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Q47MV7 (PROB_THEFY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:Tfu_2179
OrganismThermobifida fusca (strain YX) [Complete proteome] [HAMAP]
Taxonomic identifier269800 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptosporangineaeNocardiopsaceaeThermobifida

Protein attributes

Sequence length388 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 – 388388Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000230070

Regions

Domain285 – 36379PUA
Nucleotide binding180 – 1812ATP By similarity
Nucleotide binding222 – 2287ATP By similarity

Sites

Binding site211ATP By similarity
Binding site611Substrate By similarity
Binding site1481Substrate By similarity
Binding site1601Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q47MV7 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: F6E921767E0854E8

FASTA38841,121
        10         20         30         40         50         60 
MGTGVGQTRA EIAQARRVVV KVGSSSLTTP QGGLDHERIR DLTDVLAERR KAGTEVVLVS 

        70         80         90        100        110        120 
SGAVAAGMAP LGLTQRPRDL ATQQAAASVG QGLLLARYTA EFARHSLTAA QILLTADDLM 

       130        140        150        160        170        180 
RRAQYRNAQR AMSRLLEIGA VPIVNENDTV ATHEIRFGDN DRLAALVAHL LRADVLVLLT 

       190        200        210        220        230        240 
DVDALYDGNP SLPTSTRITQ VNGPEDLVGV DLGSANKRGV GTGGMITKVE SARIATEAGV 

       250        260        270        280        290        300 
ATVLTSAANA RAALRGDPVG TFFVPAKHRR PSSRQLWLAH ATAGRGSVFL DPGAVHAVVT 

       310        320        330        340        350        360 
EKASLLPAGV IKVEGDFNAG DPVDLRDENG VLVARGLVNY DSAEIPDLMG RSTRWLAREL 

       370        380 
GAEYSREIVH RDDLVVLRNG STSDREAC 

« Hide

References

[1]"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX."
Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N.
J. Bacteriol. 189:2477-2486(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000088 Genomic DNA. Translation: AAZ56212.1.
RefSeqYP_290235.1. NC_007333.1.

3D structure databases

ProteinModelPortalQ47MV7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269800.Tfu_2179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ56212; AAZ56212; Tfu_2179.
GeneID3581395.
KEGGtfu:Tfu_2179.
PATRIC23905028. VBITheFus33945_2338.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAHGEISIR.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycTFUS269800:GI42-2196-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.
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.
PROSITEPS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_THEFY
AccessionPrimary (citable) accession number: Q47MV7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 58 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