UniProt: Q91753

Database: UniProt
Entry: Q91753_XENLA

LinkDB:  Q91753_XENLA 
Original site:  Q91753_XENLA

All links

Ontology (10)   
   GO (10)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   XENBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
3D Structure (1)   
   PDB (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
Literature (3)   
   PubMed (3)   
All databases (30)   

Download RDF

ID   Q91753_XENLA            Unreviewed;       458 AA.
AC   Q91753;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   Name=gck.L {ECO:0000313|RefSeq:NP_001079298.1,
GN   ECO:0000313|Xenbase:XB-GENE-981994};
GN   Synonyms=gck {ECO:0000313|RefSeq:NP_001079298.1,
GN   ECO:0000313|Xenbase:XB-GENE-981994}, gck-A
GN   {ECO:0000313|EMBL:AAI69458.1, ECO:0000313|RefSeq:NP_001079298.1}, glk
GN   {ECO:0000313|RefSeq:NP_001079298.1}, hhf3
GN   {ECO:0000313|RefSeq:NP_001079298.1}, hk4
GN   {ECO:0000313|RefSeq:NP_001079298.1}, hkiv
GN   {ECO:0000313|RefSeq:NP_001079298.1}, hxkp
GN   {ECO:0000313|RefSeq:NP_001079298.1}, mody2
GN   {ECO:0000313|RefSeq:NP_001079298.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:CAA63761.1, ECO:0000313|Proteomes:UP000186698};
RN   [1] {ECO:0000313|EMBL:CAA63761.1, ECO:0000313|RefSeq:NP_001079298.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8626423; DOI=10.1074/jbc.271.11.6292;
RA   Veiga-da-Cunha M., Courtois S., Michel A., Gosselain E.,
RA   Van Schaftingen E.;
RT   "Amino acid conservation in animal glucokinases. Identification of residues
RT   implicated in the interaction with the regulatory protein.";
RL   J. Biol. Chem. 271:6292-6297(1996).
RN   [2] {ECO:0000313|RefSeq:NP_001079298.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [3] {ECO:0000313|EMBL:AAI69458.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocytes {ECO:0000313|EMBL:AAI69458.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:NP_001079298.1, ECO:0007829|PDB:3W0L}
RP   X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS).
RX   PubMed=23733961; DOI=10.1073/pnas.1300457110;
RA   Choi J.M., Seo M.H., Kyeong H.H., Kim E., Kim H.S.;
RT   "Molecular basis for the role of glucokinase regulatory protein as the
RT   allosteric switch for glucokinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:10171-10176(2013).
RN   [5] {ECO:0000313|RefSeq:NP_001079298.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000435};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000256|ARBA:ARBA00000435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000417};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000256|ARBA:ARBA00000417};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004888}.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC169458; AAI69458.1; -; mRNA.
DR   EMBL; BC170499; AAI70499.1; -; mRNA.
DR   EMBL; X93494; CAA63761.1; -; mRNA.
DR   RefSeq; NP_001079298.1; NM_001085829.1.
DR   PDB; 3W0L; X-ray; 2.92 A; A/C=1-458.
DR   PDBsum; 3W0L; -.
DR   GeneID; 378602; -.
DR   KEGG; xla:378602; -.
DR   AGR; Xenbase:XB-GENE-981994; -.
DR   CTD; 378602; -.
DR   Xenbase; XB-GENE-981994; gck.L.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 378602; Expressed in liver and 8 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004340; F:glucokinase activity; ISS:UniProtKB.
DR   GO; GO:0005536; F:glucose binding; ISS:UniProtKB.
DR   GO; GO:0006007; P:glucose catabolic process; ISS:UniProtKB.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF3; HEXOKINASE-4; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3W0L};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362007};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          8..208
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          215..448
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   458 AA;  51087 MW;  5C4E695C4115E4B6 CRC64;
     METFDQNEVD QILSEFHLQE EDLHVLMCRM QAEMERGLHL ETNEEASVKM LPTYVRSTPD
     GSEVGDFLAL DLGGTNFRVM LVKVGEDLEG QWKVETKHKM YSIPVDAMTG TAEMLFDYIA
     ECISDYLDQQ NMKHKKLPLG FTFSFPVRHE DIDKGILLNW TKGFKASGAE GNNVVGLLRD
     AIKRRGDFEM DVVAMVNDTV ATMISCYYED HHCEVGLIVG TGCNACYMEE MSNVELVEGE
     EGRMCVNTEW GAFGDTGELE DFRLEYDRVV DEASLNPGQQ LYEKMIGGKY MGELVRLVLI
     KMVNENLLFG GESSEKLKTR GAFETQFVSQ IEADTSDFKQ TLNILRTLGV QATIGDCHAV
     RLACESVSTR AAIMCSAGLA GILNRMRQSR REELLRITVG VDGSVYKLHP SFKDKFHATV
     LKLTSGCEIT FIQSEEGSGR GAALISAVAY KMAVMIGH
//

DBGET integrated database retrieval system