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GLPK1_CLOTE
ID   GLPK1_CLOTE             Reviewed;         498 AA.
AC   Q893Q3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Glycerol kinase 1 {ECO:0000255|HAMAP-Rule:MF_00186};
DE            EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase 1 {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase 1 {ECO:0000255|HAMAP-Rule:MF_00186};
DE            Short=GK 1 {ECO:0000255|HAMAP-Rule:MF_00186};
GN   Name=glpK1 {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=CTC_01758;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC   -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC       metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
CC       glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC         Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=2.7.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00186};
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation and inhibited by
CC       fructose 1,6-bisphosphate (FBP). {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- SUBUNIT: Homotetramer and homodimer (in equilibrium).
CC       {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00186}.
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DR   EMBL; AE015927; AAO36289.1; -; Genomic_DNA.
DR   RefSeq; WP_011099949.1; NC_004557.1.
DR   AlphaFoldDB; Q893Q3; -.
DR   SMR; Q893Q3; -.
DR   STRING; 212717.CTC_01758; -.
DR   EnsemblBacteria; AAO36289; AAO36289; CTC_01758.
DR   GeneID; 64179319; -.
DR   KEGG; ctc:CTC_01758; -.
DR   HOGENOM; CLU_009281_2_3_9; -.
DR   OMA; FMLMNIG; -.
DR   OrthoDB; 233605at2; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000001412; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00186; Glycerol_kin; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR005999; Glycerol_kin.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..498
FT                   /note="Glycerol kinase 1"
FT                   /id="PRO_0000059445"
FT   BINDING         12..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         82..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         243..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         409..413
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   498 AA;  55362 MW;  C69BC72DBF023DFD CRC64;
     MAKYVMALDQ GTTSSRCIIF NERGLIVSVA QREFKQIYPK GGWVEHDPME IWATQFSVAT
     EAMAKANIEA SEIASIGITN QRETTIVWDK RTGLPVYNAI VWQCRRTAQI CDELKEKGLT
     ETIRNKTGLV LDAYFSGTKI KWILDNVAGA REEAEKGNLI FGTVDTWLIW NLTKGKVHVT
     DYSNASRTMI YNIHELKWDD ELLEALDIPK SMLPEVKPSS YVYGETNSTL FGSSIPIAGV
     AGDQQAALFG QMCHQEGTAK STYGTGCFLL MNTGEKAVKS ENGLLTTIAF GIDDKVEYAL
     EGSIFIGGAA IQWLRDELRM LKDSPESERY ATAVEDTNGV YMVPAFVGLG APYWDPYARG
     AIVGLTRGAT KEHFIRATLE SLAYQTYDVL NAMREDSGID LKALRVDGGA SANDFLMQFQ
     ADILGVPVQR PEVIETTALG AAYLAGLAVG YWKDKKDVAQ NWAISKTFEP DMIKERREEL
     LEGWHEAVKR SMNWEKSE
 
 
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