Q6HHC1 (PROB_BACHK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate 5-kinase
EC=2.7.2.11

Alternative name(s):
Gamma-glutamyl kinase
Short name=GK

Gene names

Name:	proB
Ordered Locus Names:	BT9727_2731

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline. HAMAP MF_00456
Catalytic activity	ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP MF_00456
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP MF_00456
Subcellular location	Cytoplasm By similarity HAMAP MF_00456.
Sequence similarities	Belongs to the glutamate 5-kinase family. Contains 1 PUA domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro glutamate 5-kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 367	367	Glutamate 5-kinase HAMAP MF_00456		PRO_0000109637
Regions
	Domain	276 – 350	75	PUA

Sequences

	Sequence		Length	Mass (Da)
	Q6HHC1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: F1468AAE500371C6	FASTA	367	39,554
	10 20 30 40 50 60 MKKQRIVVKI GSSSLADSHE GISKEQLSDH VAALARLKEE GHEVLLITSG AVAAGFSALG 70 80 90 100 110 120 YPSRPVTIKG KQAAAAVGQS LLMQAYTEEF RKYGIVTAQL LLTRSDFSRK EQYSNAYATL 130 140 150 160 170 180 GELLNRSALP IINENDSISL EELTFGDNDM LSALVSGLVS ADMLMIFTDV NGLYDKNPQK 190 200 210 220 230 240 NEDAKKYYFL PEVTEEIASL AGDAGSKLGT GGMKSKIDAA KTALSLGVSV FIGTGRGQEK 250 260 270 280 290 300 FVDVLKGKGD GTYVGNAPQK EMKMNKQWIA LHSVVSGQIE IDAGAATAII QHGKSLLPAG 310 320 330 340 350 360 VTNVSGFFQV GEVVEVMTQQ GRVIGKGQCT YSAEELRDVK GMQSQHIQAR GERHSYEVIH RDHWVSL

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT61246.1.
RefSeq	YP_037055.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HHC1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000076454; EBBACP00000074540; EBBACG00000076445.
GeneID	2857940.
GenomeReviews	Gene locus BT9727_2731 in contig AE017355_GR.
KEGG	btk:BT9727_2731.
NMPDR	fig|281309.1.peg.2695.
PATRIC	18986343. VBIBacThu119411_2898.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000001887.
HOGENOM	HBG507643.
OMA	TFGDNDM.
ProtClustDB	PRK05429.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_2731-MONOMER.
Family and domain databases
HAMAP	MF_00456. ProB. [Tree]
InterPro	IPR001048. Asp/Glu/Uridylate_kinase. IPR001057. Glu/AcGlu_kinase. IPR011529. Glu_5kinase. IPR005715. Glu_5kinase/COase_Synthase. IPR019797. Glutamate_5-kinase_CS. IPR002478. PUA. IPR015947. PUA-like_domain. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
KO	K00931.
Pfam	PF00696. AA_kinase. 1 hit. PF01472. PUA. 1 hit. [Graphical view]
PIRSF	PIRSF000729. GK. 1 hit.
PRINTS	PR00474. GLU5KINASE.
SMART	SM00359. PUA. 1 hit. [Graphical view]
SUPFAM	SSF53633. Aa_kinase. 1 hit. SSF88697. PUA-like. 1 hit.
TIGRFAMs	TIGR01027. ProB. 1 hit.
PROSITE	PS00902. GLUTAMATE_5_KINASE. 1 hit. PS50890. PUA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROB_BACHK

Accession

Primary (citable) accession number: Q6HHC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program