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Database: UniProt
Entry: A0A3B3Y7J4_9TELE
LinkDB: A0A3B3Y7J4_9TELE
Original site: A0A3B3Y7J4_9TELE 
ID   A0A3B3Y7J4_9TELE        Unreviewed;       919 AA.
AC   A0A3B3Y7J4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Hexokinase-1 {ECO:0000256|ARBA:ARBA00044081};
DE            EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324};
DE   AltName: Full=Hexokinase type I {ECO:0000256|ARBA:ARBA00044308};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000023304.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000023304.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:10948, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00043797};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10949;
CC         Evidence={ECO:0000256|ARBA:ARBA00043797};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00043834};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC         Evidence={ECO:0000256|ARBA:ARBA00043834};
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004450}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225}.
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DR   RefSeq; XP_014863159.1; XM_015007673.1.
DR   STRING; 48701.ENSPMEP00000003595; -.
DR   Ensembl; ENSPMET00000010583.1; ENSPMEP00000023304.1; ENSPMEG00000004761.1.
DR   Ensembl; ENSPMET00000010593.1; ENSPMEP00000003595.1; ENSPMEG00000004761.1.
DR   GeneID; 106930240; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000261480; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 2.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.40.367.20; -; 2.
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:SF10; HEXOKINASE-1; 1.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 4.
DR   PROSITE; PS00378; HEXOKINASE_1; 2.
DR   PROSITE; PS51748; HEXOKINASE_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Inflammatory response {ECO:0000256|ARBA:ARBA00023198};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          22..218
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          226..459
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
FT   DOMAIN          470..667
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          674..907
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   919 AA;  102776 MW;  AE6089A26213D88F CRC64;
     MIAAQLLAYY FTELKDDQLK KIDKYLYSMR FSDETLRDIM GRFRRDMENG LGRDTNPTAT
     VKMLPTFVRS IPDGSEKGDF IALDLGGSNF RILRVKVTQD KKQPVQMESQ VYDTPDDIIH
     GSGTQLFDHV AECLGDFMEK QKIKDKRLPV GFTFSFPCVQ SKLDEAILVT WTKKFKANGV
     EGMDVVKLLN KAIKKRGDYQ ADIMAVVNDT VGTMMTCGFD DQRCEVGIII GTGTNACYME
     ELRHIDLVEG DEGRMCINTE WGAFGDNGSL EDIRTEFDRE IDRGSLNPGK QLFEKMASGM
     YMGELVRLIL VKMAKEGLLF EGRITPELLT KGKIETKHVS AIEKTKEGLK KCMEILTRLG
     VEPSDEDCLA VRHVCTIVSF RSANLISATL GAILSRLKDN KGVARLRTTV GIDGSLYKMH
     PQYARRLHKT VRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLTDQARQI QETLAEFRLS
     KGQLLEVKKR MRMEIERGLK KDTHKEATVK MLPTFVRSTP DGTENGDFLA LDLGGTNFRV
     LLVKIRSGKK RTVEMHNKIY AIPIEVMQGT GEELFDHIVH CISDFLDYMG MKSARLPLGF
     TFSFPCHQTS LDAGILVTWT KGFKATDCEG EDVVELLREA IKRKEEFELD VVAIVNDTVG
     TMMTCAYEEP TCEVGLIAGT GSNACYMEEL KNIEIVGGTE GRMCVNMEWG AFGDNGCLDD
     IRTKYDQAVD ENSLNEGKQR YEKMCSGMYL GEIVRQILID LTKRGFLFRG QISETLKTRG
     IFETKFLSQI ESDRLALLQV RAILQQLGLD STCDDSIIVK EVCGTVSRRA AQICGAGMAA
     VVDKIRENRG LDHLDITVGV DGTLYKLHPH FSRIFHQTVK ELAPKCDVNF LLSEDGSGKG
     AALITAVGCR QRELDAQQH
//
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