Reviewed, UniProtKB/Swiss-Prot Q7V436 (ARGJ_PROMM)

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:	PMT_2135

Organism

Prochlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]

Taxonomic identifier

74547 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	427 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	acetyl-CoA:L-glutamate 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 – 210	210	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002209
	Chain	211 – 427	217	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002210
Sites
	Site	210 – 211	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7V436-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: AAC9BCFA7C311F12	FASTA	427	44,318
	10 20 30 40 50 60 MALVEDVFSL SPKAVSSALA SLWRPIQGGV SAPLGFQAAG ITAGLKDSGK PDLALLLAPE 70 80 90 100 110 120 GAVCAGMFTT SLVRAACVDL CVDHLQACGG KARAVLINSG QANACTGERG WLDSLRASQA 130 140 150 160 170 180 LAGRLELPVE QVLICSTGVI GVPIPMDTLL AGLDPLVEAL SDEGGAEAAG AILTTDLVEK 190 200 210 220 230 240 QFALEAELGG RSVRIGGMAK GSGMIHPDMA TMLGYLSCDV GVEVDAWQAM LKRVVDCSFN 250 260 270 280 290 300 AMTVDGDTST NDSCLAFAAG ELLEQEHLQA LEAGLLVAAQ QLAKAIARDG EGATCLLEVQ 310 320 330 340 350 360 VEGVVGDVEA RRIARTVCGS SLVKTAVHGR DPNWGRIVAA AGCAGVPFDP AAVALWLGPH 370 380 390 400 410 420 QLMEFGEPLP FDRLAASRYM QERVDGSYLC DDTVQIRLVV GDGSGDGMAW GCDLSDQYVR INADYTT

References

[1]

"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W. Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX548175 Genomic DNA. Translation: CAE22309.1.
RefSeq	NP_895959.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q7V436.
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	1727636.
GenomeReviews	Gene locus PMT_2135 in contig BX548175_GR.
KEGG	pmt:PMT2135.
NMPDR	fig|74547.1.peg.2126.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7V436.
OMA	QNRFCAA
Enzyme and pathway databases
BioCyc	PMAR74547:PMT2135-MON.
Family and domain databases
HAMAP	MF_01106. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_PROMM

Accession

Primary (citable) accession number: Q7V436

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	October 1, 2003
Last modified:	November 24, 2009
This is version 42 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)