Reviewed, UniProtKB/Swiss-Prot Q07905 (ARGB_BACST)

Names and origin

Protein names

Recommended name:
    Acetylglutamate kinase
    EC=2.7.2.8
Alternative name(s):
    NAG kinase
      Short name=AGK
    N-acetyl-L-glutamate 5-phosphotransferase

Gene names

Name:

argB

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP MF_00082
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP MF_00082
Subunit structure	Homodimer. HAMAP MF_00082
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the acetylglutamate kinase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP proline biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP acetylglutamate kinase activity Inferred from electronic annotation. Source: HAMAP glutamate 5-kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 258	258	Acetylglutamate kinase HAMAP MF_00082		PRO_0000112586
Regions
	Region	41 – 42	2	Substrate binding By similarity
Sites
	Binding site	63	1	Substrate By similarity
	Binding site	156	1	Substrate By similarity
	Site	8	1	Transition state stabilizer By similarity
	Site	215	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q07905-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 2A409D3A529AF028	FASTA	258	26,935
	10 20 30 40 50 60 MGKTVVIKCG GSVLDELSPA FFASVNAMRK QGMEVVIVHG GGPEIGQMLK TLRVPSEFVN 70 80 90 100 110 120 GLRKTTKDVL AVVEMVLSGK VNKQLASMLR QHGLPAVGVS GVDGGLLEAE PIDLAKLGYV 130 140 150 160 170 180 GRVKTVRSQL LRTLLAAGYI PVISPLGIDQ NGQTYNINAD TAAGAVAAAI GASQLAFVTN 190 200 210 220 230 240 VPGILRDGAL VAEATAEMIE RLIEDGVITG GMIPKVQAAL SALSDALPEV MIVSGKTTFY 250 QNGTWHGTTI RKEVGVYL

References

[1]

"Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase." Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I., Pierard P., Glansdorff N. J. Gen. Microbiol. 139:393-402(1993) [PubMed: 8473852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCIB 8224 / CCM 2186.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L06036 Genomic DNA. Translation: AAA22198.1.
PIR	I39767.
3D structure databases
HSSP	HSSP built from PDB template 1GS5 based on UniProtKB P11445.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.7.2.8. 266715.
Family and domain databases
HAMAP	MF_00082. [Tree]
InterPro	IPR004662. AcgluKinase. IPR001048. Asp/Glu/Uridylate_kinase. IPR011148. GlcNAc_kinase. IPR001057. Glu_5kinase. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. [Graphical view]
PIRSF	PIRSF000728. NAGK. 1 hit.
PRINTS	PR00474. GLU5KINASE.
TIGRFAMs	TIGR00761. argB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGB_BACST

Accession

Primary (citable) accession number: Q07905

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 65 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)