Xanthomonas fuscans subsp. fuscans

Q7CQV5 sp|Q7CQV5|IAAA_SALTY

S=708 I=50 E=4.00868e-77

Putative asparaginase

Pubmed 16672512

prodomImg

333

S=675 I=48 E=3.56719e-73

Isoaspartyl peptidase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

Pubmed 11325937

prodomImg

A0PCJ8 sp|A0PCJ8|A0PCJ8_STRCL

P50287 sp|P50287|ASPG1_ARATH

S=612 I=44 E=1.54777e-65

Putative asparaginase

Pubmed 10223939,17317567

prodomImg

Q9ZSD6 sp|Q9ZSD6|ASPG_LUPLU

S=558 I=40 E=5.35798e-59

Isoaspartyl peptidase/L-asparaginase 1 EC=3.4.19.5 ; Alternative splicing Autocatalytic cleavage Hydrolase Protease

Pubmed 7630960

prodomImg

P30364 sp|P30364|ASPG_LUPAN

S=556 I=40 E=9.69357e-59

Isoaspartyl peptidase/L-asparaginase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

Pubmed 15265041,16725155

prodomImg

P30362 sp|P30362|ASPG_LUPAR

S=555 I=40 E=1.30384e-58

Isoaspartyl peptidase/L-asparaginase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

Pubmed 1391778

prodomImg

Q2PW34 sp|Q2PW34|Q2PW34_PHAVU

S=543 I=41 E=3.74136e-57

Isoaspartyl peptidase/L-asparaginase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

Pubmed 1377963

prodomImg

332

S=513 I=37 E=1.82425e-53

L-asparaginase 2 EC=3.5.1.1 ; Hydrolase

Pubmed 16705405

prodomImg

Q8VI04 sp|Q8VI04|ASGL1_RAT

258

S=454 I=45 E=2.23575e-46

L-asparaginase EC=3.5.1.1 ; Cytoplasm Hydrolase

Pubmed 11984834,12753071

prodomImg

Q7L266 sp|Q7L266|ASGL1_HUMAN

P37595 sp|P37595|IAAA_ECOLI

S=447 I=37 E=1.87642e-45

L-asparaginase EC=3.5.1.1 ; Alternative splicing Cytoplasm Hydrolase

Pubmed 11984834,14654938

prodomImg

Q7CQV5 sp|Q7CQV5|IAAA_SALTY

S=684 I=47 E=2.12015e-74

Isoaspartyl peptidase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

prodomImg

333

S=675 I=48 E=2.45682e-73

Isoaspartyl peptidase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

prodomImg

P50288 sp|P50288|ASPG_LUPAL

S=560 I=39 E=2.51445e-59

Isoaspartyl peptidase/L-asparaginase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

prodomImg

IPR000246 [PF01112]

335

Peptidase T2, asparaginase 2

291

304

[tmhmm]

PD412181

319

S=640 I=51 E=4.57528e-70

PDA4H621

139

245

S=277 I=49 E=3.86957e-26

PDA9A888

177

S=178 I=31 E=3.69968e-14

PD840411

238

S=165 I=29 E=1.69997e-12

PD526666

144

S=156 I=33 E=1.82125e-11

PDA2B2I6

264

333

S=117 I=37 E=9.26819e-07

PD932517

258

329

S=106 I=31 E=2.37452e-05

Q47898 sp|Q47898|ASPG_ELIMR

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ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one wnkgdxQX)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	21 hits
	Swiss-Prot ncbi-blastp	39 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	1 hits
	HAMAP scan	0 hits
	IprScan	4 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr02210.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr02210.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr02210.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr02210.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

XFF4834R_chr16530939_1772342_f3_XFF4834R-XFF4834R_chr15380 XFF4834R_chr15380

ID	XFF4834R_chr16530939_1772342_f3_XFF4834R-XFF4834R_chr15380
AC	XFF4834R_chr15380
LT	XFF4834R_chr15380
OR	XFF4834R_chr from 1770939 to 1772342 on strand +
DE	putative asparaginase
IP	Peptidase T2, asparaginase 2; Twin-arginine translocation pathway, signal sequence
CL	1.7.13 Amino acid conversion GO:0006520
EC
GO	InterPro Molecular Function: hydrolase activity (GO:0016787) Curated : (GO:0006529)
PM
AN	classification according to GenProtEC for asparaginase
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by darrasse (20120402)
MW	50312.1 Da
SQ	467 aa
	........10........20........30........40........50 \| \| \| \| \| MAPLSRPGLHGRCSRRGRHDAERDRCLRAPGNSVVRQPTAWRCGTFQQRR CIAGQARRDPCLSRARRSQPGKGCARIRIRQRRNKVYPHATLSHDGKLVP HCAAARFRHGVIRMLQRRHFLKSATLGAIASGLAGWGARAQAAAGATPGM RPTALPRGAARVISTWDFGVAANQEAWKILSSGGIALDAVEAGVRVPEAD PNNPTVGLGGYPDRDGRVTLDACIMDHLGNCGAVASLEDVVHAISVARAV MEKTPHVMLVGDGARQFAFEQGFPKTTLLTPSSEAAWKEWLKTSKYSPEA NVENRAWRDAKLPGGKDNHDTIGMLALDTHGNLSGACTTSGMAWKMHGRV GDSPIIGAGLYVDNEVGGATSTGVGEEVIRNVGSFAVVEMMRQGKLPADA CREVVMRLIRRKPELTRTLQVGFLAMNKRGEVGAFAIQKGFSYAVCDAQR QDLLVPGESHYTSEPAA

