3 hits
XFF4834R_chr00130 | pdxJ | XFF4834R_chr00130 | probable pyridoxal phosphate biosynthetic protein PdxJ |
XFF4834R_chr08680 | pdxA | XFF4834R_chr08680 | probable 4-hydroxythreonine-4-phosphate dehydrogenase |
XFF4834R_chr16180 | pdxH | XFF4834R_chr16180 | putative pyridoxine/pyridoxamine 5'-phosphate oxidase |
![]() XFF4834R_chr_0016 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr00140 |
ID | pdxJ |
AC | XFF4834R_chr00130 |
LT | XFF4834R_chr00130 |
OR | XFF4834R_chr from 14490 to 15257 on strand - |
DE | probable pyridoxal phosphate biosynthetic protein PdxJ |
IP | Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ; Aldolase-type TIM barrel |
CL | 1.5.3.6 Pyridoxine (vitamin B6) GO:0008615 |
EC | |
GO |
InterPro Biological Process: metabolic process (GO:0008152) Biological Process: pyridoxine biosynthetic process (GO:0008615) Cellular Component: cytoplasm (GO:0005737) Molecular Function: catalytic activity (GO:0003824) Curated |
PM | |
AN | |
CC | COG: [H] Coenzyme transport and metabolism; |
CC | MODEL: acur |
CC | STATUS: curated by pieretti (20100324) |
MW | 26535.4 Da |
SQ | 255 aa |
........10........20........30........40........50 |
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1 |
248 |
S=478 I=47 E=1.86777e-49 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
Pubmed 18524787 |
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1 |
249 |
S=474 I=45 E=6.167e-49 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
Pubmed 17107561 |
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40 |
172 |
S=281 I=48 E=1.31441e-25 |
GdpxJ protein |
Pubmed 12949166 |
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40 |
172 |
S=281 I=48 E=1.56481e-25 |
GdpxJ protein |
Pubmed 12949166 |
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40 |
172 |
S=281 I=48 E=1.57851e-25 |
GdpxJ protein |
Pubmed 12949166 |
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4 |
243 |
S=281 I=33 E=1.64885e-25 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
Pubmed 9870699 |
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40 |
172 |
S=280 I=48 E=1.84674e-25 |
GdpxJ protein |
Pubmed 12949166 |
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5 |
241 |
S=280 I=34 E=1.94592e-25 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
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40 |
172 |
S=280 I=48 E=1.98015e-25 |
GdpxJ protein |
Pubmed 12949166 |
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40 |
172 |
S=280 I=48 E=2.03262e-25 |
GdpxJ protein |
Pubmed 12949166 |
|
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1 |
255 |
S=1084 I=85 E=5.63014e-123 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
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1 |
255 |
S=1075 I=84 E=6.63896e-122 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
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1 |
255 |
S=1043 I=81 E=4.58792e-118 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
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1 |
255 |
S=1040 I=80 E=1.20759e-117 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
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1 |
255 |
S=1040 I=80 E=1.20759e-117 |
Pyridoxine 5'-phosphate synthase EC=2.6.99.2 ; Cytoplasm biosynthesis Transferase |
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IPR013785 [G3DSA:3.20.20.70] | 5 |
253 |
Aldolase-type TIM barrel |
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IPR004569 [PF03740] | 4 |
248 |
Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ |
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IPR004569 [TIGR00559] | 4 |
250 |
Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ |
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[seg] | 27 |
38 |
- |
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[seg] | 176 |
194 |
- |
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9 |
251 |
S=303 I=34 E=2.7707e-29 |
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IPR004569 [SSF63892] | 1 |
253 |
Pyridoxal phosphate (active vitamin B6) biosynthesis PdxJ |
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Miscellaneous analyses
![]() XFF4834R_chr08670 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr08690 |
ID | pdxA |
AC | XFF4834R_chr08680 |
LT | XFF4834R_chr08680 |
OR | XFF4834R_chr from 1007737 to 1008708 on strand - |
DE | probable 4-hydroxythreonine-4-phosphate dehydrogenase |
IP | Pyridoxal phosphate (active vitamin B6) biosynthesis PdxA |
CL | 1.5.3.6 Pyridoxine (vitamin B6) GO:0008615 |
EC | |
GO |
InterPro Biological Process: pyridoxine biosynthetic process (GO:0008615) Biological Process: oxidation reduction (GO:0055114) Molecular Function: 4-hydroxythreonine-4-phosphate dehydrogenase activity (GO:0050570) Molecular Function: NAD or NADH binding (GO:0051287) Curated |
PM | |
AN | |
