C8NJ82 (C8NJ82_COREF) 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 EMBL EEW51320.1
ORF Names:	HMPREF0290_0057 EMBL EEW51320.1

Organism

Corynebacterium efficiens YS-314 EMBL EEW51320.1

Taxonomic identifier

196164 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	388 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
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 EEW51320.1 Transferase
PTM	Autocatalytic cleavage HAMAP MF_01106
Technical term	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	182 – 183	2	Cleavage; by autolysis By similarity HAMAP MF_01106

Sequences

	Sequence		Length	Mass (Da)
	C8NJ82 [UniParc]. Last modified November 3, 2009. Version 1. Checksum: 3C298BFD2466730E	FASTA	388	39,543
	10 20 30 40 50 60 MAQTGITAPK GFVASATTAG IKPSGKPDMA LVVNQGPEYT AAAVFTRNRV IASPVKVSRE 70 80 90 100 110 120 NVADGQLKAV LYNAGNANAC NGTQGDADAR ESVNTLATKL GLAPEDIGVC STGLIGELLP 130 140 150 160 170 180 MDKVTAGIEA LTAEGALGDN GAAAAQAIMT TDTVDKETVV FADGWTVGAM GKGVGMMAPS 190 200 210 220 230 240 LATMLVCLTT DASITPAMAR IALAKATAVT FETLDIDGST STNDTVFLLA SGASGVKPTQ 250 260 270 280 290 300 DELNDAVFAA CSDLAEQMQA DAEGVTKRVS VTVTGTTTDE MAINAARTIA RDNLFKCAMF 310 320 330 340 350 360 GSDPNWGRVL AAVGMADADM DPDHIAVYFN DQAVCLDSTG APGAREVDLS GADIAVRVDL 370 380 GAGGEGQATV RTTDLSYSYV EINSAYST

References

[1]

Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R. , Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K., Petrosino J., Highlander S., Gibbs R. Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: YS-314 EMBL EEW51320.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ACLI01000008 Genomic DNA. Translation: EEW51320.1.
RefSeq	NP_738137.1. NC_004369.1.
3D structure databases
ProteinModelPortal	C8NJ82.
ModBase	Search...
Protein-protein interaction databases
STRING	C8NJ82.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1031984.
PATRIC	21489181. VBICorEff9312_1517.
Phylogenomic databases
OMA	GRDPNWG.
ProtClustDB	PRK05388.
Family and domain databases
HAMAP	MF_01106. ArgJ. [Tree]
InterPro	IPR002813. Arg_biosynth_ArgJ. IPR016117. Pept_S58_DmpA/Arg_biosyn_ArgJ. [Graphical view]
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

C8NJ82_COREF

Accession

Primary (citable) accession number: C8NJ82

Entry history

Integrated into UniProtKB/TrEMBL:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	December 14, 2011
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)