Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B0K0T1 (PROB_THEPX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Teth514_1519
OrganismThermoanaerobacter sp. (strain X514) [Complete proteome] [HAMAP]
Taxonomic identifier399726 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter

Protein attributes

Sequence length372 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 – 372372Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000193712

Regions

Domain272 – 35079PUA
Nucleotide binding165 – 1662ATP By similarity
Nucleotide binding207 – 2137ATP By similarity

Sites

Binding site61ATP By similarity
Binding site461Substrate By similarity
Binding site1331Substrate By similarity
Binding site1451Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B0K0T1 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 3AF1E65FBB58EE5E

FASTA37241,186
        10         20         30         40         50         60 
MRIVVKVGTS TLTYENGKLN LEIMEKLVRQ IANLLNRGEE VVLVTSGAIG AGMGKLNLKE 

        70         80         90        100        110        120 
KPKTIPEKQS LAAIGQGLLI EIYEKFFNEY GKITAQVLLT KEDFSDRRRY LNVSYTLSNL 

       130        140        150        160        170        180 
LKWGVVPIIN ENDTVTVDEI KIGDNDTLAA LLASLVEADI LIILTDIDGL YDKDPRIYKE 

       190        200        210        220        230        240 
AKIIEVVEEF SDELFKIAGS AGTKRGTGGM YTKIQAAKIC WNSGVKMIIA NGKIDNVLNQ 

       250        260        270        280        290        300 
IANGEKIGTT FLPMKKPISS RKVWIAFNAK VSGRLFIDEG AAKAIIKHGK SLLPSGVVKT 

       310        320        330        340        350        360 
EGDYDVGDCV AVVDHQEKEI ARGLINYSSE EVEKIKGCKT HEIEKILGYK YYDEVIHRDN 

       370 
LVILERGEKF GS 

« Hide

References

[1]"Complete sequence of Thermoanaerobacter sp. X514."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X514.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000923 Genomic DNA. Translation: ABY92806.1.
RefSeqYP_001663142.1. NC_010320.1.

3D structure databases

ProteinModelPortalB0K0T1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399726.Teth514_1519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY92806; ABY92806; Teth514_1519.
GeneID5876717.
KEGGtex:Teth514_1519.
PATRIC23892692. VBITheSp86957_1577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMAHIANGKT.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycTSP399726:GHCK-1558-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_THEPX
AccessionPrimary (citable) accession number: B0K0T1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 18, 2008
Last modified: May 14, 2014
This is version 50 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