A9BI98 (A9BI98_PETMO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Arginine biosynthesis bifunctional protein ArgJ HAMAP MF_01106

Gene names

Name:	argJ HAMAP MF_01106
Ordered Locus Names:	Pmob_1696

Organism

Petrotoga mobilis (strain DSM 10674 / SJ95) [Complete proteome] [HAMAP]

Taxonomic identifier

403833 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Petrotoga

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
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	Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01106 N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + 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. HAMAP MF_01106
Subcellular location	Cytoplasm By similarity HAMAP MF_01106.
Miscellaneous	Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway By similarity. HAMAP MF_01106
Sequence similarities	Belongs to the ArgJ family. HAMAP MF_01106

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis HAMAP MF_01106
Cellular component	Cytoplasm HAMAP MF_01106
Molecular function	Acyltransferase HAMAP MF_01106 EMBL ABX32389.1 Transferase
PTM	Autocatalytic cleavage HAMAP MF_01106
Technical term	Complete proteome Multifunctional enzyme HAMAP MF_01106
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
Sites
	Site	190 – 191	2	Cleavage; by autolysis By similarity HAMAP MF_01106

Sequences

	Sequence		Length	Mass (Da)
	A9BI98 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 13F7DF4B5944F4E1	FASTA	408	44,370
	10 20 30 40 50 60 MESTEIMQED IVLPLGFKVW GIHCGIKKSK KDLGLIYSEK KANASAVFTT NKVKAAPVIL 70 80 90 100 110 120 SMENIKDNEI QAVIVNSGNA NACTGVKGYS DAISMAEKTA QILNLKSEDV FVSSTGVIGV 130 140 150 160 170 180 PLPIEKILNG IESFEKNIDL TNDDLLSFAQ AIMTTDTFPK INSTQVVIGG KKITLTGVAK 190 200 210 220 230 240 GSGMIHPNMA TMLSFIMTDA NISKSALNKA LKHSVDNSFN LITVDGDTST NDTVLILANK 250 260 270 280 290 300 QAKNEEITED SSEYNLFQKA LYEVVENLAK KIVMDGEGAT KFFEVQVKNA KTKEDAKLIS 310 320 330 340 350 360 RSIAKSNLVK TAIHGEDANW GRVLAAAGYS GGNFDPDKVD VWFQSCVGKI QLCQDGHFID 370 380 390 400 FNEVKAKEIL GKKELKIIVD LKDGEESAIS WGCDLSYKYV EINGGYRT

References

[1]

"Complete sequence of Petroga mobilis SJ95." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Mikhailova N., Noll K., Richardson P. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 10674 / SJ95.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000879 Genomic DNA. Translation: ABX32389.1.
RefSeq	YP_001568712.1. NC_010003.1.
3D structure databases
ProteinModelPortal	A9BI98.
ModBase	Search...
Protein-protein interaction databases
STRING	A9BI98.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5757201.
GenomeReviews	Gene locus Pmob_1696 in contig CP000879_GR.
KEGG	pmo:Pmob_1696.
PATRIC	22921216. VBIPetMob40494_1822.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284202.
OMA	GRDPNWG.
ProtClustDB	PRK05388.
Enzyme and pathway databases
BioCyc	PMOB403833:PMOB_1696-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

A9BI98_PETMO

Accession

Primary (citable) accession number: A9BI98

Entry history

Integrated into UniProtKB/TrEMBL:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)