ID S7PAY7_MYOBR Unreviewed; 975 AA.
AC S7PAY7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=hexokinase {ECO:0000256|ARBA:ARBA00012324};
DE EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324};
DE Flags: Fragment;
GN ORFNames=D623_10032514 {ECO:0000313|EMBL:EPQ07328.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07328.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
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}.
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DR EMBL; KE162186; EPQ07328.1; -; Genomic_DNA.
DR AlphaFoldDB; S7PAY7; -.
DR eggNOG; KOG1369; Eukaryota.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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; -; 3.
DR Gene3D; 3.40.367.20; -; 3.
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:SF1; HEXOKINASE-3; 1.
DR Pfam; PF00349; Hexokinase_1; 2.
DR Pfam; PF03727; Hexokinase_2; 3.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 5.
DR PROSITE; PS00378; HEXOKINASE_1; 2.
DR PROSITE; PS51748; HEXOKINASE_2; 2.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPQ07328.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 45..242
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 250..469
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT DOMAIN 480..671
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 678..796
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT DOMAIN 852..965
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPQ07328.1"
SQ SEQUENCE 975 AA; 105184 MW; 38D7EDC0C701D5F8 CRC64;
PIGGYSQLWN HMDSIGPVGL WQEEAAPGSP QEGLPCSPDS SELAQECLNQ FKVTSTQLRQ
IQASLLRSME QALTGQASPA PAVRMLPTYV GSTPHGTEQG DFVVLELGAT GASLRVLWVT
LTGTEGHRIE PRSQEFLIPQ EVMLGPGQQL FDFAARCLSE FLDAHPVDRQ GLQLGFNFSF
PCHQTGLDKS TLISWTKGFR CSGVEGQDVV QLLRDAIERQ GACSIDVVAV VNDTVGTMMG
CELGTVPCEV GLVVDTGTNA CYMEEARHVA VLDEDRGRVC VSIEWGSFGD DGALGSVLTT
FDRILDQESL NPGAQRFEKM IGGLYLGELV RQVLAHLAQH GVLFGGCTSR ALLSRGGILL
EHVAEMEDAS AGTARVHAIL RDLGLNPGAS DAELPCPAAL AAVLTRLQHS REQQTLQIAV
ATGGRVFEHH PRFLSVLQET VTLLAPECDV SFIPSVDGGG QGVAMVTAVA ARLAAHRRLL
EETLAPFRLN REQLAVVQAQ MREAMVKGLQ GEASSLRMLP TYVRATPDGS ERGDFLALDL
GGTNFRVLLV HVATEGVQIT NQVYSIPECV AQGSGQQLFD HIVDCILDFQ QKQGLSGQSL
PLGFTFSFPC RQLGLDQGIL LNWTKGFNAS DCEGQDVVLL LREALERRQA MKLTVVAIVN
DTVGTMMSCG YEDPRCEVGL IVGTGTNACY MEELRNVAGV AGDLGHMCIN MEWGAFGDDG
SLDTLSTCFD ASVDRASINP GKQRFEKMIS GMYLGEIVRH ILLHLTSLGV LFRGQQTQSL
QTRDIFKTKF LSEIERCRAV HYRLPPPKGV FLFTLGGRLV GGRSTQEDRS HERGANARPY
LCVLFLPVPS DSLALRQVRA ILEDLGLPLT SDDTLMVLEV CQAVSQRAAQ LCGAGVAAVV
EKIRENRGLE ELTVSVGVDG TLYKLHPHFS RLVAATVQEL APCCAVTFLQ SEDGSGKGAA
LVTAVACRLA KQAHV
//
