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Database: UniProt/SWISS-PROT
Entry: HXK1_PONAB
LinkDB: HXK1_PONAB
Original site: HXK1_PONAB 
ID   HXK1_PONAB              Reviewed;         917 AA.
AC   Q5RC71;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   05-DEC-2018, entry version 65.
DE   RecName: Full=Hexokinase-1;
DE            EC=2.7.1.1;
DE   AltName: Full=Hexokinase type I;
DE            Short=HK I;
GN   Name=HK1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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;
CC         EC=2.7.1.1;
CC   -!- ACTIVITY REGULATION: Hexokinase is an allosteric enzyme inhibited
CC       by its product Glc-6-P. {ECO:0000250}.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBUNIT: Monomer. Interacts with VDAC1. The HK1-VDAC1 complex
CC       interacts with ATF2 (By similarity). Interacts with RABL2/RABL2A;
CC       binds preferentially to GTP-bound RABL2 (By similarity). Interacts
CC       (via N-terminal spermatogenic cell-specific region) with PFKM (via
CC       C-terminus) (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P17710}.
CC   -!- DOMAIN: The N- and C-terminal halves of this hexokinase show
CC       extensive sequence similarity to each other. The catalytic
CC       activity is associated with the C-terminus while regulatory
CC       function is associated with the N-terminus. Each domain can bind a
CC       single glucose and Gluc-6-P molecule (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: In vertebrates there are four major glucose-
CC       phosphorylating isoenzymes, designated hexokinase I, II, III and
CC       IV (glucokinase).
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000305}.
DR   EMBL; CR858409; CAH90636.1; -; mRNA.
DR   RefSeq; NP_001125344.1; NM_001131872.1.
DR   ProteinModelPortal; Q5RC71; -.
DR   SMR; Q5RC71; -.
DR   STRING; 9601.ENSPPYP00000002765; -.
DR   PRIDE; Q5RC71; -.
DR   GeneID; 100172246; -.
DR   KEGG; pon:100172246; -.
DR   CTD; 3098; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   eggNOG; COG5026; LUCA.
DR   HOVERGEN; HBG005020; -.
DR   InParanoid; Q5RC71; -.
DR   KO; K00844; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005623; C:cell; IEA:GOC.
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:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; PTHR19443; 4.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 2.
DR   PROSITE; PS51748; HEXOKINASE_2; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Glycolysis; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN         1    917       Hexokinase-1.
FT                                /FTId=PRO_0000286047.
FT   DOMAIN       16    458       Hexokinase 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01084}.
FT   DOMAIN      464    906       Hexokinase 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01084}.
FT   NP_BIND      84     89       ATP 1. {ECO:0000255}.
FT   NP_BIND     425    426       ATP 1. {ECO:0000250}.
FT   NP_BIND     532    537       ATP 2. {ECO:0000250}.
FT   NP_BIND     747    748       ATP 2. {ECO:0000250}.
FT   NP_BIND     784    788       ATP 2. {ECO:0000250}.
FT   NP_BIND     863    867       ATP 2. {ECO:0000250}.
FT   REGION        1     12       Hydrophobic.
FT   REGION       13    475       Regulatory.
FT   REGION       73    207       Hexokinase small subdomain 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION       84     88       Glucose-6-phosphate 1 binding.
FT                                {ECO:0000250}.
FT   REGION      172    173       Substrate 1 binding. {ECO:0000250}.
FT   REGION      208    447       Hexokinase large subdomain 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      208    209       Substrate 1 binding. {ECO:0000250}.
FT   REGION      291    294       Substrate 1 binding. {ECO:0000250}.
FT   REGION      413    415       Glucose-6-phosphate 1 binding.
FT                                {ECO:0000250}.
FT   REGION      476    917       Catalytic.
FT   REGION      521    655       Hexokinase small subdomain 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      532    536       Glucose-6-phosphate 2 binding.
FT                                {ECO:0000250}.
FT   REGION      603    604       Substrate 2 binding. {ECO:0000250}.
FT   REGION      620    621       Substrate 2 binding. {ECO:0000250}.
FT   REGION      656    895       Hexokinase large subdomain 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01084}.
FT   REGION      656    657       Substrate 2 binding. {ECO:0000250}.
FT   REGION      861    863       Glucose-6-phosphate 2 binding.
FT                                {ECO:0000250}.
FT   BINDING      30     30       ATP 1. {ECO:0000250}.
FT   BINDING     155    155       Substrate 1. {ECO:0000250}.
FT   BINDING     209    209       Glucose-6-phosphate 1. {ECO:0000250}.
FT   BINDING     232    232       Glucose-6-phosphate 1. {ECO:0000250}.
FT   BINDING     235    235       Substrate 1. {ECO:0000250}.
FT   BINDING     260    260       Substrate 1. {ECO:0000250}.
FT   BINDING     449    449       Glucose-6-phosphate 1. {ECO:0000250}.
FT   BINDING     603    603       Glucose-6-phosphate 2. {ECO:0000250}.
FT   BINDING     657    657       Glucose-6-phosphate 2. {ECO:0000250}.
FT   BINDING     680    680       ATP 2. {ECO:0000250}.
FT   BINDING     680    680       Glucose-6-phosphate 2. {ECO:0000250}.
FT   BINDING     683    683       Substrate 2. {ECO:0000250}.
FT   BINDING     708    708       Substrate 2. {ECO:0000250}.
FT   BINDING     742    742       Substrate 2. {ECO:0000250}.
FT   BINDING     897    897       Glucose-6-phosphate 2. {ECO:0000250}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:P19367}.
FT   MOD_RES     337    337       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05708}.
SQ   SEQUENCE   917 AA;  102363 MW;  BCB4765425999C79 CRC64;
     MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT
     VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH
     GSGSQLFDHV AECLGDFMEK RKIKDKKSPV GFTFSFPCQQ SKIDEAVLIT WTKRFKASGV
     EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQHCEVGLII GTGTNACYME
     ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE IDRGSLNPGK QLFEKMVSGM
     YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG
     VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH
     PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT
     KDMLLEVKKR MRAEMELGLR KQTHNNAAVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV
     LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF
     TFSFPCKQTS LDAGILITWT KGFKATDCVG NDVATLLRDA IKRREEFDLD VVAVVNDTVG
     TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD
     IRTHYDRLVD EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISEPLKTRG
     IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSRRA AQLCGAGMAA
     VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG
     AALITAVGVR LRTEASS
//
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