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Protein

Amino-acid acetyltransferase

Gene

argA

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.UniRule annotationSAAS annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei134 – 1341CoenzymeA 1Combined sources
Binding sitei152 – 1521CoenzymeA 2Combined sources
Binding sitei357 – 3571CoenzymeA 3; via carbonyl oxygenCombined sources
Binding sitei394 – 3941CoenzymeA 3; via carbonyl oxygenCombined sources
Binding sitei398 – 3981CoenzymeA 3Combined sources

GO - Molecular functioni

  1. acetyl-CoA:L-glutamate N-acetyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationSAAS annotation, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciNGON242231:GI2G-24-MONOMER.
UniPathwayiUPA00068; UER00106.

Names & Taxonomyi

Protein namesi
Recommended name:
Amino-acid acetyltransferaseUniRule annotation (EC:2.3.1.-UniRule annotation, EC:2.3.1.1UniRule annotation)
Alternative name(s):
N-acetylglutamate synthaseUniRule annotation
Gene namesi
Name:argAUniRule annotation
Ordered Locus Names:NGO0027Imported
OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)Imported
Taxonomic identifieri242231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000535: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi242231.NGO0027.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R8VX-ray2.50A1-436[»]
2R98X-ray2.40A1-436[»]
3B8GX-ray2.60A1-436[»]
3D2MX-ray2.21A1-436[»]
3D2PX-ray2.56A/B1-436[»]
ProteinModelPortaliQ5FAK7.
SMRiQ5FAK7. Positions 5-436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5FAK7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini287 – 436150N-acetyltransferaseUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 1522CoenzymeA 1 bindingCombined sources
Regioni357 – 3593CoenzymeA 1 bindingCombined sources
Regioni357 – 3593CoenzymeA 2 bindingCombined sources
Regioni364 – 3707CoenzymeA 1 bindingCombined sources
Regioni364 – 3707CoenzymeA 3 bindingCombined sources
Regioni365 – 3706CoenzymeA 2 bindingCombined sources
Regioni392 – 3987CoenzymeA 1 bindingCombined sources
Regioni394 – 3985CoenzymeA 2 bindingCombined sources

Sequence similaritiesi

Belongs to the acetyltransferase family. ArgA subfamily.UniRule annotation
Contains 1 N-acetyltransferase domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0548.
HOGENOMiHOG000262225.
KOiK14682.
OMAiPYIHAFR.
OrthoDBiEOG6T1WVF.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.630.30. 1 hit.
HAMAPiMF_01105. N_acetyl_glu_synth.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GNAT_dom.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000423. ArgA. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5FAK7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPDSFVAH FREAAPYIRQ MRGTTLVAGI DGRLLEGGTL NKLAADIGLL
60 70 80 90 100
SQLGIRLVLI HGAYHFLDRL AAAQGRTPHY CRGLRVTDET SLGQAQQFAG
110 120 130 140 150
TVRSRFEAAL CGSVSGFARA PSVPLVSGNF LTARPIGVID GTDMEYAGVI
160 170 180 190 200
RKTDTAALRF QLDAGNIVWM PPLGHSYGGK TFNLDMVQAA ASVAVSLQAE
210 220 230 240 250
KLVYLTLSDG ISRPDGTLAE TLSAQEAQSL AEHAASETRR LISSAVAALE
260 270 280 290 300
GGVHRVQILN GAADGSLLQE LFTRNGIGTS IAKEAFVSIR QAHSGDIPHI
310 320 330 340 350
AALIRPLEEQ GVLLHRSREY LENHISEFSI LEHDGDLYGC AALKTFAEAD
360 370 380 390 400
CGEIACLAVS PQAQDGGYGE RLLAHIIDKA RGIGISRLFA LSTNTGEWFA
410 420 430
ERGFQTASED ELPETRRKDY RSNGRNPHIL VRRLHR
Length:436
Mass (Da):47,003
Last modified:March 15, 2005 - v1
Checksum:i6019B9B2B4FC8A0C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004969 Genomic DNA. Translation: AAW88796.1.
RefSeqiWP_010950974.1. NC_002946.2.
YP_207208.1. NC_002946.2.

Genome annotation databases

EnsemblBacteriaiAAW88796; AAW88796; NGO0027.
GeneIDi3283070.
KEGGingo:NGO0027.
PATRICi20332884. VBINeiGon24812_0027.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004969 Genomic DNA. Translation: AAW88796.1.
RefSeqiWP_010950974.1. NC_002946.2.
YP_207208.1. NC_002946.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R8VX-ray2.50A1-436[»]
2R98X-ray2.40A1-436[»]
3B8GX-ray2.60A1-436[»]
3D2MX-ray2.21A1-436[»]
3D2PX-ray2.56A/B1-436[»]
ProteinModelPortaliQ5FAK7.
SMRiQ5FAK7. Positions 5-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi242231.NGO0027.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW88796; AAW88796; NGO0027.
GeneIDi3283070.
KEGGingo:NGO0027.
PATRICi20332884. VBINeiGon24812_0027.

Phylogenomic databases

eggNOGiCOG0548.
HOGENOMiHOG000262225.
KOiK14682.
OMAiPYIHAFR.
OrthoDBiEOG6T1WVF.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00106.
BioCyciNGON242231:GI2G-24-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5FAK7.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.630.30. 1 hit.
HAMAPiMF_01105. N_acetyl_glu_synth.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GNAT_dom.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000423. ArgA. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of Neisseria gonorrhoeae."
    Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
    , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700825 / FA 1090Imported.
  2. "The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation."
    Shi D., Sagar V., Jin Z., Yu X., Caldovic L., Morizono H., Allewell N.M., Tuchman M.
    J. Biol. Chem. 283:7176-7184(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH COENZYMEA.
  3. "Mechanism of allosteric inhibition of N-acetyl-L-glutamate synthase by L-arginine."
    Min L., Jin Z., Caldovic L., Morizono H., Allewell N.M., Tuchman M., Shi D.
    J. Biol. Chem. 284:4873-4880(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH COENZYMEA.

Entry informationi

Entry nameiQ5FAK7_NEIG1
AccessioniPrimary (citable) accession number: Q5FAK7
Entry historyi
Integrated into UniProtKB/TrEMBL: March 15, 2005
Last sequence update: March 15, 2005
Last modified: March 4, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA fulfills an anaplerotic role.UniRule annotation

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.