Reviewed, UniProtKB/Swiss-Prot P62061 (ARGJ_GEOSL)

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:	GSU2049

Organism

Geobacter sulfurreducens [Complete proteome] [HAMAP]

Taxonomic identifier

35554 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter

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 – 178	178	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002169
	Chain	179 – 393	215	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002170
Sites
	Site	178 – 179	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P62061-1 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: 8808BFB962CB9C57	FASTA	393	40,986
	10 20 30 40 50 60 MNVKGFRFSA VEAAIKKPGR LDLALICSDA PAAVAAVYTT NKVKAAPVLL DMERTTSGTC 70 80 90 100 110 120 RAVVVNSGNA NACTGDRGME DARETTSLVA ERIGASEHEV LVCSTGVIGV PLPMERIRGG 130 140 150 160 170 180 IPSLVAGLGS ATLDQIAAAI MTTDTFPKLE ARTGTAGGVG YTIAGIAKGA GMIMPNMATM 190 200 210 220 230 240 LAFVVTDAAV DPQWLDRVFR RANDTSFNAI TVDGDMSTND TAIIMANGAA GNPVLSEGSE 250 260 270 280 290 300 GAAEFAVLLE EVLLSLAKLI VKDGEGATKF VEVTVKGARS DADAKRAAMA VANSCLVKTA 310 320 330 340 350 360 FFGQDANWGR IFAAVGYSGA DVEPDRAELF FDDVRMVQGG VFAGGDAEAR GTGVLRKKEF 370 380 390 TVTVDLHLGD GRATVYTSDL SYDYVKINAD YRT

References

[1]

"Genome of Geobacter sulfurreducens: metal reduction in subsurface environments." Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.L., Kolonay J.F. , Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R., Fraser C.M. Science 302:1967-1969(2003) [PubMed: 14671304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51573 / DSM 12127 / PCA.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017180 Genomic DNA. Translation: AAR35425.1.
RefSeq	NP_953098.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	2686046.
GenomeReviews	Gene locus GSU2049 in contig AE017180_GR.
KEGG	gsu:GSU2049.
NMPDR	fig|243231.1.peg.2036.
TIGR	GSU2049.
Phylogenomic databases
HOGENOM	P62061.
OMA	P62061. VHENSAY.
Enzyme and pathway databases
BioCyc	GSUL243231:GSU_2049-MON.
BRENDA	2.3.1.1. 276898. 2.3.1.35. 276898.
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_GEOSL

Accession

Primary (citable) accession number: P62061

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	June 16, 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)