Reviewed, UniProtKB/Swiss-Prot P38434 (ARGJ_NEIGO)

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

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

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. 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. 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	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 – 189	189	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002197
	Chain	190 – 406	217	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002198
Sites
	Site	189 – 190	2	Cleavage; by autolysis By similarity
Experimental info
	Sequence conflict	120	1	G → A in AAB21605. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P38434-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 5515EA4EB7503814	FASTA	406	42,866
	10 20 30 40 50 60 MAVNLTEKTA EQLPDIDGIA LYTAQAGVKK PGHTDLTLIA VAAGSTVGAV FTTNRFCAAP 70 80 90 100 110 120 VHIAKSHLFD EDGVRALVIN TGNANAGTGA QGRIDALAVC AAAARQIGCK PNQVMPFSTG 130 140 150 160 170 180 VILEPLPADK IIAALPKMQP AFWNEAARAI MTTDTVPKAA SREGKVGDQH TVRATGIAKG 190 200 210 220 230 240 SGMIHPNMAT MLGFIATDAK VSQPVLQLMT QEIADETFNT ITVDGDTSTN DSFVIIATGK 250 260 270 280 290 300 NSQSEIDNIA DPRYAQLKEL LCSLALELAQ AIVRDGEGAT KFITVRVENA KTCDEARQAA 310 320 330 340 350 360 YAAARSPLVK TAFFASDPNL GKRLAAIGYA DVADLDTDLV EMYLDDILVA EHGGRAASYT 370 380 390 400 EAQGQAVMSK DEITVRIKLH RGQAAATVYT CDLSHGYVSI NADYRS

References

[1]	"Sequence analysis and complementation studies of the argJ gene encoding ornithine acetyltransferase from Neisseria gonorrhoeae." Martin P.R., Mulks M.H. J. Bacteriol. 174:2694-2701(1992) [PubMed: 1339419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CDC 50.
[2]	"Molecular characterization of the argJ mutation in Neisseria gonorrhoeae strains with requirements for arginine, hypoxanthine, and uracil." Martin P.R., Mulks M.H. Infect. Immun. 60:970-975(1992) [PubMed: 1339413] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NRL 30465.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M65216 Genomic DNA. Translation: AAA25447.1. S85363 Genomic DNA. Translation: AAB21605.2.
PIR	A43850.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.1. 588. 2.3.1.35. 588.
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_NEIGO

Accession

Primary (citable) accession number: P38434
Secondary accession number(s): Q53567

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 61 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)