Q040B1 (Q040B1_LEUMM) 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:	LEUM_0059

Organism

Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / NCDO 523) [Complete proteome] [HAMAP]

Taxonomic identifier

203120 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Leuconostoc

Protein attributes

Sequence length	404 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 ABJ61211.1 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)
	Q040B1 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 34B9C1512DB0591C	FASTA	404	42,741
	10 20 30 40 50 60 MTELLNQITT LSTADIAAPI GFHADGQHVG LKHKSKDLGW IYSDVIASVA GVFTTNLVQA 70 80 90 100 110 120 APVQLDKKTI RNGQLQAIIV NSGNANAVTG SIGVSHAESM QEFTAQQLNI DTSLVGVAST 130 140 150 160 170 180 GIIGKVLPID KIINGIKQLK IDGDTNGFAH AIMTTDTKEK SITIQSTIQG KIVTMSGVAK 190 200 210 220 230 240 GSGMLHPNMA TMLGFITTDI NIDAKLLQQA LSEDVETSFN QITIDGDTST NDTVLVMANG 250 260 270 280 290 300 LAGHKMIENH TAEYEQFKDM LHTVTTALSI AIANDGEGAT KLIAVAVNHA QSALDARMVA 310 320 330 340 350 360 KKIVGSSLVK TAIFGKDPNW GRIIAAIGAS NVDLNPNLID ISINKIAVLV NGAPADFNAD 370 380 390 400 TMAEKLEEHD IHIDVDLHAG TESGCAWGSD LTYEYVKINA LYTT

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000414 Genomic DNA. Translation: ABJ61211.1.
RefSeq	YP_817584.1. NC_008531.1.
3D structure databases
ProteinModelPortal	Q040B1.
SMR	Q040B1. Positions 191-402.
ModBase	Search...
Protein-protein interaction databases
STRING	Q040B1.
Protein family/group databases
MEROPS	T05.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4422012.
GenomeReviews	Gene locus LEUM_0059 in contig CP000414_GR.
KEGG	lme:LEUM_0059.
NMPDR	fig|203120.1.peg.1874.
PATRIC	22408103. VBILeuMes50664_0090.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1364.
HOGENOM	HBG284202.
OMA	GRDPNWG.
PhylomeDB	Q040B1.
ProtClustDB	CLSK2318599.
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

Q040B1_LEUMM

Accession

Primary (citable) accession number: Q040B1

Entry history

Integrated into UniProtKB/TrEMBL:	November 14, 2006
Last sequence update:	November 14, 2006
Last modified:	December 14, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)