Q31ED4 (ARGB_THICR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylglutamate kinase
EC=2.7.2.8

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

Gene names

Name:	argB
Ordered Locus Names:	Tcr_1899

Organism

Thiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]

Taxonomic identifier

317025 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Thiomicrospira › Thiomicrospira crunogena

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. HAMAP-Rule MF_00082
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. HAMAP-Rule MF_00082
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the acetylglutamate kinase family.
Sequence caution	The sequence ABB42489.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
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 – 298	298	Acetylglutamate kinase HAMAP-Rule MF_00082		PRO_0000264781
Regions
	Region	68 – 69	2	Substrate binding By similarity
Sites
	Binding site	90	1	Substrate By similarity
	Binding site	195	1	Substrate By similarity
	Site	33	1	Transition state stabilizer By similarity
	Site	255	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q31ED4 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: 51A7B4456EBAE057	FASTA	298	31,990
	10 20 30 40 50 60 MNLNKAQAQN IASVLAEALP YIQRFSGKTI VVKYGGNAMT EEALKNGFAR DIVLMKLVGM 70 80 90 100 110 120 NPVVVHGGGP QIGHLLERVG KQSEFIQGMR VTDSETMDIV EMVLGGMVNK EIVNLIHQHN 130 140 150 160 170 180 GNAVGLTGKD GNLIRAKKME MTAFNEDLNA PELIDLGHVG EVERINTKVL DMLIQDDFIP 190 200 210 220 230 240 VIAPVGVDEQ GHSYNINADL VAGKVAEALH AEKLMLLTNT PGLLDKQGEL LTGLNAESVA 250 260 270 280 290 ALIEDGTIYG GMLPKIQCAL DAVQNGVESS HIIDGRVEHA VMLEVFTDEG VGTLITSH

References

[1]

"The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena XCL-2." Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L., Hauser L.J. , Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E., Zeruth G.T. PLoS Biol. 4:1-17(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: XCL-2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000109 Genomic DNA. Translation: ABB42489.1. Different initiation.
RefSeq	YP_392163.1. NC_007520.2.
3D structure databases
HSSP	HSSP built from PDB template 2BUF based on UniProtKB Q9HTN2.
ProteinModelPortal	Q31ED4.
SMR	Q31ED4. Positions 3-297.
ModBase	Search...
Protein-protein interaction databases
STRING	317025.Tcr_1899.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABB42489; ABB42489; Tcr_1899.
GeneID	3761093.
KEGG	tcx:Tcr_1899.
PATRIC	23975902. VBIThiCru83387_1979.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0548.
HOGENOM	HOG000233259.
KO	K00930.
ProtClustDB	PRK00942.
Enzyme and pathway databases
UniPathway	UPA00068; UER00107.
Family and domain databases
Gene3D	3.40.1160.10. 1 hit.
HAMAP	MF_00082_B. ArgB_B.
InterPro	IPR004662. AcgluKinase. IPR001048. Asp/Glu/Uridylate_kinase. IPR001057. Glu/AcGlu_kinase. [Graphical view]
Pfam	PF00696. AA_kinase. 1 hit. [Graphical view]
PIRSF	PIRSF000728. NAGK. 1 hit.
PRINTS	PR00474. GLU5KINASE.
SUPFAM	SSF53633. Aa_kinase. 1 hit.
TIGRFAMs	TIGR00761. argB. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ARGB_THICR

Accession

Primary (citable) accession number: Q31ED4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 12, 2006
Last modified:	May 1, 2013
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program