XFF4834R_chr02210 lcl|iaaA-XFF4834R_chr02210

179

406

S=321 I=38 E=3.68603e-32

L-asparaginase

YP_364953.1 lcl|XCV3222

114

467

S=1731 I=93 E=0

asparaginase precursor

NP_643401.2 lcl|aspG-XAC3092

114

467

S=1730 I=93 E=0

asparaginase

NP_638262.2 lcl|aspG-XCC2914

114

467

S=1638 I=88 E=0

asparaginase

lcl|XALc_2229

114

467

S=1461 I=79 E=9.73469e-170

putative asparaginase protein

NP_635624.1 lcl|ansA-XCC0229

179

406

S=327 I=39 E=2.34583e-32

asparaginase

NP_640604.1 lcl|ansA-XAC0248

179

406

S=321 I=38 E=1.4013e-31

asparaginase

YP_361985.1 lcl|XCV0254

179

406

S=318 I=39 E=2.64817e-31

asparaginase precursor

NP_643403.1 lcl|XAC3094-XAC3094

S=147 I=72 E=1.58306e-10

hypothetical protein

S=955 I=62 E=7.93071e-107

457

N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase EC=3.5.1.26 ; Hydrolase Periplasm Signal

Pubmed 7840643,8250923

prodomImg

O02467 sp|O02467|ASPG_SPOFR

P20933 sp|P20933|ASPG_HUMAN

455

S=502 I=41 E=4.94113e-52

N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase EC=3.5.1.26 ; Disulfide bond Glycoprotein Hydrolase Lysosome

Pubmed 8877373

prodomImg

P30919 sp|P30919|ASPG_RAT

451

S=407 I=36 E=2.01025e-40

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase EC=3.5.1.26 ; Disease mutation Disulfide bond Glycoprotein Hydrolase Lysosome Polymorphism Signal

Pubmed 2401370,2265705

prodomImg

Q64191 sp|Q64191|ASPG_MOUSE

415

S=384 I=41 E=1.27428e-37

N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase EC=3.5.1.26 ; Disulfide bond Glycoprotein Hydrolase Lysosome Signal

Pubmed 2775174

prodomImg

Q7CQV5 sp|Q7CQV5|IAAA_SALTY

415

S=380 I=40 E=3.69163e-37

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase EC=3.5.1.26 ; Disulfide bond Glycoprotein Hydrolase Lysosome Signal

Pubmed 8586423

prodomImg

174

432

S=367 I=38 E=1.376e-35

Isoaspartyl peptidase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

Pubmed 11325937

prodomImg

Q8VI04 sp|Q8VI04|ASGL1_RAT

169

431

S=346 I=38 E=4.53569e-33

L-asparaginase EC=3.5.1.1 ; Cytoplasm Hydrolase

Pubmed 11984834,12753071

prodomImg

Q9ZSD6 sp|Q9ZSD6|ASPG_LUPLU

187

432

S=317 I=35 E=1.28806e-29

Isoaspartyl peptidase/L-asparaginase EC=3.4.19.5 ; Autocatalytic cleavage Hydrolase Protease

Pubmed 15265041,16725155

prodomImg

A0PCJ8 sp|A0PCJ8|A0PCJ8_STRCL

171

459

S=303 I=34 E=8.10076e-28

Putative asparaginase

Pubmed 10223939,17317567

prodomImg

Q7L266 sp|Q7L266|ASGL1_HUMAN

177

400

S=298 I=38 E=2.89305e-27

L-asparaginase EC=3.5.1.1 ; Alternative splicing Cytoplasm Hydrolase

Pubmed 11984834,14654938

prodomImg

Q47898 sp|Q47898|ASPG_ELIMR

S=955 I=62 E=5.45744e-107

457

N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase EC=3.5.1.26 ; Hydrolase Periplasm Signal

prodomImg

O02467 sp|O02467|ASPG_SPOFR

455

S=502 I=41 E=3.40019e-52

N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase EC=3.5.1.26 ; Disulfide bond Glycoprotein Hydrolase Lysosome

prodomImg

IPR000246 [PF01112]

162

441

Peptidase T2, asparaginase 2

IPR006311 [TIGR01409]