CC | COG: [H] Coenzyme transport and metabolism; |
CC | MODEL: XFF4834R |
CC | STATUS: curated by pieretti (20100331) |
MW | 33746.8 Da |
SQ | 323 aa |
........10........20........30........40........50 |
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PDXA_MF_00536 | raw_score=6792 norm_score=34.304 | 4-hydroxythreonine-4-phosphate dehydrogenase [pdxA]. |
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NP_641216.1 lcl|pdxA-XAC0864 |
1 |
308 |
S=1542 I=98 E=8.81105e-180 |
4-hydroxythreonine-4-phosphate dehydrogenase |
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YP_362632.1 lcl|pdxA-XCV0901 |
1 |
308 |
S=1513 I=96 E=2.70644e-176 |
4-hydroxythreonine-4-phosphate dehydrogenase |
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NP_636183.1 lcl|pdxA-XCC0792 |
2 |
308 |
S=1391 I=88 E=1.72836e-161 |
4-hydroxythreonine-4-phosphate dehydrogenase |
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2 |
308 |
S=1068 I=75 E=2.45525e-122 |
probable 4-hydroxythreonine-4-phosphate dehydrogenase protein |
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6 |
308 |
S=732 I=52 E=5.48374e-80 |
4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthes |
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4 |
308 |
S=659 I=52 E=3.25393e-71 |
4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthesis Zin |
Pubmed 19077236 |
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2 |
305 |
S=437 I=38 E=2.49227e-44 |
4-hydroxythreonine-4-phosphate dehydrogenase 2 EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Plasmid Pyridoxine bio |
Pubmed 11481431 |
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4 |
308 |
S=412 I=35 E=2.78439e-41 |
Phosphate biosynthetic protein PdxA ; Cytoplasm Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthesis |
Pubmed 17971441 |
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4 |
305 |
S=410 I=36 E=4.61687e-41 |
4-hydroxythreonine-4-phosphate dehydrogenase 3 EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Plasmid Pyridoxine bio |
Pubmed 11481431 |
|
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4 |
308 |
S=404 I=33 E=2.64027e-40 |
4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 ; Cytoplasm Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthesis |
Pubmed 10484179 |
|
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97 |
308 |
S=345 I=39 E=3.38002e-33 |
Pyridoxal phosphate biosynthetic protein |
Pubmed 17894863 |
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83 |
308 |
S=315 I=38 E=1.73658e-29 |
PdxA homolog ; Plasmid |
Pubmed 8828207 |
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6 |
308 |
S=280 I=31 E=2.65327e-25 |
1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase |
Pubmed 16517628 |
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6 |
308 |
S=273 I=31 E=1.93689e-24 |
1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase |
Pubmed 16517628 |
|
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1 |
308 |
S=1542 I=98 E=2.30413e-178 |
4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthesis Zin |
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2 |
308 |
S=1415 I=91 E=6.53481e-163 |
4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthesis Zin |
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2 |
308 |
S=1400 I=89 E=4.18212e-161 |
4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthesis Zin |
||
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2 |
308 |
S=1391 I=88 E=4.51972e-160 |
4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthesis Zin |
||
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2 |
308 |
S=1391 I=88 E=4.51972e-160 |
4-hydroxythreonine-4-phosphate dehydrogenase EC=1.1.1.262 ; Cobalt Cytoplasm Magnesium Metal-binding NAD NADP Oxidoreductase Pyridoxine biosynthesis Zin |
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IPR005255 [MF_00536] | 2 |
320 |
Pyridoxal phosphate (active vitamin B6) biosynthesis PdxA |
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IPR005255 [PF04166] | 24 |
317 |
Pyridoxal phosphate (active vitamin B6) biosynthesis PdxA |
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IPR005255 [TIGR00557] | 6 |
320 |
Pyridoxal phosphate (active vitamin B6) biosynthesis PdxA |
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[seg] | 309 |
323 |
- |
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11 |
308 |
S=666 I=50 E=3.51522e-73 |
Access unfiltered results
Miscellaneous analyses
![]() XFF4834R_chr16170 |
![]() DrawMap |
XML file
FASTA file |
Extract Sequence |
Codon Usage |
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![]() XFF4834R_chr16190 |
ID | pdxH |
AC | XFF4834R_chr16180 |
LT | XFF4834R_chr16180 |
OR | XFF4834R_chr from 1873590 to 1874189 on strand + |
DE | putative pyridoxine/pyridoxamine 5'-phosphate oxidase |
