Reviewed, UniProtKB/Swiss-Prot Q3SVN6 (ARGJ_NITWN)

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:	Nwi_0388

Organism

Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391) [Complete proteome] [HAMAP]

Taxonomic identifier

323098 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Nitrobacter

Protein attributes

Sequence length	417 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 – 198	198	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000227236
	Chain	199 – 417	219	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000227237
Sites
	Site	198 – 199	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3SVN6-1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 91D8E41E5370DC74	FASTA	417	43,321
	10 20 30 40 50 60 MSTAISPLAP TDVPDLPEIA GVRLATAAAG IRYKGRTDVL LALLDEGTTV AGVFTRSRCP 70 80 90 100 110 120 SAPVEWCRAR LKDGHHAKAG LALVVNSGNA NAFTGKTGRQ ATKLTAGIAA KAAGCKASDI 130 140 150 160 170 180 YLASTGVIGE PLDATKFNGV LETLASEAAP DRWMDAARAI MTTDTFPKVA TARVKLGKAA 190 200 210 220 230 240 VTINGIAKGA GMIAPDMATM LSFIFTDAPI TATALQSLLK SGVEDTFNAV TIDSDTSTSD 250 260 270 280 290 300 TLLAFATGAA GARGAPRISR AGDPRLKAFV KAFHGVLADL AEQVARDGEG ARKLVEVIVE 310 320 330 340 350 360 GATSKASARK IAKSIANSPL VKTAIAGEDA NWGRVVMAVG KAGEPADRDK LSIYFNGIRV 370 380 390 400 410 AKSGARDPSY DEAEVSKAMK NDRIQIKTTL GLGKGRDRVL TCDLTKEYVA INGDYRS

References

[1]

"Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255." Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J. Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed: 16517654] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000115 Genomic DNA. Translation: ABA03655.1.
RefSeq	YP_317007.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q3SVN6.
Genome annotation databases
GeneID	3676973.
GenomeReviews	Gene locus Nwi_0388 in contig CP000115_GR.
KEGG	nwi:Nwi_0388.
NMPDR	fig|323098.3.peg.559.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3SVN6.
OMA	IVNSGNA.
Enzyme and pathway databases
BioCyc	NWIN323098:NWI_0388-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_NITWN

Accession

Primary (citable) accession number: Q3SVN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	October 11, 2005
Last modified:	November 3, 2009
This is version 30 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)