115

140

Twin-arginine translocation pathway, signal sequence

132

149

PD412181

164

457

S=502 I=43 E=2.91377e-53

PDA7W471

113

S=169 I=67 E=5.51454e-13

PDA4H621

256

365

S=147 I=35 E=2.64457e-10

PD633218

S=147 I=72 E=3.04046e-10

PDA2U930

114

163

S=120 I=58 E=5.29892e-07

IPR001920 [G3DSA:3.40.50.1860]

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Move your mouse over each field to get more informations
ID
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EC
GO
PM
CC
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Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	21 hits
	Swiss-Prot ncbi-blastp	38 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	1 hits
	HAMAP scan	0 hits
	IprScan	3 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr15380.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr15380.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr15380.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr15380.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

XFF4834R_chr_2211526_2212230_r1_XFF4834R-XFF4834R_chr19310 XFF4834R_chr19310

ID	XFF4834R_chr_2211526_2212230_r1_XFF4834R-XFF4834R_chr19310
AC	XFF4834R_chr19310
LT	XFF4834R_chr19310
OR	XFF4834R_chr from 2211526 to 2212230 on strand -
DE	putative Asp/Glu racemase
IP	Aspartate racemase; Asp/Glu/hydantoin racemase
CL	1.7.13 Amino acid conversion GO:0006520
EC
GO	InterPro Biological Process: metabolic process (GO:0008152) Biological Process: cellular amino acid metabolic process (GO:0006520) acting on amino acids and derivatives (GO:0016855) Curated
PM
AN	CL: also 1.6.7 Peptidoglycan (murein) : Aspartate racemase (EC:5.1.1.13) and glutamate racemase (EC:5.1.1.3) are two evolutionary related bacterial enzymes that do not seem to require a cofactor for their activity [1]. Glutamate racemase, which interconverts L-glutamate into D-glutamate, is required for the biosynthesis of peptidoglycan and some peptide-based antibiotics such as gramicidin S.
CC	COG: [M] Cell wall/membrane/envelope biogenesis;
CC	MODEL: XFF4834R
CC	STATUS: curated by irobene (20100825)
MW	25068.6 Da
SQ	234 aa
	........10........20........30........40........50 \| \| \| \| \| MPVPSMTIGLIGGMSWESTLPYYRIINQRVRHACGGLHSAKLLLYSVNFH EIERLQHTGDWDGAGQAMAAAARALQAAGADFIVLCTNTMHCVADAITAA TPLPLLHIADATADALVAAGISRIGLLGTRFTMEQPFYRQRLQARGPDVL VPPAEARAQLHRVIYDELCQGVIKPESRQYVCQVMTELGQHGAQAIILGC TEISLLVDSTDAQLPLFDTTALHAEAAALASLSG

YP_363563.1 XCV1832

220

S=961 I=83 E=1.35195e-109

putative aspartate racemase

NP_642129.1 ygeA-XAC1802

220

S=947 I=83 E=7.26766e-108

putative resistance protein

NP_637151.1 ygeA-XCC1785

220

S=916 I=79 E=3.73396e-104

putative resistance protein

P03813 acc=P03813

219

S=549 I=49 E=5.44101e-58

Uncharacterized protein ygeA ; Isomerase

Pubmed 6350602,2836407

prodomImg

Q9RQR2 acc=Q9RQR2

220

S=472 I=44 E=9.68526e-49

Aspartate racemase

Pubmed 8318541,8086457

prodomImg

Q8GL47 acc=Q8GL47

220

S=269 I=30 E=4.07149e-24

Putative aminoacid racemase Orfc372-4

Pubmed 12618374

prodomImg

P70716 acc=P70716

170

S=217 I=33 E=9.03516e-18

LysA activator protein

Pubmed 9020051

prodomImg

O58403 acc=O58403

218

S=178 I=28 E=3.96452e-13

228aa long hypothetical aspartate racemase

Pubmed 12051922

prodomImg

P03813 acc=P03813

219

S=549 I=49 E=3.71278e-58

Uncharacterized protein ygeA ; Isomerase

prodomImg

P29079 acc=P29079

218

S=145 I=26 E=2.81639e-09

Aspartate racemase EC=5.1.1.13 ; Isomerase

prodomImg

P32960 acc=P32960

220

S=131 I=23 E=1.47491e-07

Probable amino-acid racemase EC=5.1.1.- ; Cell shape wall biogenesis/degradation Isomerase Peptidoglycan synthesis Sporulation

prodomImg

110

234

Asp/Glu racemase

IPR015942 [PF01177]

227

Asp/Glu/hydantoin racemase

IPR004380 [TIGR00035]

234

Aspartate racemase

IPR018187 [PS00924]

