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Database: UniProt
Entry: Q88ZF1
LinkDB: Q88ZF1
Original site: Q88ZF1 
ID   GLPK1_LACPL             Reviewed;         505 AA.
AC   Q88ZF1; F9UTW7;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   19-FEB-2014, entry version 69.
DE   RecName: Full=Glycerol kinase 1;
DE            EC=2.7.1.30;
DE   AltName: Full=ATP:glycerol 3-phosphotransferase 1;
DE   AltName: Full=Glycerokinase 1;
DE            Short=GK 1;
GN   Name=glpK1; OrderedLocusNames=lp_0370;
OS   Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D.,
RA   Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M.,
RA   Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A.,
RA   Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B.,
RA   De Vos W.M., Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3-
CC       phosphate.
CC   -!- ENZYME REGULATION: Activated by phosphorylation and inhibited by
CC       fructose 1,6-bisphosphate (FBP) (By similarity).
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC   -!- SUBUNIT: Homotetramer and homodimer (in equilibrium) (By
CC       similarity).
CC   -!- PTM: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), including enzyme I, and histidine-containing protein
CC       (HPr) are required for the phosphorylation, which leads to the
CC       activation of the enzyme (By similarity).
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
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DR   EMBL; AL935263; CCC77887.1; -; Genomic_DNA.
DR   RefSeq; YP_004888401.1; NC_004567.2.
DR   ProteinModelPortal; Q88ZF1; -.
DR   SMR; Q88ZF1; 5-490.
DR   STRING; 220668.lp_0370; -.
DR   EnsemblBacteria; CCC77887; CCC77887; lp_0370.
DR   GeneID; 1064209; -.
DR   KEGG; lpl:lp_0370; -.
DR   PATRIC; 22247255; VBILacPla27411_0314.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; KMAGSAQ; -.
DR   ProtClustDB; PRK00047; -.
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; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    505       Glycerol kinase 1.
FT                                /FTId=PRO_0000059460.
FT   NP_BIND      13     15       ATP (By similarity).
FT   NP_BIND     411    415       ATP (By similarity).
FT   REGION       83     84       Substrate binding (By similarity).
FT   REGION      245    246       Substrate binding (By similarity).
FT   BINDING      13     13       Substrate (By similarity).
FT   BINDING      17     17       ATP (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   BINDING     267    267       ATP (By similarity).
FT   BINDING     310    310       ATP; via carbonyl oxygen (By similarity).
FT   BINDING     314    314       ATP; via amide nitrogen (By similarity).
FT   BINDING     329    329       ATP (By similarity).
FT   MOD_RES     231    231       Phosphohistidine; by HPr (By similarity).
SQ   SEQUENCE   505 AA;  55818 MW;  09D135885F9AB76A CRC64;
     MTDKYIMAID EGTTSTRAII FDHAGHKVAD SQREFPQYFP QPGWVEHNAN EIWNAVLSTI
     ANAFIESGIK PAQISGIGIT NQRETTIVWD KQTGLPIYNA IVWQSRQTAP IAEKLVKDGY
     GDLIHQHTGL VTDAYFSATK IRWILDHVKG AQERAEKGEL LFGTIDTWLL WKLTGGATHV
     TDYSNASRTM LFNIHDLKWD DQILQLLNIP AAMLPEVRTN SEVYGKTKDY HFFGSEVPIS
     GMAGDQQAAL FGQLAFEPGT VKNTYGTGAF IVMNTGEKPQ LSDNNLLTTI GYGINGKVYY
     ALEGSIFVAG SAIQWLRDGI RLVESAPDSE RAARESHNEN EVYVVPAFTG LGAPYWDSEA
     RGSVFGLTRG TTREDFIKAT LQALAYQTRD VVETMKKDSG IEIPVLKVDG GAARNDWLMQ
     FQADILDTQI MRAANLETTA LGAAFLAGLS VGYWQDLEEL KASYKPGTSF DPEMGPAERT
     NLYEGWQAAV KATQVFKHTP YHAGK
//
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