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B4TPU7

- GLPK_SALSV

UniProt

B4TPU7 - GLPK_SALSV

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Protein
Glycerol kinase
Gene
glpK, SeSA_A4302
Organism
Salmonella schwarzengrund (strain CVM19633)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate By similarity.UniRule annotation

Catalytic activityi

ATP + glycerol = ADP + sn-glycerol 3-phosphate.UniRule annotation

Enzyme regulationi

Activity of this regulatory enzyme is affected by several metabolites. Allosterically and non-competitively inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141Substrate By similarity
Binding sitei18 – 181ATP By similarity
Binding sitei136 – 1361Substrate By similarity
Binding sitei268 – 2681ATP By similarity
Binding sitei311 – 3111ATP; via carbonyl oxygen By similarity
Binding sitei315 – 3151ATP; via amide nitrogen By similarity
Binding sitei330 – 3301ATP By similarity
Metal bindingi479 – 4791Zinc; shared with EIIA-Glc By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 163ATP By similarity
Nucleotide bindingi412 – 4165ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glycerol kinase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glycerol catabolic process Source: UniProtKB-UniPathway
  2. glycerol metabolic process Source: UniProtKB
  3. glycerol-3-phosphate metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycerol metabolism

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciSENT439843:GHHR-1874-MONOMER.
UniPathwayiUPA00618; UER00672.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol kinase (EC:2.7.1.30)
Alternative name(s):
ATP:glycerol 3-phosphotransferase
Glycerokinase
Short name:
GK
Gene namesi
Name:glpK
Ordered Locus Names:SeSA_A4302
OrganismiSalmonella schwarzengrund (strain CVM19633)
Taxonomic identifieri439843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001865: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Glycerol kinaseUniRule annotation
PRO_1000098761Add
BLAST

Interactioni

Subunit structurei

Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization By similarity.

Protein-protein interaction databases

STRINGi439843.SeSA_A4302.

Structurei

3D structure databases

ProteinModelPortaliB4TPU7.
SMRiB4TPU7. Positions 3-501.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 852Substrate binding By similarity
Regioni234 – 2363Allosteric FBP inhibitor bindingUniRule annotation
Regioni246 – 2472Substrate binding By similarity

Sequence similaritiesi

Belongs to the FGGY kinase family.

Phylogenomic databases

eggNOGiCOG0554.
HOGENOMiHOG000222134.
OMAiHFFGVEV.
OrthoDBiEOG6RZB46.

Family and domain databases

HAMAPiMF_00186. Glycerol_kin.
InterProiIPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
PfamiPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01311. glycerol_kin. 1 hit.
PROSITEiPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B4TPU7-1 [UniParc]FASTAAdd to Basket

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MTEKKYIVAL DQGTTSSRAV VMDHDANIVS VSQREFEQIY PKPGWVEHDP    50
MEIWASQSST LVEVLAKADI SSDQIAAIGI TNQRETAIVW ERETGKPIYN 100
AIVWQCRRTA DICEQLKRDG LEDYIRDNTG LVVDPYFSGT KVKWILDHVE 150
GSRERAKRGE LLFGTVDTWL IWKMTQGRVH VTDYTNASRT MLFNIHDLDW 200
DDKMLDVLDI PRAMLPQVRK SSEVYGQTNI GGKGGTRIPI AGIAGDQQAA 250
LFGQLCVKEG MAKNTYGTGC FMLMNTGEKA VKSENGLLTT IACGPSGEVN 300
YALEGAVFMA GASIQWLRDE MKLISDAFDS EYFATKVKDT NGVYVVPAFT 350
GLGAPYWDPY ARGAIFGLTR GVNSNHIIRA TLESIAYQTR DVLEAMQADS 400
GIRLHALRVD GGAVANNFLM QFQSDILGTR VERPEVREVT ALGAAYLAGL 450
AVGYWQNLDE LQEKAVIERE FRPGIETTER NYRYSGWKKA VKRAMAWEEH 500
DK 502
Length:502
Mass (Da):56,052
Last modified:September 23, 2008 - v1
Checksum:iA780A522CA16C1B4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001127 Genomic DNA. Translation: ACF90443.1.
RefSeqiYP_002117007.1. NC_011094.1.

Genome annotation databases

EnsemblBacteriaiACF90443; ACF90443; SeSA_A4302.
PATRICi32377167. VBISalEnt87589_4275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001127 Genomic DNA. Translation: ACF90443.1 .
RefSeqi YP_002117007.1. NC_011094.1.

3D structure databases

ProteinModelPortali B4TPU7.
SMRi B4TPU7. Positions 3-501.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439843.SeSA_A4302.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF90443 ; ACF90443 ; SeSA_A4302 .
PATRICi 32377167. VBISalEnt87589_4275.

Phylogenomic databases

eggNOGi COG0554.
HOGENOMi HOG000222134.
OMAi HFFGVEV.
OrthoDBi EOG6RZB46.

Enzyme and pathway databases

UniPathwayi UPA00618 ; UER00672 .
BioCyci SENT439843:GHHR-1874-MONOMER.

Family and domain databases

HAMAPi MF_00186. Glycerol_kin.
InterProi IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view ]
Pfami PF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01311. glycerol_kin. 1 hit.
PROSITEi PS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
    Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
    J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CVM19633.

Entry informationi

Entry nameiGLPK_SALSV
AccessioniPrimary (citable) accession number: B4TPU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 39 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

Allosteric enzyme, Complete proteome

Documents

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

External Data

Dasty 3

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