196

206

Asp/Glu racemase, active site

109

119

221

233

PDA1F9U0

124

179

S=201 I=63 E=6.09043e-17

PD355676

124

S=183 I=44 E=9.73629e-15

PD797741

120

218

S=117 I=24 E=1.11193e-06

PD434072

S=106 I=68 E=2.49953e-05

PDA3C2S1

220

S=105 I=28 E=3.10829e-05

IPR001920 [SSF53681]

120

Asp/Glu racemase

IPR001920 [SSF53681]

108

219

Asp/Glu racemase

raw_score=5367 norm_score=30.789

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Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one DsDjvXB6)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	13 hits
	Swiss-Prot ncbi-blastp	3 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	0 hits
	IprScan	9 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr19310.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr19310.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr19310.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr19310.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

argC XFF4834R_chr23510

ID	argC
AC	XFF4834R_chr23510
LT	XFF4834R_chr23510
OR	XFF4834R_chr from 2721861 to 2722811 on strand -
DE	N-acetyl-gamma-glutamylphosphate reductase, NAD(P)-binding
IP	Semialdehyde dehydrogenase, NAD-binding; N-acetyl-gamma-glutamyl-phosphate reductase; Semialdehyde dehydrogenase, dimerisation region
CL	1.7.13 Amino acid conversion GO:0006520
EC
GO	InterPro Biological Process: cellular amino acid biosynthetic process (GO:0008652) Biological Process: arginine biosynthetic process (GO:0006526) Biological Process: cellular amino acid metabolic process (GO:0006520) Cellular Component: cytoplasm (GO:0005737) Molecular Function: protein dimerization activity (GO:0046983) Molecular Function: NAD or NADH binding (GO:0051287) Molecular Function: N-acetyl-gamma-glutamyl-phosphate reductase activity (GO:0003942) NAD or NADP as acceptor (GO:0016620) Curated
PM
AN
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by jacques (20110221)
MW	34213.8 Da
SQ	316 aa
	........10........20........30........40........50 \| \| \| \| \| MTVQPKTIGIVGARGHTGSELIKLVAAHPQLQLSFVSSRELAGQRVAEHN DAYQGELRYENLDADAVAVKAADVVILALPNGKAAPFVAAIDAATPQTLV IDLSADYRFDPAWYYGLPELTRGSYAGQRRISNPGCYATAMQLTIAPLLD QLAGPPQCFGVSGYSGAGTTPSDKNNPELLSNNLMPYALTNHMHEREVSA QLGVPVEFMPHVAPHFRGITMTVNLWLQQPLTREQIQARYTQRYADEPLI EIVDEAPWVSRIAGKHGVQIGGITLAPGNKRVVVVATLDNMLKGAATQAM QNLNLALGWDELMAIR

Domain decomposition

ARGC_MF_00150

N-acetyl-gamma-glutamyl-phosphate reductase [argC].

NP_642662.1 lcl|argC-XAC2346

316

S=1556 I=93 E=0

N-acetyl-gamma-glutamyl-phosphate reductase

YP_364276.1 lcl|argC-XCV2545

316

S=1517 I=91 E=8.46478e-177

N-acetyl-gamma-glutamyl-phosphate reductase

NP_637598.1 lcl|argC-XCC2243

315

S=1417 I=84 E=1.09811e-164

N-acetyl-gamma-glutamyl-phosphate reductase

lcl|argC-XALc_1890

315

S=1258 I=73 E=2.51794e-145

probable n-acetyl-gamma-glutamyl phosphate reductase, nad(p)-binding protein

P54898 sp|P54898|ARG56_NEUCR

P78586 sp|P78586|ARG56_CANAL

S=800 I=50 E=2.68683e-88

Protein arg-6, mitochondrial EC=1.2.1.38 EC=2.7.2.8 ; Amino-acid biosynthesis Arginine ATP-binding Kinase Mitochondrion Multifunctional enzyme

Pubmed 7907589

prodomImg

P31318 sp|P31318|ARG56_SCHPO

S=779 I=50 E=1.04523e-85

Protein ARG5,6, mitochondrial EC=1.2.1.38 EC=2.7.2.8 ; Amino-acid biosynthesis Arginine ATP-binding Kinase Mitochondrion Multifunctional enzyme NADP

Pubmed 9043106

prodomImg

Q01217 sp|Q01217|ARG56_YEAST

S=767 I=46 E=2.70132e-84

Protein arg11, mitochondrial EC=1.2.1.38 EC=2.7.2.8 ; Amino-acid biosynthesis Arginine ATP-binding Cleavage pair of basic residues Kinase Mi

Pubmed 1313366

prodomImg

Q0W932 sp|Q0W932|ARGC_UNCMA

S=722 I=46 E=7.08052e-79

Protein ARG5,6, mitochondrial EC=1.2.1.38 EC=2.7.2.8 ; Amino-acid biosynthesis Arginine ATP-binding Kinase Mitochondrion Multifunctional enzyme

