D1ED56 (D1ED56_NEIGO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended 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

Organism

Neisseria gonorrhoeae SK-93-1035 EMBL EEZ58476.1

Taxonomic identifier

528360 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › Neisseria gonorrhoeae

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis HAMAP-Rule MF_01105 SAAS SAAS000182
Cellular component	Cytoplasm HAMAP-Rule MF_01105 SAAS SAAS000182
Molecular function	Acyltransferase HAMAP-Rule MF_01105 SAAS SAAS000182 Transferase
Technical term	3D-structure PDB 4I49
Gene Ontology (GO)
Biological_process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Domain	287 – 436	150	N-acetyltransferase By similarity HAMAP-Rule MF_01105

Sequences

	Sequence		Length	Mass (Da)
	D1ED56 [UniParc]. Last modified January 19, 2010. Version 1. Checksum: E29044A0B76C7B02	FASTA	436	47,006
	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

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. , 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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

EQ973086 Genomic DNA. Translation: EEZ58476.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4I49	X-ray	2.75	A	1-436	[»]

ProteinModelPortal

D1ED56.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EEZ58476; EEZ58476; NGLG_00316.

PATRIC

28195341. VBINeiGon43547_0285.

Enzyme and pathway databases

UniPathway

UPA00068; UER00106.

Family and domain databases

Gene3D

3.40.1160.10. 1 hit.
3.40.630.30. 1 hit.

HAMAP

MF_01105. N_acetyl_glu_synth.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GNAT_dom.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]

Pfam

PF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000423. ArgA. 1 hit.

SUPFAM

SSF53633. Aa_kinase. 1 hit.
SSF55729. Acyl_CoA_acyltransferase. 1 hit.

TIGRFAMs

TIGR01890. N-Ac-Glu-synth. 1 hit.

PROSITE

PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

D1ED56_NEIGO

Accession

Primary (citable) accession number: D1ED56

Entry history

Integrated into UniProtKB/TrEMBL:	January 19, 2010
Last sequence update:	January 19, 2010
Last modified:	May 1, 2013
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)