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D1ED56 (D1ED56_NEIGO) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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
ORF Names:NGLG_00316 EMBL EEZ58476.1
OrganismNeisseria gonorrhoeae SK-93-1035 EMBL EEZ58476.1
Taxonomic identifier528360 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

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.

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

Contains N-acetyltransferase domain. SAAS SAAS000182

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis HAMAP-Rule MF_01105 SAAS SAAS000182
   Cellular componentCytoplasm HAMAP-Rule MF_01105
   Molecular functionAcyltransferase HAMAP-Rule MF_01105 SAAS SAAS000182
Transferase
   Technical term3D-structure PDB 4I49
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetyl-CoA:L-glutamate N-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain287 – 436150N-acetyltransferase By similarity HAMAP-Rule MF_01105
Region265 – 2673Sulfate binding PDB 4I49

Sites

Binding site461Sulfate PDB 4I49

Sequences

Sequence LengthMass (Da)Tools
D1ED56 [UniParc].

Last modified January 19, 2010. Version 1.
Checksum: E29044A0B76C7B02

FASTA43647,006
        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 GILLHRSREY LENHISEFSI LEHDGNLYGC AALKTFAEAD CGEIACLAVS 

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

       430 
RSNGRNSHIL VRRLHR 

« Hide

References

[1]"The Genome Sequence of Neisseria gonorrhoeae strain SK-93-1035."
The Broad Institute Genome Sequencing Platform
Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C. expand/collapse author list , Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Whittington W., Seifert H., Lander E., Nusbaum C., Galagan J., Birren B.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: SK-93-1035 EMBL EEZ58476.1.
[2]"Structure of the complex of Neisseria gonorrhoeae N-acetyl-L-glutamate synthase with a bound bisubstrate analog."
Zhao G., Allewell N.M., Tuchman M., Shi D.
Biochem. Biophys. Res. Commun. 430:1253-1258(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SULFATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EQ973086 Genomic DNA. Translation: EEZ58476.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I49X-ray2.75A1-436[»]
ProteinModelPortalD1ED56.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEEZ58476; EEZ58476; NGLG_00316.
PATRIC28195341. VBINeiGon43547_0285.

Enzyme and pathway databases

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. SSF53633. 1 hit.
SSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD1ED56_NEIGO
AccessionPrimary (citable) accession number: D1ED56
Entry history
Integrated into UniProtKB/TrEMBL: January 19, 2010
Last sequence update: January 19, 2010
Last modified: June 11, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)