Reviewed, UniProtKB/Swiss-Prot Q8EYV8 (ARGJ_LEPIN)

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:	LA_4105

Organism

Leptospira interrogans [Complete proteome] [HAMAP]

Taxonomic identifier

173 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	385 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 – 178	178	Arginine biosynthesis bifunctional protein argJ alpha chain By similarity		PRO_0000002181
	Chain	179 – 385	207	Arginine biosynthesis bifunctional protein argJ beta chain By similarity		PRO_0000002182
Sites
	Site	178 – 179	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8EYV8-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 8A525296D0AD7C2F	FASTA	385	41,445
	10 20 30 40 50 60 MHMPKGFLSF GINIGIKDDT KDFGVIYSEI PCKATAVFTK NNFPGAPVIV GKEHVRSGVL 70 80 90 100 110 120 QAIVINSKNS NVATGEKGIQ NSREICKIIG ESLGIKETLV LPSSTGVIGV PLKMEIILPA 130 140 150 160 170 180 CKKAKSLLKP GNLEEVAEAI MTTDTRKKIS SRNIKTKSGQ GTIYGIAKGA GMIEPNMATM 190 200 210 220 230 240 LCYILSDVSL PEGTDLYSIL KSSVDQSFNC LTIDSDTSTS DTVALLCNGL SGESSVQDFS 250 260 270 280 290 300 KALTEICIDL TKLIATDGEG ATKLIELTIS GAKSEAQARK IGKSILNSPL VKTAIYGGDP 310 320 330 340 350 360 NWGRLIMAVG KVFDEPIPFE GLQIYFGTLP VKEANPETLK KLSEYLKNNT EISLNVVLNV 370 380 GTISMKFWGC DFTEKYIEEN AYYTT

References

[1]

"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing." Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P. Nature 422:888-893(2003) [PubMed: 12712204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 56601 / Serogroup Icterohaemorrhagiae / Serovar lai.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE010300 Genomic DNA. Translation: AAN51303.1.
RefSeq	NP_714285.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	T05.001.
Genome annotation databases
GeneID	1153447.
GenomeReviews	Gene locus LA_4105 in contig AE010300_GR.
KEGG	lil:LA4105.
NMPDR	fig|189518.1.peg.4104.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8EYV8.
OMA	ALRGVRM.
Enzyme and pathway databases
BioCyc	LINT189518:LA4104-MON.
BRENDA	2.3.1.1. 258108. 2.3.1.35. 258108.
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_LEPIN

Accession

Primary (citable) accession number: Q8EYV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 46 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)