Reviewed, UniProtKB/Swiss-Prot Q93EJ3 (ARGJ_HELHP)

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:	HH_1291

Organism

Helicobacter hepaticus [Complete proteome] [HAMAP]

Taxonomic identifier

32025 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	404 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 – 195	195	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002173
	Chain	196 – 404	209	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002174
Sites
	Site	195 – 196	2	Cleavage; by autolysis By similarity
Experimental info
	Sequence conflict	294	1	A → S in AAL16719. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q93EJ3-1 [UniParc]. Last modified July 25, 2003. Version 2. Checksum: 15DA9D780497BE3A	FASTA	404	43,797
	10 20 30 40 50 60 MFEIIPIKGG VNAPQGFYAD GVSAGLKPPL PNGAPALDVA FLYSEDVLKP FTLFTSNRFQ 70 80 90 100 110 120 AAPITHFKHF IKGKESNFVL INTKNANAMT GERGVQDVCD ILSSLTQKFP FIQNPIMSST 130 140 150 160 170 180 GVIGQYLPKE KIIASFASFD FNAKCENAHT RAADAIRTTD AFSKEIALRV RLDNGESFCI 190 200 210 220 230 240 GAMAKGAGMI QPALATMLCF ITTDALVPQN EGDRILRECA KTSFNAISVD GDMSTNDSVF 250 260 270 280 290 300 LFANGRSGVY NEAAFKEALK MIMHKLATDM VRDGEGSTKL VAFEVCGARD ESQAICAAKA 310 320 330 340 350 360 LTNSLLVKTA IYGEDPNWGR IASTIGASGV ECNEESLRIA FDSVVVFDRG QICFDEENEA 370 380 390 400 RAAAVMEQES FRITCDLGIG EGHFVAYGCD LGYRYIDINA DYRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus." Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. , Shen Z., Weber J., Frosch M., Fox J.G. Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed: 12810954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51449 / 3B1.
[2]	"Helicobacter hepaticus genome: construction of an ordered cosmid library and sequence analysis of the selected genomic regions." Ge Z., Feng Y., Fox J.G. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-305. Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017125 Genomic DNA. Translation: AAP77888.1. AF358673 Genomic DNA. Translation: AAL16719.1.
RefSeq	NP_860822.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	1492979.
GenomeReviews	Gene locus HH_1291 in contig AE017125_GR.
KEGG	hhe:HH1291.
NMPDR	fig|235279.1.peg.1291.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q93EJ3.
OMA	IVNSGNA.
Enzyme and pathway databases
BioCyc	HHEP235279:HH_1291-MON.
BRENDA	2.3.1.1. 279780. 2.3.1.35. 279780.
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_HELHP

Accession

Primary (citable) accession number: Q93EJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	July 25, 2003
Last modified:	November 3, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)