ID   GLK1_TRIVA              Reviewed;         375 AA.
AC   Q9GTW9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Glucokinase 1;
DE            EC=2.7.1.2;
DE   AltName: Full=Glucose kinase 1;
DE   AltName: Full=Hexokinase-1;
GN   Name=GK1;
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 30001 / NIH-C1;
RX   PubMed=11250082; DOI=10.1016/s0378-1119(01)00329-8;
RA   Wu G., Henze K., Mueller M.;
RT   "Evolutionary relationships of the glucokinase from the amitochondriate
RT   protist, Trichomonas vaginalis.";
RL   Gene 264:265-271(2001).
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=2.7.1.2;
CC   -!- SUBUNIT: Monomer.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the bacterial glucokinase family. {ECO:0000305}.
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DR   EMBL; AF248652; AAG17616.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9GTW9; -.
DR   SMR; Q9GTW9; -.
DR   VEuPathDB; TrichDB:TVAG_092750; -.
DR   VEuPathDB; TrichDB:TVAGG3_0060660; -.
DR   eggNOG; ENOG502S3Y5; Eukaryota.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   PANTHER; PTHR47450; GLUCOKINASE; 1.
DR   PANTHER; PTHR47450:SF1; GLUCOKINASE; 1.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Glycolysis; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..375
FT                   /note="Glucokinase 1"
FT                   /id="PRO_0000215151"
FT   BINDING         25..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   375 AA;  41585 MW;  229F76B24637BE21 CRC64;
     MFSIDLIQQI KEWKRGSTLP ICLGCDVGGS GLRVRLSDFH DSAKYVDLGH AKAQKTAELL
     KVLEDLQQKI LQVEPTTVCL GAAIAVAGPI KNNTVILTNW KGPAEERTLS ITQLPKGLFP
     KDRSYFLNDL EAGAYGVIAA YEQSILEENF VQLFTDRAPT GPILAKGRTA VLAMGSGLGA
     ALVTRTPLLK NPLVLPTELG HLQIAPNMAT HKYFQDEQEL IQHISDHYYG GKLDPEYEDI
     CSGRGLQLAF QFYHKKLTGE VLPLEQIDAG DVAKKAIAGE KDAYNALRAH YIFYLRAAKA
     IATSLSCESC VLSLDNQVKN HPFVMKIAKE LEEEFYEFIR PDWMTSVRVY SQKSILNFNI
     LGTDYMAHAI ANKPQ
//