Pubmed 1851947

prodomImg

311

S=407 I=34 E=9.80687e-41

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

Pubmed 16857943

prodomImg

A5ULI7 sp|A5ULI7|ARGC_METS3

B7JAI2 sp|B7JAI2|ARGC_ACIF2

S=371 I=30 E=2.78266e-36

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

Pubmed 17563350

prodomImg

304

S=340 I=33 E=1.29892e-32

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

Pubmed 19077236

prodomImg

B0TCA6 sp|B0TCA6|ARGC_HELMI

P54895 sp|P54895|ARGC_STRCO

S=338 I=32 E=2.63203e-32

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

Pubmed 18441057

prodomImg

311

S=320 I=30 E=4.06341e-30

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

Pubmed 8180696

prodomImg

Q9Z4S2 sp|Q9Z4S2|ARGC_THENN

311

S=318 I=30 E=7.28763e-30

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

Pubmed 10931207

prodomImg

Q8PK31 sp|Q8PK31|ARGC_XANAC

316

S=1556 I=93 E=4.19158e-180

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

prodomImg

Q3BSI7 sp|Q3BSI7|ARGC_XANC5

316

S=1517 I=91 E=2.20876e-175

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

prodomImg

Q2P2F6 sp|Q2P2F6|ARGC_XANOM

S=1479 I=89 E=1.03017e-170

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

prodomImg

B0RS54 sp|B0RS54|ARGC_XANCB

S=1429 I=85 E=1.23098e-164

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

prodomImg

Q8P8J8 sp|Q8P8J8|ARGC_XANCP

S=1417 I=84 E=2.86536e-163

N-acetyl-gamma-glutamyl-phosphate reductase EC=1.2.1.38 ; Amino-acid biosynthesis Arginine Cytoplasm NADP Oxidoreductase

prodomImg

[MF_00150]

316

IPR000534 [PF01118]

128

Semialdehyde dehydrogenase, NAD-binding

IPR012280 [PF02774]

145

293

Semialdehyde dehydrogenase, dimerisation region

IPR000534 [SM00859]

128

Semialdehyde dehydrogenase, NAD-binding

IPR000706 [TIGR01850]

316

N-acetyl-gamma-glutamyl-phosphate reductase

IPR000706 [PS01224]

131

147

N-acetyl-gamma-glutamyl-phosphate reductase

PD003765

162

315

S=252 I=39 E=5.10783e-23

PDA809O0

S=140 I=57 E=1.59713e-09

PDA1H1L0

118

S=124 I=67 E=1.36288e-07

PDA8F7A0

100

155

S=115 I=39 E=2.01599e-06

Q8P8J2 sp|Q8P8J2|AOTC_XANCP

Suggest an annotation
Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one xo5pC4J8)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	44 hits
	Swiss-Prot ncbi-blastp	0 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	1 hits
	IprScan	7 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23510.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23510.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23510.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23510.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

argF XFF4834R_chr23570

ID	argF
AC	XFF4834R_chr23570
LT	XFF4834R_chr23570
OR	XFF4834R_chr from 2727925 to 2728950 on strand -
DE	N-acetyl ornithine carbamoyltransferase
IP	Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding region; Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
CL	1.7.13 Amino acid conversion GO:0006520
EC
GO	InterPro Biological Process: cellular amino acid metabolic process (GO:0006520) Molecular Function: carboxyl- or carbamoyltransferase activity (GO:0016743) Molecular Function: amino acid binding (GO:0016597) Curated
PM
AN	chgt nom cf publi fonctionnel chez Xcc
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by jacques (20110221)
MW	38065.1 Da
SQ	341 aa
	........10........20........30........40........50 \| \| \| \| \| MSLKHFLNTQDWSRAELDALLTQAALFKRNKLGSELKGKSIALVFFNPSM RTRTSFELGAFQLGGHAVVLQPGKDAWPIEFNLGTVMDGDTEEHIAEVAR VLGRYVDLIGVRAFPKFVDWSKDREDQVLKSFAKYSPVPVINMETITHPC QELAHALALQEHFGTQDLRGKKYVLTWTYHPKPLNTAVANSALTIATRMG MDVTLLCPTPDYILDQRYMDWAAQNVAESGGSLQVSHDIDSAYAGADVVY AKSWGALPFFGNWEPEKPIRDQYQHFIVDERKMALTNNGVFSHCLPLRRN VKATDAVMDSPNCIAIDEAENRLHVQKAIMAALVGQGSRDS

YP_364282.1 lcl|argF-XCV2551

340

S=1810 I=98 E=0

N-acetylornithine carbamoyltransferase

NP_637604.1 lcl|argF-XCC2249

336

S=1807 I=99 E=0

N-acetylornithine carbamoyltransferase

NP_642668.1 lcl|argF-XAC2352

337

S=1805 I=99 E=0

N-acetylornithine carbamoyltransferase

lcl|argF-XALc_1896

341

S=1754 I=94 E=0

probable ornithine carbamoyltransferase, chain f protein

lcl|PyrB-XALc_2155

335

S=126 I=25 E=3.30765e-08

putative aspartate carbamoyltransferase, catalytic subunit protein

Q8A1E9 sp|Q8A1E9|AOTC_BACTN

S=1807 I=99 E=0

N-acetylornithine carbamoyltransferase EC=2.1.3.9 ; Amino-acid biosynthesis Arginine Cytoplasm

