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Protein

Glutamate 5-kinase

Gene

proB

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
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

Pathway:iL-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101ATPUniRule annotation
Binding sitei50 – 501SubstrateUniRule annotation
Binding sitei137 – 1371SubstrateUniRule annotation
Binding sitei149 – 1491Substrate; via amide nitrogenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1702ATPUniRule annotation
Nucleotide bindingi211 – 2177ATPUniRule annotation

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

BioCyciECOL595496:GI18-235-MONOMER.
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:BWG_0224
OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
Taxonomic identifieri595496 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Glutamate 5-kinasePRO_1000206269Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC4ZT99.
SMRiC4ZT99. Positions 3-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini275 – 35379PUAUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0263.
HOGENOMiHOG000246369.
KOiK00931.
OMAiMNKQWIA.
OrthoDBiEOG6PGK7G.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB.
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.

C4ZT99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS
60 70 80 90 100
GAIAAGREHL GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ
110 120 130 140 150
MLLTRADMED RERFLNARDT LRALLDNNIV PVINENDAVA TAEIKVGDND
160 170 180 190 200
NLSALAAILA GADKLLLLTD QKGLYTADPR SNPQAELIKD VYGIDDALRA
210 220 230 240 250
IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIAAGSKPG VIGDVMEGIS
260 270 280 290 300
VGTLFHAQAT PLENRKRWIF GAPPAGEITV DEGATAAILE RGSSLLPKGI
310 320 330 340 350
KSVTGNFSRG EVIRICNLEG RDIAHGVSRY NSDALRRIAG HHSQEIDAIL
360
GYEYGPVAVH RDDMITR
Length:367
Mass (Da):39,057
Last modified:July 28, 2009 - v1
Checksum:i5541040202EBCCE8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR63277.1.
RefSeqiWP_001285288.1. NC_012759.1.

Genome annotation databases

EnsemblBacteriaiACR63277; ACR63277; BWG_0224.
KEGGiebw:BWG_0224.
PATRICi18269374. VBIEscCol60876_0244.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR63277.1.
RefSeqiWP_001285288.1. NC_012759.1.

3D structure databases

ProteinModelPortaliC4ZT99.
SMRiC4ZT99. Positions 3-367.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACR63277; ACR63277; BWG_0224.
KEGGiebw:BWG_0224.
PATRICi18269374. VBIEscCol60876_0244.

Phylogenomic databases

eggNOGiCOG0263.
HOGENOMiHOG000246369.
KOiK00931.
OMAiMNKQWIA.
OrthoDBiEOG6PGK7G.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.
BioCyciECOL595496:GI18-235-MONOMER.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB.
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...

Publicationsi

  1. "Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
    Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
    J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MC4100 / BW2952.

Entry informationi

Entry nameiPROB_ECOBW
AccessioniPrimary (citable) accession number: C4ZT99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: July 22, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3

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 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.