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B8GQQ4 (PROB_THISH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:Tgr7_3209
OrganismThioalkalivibrio sp. (strain HL-EbGR7) [Complete proteome] [HAMAP]
Taxonomic identifier396588 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceInferred 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 HAMAP-Rule MF_00456.

Sequence similarities

Belongs to the glutamate 5-kinase family.

Contains 1 PUA domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP 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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000193713

Regions

Domain283 – 36179PUA
Nucleotide binding176 – 1772ATP By similarity

Sites

Binding site171ATP By similarity
Binding site571Substrate By similarity
Binding site1441Substrate By similarity
Binding site1561Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B8GQQ4 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 65F393B52FFBD963

FASTA37540,622
        10         20         30         40         50         60 
MTQTRQQLGK ARRWIIKIGS ALLTNEGRGL DHEALAGWAE QIARLRASGR EVVLVSSGAV 

        70         80         90        100        110        120 
AEGMSRLGWT TRPHALHELQ AAAAVGQMGL VQAYESIFQR HGLRAAQVLL THDDLSNRRR 

       130        140        150        160        170        180 
YLNARSTLRT LLALGVIPVV NENDTVATDE IRFGDNDTLA ALVGNLTEAQ VLVILTDQKG 

       190        200        210        220        230        240 
LFDRDPRAHA DAQLVSEGLA MDPELLKLAA PTFGQLGRGG MATKLHAAAR AARSGAYTLI 

       250        260        270        280        290        300 
ASGREPRVLE RIAEGEQIGT LLCPDKEPLA ARKQWIAGQL IAKGELILDT GATKVLREAG 

       310        320        330        340        350        360 
RSLLPVGVTH VKGEFSRGDV VTCVDPDGRP VARGLVNYSA DEARRIMKHR ADEIEGILGY 

       370 
VDEPELIHRD NLVLL 

« Hide

References

[1]"Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7."
Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N., Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.
Stand. Genomic Sci. 4:23-35(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HL-EbGR7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001339 Genomic DNA. Translation: ACL74278.1.
RefSeqYP_002515265.1. NC_011901.1.

3D structure databases

ProteinModelPortalB8GQQ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING396588.Tgr7_3209.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL74278; ACL74278; Tgr7_3209.
GeneID7315582.
KEGGtgr:Tgr7_3209.
PATRIC23965918. VBIThiSp19295_3175.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
KOK00931.
OMARLMRAYE.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycTSUL396588:GH5B-3259-MONOMER.
UniPathwayUPA00098; UER00359.

Family and domain databases

Gene3D2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPMF_00456. ProB.
InterProIPR001048. 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]
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_THISH
AccessionPrimary (citable) accession number: B8GQQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways