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A0PXA5 (PROB_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:NT01CX_0902
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length379 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 – 379379Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000081052

Regions

Domain284 – 36279PUA
Nucleotide binding177 – 1782ATP By similarity
Nucleotide binding219 – 2257ATP By similarity

Sites

Binding site181ATP By similarity
Binding site581Substrate By similarity
Binding site1451Substrate By similarity
Binding site1571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PXA5 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: A92EA6996C4595E8

FASTA37940,928
        10         20         30         40         50         60 
MNNLRETYIK DVKRIVVKVG TSTLTYPTGL LNLNKIENLV RQLSDAQNRG IEVILVSSGA 

        70         80         90        100        110        120 
IGAGIGKLGL KERPKTIPEK QAAAAVGQGI LLHMYEKIFS EYGKPVGQIL LTREDLSHRT 

       130        140        150        160        170        180 
RFLNASNTFY SLLEQGVIPI VNENDAIVVD EIKFGDNDTL SAMVASLVDA DLLILVTDID 

       190        200        210        220        230        240 
GLYDSNPKTN PDAKFIPVVD EITEDIVAAA GGAGSSLGTG GMATKINAGK IATSSGSSMV 

       250        260        270        280        290        300 
IVNGDNRNFL TDILDGKEIG TLFLGQEDHV KAKKHWMAFA TKPTGSIIVD DGAEKALVNH 

       310        320        330        340        350        360 
NKSLLPKGII SIDGTFQEGE VVSILNSKKE EIAHGITNYN SMEIDLIKGL DSNIIEDKLG 

       370 
YKNYDEVIHK NNLVILENL 

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000382 Genomic DNA. Translation: ABK60430.1.
RefSeqYP_877007.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0PXA5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386415.NT01CX_0902.

Proteomic databases

PRIDEA0PXA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK60430; ABK60430; NT01CX_0902.
GeneID4539605.
KEGGcno:NT01CX_0902.
PATRIC19477466. VBICloNov112828_0034.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMATVIHRDN.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycCNOV386415:GH98-35-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_CLONN
AccessionPrimary (citable) accession number: A0PXA5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 51 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