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Database: UniProt
Entry: A0A452GIW0_9SAUR
LinkDB: A0A452GIW0_9SAUR
Original site: A0A452GIW0_9SAUR 
ID   A0A452GIW0_9SAUR        Unreviewed;       889 AA.
AC   A0A452GIW0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Hexokinase-2 {ECO:0000256|ARBA:ARBA00039453};
DE            EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324};
DE   AltName: Full=Hexokinase type II {ECO:0000256|ARBA:ARBA00041371};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000001534.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000001534.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   -!- 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   AlphaFoldDB; A0A452GIW0; -.
DR   STRING; 38772.ENSGAGP00000001534; -.
DR   Ensembl; ENSGAGT00000001750.1; ENSGAGP00000001534.1; ENSGAGG00000001241.1.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000291020; 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; -; 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:SF4; HEXOKINASE-2; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..191
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          198..431
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
FT   DOMAIN          443..639
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          646..879
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   889 AA;  99006 MW;  1CC3CA81B89A033C CRC64;
     MRLSDETLQE VSERFRKEME KGLGADTNPT ASVKMLPSFV RSTPDGTENG DFLALDLGGT
     NFRVLRVKVS DNGLRKVEME NQIYAIPEDL MRGSGVQLFD HIAECLANFM EKLNMKDKKL
     PLGFTFSFPC HQTKLDESIL VTWTKGFKSS GVEGKDVVAM IRKAIKKRGD FDIDLVAVVN
     DTVGTMMTCG YDDHNCEVGL IVGTGTNACY MEEMRHIDLV EGDEGRMCIN MEWGAFGDDG
     VLNDIRTEFD REIDMGSLNP GKQLFEKMIS GMYMGELVRL ILVKMAKEEL LFDGRLTPSL
     LTTGHFETGY VSAIEKEKEG LQKAHEILTK LGLDPSAEDC IATQHICQIV STRSANLCGA
     TLAAVLRRIK ENKGVDRLRS TIGVDGSVYK KHPHFARRLQ KTVRKLLPDC DIRFVRSEDG
     SGKGAAMVTA VAYRLAAQHK ARQKTLEALK LSHEQLLEVK NRMRIEMERG LSKASHPDAT
     VKMLPTYVCA TPDGTEKGDF LALDLGGTNF RVLLVRVRNG IRRGVEMHNK IYSIPQEIMQ
     GTGEELFDHI VHCISDFLEY MGMKGVSLPL GFTFSFPCQQ NNLDEGILLK WTKGFKATGC
     EGEDVVNLLK EAIHRREEFD LDVVAVVNDT VGTMMTCGYE DPYCEVGLIV GTGSNACYME
     EMRNVELVEG EEGRMCINME WGAFGDNGCL DDFQTEFDVA VDELSLNAGK QRFEKMISGM
     YLGEIVRNIL IDFTKRGLLF RGRISERLKT RGIFETKFLS QIESDCLALL QVRSILQHLG
     LESTCDDSII VKEVCTVVAR RAAQLCGAGM AAVVDKIREN RKLDFLKVTV GVDGTLYKLH
     PHFSSIMHET VKQLTPKCEV TFLQSEDGSG KGAALITAVA CRIREAGQR
//
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