lcl|hisC3-XCV3538 |
62 |
355 |
S=193 I=30 E=2.63929e-16 |
putative aminotransferase |
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NP_643730.1 lcl|hisC-XAC3423 |
62 |
266 |
S=192 I=32 E=4.26328e-16 |
putative aminotransferase |
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1 |
359 |
S=716 I=43 E=5.26977e-78 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
||
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1 |
359 |
S=711 I=43 E=2.10788e-77 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
Pubmed 10222209 |
|
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2 |
356 |
S=667 I=41 E=3.86445e-72 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
Pubmed 3062174 |
|
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3 |
357 |
S=619 I=34 E=2.46491e-66 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
Pubmed 9767718 |
|
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1 |
356 |
S=607 I=35 E=7.99127e-65 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
Pubmed 17592475 |
|
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1 |
359 |
S=584 I=35 E=5.19983e-62 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
Pubmed 17107561 |
|
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9 |
355 |
S=536 I=31 E=2.98719e-56 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
Pubmed 17038625 |
|
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9 |
358 |
S=448 I=32 E=1.56624e-45 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
Pubmed 3302607 |
|
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6 |
356 |
S=445 I=33 E=3.68075e-45 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
Pubmed 2697466 |
|
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10 |
356 |
S=421 I=32 E=2.37423e-42 |
Histidinol-phosphate aminotransferase EC=2.6.1.9 ; Amino-acid biosynthesis Histidine Pyridoxal |
||
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IPR015421 [G3DSA:3.40.640.10] | 53 |
262 |
Pyridoxal phosphate-dependent transferase, major region, subdomain 1 |
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[MF_01023] | 9 |
359 |
- |
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IPR004839 [PF00155] | 29 |
355 |
Aminotransferase, class I/II |
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IPR005861 [TIGR01141] | 11 |
358 |
Histidinol-phosphate aminotransferase |
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6 |
88 |
S=155 I=43 E=2.95586e-11 |
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146 |
174 |
S=136 I=93 E=5.57666e-09 |
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271 |
355 |
S=133 I=34 E=1.44246e-08 |
![]() |
175 |
206 |
S=128 I=84 E=4.76271e-08 |
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203 |
356 |
S=128 I=33 E=5.15149e-08 |
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266 |
356 |
S=123 I=31 E=1.85588e-07 |
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87 |
143 |
S=123 I=40 E=1.95555e-07 |
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71 |
143 |
S=123 I=42 E=2.04268e-07 |
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263 |
359 |
S=119 I=33 E=6.80359e-07 |
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316 |
356 |
S=114 I=59 E=2.918e-06 |
Access unfiltered results
![]() |
Set of Uniprot with relevant PubMed cross-references ncbi-blastp |
103 hits |
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Swiss-Prot ncbi-blastp |
0 hits |
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Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp |
5 hits |
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HAMAP scan |
1 hits |
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IprScan |
4 hits |
Miscellaneous analyses
![]() XFF4834R_chr19750 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr19770 |
ID | hisB |
AC | XFF4834R_chr19760 |
LT | XFF4834R_chr19760 |
OR | XFF4834R_chr from 2269337 to 2270464 on strand + |
DE | bifunctional histidinol-phosphatase/imidazoleglycerol-phosphate dehydratase protein |
IP | Imidazoleglycerol-phosphate dehydratase; Histidinol-phosphatase; HAD-superfamily hydrolase, subfamily IIIA; Polynucleotide kinase 3 phosphatase, central region; Imidazoleglycerol-phosphate dehydratase, conserved site |
CL | 1.5.1.16 Histidine GO:0000105 |
EC | |
GO |
InterPro Biological Process: histidine biosynthetic process (GO:0000105) Cellular Component: cytoplasm (GO:0005737) Molecular Function: histidinol-phosphatase activity (GO:0004401) Molecular Function: imidazoleglycerol-phosphate dehydratase activity (GO:0004424) Molecular Function: catalytic activity (GO:0003824) Curated |
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by jacques (20110309) |
MW | 41857.9 Da |
