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A6WXS1 (PROB_OCHA4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:Oant_1055
OrganismOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168) [Complete proteome] [HAMAP]
Taxonomic identifier439375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Protein attributes

Sequence length378 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 – 378378Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000081082

Regions

Domain279 – 35678PUA
Nucleotide binding173 – 1742ATP By similarity

Sites

Binding site141ATP By similarity
Binding site541Substrate By similarity
Binding site1411Substrate By similarity
Binding site1531Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A6WXS1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: A46FD7ADBEC43901

FASTA37840,019
        10         20         30         40         50         60 
MLKQLKNYRR IVVKIGSALL VDRAAGLKRD WLESLGQDIA ALHHAGVEVL VVSSGAIALG 

        70         80         90        100        110        120 
RTVLGLPKKA LKLEESQAAA AAGQIALAKA YADVLGGHSI RSGQILVTLS DTEERRRYLN 

       130        140        150        160        170        180 
ARATIETLLK LKAVPVINEN DTVATTEIRY GDNDRLAARV ATMMGADLLV LLSDIDGLYT 

       190        200        210        220        230        240 
APPHKNPDAE FLPLVETITP QIEAMAGAAA SELSRGGMKT KLDAGKIANA AGTAMIITSG 

       250        260        270        280        290        300 
TRFGPLSAID RGERATLFEP ARAPVNAWKT WISGNLEPAG RLTVDAGAAK ALKSGKSLLP 

       310        320        330        340        350        360 
AGVKEIDGQF ERGDTVAVLN EDGREIARGL IAYDAEDARK IAGHKSDEIS EILGYDARAA 

       370 
MIHRNDLVVR AASNAEVA 

« Hide

References

[1]"Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic pathogen and symbiont of several eukaryotic hosts."
Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.
J. Bacteriol. 193:4274-4275(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49188 / DSM 6882 / NCTC 12168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000758 Genomic DNA. Translation: ABS13775.1.
RefSeqYP_001369604.1. NC_009667.1.

3D structure databases

ProteinModelPortalA6WXS1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439375.Oant_1055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS13775; ABS13775; Oant_1055.
GeneID5380305.
KEGGoan:Oant_1055.
PATRIC20467177. VBIOchAnt73124_1103.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycOANT439375:GJIT-1071-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_OCHA4
AccessionPrimary (citable) accession number: A6WXS1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 52 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