IP | Pyridoxamine 5'-phosphate oxidase; Pyridoxine 5'-phosphate oxidase, dimerisation, C-terminal; Pyridoxamine 5'-phosphate oxidase, conserved site |
CL | 1.5.3.6 Pyridoxine (vitamin B6) GO:0008615 |
EC | |
GO |
InterPro Biological Process: pyridoxine biosynthetic process (GO:0008615) Biological Process: oxidation reduction (GO:0055114) Molecular Function: pyridoxamine-phosphate oxidase activity (GO:0004733) Molecular Function: FMN binding (GO:0010181) acting on the CH-NH2 group of donors (GO:0016638) Curated |
PM | |
AN | |
CC | COG: [H] Coenzyme transport and metabolism; |
CC | MODEL: acur |
CC | STATUS: curated by pieretti (20100408) |
MW | 22266.8 Da |
SQ | 199 aa |
........10........20........30........40........50 |
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PDXH_MF_01629 | raw_score=5115 norm_score=34.851 | Pyridoxine/pyridoxamine 5'-phosphate oxidase [pdxH]. |
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NP_643318.1 lcl|pdxH-XAC3009 |
1 |
199 |
S=935 I=91 E=1.59401e-106 |
pyridoxamine 5'-phosphate oxidase |
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YP_364890.1 lcl|pdxH-XCV3159 |
1 |
199 |
S=930 I=90 E=7.45939e-106 |
pyridoxamine 5'-phosphate oxidase |
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NP_638188.1 lcl|pdxH-XCC2840 |
1 |
199 |
S=914 I=88 E=5.88495e-104 |
pyridoxamine 5'-phosphate oxidase |
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21 |
199 |
S=673 I=73 E=9.94889e-75 |
putative pyridoxamine 5'-phosphate oxidase protein |
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25 |
199 |
S=476 I=55 E=2.24067e-49 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
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22 |
199 |
S=429 I=49 E=1.04418e-43 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
Pubmed 7524725 |
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26 |
199 |
S=397 I=48 E=8.08196e-40 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
Pubmed 15618402 |
|
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26 |
199 |
S=394 I=43 E=2.3009e-39 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
Pubmed 16707693 |
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26 |
199 |
S=384 I=43 E=3.34468e-38 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
Pubmed 15637156 |
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26 |
199 |
S=381 I=44 E=7.86017e-38 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
Pubmed 17107561 |
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26 |
181 |
S=355 I=45 E=9.49832e-35 |
Pyridoxine-5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase Phosphoprotein Pyridoxal biosynthesis |
Pubmed 9601034 |
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26 |
199 |
S=355 I=43 E=1.03636e-34 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
Pubmed 17592475 |
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26 |
181 |
S=351 I=46 E=3.19132e-34 |
Pyridoxine 5'-phosphate oxidase |
Pubmed 18424774 |
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26 |
181 |
S=351 I=47 E=3.79928e-34 |
Pyridoxine 5'-phosphate oxidase |
Pubmed 16636282 |
|
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1 |
199 |
S=935 I=91 E=3.82445e-105 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
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1 |
199 |
S=930 I=90 E=1.7897e-104 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
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1 |
199 |
S=914 I=88 E=1.24971e-102 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
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1 |
199 |
S=914 I=88 E=1.24971e-102 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
||
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1 |
199 |
S=914 I=88 E=1.41195e-102 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase EC=1.4.3.5 ; Flavoprotein FMN Oxidoreductase biosynthesis |
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IPR012349 [G3DSA:2.30.110.10] | 2 |
199 |
FMN-binding split barrel |
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IPR000659 [MF_01629] | 3 |
199 |
Pyridoxamine 5'-phosphate oxidase |
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IPR011576 [PF01243] | 1 |
105 |
Pyridoxamine 5'-phosphate oxidase-like, FMN-binding domain |
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IPR019576 [PF10590] | 158 |
199 |
Pyridoxine 5'-phosphate oxidase, dimerisation, C-terminal |
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IPR019740 [PS01064] | 168 |
181 |
Pyridoxamine 5'-phosphate oxidase, conserved site |
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[seg] | 4 |
19 |
- |
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101 |
199 |
S=273 I=56 E=1.38379e-25 |
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26 |
99 |
S=219 I=59 E=5.27249e-19 |
Access unfiltered results
Miscellaneous analyses