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GLK_NEIG2
ID   GLK_NEIG2               Reviewed;         328 AA.
AC   B4RM12;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Glucokinase {ECO:0000255|HAMAP-Rule:MF_00524};
DE            EC=2.7.1.2 {ECO:0000255|HAMAP-Rule:MF_00524};
DE   AltName: Full=Glucose kinase {ECO:0000255|HAMAP-Rule:MF_00524};
GN   Name=glk {ECO:0000255|HAMAP-Rule:MF_00524}; OrderedLocusNames=NGK_1172;
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=521006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945;
RX   PubMed=18586945; DOI=10.1128/jb.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00524};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00524}.
CC   -!- SIMILARITY: Belongs to the bacterial glucokinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00524}.
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DR   EMBL; CP001050; ACF29849.1; -; Genomic_DNA.
DR   RefSeq; WP_003688729.1; NC_011035.1.
DR   AlphaFoldDB; B4RM12; -.
DR   SMR; B4RM12; -.
DR   EnsemblBacteria; ACF29849; ACF29849; NGK_1172.
DR   GeneID; 66753060; -.
DR   KEGG; ngk:NGK_1172; -.
DR   HOGENOM; CLU_042582_1_0_4; -.
DR   OMA; NNHWRLS; -.
DR   OrthoDB; 992687at2; -.
DR   Proteomes; UP000002564; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR00749; glk; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..328
FT                   /note="Glucokinase"
FT                   /id="PRO_1000127712"
FT   BINDING         16..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   328 AA;  35084 MW;  865E894DDE3E6FF4 CRC64;
     MSSTPNKHAD YPRLVADIGG TNARFALETA PCVIEKVAVL PCKEYDTVTD AVRAYLNQSG
     ATGVRHAAFA IANPILGDWV QMTNHHWAFS IETTRQALGL DTLILLNDFT AQALAVTQTS
     SKDLMQVGGQ KPVEFAPKAV IGPGTGLGVS GLVHSPAGWV ALAGEGGHTS FPPFDDMEVL
     IWQYAKNKYR HVSAERFLSG AGLSLIYETL AAKQKAEPAK LMPSEITEKA LNCESPLCRQ
     ALDIFCAMLG TVASNLALTL GARGGVYLCG GIIPRMLDYF KTSPFRSRFE NKGRFEAYLA
     AIPVYVVLSE FPGIAGAAAA LGNHLKNV
 
 
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