Pubmed 15731101

prodomImg

Q51742 sp|Q51742|OTC_PYRFU

S=476 I=36 E=4.84331e-49

N-acetylornithine carbamoyltransferase EC=2.1.3.9 ; Amino-acid biosynthesis Arginine Cytoplasm

Pubmed 12095263

prodomImg

A8Z5X7 sp|A8Z5X7|A8Z5X7_SULMW

S=451 I=38 E=6.3859e-46

Ornithine carbamoyltransferase EC=2.1.3.3 ; Amino-acid biosynthesis Arginine Cytoplasm

Pubmed 9288929,9288930

prodomImg

A5UMK3 sp|A5UMK3|OTC_METS3

S=446 I=32 E=2.12696e-45

Putative ornithine carbamoyltransferase

Pubmed 18048332

prodomImg

330

S=401 I=34 E=6.75385e-40

Ornithine carbamoyltransferase EC=2.1.3.3 ; Amino-acid biosynthesis Arginine Cytoplasm

Pubmed 17563350

prodomImg

O50039 sp|O50039|OTC_ARATH

A2BM26 sp|A2BM26|OTC_HYPBU

S=386 I=36 E=3.85913e-38

Ornithine carbamoyltransferase, chloroplastic EC=2.1.3.3 ; Amino-acid biosynthesis Arginine Plastid Transit peptide

Pubmed 10561504

prodomImg

S=360 I=36 E=5.9012e-35

Ornithine carbamoyltransferase EC=2.1.3.3 ; Amino-acid biosynthesis Arginine Cytoplasm

Pubmed 17350933

prodomImg

Q43814 sp|Q43814|OTC_PEA

P18186 sp|P18186|OTC_BACSU

S=356 I=33 E=1.72457e-34

Ornithine carbamoyltransferase, chloroplastic EC=2.1.3.3 ; Amino-acid biosynthesis Arginine Plastid Transit peptide

Pubmed 8914525

prodomImg

337

S=352 I=33 E=5.64476e-34

Ornithine carbamoyltransferase EC=2.1.3.3 ; Amino-acid biosynthesis Arginine Cytoplasm

Pubmed 2117745,8025667

prodomImg

Q9SEX4 sp|Q9SEX4|Q9SEX4_CANLI

Q8P8J2 sp|Q8P8J2|AOTC_XANCP

S=352 I=31 E=5.89628e-34

Ornithine carbamoyltransferase EC=2.1.3.3 Ornithine carbamoyltransferase OOCT1

Pubmed 10987149

prodomImg

Q8PK25 sp|Q8PK25|AOTC_XANAC

S=1807 I=99 E=0

N-acetylornithine carbamoyltransferase EC=2.1.3.9 ; Amino-acid biosynthesis Arginine Cytoplasm

prodomImg

337

S=1805 I=99 E=0

N-acetylornithine carbamoyltransferase EC=2.1.3.9 ; Amino-acid biosynthesis Arginine Cytoplasm

prodomImg

Q87EL4 sp|Q87EL4|AOTC_XYLFT

Q9PEN0 sp|Q9PEN0|AOTC_XYLFA

S=1571 I=84 E=0

N-acetylornithine carbamoyltransferase EC=2.1.3.9 ; Amino-acid biosynthesis Arginine Cytoplasm

prodomImg

Q8A1E9 sp|Q8A1E9|AOTC_BACTN

S=1567 I=84 E=0

N-acetylornithine carbamoyltransferase EC=2.1.3.9 ; Amino-acid biosynthesis Arginine Cytoplasm

prodomImg

S=476 I=36 E=3.33515e-49

N-acetylornithine carbamoyltransferase EC=2.1.3.9 ; Amino-acid biosynthesis Arginine Cytoplasm

prodomImg

[G3DSA:3.40.50.1370]

149

[G3DSA:3.40.50.1370]

151

336

IPR006132 [PF02729]

162

Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding

IPR006131 [PF00185]

