Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate 5-kinase

Gene

proB

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.UniRule annotation

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.UniRule annotation

Pathwayi: L-proline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate 5-kinase (proB)
  2. Gamma-glutamyl phosphate reductase (proA)
This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei13ATPUniRule annotation1
Binding sitei52SubstrateUniRule annotation1
Binding sitei139SubstrateUniRule annotation1
Binding sitei151Substrate; via amide nitrogenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi171 – 172ATPUniRule annotation2
Nucleotide bindingi211 – 217ATPUniRule annotation7

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate 5-kinaseUniRule annotation (EC:2.7.2.11UniRule annotation)
Alternative name(s):
Gamma-glutamyl kinaseUniRule annotation
Short name:
GKUniRule annotation
Gene namesi
Name:proBUniRule annotation
Ordered Locus Names:TTHA1927
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001097481 – 370Glutamate 5-kinaseAdd BLAST370

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1927.

Structurei

3D structure databases

ProteinModelPortaliQ5SH03.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini275 – 353PUAUniRule annotationAdd BLAST79

Sequence similaritiesi

Belongs to the glutamate 5-kinase family.UniRule annotation
Contains 1 PUA domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CGT. Bacteria.
COG0263. LUCA.
HOGENOMiHOG000246369.
KOiK00931.
OMAiREPRIAN.
PhylomeDBiQ5SH03.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB. 1 hit.
InterProiIPR001048. 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]
PfamiPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFiPIRSF000729. GK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SH03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPGLSAKRL VVKVGSAVLT GERGLDLEAM AEIARQVAAL REEGREVVLV
60 70 80 90 100
SSGAVAAGMR RLGLKERPKD MPKKQALAAL GQPLLMAFWQ EAFAPFGLPV
110 120 130 140 150
AQVLLTAEDL SSRSRYLNAK ATLRALLDLG AIPVINENDT VAFEEIRFGD
160 170 180 190 200
NDQLSARVAA LVEAGLLALL SDVDALYEED PKKNPQARPI PEVESVEAVL
210 220 230 240 250
AHAGEENPLG SGGMKSKLLA ARIAGRVGIP TLLLPGKRPG VLLQALSGAP
260 270 280 290 300
LGTYFHARRR YRGEKAWLFG LLRPKGELVL DRGAVRALKE RGASLLPAGV
310 320 330 340 350
KEVRGRFSRG EAVRLLSEEG EEVGVGLANY ASEEIARIKG RRSAEIEAVL
360 370
GYRYTEEVVH RDHLALKEEA
Length:370
Mass (Da):39,890
Last modified:December 21, 2004 - v1
Checksum:i8B67CD67D2A057BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71750.1.
RefSeqiWP_008633899.1. NC_006461.1.
YP_145193.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71750; BAD71750; BAD71750.
GeneIDi3169812.
KEGGittj:TTHA1927.
PATRICi23958833. VBITheThe93045_1898.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71750.1.
RefSeqiWP_008633899.1. NC_006461.1.
YP_145193.1. NC_006461.1.

3D structure databases

ProteinModelPortaliQ5SH03.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1927.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71750; BAD71750; BAD71750.
GeneIDi3169812.
KEGGittj:TTHA1927.
PATRICi23958833. VBITheThe93045_1898.

Phylogenomic databases

eggNOGiENOG4105CGT. Bacteria.
COG0263. LUCA.
HOGENOMiHOG000246369.
KOiK00931.
OMAiREPRIAN.
PhylomeDBiQ5SH03.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB. 1 hit.
InterProiIPR001048. 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]
PfamiPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFiPIRSF000729. GK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPROB_THET8
AccessioniPrimary (citable) accession number: Q5SH03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.