SQ | 375 aa |
........10........20........30........40........50 |
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HIS7_MF_00076 | raw_score=4622 norm_score=36.141 | Imidazoleglycerol-phosphate dehydratase [hisB]. |
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HIS7_MF_01022 | raw_score=12083 norm_score=52.870 | Histidine biosynthesis bifunctional protein hisB [hisB]. |
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YP_363608.1 lcl|hisB-XCV1877 |
1 |
375 |
S=1888 I=94 E=0 |
imidazole glycerol-phosphate dehydratase/histidinol phosphatase |
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NP_642157.1 lcl|hisB-XAC1831 |
1 |
375 |
S=1871 I=94 E=0 |
imidazole glycerol-phosphate dehydratase/histidinol phosphatase |
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NP_637176.1 lcl|hisB-XCC1811 |
1 |
375 |
S=1830 I=91 E=0 |
imidazole glycerol-phosphate dehydratase/histidinol phosphatase |
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1 |
375 |
S=1564 I=79 E=0 |
probable histidine biosynthesis bifunctional protein hisb (includes:histidinol-phosphatase / imidazoleglycerol-phosphate dehydratase (igpd)). |
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5 |
375 |
S=941 I=51 E=2.43973e-105 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
Pubmed 10222209 |
|
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5 |
375 |
S=940 I=51 E=3.51864e-105 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
||
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5 |
375 |
S=935 I=50 E=1.5491e-104 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
Pubmed 3062174 |
|
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3 |
375 |
S=852 I=45 E=1.73566e-94 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
Pubmed 9767718 |
|
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169 |
375 |
S=430 I=43 E=2.17947e-43 |
Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Amino-acid biosynthesis Cytoplasm Histidine Lyase |
Pubmed 7730278 |
|
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169 |
375 |
S=426 I=42 E=6.42506e-43 |
Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Amino-acid biosynthesis Cytoplasm Histidine Lyase |
Pubmed 17563350 |
|
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163 |
375 |
S=420 I=41 E=3.51759e-42 |
Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Amino-acid biosynthesis Cytoplasm Histidine Lyase |
Pubmed 2664449 |
|
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167 |
375 |
S=414 I=42 E=2.13822e-41 |
Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Histidine biosynthesis Lyase |
Pubmed 18043670 |
|
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169 |
375 |
S=414 I=44 E=2.19488e-41 |
Imidazoleglycerol-phosphate dehydratase EC=4.2.1.19 ; Amino-acid biosynthesis Cytoplasm Histidine Lyase |
Pubmed 12754231 |
|
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173 |
375 |
S=413 I=41 E=2.56784e-41 |
Imidazoleglycerol-phosphate dehydratase 1 EC=4.2.1.19 ; Alternative splicing Amino-acid biosynthesis Histidine Lyase |
Pubmed 8066131 |
|
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1 |
375 |
S=1888 I=94 E=0 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
||
![]() |
1 |
375 |
S=1882 I=94 E=0 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
||
![]() |
1 |
375 |
S=1882 I=94 E=0 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
||
![]() |
1 |
375 |
S=1882 I=94 E=0 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
||
![]() |
1 |
375 |
S=1871 I=94 E=0 |
Histidine biosynthesis bifunctional protein hisB EC=3.1.3.15 EC=4.2.1.19 ; Amino-acid Cytoplasm Hydrolase Lyase Multifunctional enzyme |
||
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[G3DSA:3.40.50.1000] | 2 |
148 |
- |
![]() |
[G3DSA:3.30.230.40] | 166 |
256 |
- |
![]() |
[G3DSA:3.30.230.40] | 275 |
375 |
- |
![]() |
IPR000807 [MF_00076] | 169 |
375 |
Imidazoleglycerol-phosphate dehydratase |
![]() |
IPR020566 [MF_01022] | 1 |
375 |
Histidine biosynthesis bifunctional protein hisB |
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IPR013954 [PF08645] | 3 |
151 |
Polynucleotide kinase 3 phosphatase, central region |
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IPR000807 [PF00475] | 198 |
358 |
Imidazoleglycerol-phosphate dehydratase |
![]() |
IPR005954 [TIGR01261] | 2 |
165 |
Histidinol-phosphatase |
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IPR006543 [TIGR01656] | 3 |
151 |
Histidinol-phosphate phosphatase |
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IPR006549 [TIGR01662] | 3 |
149 |
HAD-superfamily hydrolase, subfamily IIIA |
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IPR020565 [PS00954] | 228 |
241 |
