Reviewed, UniProtKB/Swiss-Prot P62060 (ARGJ_DESVH)

Names and origin

Protein names

Recommended name:
    Arginine biosynthesis bifunctional protein argJ
Cleaved into the following 2 chains:
    1- Recommended name:
            Arginine biosynthesis bifunctional protein argJ alpha chain
    2- Recommended name:
            Arginine biosynthesis bifunctional protein argJ beta chain
Including the following 2 domains:
    1- Recommended name:
            Glutamate N-acetyltransferase
              EC=2.3.1.35
        Alternative name(s):
            Ornithine acetyltransferase
              Short name=OATase
            Ornithine transacetylase
    2- Recommended name:
            Amino-acid acetyltransferase
              EC=2.3.1.1
        Alternative name(s):
            N-acetylglutamate synthase
              Short name=AGS

Gene names

Name:	argJ
Ordered Locus Names:	DVU_0823

Organism

Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Complete proteome] [HAMAP]

Taxonomic identifier

882 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate By similarity.
Catalytic activity	N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate. HAMAP MF_01106 Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1. HAMAP MF_01106 Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01106
Subunit structure	Heterotetramer of two alpha and two beta chains By similarity.
Subcellular location	Cytoplasm Probable.
Miscellaneous	Some bacteria possess a monofunctional argJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway. HAMAP MF_01106
Sequence similarities	Belongs to the argJ family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme
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 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
Molecule processing
	Chain	1 – 181	181	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002167
	Chain	182 – 393	212	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002168
Sites
	Site	181 – 182	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62060-1 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: 82F0B1335BA11746	FASTA	393	41,361
	10 20 30 40 50 60 MSASPKGFRF ATVSAGFRKE ARPDLALIVS DTPATAAGVF TTNRFQAAPV VVARENLSAR 70 80 90 100 110 120 PVARAVVINS GQANACTGDE GMTNCRTTLD LVGKACGIPA AEVLPASTGV IGAQLHMDKW 130 140 150 160 170 180 REAAPRLAAA LGQNTHHDFA RAIMTTDAFP KVAERELAIA GTTVRLVGMA KGAGMICPNM 190 200 210 220 230 240 ATMLSVVLCD AAVTPEAWQR LFLDAVDRTF NRVTVDGDTS TNDTVFGLAN GASGVTVEGE 250 260 270 280 290 300 DLAKLGEALT DVLARLAYML VQDGEGATKV MRVKVSGAVD DAEAEAVART VGHSQLVKTA 310 320 330 340 350 360 MYGRDANWGR IVAAVGRSGA SFKAEDVVVT LCGVELFRNG QPTDLDFDTL LREPLKGRDV 370 380 390 TVDIELGAGT GHYELLASDL THDYVNCNAD YRS

References

[1]

"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. , Haft D.H., Selengut J., Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M. Nat. Biotechnol. 22:554-559(2004) [PubMed: 15077118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017285 Genomic DNA. Translation: AAS95303.1.
RefSeq	YP_010044.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P62060.
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	2796170.
GenomeReviews	Gene locus DVU_0823 in contig AE017285_GR.
KEGG	dvu:DVU0823.
NMPDR	fig|882.1.peg.819.
TIGR	DVU_0823.
Phylogenomic databases
HOGENOM	P62060.
OMA	VHENSAY.
Enzyme and pathway databases
BioCyc	DVUL882:DVU_0823-MON.
Family and domain databases
HAMAP	MF_01106. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. [Graphical view]
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
ProDom	PD004193. ArgJ. 2 hits. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_DESVH

Accession

Primary (citable) accession number: P62060

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	November 3, 2009
This is version 44 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)