ID A0A0F8C8C5_LARCR Unreviewed; 919 AA.
AC A0A0F8C8C5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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};
GN ORFNames=EH28_03154 {ECO:0000313|EMBL:KKF27115.1};
OS Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Larimichthys.
OX NCBI_TaxID=215358 {ECO:0000313|EMBL:KKF27115.1};
RN [1] {ECO:0000313|EMBL:KKF27115.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSNF {ECO:0000313|EMBL:KKF27115.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KKF27115.1};
RX PubMed=25835551;
RA Ao J., Mu Y., Xiang L.X., Fan D., Feng M., Zhang S., Shi Q., Zhu L.Y.,
RA Li T., Ding Y., Nie L., Li Q., Dong W.R., Jiang L., Sun B., Zhang X.,
RA Li M., Zhang H.Q., Xie S., Zhu Y., Jiang X., Wang X., Mu P., Chen W.,
RA Yue Z., Wang Z., Wang J., Shao J.Z., Chen X.;
RT "Genome Sequencing of the Perciform Fish Larimichthys crocea Provides
RT Insights into Molecular and Genetic Mechanisms of Stress Adaptation.";
RL PLoS Genet. 11:E1005118-E1005118(2015).
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}.
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; KQ041417; KKF27115.1; -; Genomic_DNA.
DR RefSeq; XP_019117413.1; XM_019261868.1.
DR AlphaFoldDB; A0A0F8C8C5; -.
DR eggNOG; KOG1369; Eukaryota.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
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, ECO:0000313|EMBL:KKF27115.1};
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; 102896 MW; EBDEDE9926031363 CRC64;
MIAAQLLAYY FTELKDDQLK KIDKYLYSMR FSDETLKDIM NRFRREMENG LGRDTNPTAT
VKMLPTFVRS IPDGSEKGDF IALDLGGSNF RILRVKVTHD KKQPVQMESQ VYDTPDDIIH
GSGSRLFDHV ADCLGDFMEK QKIKDKKLPV GFTFSFPCAQ SKLDEAVLLT WTKKFKASGV
EGMDVVKLLN KAIKKRGDYE ADIMAVVNDT VGTMMTCGFD DQRCEVGIII GTGTNACYME
ELRHIDLVEG DEGRMCINTE WGSFGDNGSI EDIRTEFDRE IDRGSINPGK QLFEKMASGM
YMGELVRLIL VKMAKEGLLF EGRITPELLT KGKIETKHVS AIEKTKEGLK KCMEILTRLG
VEPSDEDCLA VQHVCTIVSF RSANLIASTL GGILSRLKEN KGVARLRTTV GIDGSLYKMH
PQYARRLHKT VRRLVPDSDV RFLLSESGSA KGAAMVTAVA YRLTEQARQI QQTMAEFRLS
KAQLLEVKKR MRVEIERGLK KDSHKEATVK MLPTFVRTTP DGTENGDFLA LDLGGTNFRV
LLVKIRSGKR RTVEMHNKIY AIPIEVMQGT GEELFDHIVH CISDFLDYMG MKSARLPLGF
TFSFPCHQTS LDAGILVTWT KGFKATDCEG EDVVELLREA IKRKEEFELD VVAIVNDTVG
TMMTCAYEEP TCEVGLIAGT GSNACYMEET KNIEIVEGNE GRMCVNMEWG AFGDNGCLDD
IRTRYDQAVD ENSLNEGKQR YEKMCSGMYL GEIVRQILID LTKRGFLFRG QISETLKTRG
IFETKFLSQI ESDRLALLQV RAILQQLGLD STCDDSIIVK EVCGTVSRRA AQICGAGMAA
VVDKIRENRG LDHLDITVGV DGTLYKLHPH FSRIFQQTVK ELAPKCDVNF LLSEDGSGKG
AALITAVGCR QRELEAQQH
//
