Q3ASI6 (ARGJ_CHLCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arginine biosynthesis bifunctional protein ArgJ

Cleaved into the following 2 chains:

1. Arginine biosynthesis bifunctional protein ArgJ alpha chain
2. Arginine biosynthesis bifunctional protein ArgJ beta chain

Including the following 2 domains:

1. Glutamate N-acetyltransferase
   EC=2.3.1.35
   Alternative name(s):
   Ornithine acetyltransferase
   Short name=OATase
   Ornithine transacetylase
2. Amino-acid acetyltransferase
   EC=2.3.1.1
   Alternative name(s):
   N-acetylglutamate synthase
   Short name=AGS

Gene names

Name:	argJ
Ordered Locus Names:	Cag_0773

Organism

Chlorobium chlorochromatii (strain CaD3) [Complete proteome] [HAMAP]

Taxonomic identifier

340177 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Chlorobium

Protein attributes

Sequence length	429 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. HAMAP MF_01106
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 HAMAP MF_01106.
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
PTM	Autocatalytic cleavage
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetyl-CoA:L-glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC glutamate N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 217	217	Arginine biosynthesis bifunctional protein ArgJ alpha chain By similarity		PRO_0000227216
	Chain	218 – 429	212	Arginine biosynthesis bifunctional protein ArgJ beta chain By similarity		PRO_0000227217
Sites
	Site	217 – 218	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3ASI6 [UniParc]. Last modified November 22, 2005. Version 1. Checksum: 3DE135D4D3687639	FASTA	429	44,607
	10 20 30 40 50 60 MLTTLNKALD TIHRLAAETV WSEGVTPMKI GDSGEFGFWP KGFSVGATAG NIRYSGRDDM 70 80 90 100 110 120 MLIVSDSPAS AAALFTTNLC CAAPVVLSRN HLQQSAASMR AIVCNSGNAN AATGKQGMAD 130 140 150 160 170 180 AQAMADAVAE QLSIKPEEVL VASTGVIGQL LPMERVHAGI VALPATLQSN SVLGAVSAIM 190 200 210 220 230 240 TTDTFPKFYA VDVALSSGTV RLCGIAKGSG MICPNMATML GFLATDAAIA PELLQTLLSE 250 260 270 280 290 300 ANRKSFNAIT VDGDTSTNDM VAMLASGAGA EVVAGSKDEA LFSAALQSLM ILLAKLIVID 310 320 330 340 350 360 GEGATKLVEI TVKGAVSNEE AELAARTIAN SSLVKTAIHG EDANWGRIIA AAGRSGARFN 370 380 390 400 410 420 EDELELWFNE MPILKKGLIA DFSEDEAAII LAQPSYSITL SLGNGSGSAT LWSCDLSKEY VEINGSYRS

References

[1]

"Complete sequence of Chlorobium chlorochromatii CaD3." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CaD3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000108 Genomic DNA. Translation: ABB28039.1.
RefSeq	YP_379082.1. NC_007514.1.
3D structure databases
ProteinModelPortal	Q3ASI6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3ASI6.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3747617.
GenomeReviews	Gene locus Cag_0773 in contig CP000108_GR.
KEGG	cch:Cag_0773.
PATRIC	21369161. VBIChlChl46571_0798.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1364.
HOGENOM	HBG284202.
OMA	GRDPNWG.
PhylomeDB	Q3ASI6.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	CCHL340177:CAG_0773-MONOMER.
Family and domain databases
HAMAP	MF_01106. ArgJ. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
KO	K00620.
PANTHER	PTHR23100. ArgJ. 1 hit.
Pfam	PF01960. ArgJ. 1 hit. [Graphical view]
ProDom	PD004193. Arg_biosynth_ArgJ. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.
TIGRFAMs	TIGR00120. ArgJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGJ_CHLCH

Accession

Primary (citable) accession number: Q3ASI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	November 22, 2005
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program