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Q5FAK7 (Q5FAK7_NEIG1) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Amino-acid acetyltransferase HAMAP-Rule MF_01105
EC=2.3.1.- HAMAP-Rule MF_01105
EC=2.3.1.1 HAMAP-Rule MF_01105
Alternative name(s):
N-acetylglutamate synthase HAMAP-Rule MF_01105
Gene names
Name:argA HAMAP-Rule MF_01105
Ordered Locus Names:NGO0027
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090) [Reference proteome] [HAMAP]
Taxonomic identifier242231 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria ›

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP-Rule MF_01105 SAAS SAAS000182

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP-Rule MF_01105 SAAS SAAS000182

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01105 SAAS SAAS000182.

Miscellaneous

In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA fulfills an anaplerotic role By similarity. HAMAP-Rule MF_01105

Sequence similarities

Belongs to the acetyltransferase family. ArgA subfamily. HAMAP-Rule MF_01105

Contains 1 N-acetyltransferase domain. HAMAP-Rule MF_01105 SAAS SAAS000182

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain287 – 436150N-acetyltransferase By similarity HAMAP-Rule MF_01105
Region151 – 1522Coenzyme A 1 binding
Region357 – 3593Coenzyme A 1 binding
Region357 – 3593Coenzyme A 2 binding PDB 3B8G
Region364 – 3707Coenzyme A 1 binding
Region364 – 3707Coenzyme A 3 binding PDB 3D2P
Region365 – 3706Coenzyme A 2 binding PDB 3B8G
Region392 – 3987Coenzyme A 1 binding
Region394 – 3985Coenzyme A 2 binding PDB 3B8G

Sites

Binding site1341Coenzyme A 1
Binding site1521Coenzyme A 2 PDB 3B8G
Binding site3571Coenzyme A 3; via carbonyl oxygen PDB 3D2P
Binding site3941Coenzyme A 3; via carbonyl oxygen PDB 3D2P
Binding site3981Coenzyme A 3 PDB 3D2P

Sequences

Sequence LengthMass (Da)Tools
Q5FAK7 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 6019B9B2B4FC8A0C

FASTA43647,003
        10         20         30         40         50         60 
MNAPDSFVAH FREAAPYIRQ MRGTTLVAGI DGRLLEGGTL NKLAADIGLL SQLGIRLVLI 

        70         80         90        100        110        120 
HGAYHFLDRL AAAQGRTPHY CRGLRVTDET SLGQAQQFAG TVRSRFEAAL CGSVSGFARA 

       130        140        150        160        170        180 
PSVPLVSGNF LTARPIGVID GTDMEYAGVI RKTDTAALRF QLDAGNIVWM PPLGHSYGGK 

       190        200        210        220        230        240 
TFNLDMVQAA ASVAVSLQAE KLVYLTLSDG ISRPDGTLAE TLSAQEAQSL AEHAASETRR 

       250        260        270        280        290        300 
LISSAVAALE GGVHRVQILN GAADGSLLQE LFTRNGIGTS IAKEAFVSIR QAHSGDIPHI 

       310        320        330        340        350        360 
AALIRPLEEQ GVLLHRSREY LENHISEFSI LEHDGDLYGC AALKTFAEAD CGEIACLAVS 

       370        380        390        400        410        420 
PQAQDGGYGE RLLAHIIDKA RGIGISRLFA LSTNTGEWFA ERGFQTASED ELPETRRKDY 

       430 
RSNGRNPHIL VRRLHR

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 1090.
[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 COENZYME A.
[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 COENZYME A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE004969 Genomic DNA. Translation: AAW88796.1.
RefSeqYP_207208.1. NC_002946.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R8VX-ray2.50A1-436[»]
2R98X-ray2.40A1-436[»]
3B8GX-ray2.60A1-436[»]
3D2MX-ray2.21A1-436[»]
3D2PX-ray2.56A/B1-436[»]
ProteinModelPortalQ5FAK7.
SMRQ5FAK7. Positions 5-436.
ModBaseSearch...

Protein-protein interaction databases

STRING242231.NGO0027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW88796; AAW88796; NGO0027.
GeneID3283070.
KEGGngo:NGO0027.
PATRIC20332884. VBINeiGon24812_0027.

Phylogenomic databases

eggNOGCOG0548.
HOGENOMHOG000262225.
KOK14682.
OMAPTGQAFN.
ProtClustDBPRK05279.

Enzyme and pathway databases

BioCycNGON242231:GI2G-24-MONOMER.
UniPathwayUPA00068; UER00106.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
3.40.630.30. 1 hit.
HAMAPMF_01105. N_acetyl_glu_synth.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GNAT_dom.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFPIRSF000423. ArgA. 1 hit.
SUPFAMSSF53633. Aa_kinase. 1 hit.
SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMsTIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5FAK7.

Entry information

Entry nameQ5FAK7_NEIG1
AccessionPrimary (citable) accession number: Q5FAK7
Entry history
Integrated into UniProtKB/TrEMBL: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info