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Q5SH03 (PROB_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 64. 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:TTHA1927
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length370 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
Reference 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 – 370370Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109748

Regions

Domain275 – 35379PUA
Nucleotide binding171 – 1722ATP By similarity
Nucleotide binding211 – 2177ATP By similarity

Sites

Binding site131ATP By similarity
Binding site521Substrate By similarity
Binding site1391Substrate By similarity
Binding site1511Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5SH03 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 8B67CD67D2A057BB

FASTA37039,890
        10         20         30         40         50         60 
MRPGLSAKRL VVKVGSAVLT GERGLDLEAM AEIARQVAAL REEGREVVLV SSGAVAAGMR 

        70         80         90        100        110        120 
RLGLKERPKD MPKKQALAAL GQPLLMAFWQ EAFAPFGLPV AQVLLTAEDL SSRSRYLNAK 

       130        140        150        160        170        180 
ATLRALLDLG AIPVINENDT VAFEEIRFGD NDQLSARVAA LVEAGLLALL SDVDALYEED 

       190        200        210        220        230        240 
PKKNPQARPI PEVESVEAVL AHAGEENPLG SGGMKSKLLA ARIAGRVGIP TLLLPGKRPG 

       250        260        270        280        290        300 
VLLQALSGAP LGTYFHARRR YRGEKAWLFG LLRPKGELVL DRGAVRALKE RGASLLPAGV 

       310        320        330        340        350        360 
KEVRGRFSRG EAVRLLSEEG EEVGVGLANY ASEEIARIKG RRSAEIEAVL GYRYTEEVVH 

       370 
RDHLALKEEA 

« Hide

References

[1]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008226 Genomic DNA. Translation: BAD71750.1.
RefSeqYP_145193.1. NC_006461.1.

3D structure databases

ProteinModelPortalQ5SH03.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71750; BAD71750; BAD71750.
GeneID3169812.
KEGGttj:TTHA1927.
PATRIC23958833. VBITheThe93045_1898.

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMARLMRAYE.
OrthoDBEOG6PGK7G.
PhylomeDBQ5SH03.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1977-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_THET8
AccessionPrimary (citable) accession number: Q5SH03
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 64 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