Imidazoleglycerol-phosphate dehydratase, conserved site |
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IPR020565 [PS00955] | 339 |
351 |
Imidazoleglycerol-phosphate dehydratase, conserved site |
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[seg] | 352 |
363 |
- |
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93 |
147 |
S=289 I=96 E=1.65261e-27 |
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280 |
351 |
S=220 I=56 E=3.62945e-19 |
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212 |
259 |
S=198 I=75 E=1.91575e-16 |
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251 |
280 |
S=153 I=93 E=4.48335e-11 |
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148 |
172 |
S=135 I=100 E=8.31226e-09 |
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28 |
83 |
S=125 I=39 E=1.07883e-07 |
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175 |
259 |
S=121 I=38 E=4.31525e-07 |
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1 |
27 |
S=120 I=81 E=4.50753e-07 |
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169 |
211 |
S=112 I=51 E=4.82912e-06 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr19760 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr19780 |
ID | hisH |
AC | XFF4834R_chr19770 |
LT | XFF4834R_chr19770 |
OR | XFF4834R_chr from 2270461 to 2271063 on strand + |
DE | imidazole glycerol phosphate synthase, glutamine amidotransferase subunit with HisF |
IP | Glutamine amidotransferase class-I, C-terminal; Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit H; Glutamine amidotransferase type 1 |
CL | 1.5.1.16 Histidine GO:0000105 |
EC | |
GO |
InterPro Biological Process: histidine biosynthetic process (GO:0000105) Cellular Component: cytoplasm (GO:0005737) Molecular Function: catalytic activity (GO:0003824) Molecular Function: transferase activity (GO:0016740) transferring pentosyl groups (GO:0016763) Curated |
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by jacques (20110309) |
MW | 21227.4 Da |
SQ | 200 aa |
........10........20........30........40........50 |
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HIS5_MF_00278 | raw_score=4101 norm_score=32.166 | Imidazole glycerol phosphate synthase subunit hisH [hisH]. |
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NP_642158.1 lcl|hisH-XAC1832 |
1 |
200 |
S=1020 I=99 E=9.51865e-117 |
imidazole glycerol phosphate synthase subunit HisH |
![]() |
YP_363609.1 lcl|hisH-XCV1878 |
1 |
200 |
S=1009 I=98 E=1.60473e-115 |
imidazole glycerol phosphate synthase subunit HisH |
![]() |
NP_637177.1 lcl|hisH-XCC1812 |
1 |
200 |
S=990 I=95 E=3.54201e-113 |
imidazole glycerol phosphate synthase subunit HisH |
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1 |
200 |
S=866 I=84 E=4.05677e-98 |
probable imidazole glycerol phosphate synthase subunit hish protein |
![]() |
3 |
197 |
S=422 I=38 E=7.96752e-43 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
Pubmed 9767718 |
|
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3 |
197 |
S=421 I=45 E=1.04401e-42 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
Pubmed 3062174 |
|
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3 |
197 |
S=412 I=44 E=1.27477e-41 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
Pubmed 10222209 |
|
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3 |
197 |
S=409 I=45 E=3.3847e-41 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
Pubmed 3062174 |
|
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4 |
194 |
S=374 I=38 E=5.08201e-37 |
Imidazole glycerol phosphate synthase subunit hisH 1 EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
Pubmed 11461915 |
|
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4 |
200 |
S=363 I=42 E=1.04701e-35 |
Imidazole glycerol phosphate synthase hisHF, chloroplastic EC=2.4.2.- EC=4.1.3.- ; Amino-acid biosynthesis Glutamine amidotransferase Histidine Lyase |
Pubmed 9654139 |
|
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2 |
198 |
S=339 I=40 E=1.08146e-32 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
Pubmed 12754231 |
|
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4 |
197 |
S=333 I=38 E=5.47394e-32 |
Imidazole glycerol phosphate synthase subunit hisH 2 EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
||
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4 |
197 |
S=331 I=35 E=8.68931e-32 |
WbuY ; Amino-acid biosynthesis Glutamine amidotransferase Histidine |
Pubmed 15629947 |
|
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1 |
196 |
S=330 I=39 E=1.13859e-31 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
Pubmed 1400209 |
|
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1 |
200 |
