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Q5FAK7

- Q5FAK7_NEIG1

UniProt

Q5FAK7 - Q5FAK7_NEIG1

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Protein

Amino-acid acetyltransferase

Gene

argA

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Status
Unreviewed - Annotation score: 2 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 1Imported
Binding sitei152 – 1521CoenzymeA 2Imported
Binding sitei357 – 3571CoenzymeA 3; via carbonyl oxygenImported
Binding sitei394 – 3941CoenzymeA 3; via carbonyl oxygenImported
Binding sitei398 – 3981CoenzymeA 3Imported

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:
PDBe
RCSB PDB
PDBj
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 bindingImported
Regioni357 – 3593CoenzymeA 1 bindingImported
Regioni357 – 3593CoenzymeA 2 bindingImported
Regioni364 – 3707CoenzymeA 1 bindingImported
Regioni364 – 3707CoenzymeA 3 bindingImported
Regioni365 – 3706CoenzymeA 2 bindingImported
Regioni392 – 3987CoenzymeA 1 bindingImported
Regioni394 – 3985CoenzymeA 2 bindingImported

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0548.
HOGENOMiHOG000262225.
KOiK14682.
OMAiDARKRKY.
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:
EMBL
GenBank
DDBJ
Links Updated
AE004969 Genomic DNA. Translation: AAW88796.1.
RefSeqiYP_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:
EMBL
GenBank
DDBJ
Links Updated
AE004969 Genomic DNA. Translation: AAW88796.1 .
RefSeqi YP_207208.1. NC_002946.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2R8V X-ray 2.50 A 1-436 [» ]
2R98 X-ray 2.40 A 1-436 [» ]
3B8G X-ray 2.60 A 1-436 [» ]
3D2M X-ray 2.21 A 1-436 [» ]
3D2P X-ray 2.56 A/B 1-436 [» ]
ProteinModelPortali Q5FAK7.
SMRi Q5FAK7. Positions 5-436.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 242231.NGO0027.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW88796 ; AAW88796 ; NGO0027 .
GeneIDi 3283070.
KEGGi ngo:NGO0027.
PATRICi 20332884. VBINeiGon24812_0027.

Phylogenomic databases

eggNOGi COG0548.
HOGENOMi HOG000262225.
KOi K14682.
OMAi DARKRKY.
OrthoDBi EOG6T1WVF.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00106 .
BioCyci NGON242231:GI2G-24-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q5FAK7.

Family and domain databases

Gene3Di 3.40.1160.10. 1 hit.
3.40.630.30. 1 hit.
HAMAPi MF_01105. N_acetyl_glu_synth.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GNAT_dom.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view ]
Pfami PF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000423. ArgA. 1 hit.
SUPFAMi SSF53633. SSF53633. 1 hit.
SSF55729. SSF55729. 1 hit.
TIGRFAMsi TIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEi PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 71 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-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3