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Database: UniProt
Entry: Q6MTY7
LinkDB: Q6MTY7
Original site: Q6MTY7 
ID   GLPK_MYCMS              Reviewed;         505 AA.
AC   Q6MTY7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   19-FEB-2014, entry version 71.
DE   RecName: Full=Glycerol kinase;
DE            EC=2.7.1.30;
DE   AltName: Full=ATP:glycerol 3-phosphotransferase;
DE   AltName: Full=Glycerokinase;
DE            Short=GK;
GN   Name=glpK; OrderedLocusNames=MSC_0258;
OS   Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type
RT   strain PG1T, the causative agent of contagious bovine pleuropneumonia
RT   (CBPP).";
RL   Genome Res. 14:221-227(2004).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3-
CC       phosphate.
CC   -!- ENZYME REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP)
CC       (By similarity).
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
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DR   EMBL; BX293980; CAE76899.1; -; Genomic_DNA.
DR   RefSeq; NP_975257.1; NC_005364.2.
DR   ProteinModelPortal; Q6MTY7; -.
DR   SMR; Q6MTY7; 4-503.
DR   STRING; 272632.MSC_0258; -.
DR   EnsemblBacteria; CAE76899; CAE76899; MSC_0258.
DR   GeneID; 2744286; -.
DR   KEGG; mmy:MSC_0258; -.
DR   PATRIC; 20017246; VBIMycMyc4973_0279.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; ALYGQLC; -.
DR   OrthoDB; EOG6RZB46; -.
DR   ProtClustDB; CLSK829635; -.
DR   BioCyc; MMYC272632:GI1G-252-MONOMER; -.
DR   UniPathway; UPA00618; UER00672.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   HAMAP; MF_00186; Glycerol_kin; 1.
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   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; Complete proteome; Glycerol metabolism; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    505       Glycerol kinase.
FT                                /FTId=PRO_1000020747.
FT   NP_BIND      15     17       ATP (By similarity).
FT   NP_BIND     415    419       ATP (By similarity).
FT   REGION       85     86       Substrate binding (By similarity).
FT   REGION      249    250       Substrate binding (By similarity).
FT   BINDING      15     15       Substrate (By similarity).
FT   BINDING      19     19       ATP (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     271    271       ATP (By similarity).
FT   BINDING     314    314       ATP; via carbonyl oxygen (By similarity).
FT   BINDING     318    318       ATP; via amide nitrogen (By similarity).
FT   BINDING     333    333       ATP (By similarity).
SQ   SEQUENCE   505 AA;  57332 MW;  7A3A2667B51F2FD9 CRC64;
     MTDSKKYILT LDEGTTSARA LITDKQGNII AVEQSEFTQY FPKEGWVEHD AIEIWNTQRS
     ALVQVLNKSG IDPSQIEAIG ITNQRETAVI WNKETGLPIY NAIVWQDQRT ADYCQTFDKD
     TLEMVKQRSG LIINPYFSGT KVKWILDNVP NARQLAKEGK LMFGTINTWL IYRLTGGEVF
     VTDHTNAQRT LLYNIHTNDW DDELLKLFDI PRNILPEIKS CSEVYGYTFK GLFSKGNEQR
     IKIASSIGDQ QSALFGQLCL EKGQVKVTYG TGCFILTNTG EEIVKSNHGL LTTVAYSFKD
     KVYYALEGSV MIAGAAVQWL RDNLRIVYNA IETEWYADQV KDDRRVYVVP SFTGLGSPYW
     DSFSRGAIFG LDRGTRREHI VRATLEAIVY QANDVVDAMR KDMKKPIEIF KVDGGAANNK
     FLMQFQSNIS QSKVIKPTNV ETTAMGAAFM VGLAVGYWEN AEELKKTYKV HFELTPELSK
     PEVDKLIKGW KVAVQRTFKW VEEIE
//
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