S=1020 I=99 E=2.28677e-115 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
||
![]() |
1 |
200 |
S=1009 I=98 E=3.85522e-114 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
||
![]() |
1 |
200 |
S=998 I=97 E=9.13168e-113 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
||
![]() |
1 |
200 |
S=998 I=97 E=9.13168e-113 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
||
![]() |
1 |
200 |
S=990 I=95 E=8.50934e-112 |
Imidazole glycerol phosphate synthase subunit hisH EC=2.4.2.- ; Amino-acid biosynthesis Cytoplasm Glutamine amidotransferase Histidine |
||
![]() |
[G3DSA:3.40.50.880] | 4 |
196 |
- |
![]() |
IPR010139 [MF_00278] | 3 |
197 |
Imidazole glycerol phosphate synthase, subunit H |
![]() |
IPR016226 [PIRSF000495] | 2 |
200 |
Imidazole glycerol phosphate synthase, glutamine amidotransferase subunit H |
![]() |
IPR000991 [PF00117] | 5 |
198 |
Glutamine amidotransferase class-I, C-terminal |
![]() |
IPR010139 [TIGR01855] | 4 |
197 |
Imidazole glycerol phosphate synthase, subunit H |
![]() |
IPR017926 [PS51273] | 3 |
200 |
Glutamine amidotransferase type 1 |
![]() |
94 |
162 |
S=138 I=38 E=3.20641e-09 |
![]() |
4 |
59 |
S=125 I=49 E=1.05781e-07 |
![]() |
61 |
116 |
S=111 I=42 E=5.99183e-06 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr19770 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
![]() |
![]() |
![]() XFF4834R_chr19790 |
ID | hisA |
AC | XFF4834R_chr19780 |
LT | XFF4834R_chr19780 |
OR | XFF4834R_chr from 2271060 to 2271794 on strand + |
DE | N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'-phosphoribosyl)-4-imidazolecarboxamide isomerase |
IP | Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; Ribulose-phosphate binding barrel |
CL | 1.5.1.16 Histidine GO:0000105 |
EC | |
GO |
InterPro Biological Process: histidine biosynthetic process (GO:0000105) Biological Process: metabolic process (GO:0008152) Molecular Function: catalytic activity (GO:0003824) Molecular Function: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity (GO:0003949) Curated |
PM | |
AN | |
CC | COG: [E] Amino acid transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by jacques (20110309) |
MW | 25757.1 Da |
SQ | 244 aa |
........10........20........30........40........50 |
![]() |
HIS4_MF_01014 | raw_score=4527 norm_score=31.624 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase [hisA]. |
![]() |
XFF4834R_chr19790 lcl|hisF-XFF4834R_chr19790 |
1 |
207 |
S=103 I=24 E=4.15382e-06 |
imidazole glycerol phosphate synthase, catalytic subunit with HisH |
![]() |
YP_363610.1 lcl|hisA-XCV1879 |
1 |
244 |
S=1057 I=86 E=4.0608e-121 |
1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase |
![]() |
NP_642159.1 lcl|hisA-XAC1833 |
1 |
244 |
S=1052 I=86 E=1.37633e-120 |
1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase |
![]() |
NP_637178.1 lcl|hisA-XCC1813 |
1 |
244 |
S=982 I=80 E=4.35939e-112 |
1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino] imidazole-4- carboxamide isomerase |
![]() |
1 |
244 |
S=802 I=67 E=2.71987e-90 |
probable1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino) imidazole-4-carboxamide isomerase protein |
![]() |
NP_637179.1 lcl|hisF-XCC1814 |
1 |
207 |
S=110 I=25 E=1.85255e-06 |
imidazole glycerol phosphate synthase subunit HisF |
![]() |
NP_642160.1 lcl|hisF-XAC1834 |
1 |
207 |
S=105 I=24 E=7.74027e-06 |
imidazole glycerol phosphate synthase subunit HisF |
![]() |
YP_363611.1 lcl|hisF-XCV1880 |
1 |
207 |
S=103 I=24 E=1.47556e-05 |
imidazole glycerol phosphate synthase subunit HisF |
![]() |
1 |
207 |
S=100 I=23 E=3.65388e-05 |
probable imidazole glycerol phosphate synthase subunit hisf protein |
![]() |
5 |
244 |
S=520 I=45 E=1.6768e-54 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm H |
Pubmed 10222209 |
|
![]() |
5 |
244 |
S=516 I=45 E=4.18854e-54 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm His |
Pubmed 3062174 |
|
![]() |
5 |
244 |
S=507 I=44 E=5.53183e-53 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Hi |
Pubmed 3062174 |
|
![]() |
5 |
244 |
S=425 I=33 E=4.89798e-43 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Hi |
Pubmed 9767718 |
|
![]() |
5 |
244 |
S=406 I=29 E=8.92403e-41 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Histidine |
Pubmed 17038625 |
|
![]() |
5 |
240 |
S=377 I=31 E=3.4386e-37 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Histidine |
Pubmed 17107561 |
|
![]() |
5 |
240 |
S=364 I=31 E=1.41069e-35 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Histidine |
Pubmed 17592475 |
|
![]() |
3 |
242 |
S=345 I=33 E=2.75593e-33 |
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase EC=5.3.1.16 ; Amino-acid biosynthesis Cytoplasm Histidine |
Pubmed 10594232 |
|
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