Reviewed, UniProtKB/Swiss-Prot Q7V3M5 (ARGJ_PROMP)

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:	PMM0050

Organism

Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]

Taxonomic identifier

59919 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	402 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 – 185	185	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002211
	Chain	186 – 402	217	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002212
Sites
	Site	185 – 186	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7V3M5-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 1B177234AB445C17	FASTA	402	43,403
	10 20 30 40 50 60 MSDGEEKPDG FSFAGIAAGL KDSNKKDLAL ILAPENSICS GLFTQSIVRA SCVDICEQRI 70 80 90 100 110 120 KKSSGLIRAI LINSGQANAC TGDYGIQHTL FATKEVSQLL GINEEEVLMC STGVIGIPIQ 130 140 150 160 170 180 IKNLIDNLPN LVKELKTNSL QNAAEAILTT DLVDKKITIE TFIEGRKVKI SGFAKGSGMI 190 200 210 220 230 240 YPNMATMLAF LTCDVGVDKE EWDKMISIAV KKSFNAISVD GETSTNDAFI GINSGKKIDK 250 260 270 280 290 300 KFLSKIQSGI DIVCQSLAKN IARDGEGANC LLEVLVEGAK SNSDAIKIAK SICNSSLVKT 310 320 330 340 350 360 AINGCDPNWG RIISAAGNSG IDFKLDFLDL YIGDFQILKK GKLNKYDSKK VANYMQTRMN 370 380 390 400 GKYLVEDIVS ISLHLNSGSE KGTAWGCDLS KKYVEINSEY TT

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	BX548174 Genomic DNA. Translation: CAE18509.1.
RefSeq	NP_892171.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q7V3M5.
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	1725721.
GenomeReviews	Gene locus PMM0050 in contig BX548174_GR.
KEGG	pmm:PMM0050.
NMPDR	fig|59919.1.peg.50.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7V3M5.
OMA	IVNSGNA.
Enzyme and pathway databases
BioCyc	PMAR167540:PMM0050-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_PROMP

Accession

Primary (citable) accession number: Q7V3M5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 41 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)