Q82C83 (PROB_STRAW) 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:	SAV_5471

Organism

Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]

Taxonomic identifier

227882 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces avermitilis

Protein attributes

Sequence length	375 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 By similarity. HAMAP-Rule MF_00456
Catalytic activity	ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP-Rule MF_00456
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP-Rule MF_00456
Subcellular location	Cytoplasm By similarity.
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	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	Glutamate 5-kinase HAMAP-Rule MF_00456		PRO_0000109729
Regions
	Domain	281 – 359	79	PUA
	Nucleotide binding	177 – 178	2	ATP By similarity
	Nucleotide binding	219 – 225	7	ATP By similarity
Sites
	Binding site	17	1	ATP By similarity
	Binding site	58	1	Substrate By similarity
	Binding site	145	1	Substrate By similarity
	Binding site	157	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q82C83 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: B1A8B1BD60C18800	FASTA	375	39,138
	10 20 30 40 50 60 MSAARQGVAQ ARRIVVKVGS SSLTTAAGGL DADRVDALVD VLAKSRSGGE KEIVLVSSGA 70 80 90 100 110 120 IAAGLAPLGL RRRPKDLARQ QAAASVGQGL LVARYTASCA RHGIRVGQVL LTSDDTSRRA 130 140 150 160 170 180 HHRNASRTLD KLLAMGALPV VNENDTVATD EIRFGDNDRL AALVAHLVRA DLLVLLSDVD 190 200 210 220 230 240 GVYDGDPSKP GTSRVAQVHG PQDLAHVEIG SAGRAGVGTG GMVTKIEAAR IAAAAGIPVV 250 260 270 280 290 300 LTSAVHAADA LAGRDTGTYF HPTGKRSADR LLWLQHASTP QGALTLDDGA VRAVVERRKS 310 320 330 340 350 360 LLPAGIAAVE GEFTAGDPVE LRDSEGRAVA RGLVSFDAKE IPQLLGRSTR ELARELGPAY 370 EREVVHRDDL VLLQP

References

[1]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

[2]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC73183.1.
RefSeq	NP_826648.1. NC_003155.4.
3D structure databases
ProteinModelPortal	Q82C83.
ModBase	Search...
Protein-protein interaction databases
STRING	227882.SAV_5471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC73183; BAC73183; SAV_5471.
GeneID	1211290.
KEGG	sma:SAV_5471.
PATRIC	23724928. VBIStrAve112782_5823.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0263.
HOGENOM	HOG000246368.
KO	K00931.
OMA	DHLQLRG.
ProtClustDB	PRK05429.
Enzyme and pathway databases
BioCyc	SAVE227882:GJU1-5545-MONOMER.
UniPathway	UPA00098; UER00359.
Family and domain databases
Gene3D	3.40.1160.10. 1 hit.
HAMAP	MF_00456. ProB.
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]
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_STRAW

Accession

Primary (citable) accession number: Q82C83

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program