Reviewed, UniProtKB/Swiss-Prot Q9ZJ14 (ARGJ_BACAM)

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

Organism

Bacillus amyloliquefaciens

Taxonomic identifier

1390 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	406 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
Enzyme regulation	Feedback inhibition by L-arginine By similarity. 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. HAMAP MF_01106
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
Technical term	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 – 192	192	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002105
	Chain	193 – 406	214	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002106
Sites
	Site	192 – 193	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9ZJ14-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 9537998AEF0CAF81	FASTA	406	43,277
	10 20 30 40 50 60 MIQLSEDQIV KVTGDVSSPK GFQAKGVHCG LRYSKKDLGV IISETPAVSA AVYTQSHFQA 70 80 90 100 110 120 APIKVTQDSL KHGPTLKAVI VNSAIANACT GEQGLKDAYT MRESFASQLG IEPELVAVSS 130 140 150 160 170 180 TGVIGEHLDM EKIHAGIELL KETPAGSGDF EEAILTTDTV IKQTCYELAI GGKTVTIGGA 190 200 210 220 230 240 AKGSGMIHPN MATMLGFVTT DAAIEEKALQ KALREITDVS FNQITVDGET STNDMVLVMA 250 260 270 280 290 300 NGCAENECLT EDHPDWPVFK KALLLTCEDL AKEIARDGEG ATKLIEAQVQ GAKNNLDANV 310 320 330 340 350 360 IAKKIVGSNL VKTAVYGTDA NWGRIIGAIG HSAAQVTAEE VEVYLGGQCL FKNNEPQPFS 370 380 390 400 ESIAKEYLEG DEITIVIKMA EGDGNGRAWG CDLTYDYIKI NASYRT

References

[1]	Kim H.K., Min K.H., Yamane G. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF001627 Genomic DNA. Translation: AAD00896.1.
3D structure databases
SMR	Q9ZJ14. Positions 11-192, 18-403, 193-404.
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Enzyme and pathway databases
BRENDA	2.3.1.1. 1130. 2.3.1.35. 1130.
Family and domain databases
HAMAP	MF_01106. ArgJ. [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_BACAM

Accession

Primary (citable) accession number: Q9ZJ14

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	May 1, 1999
Last modified:	February 9, 2010
This is version 47 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)