Reviewed, UniProtKB/Swiss-Prot Q87M87 (ARGA_VIBPA)

Names and origin

Protein names

Recommended name:
    Amino-acid acetyltransferase
    EC=2.3.1.1
Alternative name(s):
    N-acetylglutamate synthase
      Short name=AGS
      Short name=NAGS

Gene names

Name:	argA
Ordered Locus Names:	VP2371

Organism

Vibrio parahaemolyticus [Complete proteome] [HAMAP]

Taxonomic identifier

670 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01105
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01105
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the acetyltransferase family. ArgA subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome
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	amino-acid 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

Molecule processing

Chain

1 – 445

445

Amino-acid acetyltransferase HAMAP MF_01105

PRO_0000186809

Regions

Domain

299 – 438

140

N-acetyltransferase

Secondary structure

1

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445

Helix Strand Turn

Details...

Beta strand

299 – 303

5

Helix

313 – 321

9

Helix

330 – 336

7

Beta strand

340 – 345

6

Beta strand

353 – 358

6

Turn

359 – 362

4

Beta strand

363 – 367

5

Helix

373 – 375

3

Helix

383 – 393

11

Turn

394 – 396

3

Beta strand

399 – 401

3

Helix

408 – 413

6

Sequences

	Sequence		Length	Mass (Da)
	Q87M87-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: B924E581D8DFF19A	FASTA	445	48,753
	10 20 30 40 50 60 MKIRSTALVK GFRQSTPYVN AHRGKTMVIM LGGEAVAHNN FGNIINDIAL MHSLGIKVVV 70 80 90 100 110 120 VYGARPQINQ LLEKQDLTTP YHKNIRITDE AALSVVMQAA GQLQLAITAR LSMSLNNTPM 130 140 150 160 170 180 AGTQLNVVSG NFVIAQPLGV DDGVDYCHSG RIRRIDTDAI NRTLDQGSIV LLGPIASSVT 190 200 210 220 230 240 GECFNLLSEE VATQLAIKLG ADKLIGFCSE QGVIDDNGNA VAELLPIEAE HVIKTLSENH 250 260 270 280 290 300 ASDSDYNTGT LRFLKGSIAA CRAGVPRSHL ISYKVDGALI QELFSFDGIG TQVVMASAEQ 310 320 330 340 350 360 VRQAGIDDIG GILELIHPLE EQGILVRRSR EQLEQEIGKF TIIEKDGLII GCAALYPYSE 370 380 390 400 410 420 ERKAEMACVA IHPDYRDGNR GLLLLNYMKH RSKSENINQI FVLTTHSLHW FREQGFYEVG 430 440 VDYLPGAKQG LYNFQRKSKI LALDL

References

[1]

"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633 / Serotype O3:K6.

Cross-references

Sequence databases

EMBLGenBankDDBJ

BA000031 Genomic DNA. Translation: BAC60634.1.

RefSeq

NP_798750.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3E0K	X-ray	2.52	A	298-445	[»]

ModBase

Search...

Genome annotation databases

GeneID

1189884.

GenomeReviews

Gene locus VP2371 in contig BA000031_GR.

KEGG

vpa:VP2371.

NMPDR

fig|223926.1.peg.2371.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q87M87.

OMA

DLIRPLE.

Enzyme and pathway databases

BioCyc

VPAR223926:VP2371-MON.

BRENDA

2.3.1.1. 3063.

Family and domain databases

HAMAP

MF_01105.
[Tree]

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GCN5-rel_AcTrfase.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]

Gene3D

G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.

Pfam

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

PIRSF

PIRSF000423. ArgA. 1 hit.

TIGRFAMs

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

PROSITE

PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ARGA_VIBPA

Accession

Primary (citable) accession number: Q87M87

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2003
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)