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ECOLI:ARGA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) argA
Protein Name(s) Amino-acid acetyltransferase

N-acetylglutamate synthase AGS NAGS

External Links
UniProt P0A6C5
EMBL Y00492
AF008115
AF008116
AF008117
AF008118
AF008119
U29581
U00096
AP009048
PIR A30372
RefSeq NP_417295.1
YP_491023.1
ProteinModelPortal P0A6C5
SMR P0A6C5
DIP DIP-48037N
IntAct P0A6C5
MINT MINT-1292378
STRING 511145.b2818
PaxDb P0A6C5
PRIDE P0A6C5
EnsemblBacteria AAC75857
BAE76887
GeneID 12933312
947289
KEGG ecj:Y75_p2752
eco:b2818
PATRIC 32121054
EchoBASE EB0061
EcoGene EG10063
eggNOG COG0548
InParanoid P0A6C5
KO K14682
OMA PYIHAFR
OrthoDB EOG6T1WVF
PhylomeDB P0A6C5
BioCyc EcoCyc:N-ACETYLTRANSFER-MONOMER
ECOL316407:JW2786-MONOMER
MetaCyc:N-ACETYLTRANSFER-MONOMER
UniPathway UPA00068
PRO PR:P0A6C5
Proteomes UP000000318
UP000000625
Genevestigator P0A6C5
GO GO:0005737
GO:0004042
GO:0004358
GO:0006526
Gene3D 3.40.1160.10
3.40.630.30
HAMAP MF_01105
InterPro IPR016181
IPR001048
IPR000182
IPR010167
Pfam PF00696
PF00583
PIRSF PIRSF000423
SUPFAM SSF53633
SSF55729
TIGRFAMs TIGR01890
PROSITE PS51186

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004358

glutamate N-acetyltransferase activity

PMID:9572954[1]

ECO:0000315

F

Fig.3 synthesis of arginine by expressing argA in plasmids

complete
CACAO 4008

enables

GO:0004358

glutamate N-acetyltransferase activity

PMID:16890[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006526

arginine biosynthetic process

PMID:1102931[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006526

arginine biosynthetic process

PMID:17651682[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004358

glutamate N-acetyltransferase activity

PMID:17651682[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004358

glutamate N-acetyltransferase activity

PMID:16890[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004042

acetyl-CoA:L-glutamate N-acetyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010167

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010167

C

Seeded From UniProt

complete

involved_in

GO:0006526

arginine biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010167

P

Seeded From UniProt

complete

enables

GO:0004042

acetyl-CoA:L-glutamate N-acetyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.1.1

F

Seeded From UniProt

complete

enables

GO:0103045

methione N-acyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.1.1

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000067685

C

Seeded From UniProt

complete

involved_in

GO:0006526

arginine biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000067685

P

Seeded From UniProt

complete

enables

GO:0004042

acetyl-CoA:L-glutamate N-acetyltransferase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000067685

F

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0028

P

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

involved_in

GO:0006526

arginine biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0055
UniPathway:UPA00068

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Rajagopal, BS et al. (1998) Use of inducible feedback-resistant N-acetylglutamate synthetase (argA) genes for enhanced arginine biosynthesis by genetically engineered Escherichia coli K-12 strains. Appl. Environ. Microbiol. 64 1805-11 PubMed GONUTS page
  2. 2.0 2.1 Marvil, DK & Leisinger, T (1977) N-acetylglutamate synthase of Escherichia coli: purification, characterization, and molecular properties. J. Biol. Chem. 252 3295-303 PubMed GONUTS page
  3. Eckhardt, T & Leisinger, T (1975) Isolation and characterization of mutants with a feedback resistant N-acetylglutamate synthase in Escherichia coli K 12. Mol. Gen. Genet. 138 225-32 PubMed GONUTS page
  4. 4.0 4.1 Takahara, K et al. (2007) Continuous spectrophotometric assays for three regulatory enzymes of the arginine biosynthetic pathway. Anal. Biochem. 368 138-47 PubMed GONUTS page