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Q3SJS7 (PROB_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:Tbd_1120
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length374 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 – 374374Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000230071

Regions

Domain281 – 35979PUA
Nucleotide binding174 – 1752ATP By similarity
Nucleotide binding216 – 2227ATP By similarity

Sites

Binding site151ATP By similarity
Binding site551Substrate By similarity
Binding site1421Substrate By similarity
Binding site1541Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SJS7 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: F46427AD32BAEC99

FASTA37439,768
        10         20         30         40         50         60 
MSTSVVRHAR RIVVKVGSSL VTADGRGLDH AALSRWAEQI AALAEQGKEV VLVSSGAIAE 

        70         80         90        100        110        120 
GIARLGWKKR PKAVNELQAA AAVGQMGLVQ AYESIFRTHK LHAAQVLLTH EDLADRTRYL 

       130        140        150        160        170        180 
NARSTLRTLL ELRVVPIINE NDTVATDEIR LGDNDTLGAL VTNLIEADCL VILTDQAGLY 

       190        200        210        220        230        240 
TADPRKVADA SLVMEAHAGD PELERMAGGA GSSVGTGGML TKILAAKRAA RSGAHTVICS 

       250        260        270        280        290        300 
GREPRVLLRL AEGEPIGSQL VARQAPLAAR RQWLADHLQL RGGLVLDDGA VRALQEDGKS 

       310        320        330        340        350        360 
LLPVGVRGVT GEFERGEVVA VVDASGREIA RGLTNYSAAE ARRIAGKPST AIEAELGYMD 

       370 
EPELIHRDNL VVLA 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ97073.1.
RefSeqYP_314878.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SJS7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_1120.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ97073; AAZ97073; Tbd_1120.
GeneID3673191.
KEGGtbd:Tbd_1120.
PATRIC23968393. VBIThiDen82923_1106.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycTDEN292415:GHWG-1147-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_THIDA
AccessionPrimary (citable) accession number: Q3SJS7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 11, 2005
Last modified: February 19, 2014
This is version 61 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