187

333

Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding region

PD816676

143

261

S=359 I=57 E=5.3049e-36

PD919839

142

S=282 I=75 E=9.86373e-27

PD000708

S=150 I=41 E=1.05273e-10

PD409592

282

335

S=112 I=42 E=4.12428e-06

Q9KWC6 sp|Q9KWC6|Q9KWC6_AGRRH

Suggest an annotation
Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one ELjSdwCV)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	120 hits
	Swiss-Prot ncbi-blastp	0 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	0 hits
	IprScan	4 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23570.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23570.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23570.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23570.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

eutB XFF4834R_chr23700

ID	eutB
AC	XFF4834R_chr23700
LT	XFF4834R_chr23700
OR	XFF4834R_chr from 2739221 to 2740630 on strand +
DE	ethanolamine ammonia-lyase, large subunit, heavy chain
IP	Ethanolamine ammonia lyase large subunit
CL	1.7.13 Amino acid conversion GO:0006520
EC
GO	InterPro Biological Process: cellular amino acid metabolic process (GO:0006520) Molecular Function: ethanolamine ammonia-lyase activity (GO:0008851) Curated
PM
AN
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by jacques (20110221)
MW	50136.5 Da
SQ	469 aa
	........10........20........30........40........50 \| \| \| \| \| MSGFAFTAGGERFRFADLKQLLAKATPARSGDQLAGLAADSGLQRVAAQM ALADLPLQHFLQEAVVPYEADEVTRLIIDQHDAAAFAAVAHLTVGGFRDW LLSAQADEAALTALAPGLTPEMVAAVSKLMRVQDLILVAQKTRVVTCFRN TLGLRGRLSTRLQPNHPTDDATGIAASVLDGLLYGNGDAVIGINPASDSL AATTALLRMLDAVISGYRIPTQSCVLAHITTTIEAIGRGVPVDLVFQSIA GTEAANASFGINLALLQEGYEAGLSLRRGSVGDNVMYFETGQGSALSANA HHGVDQQTCEVRAYAVARHYKPLLVNTVVGFIGPEYLYDGKQIIRAGLED HFCGKLLGVPMGCDICYTNHAEADQDDMDMLLTLLGTAGINFIMGIPGSD DVMLNYQTTSFHDALYARQALGLRAAPEFEQWLEQHDILQLRDGRFELGS EVPAPFRRALAQVSGRTTP

NP_642681.1 lcl|eutA-XAC2365

469

S=2040 I=84 E=0

ethanolamine ammonia-lyase large subunit

YP_364294.1 lcl|eutA-XCV2563

469

S=2013 I=83 E=0

ethanolamine ammonia-lyase, large subunit

NP_637615.1 lcl|eutA-XCC2260

463

S=1854 I=78 E=0

ethanolamine ammonia-lyase large subunit

446

S=1297 I=57 E=2.41345e-148

Riorf58 protein ; Plasmid

Pubmed 10907845,11273700

prodomImg

Q59781 sp|Q59781|Q59781_RHOER

435

S=1279 I=58 E=4.59319e-146

Ethanolamine ammonia-lyase large subunit EC=4.3.1.7

Pubmed 7836301,8069783

prodomImg

P19264 sp|P19264|EUTB_SALTY

S=970 I=45 E=1.11245e-108

Ethanolamine ammonia-lyase heavy chain EC=4.3.1.7 ; Cobalamin Cobalt

Pubmed 2197274,10464203

prodomImg

P0AEJ6 sp|P0AEJ6|EUTB_ECOLI

S=971 I=45 E=5.69117e-109

Ethanolamine ammonia-lyase heavy chain EC=4.3.1.7 ; Cobalt

prodomImg

P0AEJ7 sp|P0AEJ7|EUTB_ECO57

S=971 I=45 E=5.69117e-109

Ethanolamine ammonia-lyase heavy chain EC=4.3.1.7 ; Cobalt

prodomImg

P19264 sp|P19264|EUTB_SALTY

S=970 I=45 E=7.65495e-109

Ethanolamine ammonia-lyase heavy chain EC=4.3.1.7 ; Cobalamin Cobalt

prodomImg

IPR010628 [PIRSF018788]

461

Ethanolamine ammonia lyase large subunit

IPR010628 [PF06751]

456

Ethanolamine ammonia lyase large subunit

102

120

149

162

200

207

373

389

PDA1G1M5

163

424

S=1042 I=76 E=1.08617e-118

PD025217

145

S=293 I=56 E=5.28073e-28

PDA1G2B7

S=170 I=67 E=4.99254e-13

PD574787

426

464

S=121 I=59 E=4.32077e-07

PDA1G924

S=112 I=68 E=4.43157e-06

raw_score=6492 norm_score=41.323

Suggest an annotation
Move your mouse over each field to get more informations
ID
DE
EC
GO
PM
CC
CL
	Your email
	Validation code (copy this one vvRFQN6e)

Access unfiltered results

	Set of Uniprot with relevant PubMed cross-references ncbi-blastp	3 hits
	Swiss-Prot ncbi-blastp	3 hits
	Xanthomonas fuscans subsp. fuscans proteome ncbi-blastp	0 hits
	HAMAP scan	0 hits
	IprScan	7 hits

Miscellaneous analyses

ERROR Tag PERLLIB Portal/Tools.pl GetLocalBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23700.xml_fasta", "https://iant.toulouse.inra.fr/bacteria/annotation/web/img/XFF4834R.png"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetNcbiBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23700.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetUniprotBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23700.xml_fasta"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

ERROR Tag PERLLIB Portal/Tools.pl GetKeggBlastButton\("/www/bacteria/annotation//site//www/bacteria/annotation//site/tmp/WBZQLsT5/XFF4834R_chr23700.xml_fasta", "blastp"\) - ERROR: No such file or directory at /www/bacteria/annotation/cgi/XFF4834R/../../lib/iANT/Entry/Display.pm line 164.

eutC XFF4834R_chr23710

ID	eutC
AC	XFF4834R_chr23710
LT	XFF4834R_chr23710
OR	XFF4834R_chr from 2740627 to 2741442 on strand +
DE	ethanolamine ammonia-lyase, small subunit (light chain)
IP	Ethanolamine ammonia-lyase light chain
CL	1.7.13 Amino acid conversion GO:0006520
EC
GO	InterPro Biological Process: cellular amino acid metabolic process (GO:0006520) Molecular Function: ethanolamine ammonia-lyase activity (GO:0008851) Curated
PM
AN
CC	COG: [E] Amino acid transport and metabolism;
CC	MODEL: XFF4834R
CC	STATUS: curated by jacques (20110221)
MW	29105.8 Da
SQ	271 aa
	........10........20........30........40........50 \| \| \| \| \| MSTPSRPPRDAWAQLRQLTPARIALGRVGTSLPTDAHLEFQLAHAQARDA VHLAFDPAPLQAALEQRGRSSILLQSAAADRHQYLQRPDLGRRLAEEAAA QLRGLTAVHGGRHDVAVVVADGLSALAVHRHAARMLDQIDALASQEGWSL APVVLVRQGRVAIGDEVGELLDARAVIVLIGERPGLSSPDSLGLYLTYTP RVGLTDAARNCISNIRAEGLSYAEAAHKLGYLLREAFRRKLSGVQLKDEA EQPALLAGPANVAPRTFLLPD

EUTC_MF_00601

Ethanolamine ammonia-lyase light chain [eutC].

NP_642682.1 lcl|eutC-XAC2366

271

S=1249 I=92 E=2.04256e-144

ethanolamine ammonia-lyase small subunit

YP_364295.1 lcl|eutC-XCV2564

271

S=1076 I=88 E=2.04236e-123

ethanolamine ammonia-lyase small subunit

NP_637616.1 lcl|eutC-XCC2261

271

S=1061 I=79 E=1.56968e-121

ethanolamine ammonia-lyase small subunit

Q9KWC7 sp|Q9KWC7|Q9KWC7_AGRRH

257

S=495 I=48 E=2.09418e-51

Riorf57 protein ; Plasmid

Pubmed 10907845,11273700

prodomImg

Q59782 sp|Q59782|EUTC_RHOER

258

S=385 I=40 E=3.61939e-38

Ethanolamine ammonia-lyase light chain EC=4.3.1.7 ; Cobalamin Cobalt

Pubmed 8069783

prodomImg

P19265 sp|P19265|EUTC_SALTY

246

S=300 I=35 E=8.96585e-28

Ethanolamine ammonia-lyase light chain EC=4.3.1.7 ; Cobalamin Cobalt

Pubmed 2197274,10464203

prodomImg

Q8PK11 sp|Q8PK11|EUTC_XANAC

S=1249 I=92 E=5.23795e-143

Ethanolamine ammonia-lyase light chain EC=4.3.1.7 ; Cobalamin Cobalt

prodomImg

Q8P8I0 sp|Q8P8I0|EUTC_XANCP

S=1061 I=79 E=4.02529e-120

Ethanolamine ammonia-lyase light chain EC=4.3.1.7 ; Cobalamin Cobalt

prodomImg

B0RS35 sp|B0RS35|EUTC_XANCB

S=1051 I=78 E=5.60173e-119

Ethanolamine ammonia-lyase light chain EC=4.3.1.7 ; Cobalamin Cobalt

prodomImg

Q4UVK6 sp|Q4UVK6|EUTC_XANC8

S=1051 I=78 E=5.60173e-119

Ethanolamine ammonia-lyase light chain EC=4.3.1.7 ; Cobalamin Cobalt

prodomImg

B0KL94 sp|B0KL94|EUTC_PSEPG

269

S=807 I=63 E=1.98704e-89

Ethanolamine ammonia-lyase light chain EC=4.3.1.7 ; Cobalamin Cobalt

prodomImg

[MF_00601]

247

IPR009246 [PIRSF018982]

265

Ethanolamine ammonia-lyase light chain

IPR009246 [PF05985]

247

Ethanolamine ammonia-lyase light chain

105

PD667617

135

271

S=471 I=71 E=1.35011e-49

PD023880

133

S=310 I=56 E=3.91747e-30

PDA1J6M5

148

173

S=108 I=81 E=1.3243e-05