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Database: UniProt
Entry: Q8FWK8
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ID   GLPK_BRUSU              Reviewed;         498 AA.
AC   Q8FWK8; G0KCH8;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   01-OCT-2014, entry version 74.
DE   RecName: Full=Glycerol kinase {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 {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE            Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
GN   Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186};
GN   OrderedLocusNames=BRA0443, BS1330_II0440;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/JB.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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: ATP + glycerol = ADP + sn-glycerol 3-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- ENZYME REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP).
CC       {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
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; AE014292; AAN33637.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM19916.1; -; Genomic_DNA.
DR   RefSeq; NP_699632.1; NC_004311.2.
DR   RefSeq; YP_005614142.1; NC_017250.1.
DR   ProteinModelPortal; Q8FWK8; -.
DR   SMR; Q8FWK8; 4-494.
DR   STRING; 204722.BRA0443; -.
DR   EnsemblBacteria; AAN33637; AAN33637; BRA0443.
DR   EnsemblBacteria; AEM19916; AEM19916; BS1330_II0440.
DR   GeneID; 1164881; -.
DR   GeneID; 12139875; -.
DR   KEGG; bms:BRA0443; -.
DR   KEGG; bsi:BS1330_II0440; -.
DR   PATRIC; 17793689; VBIBruSui107850_2660.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; HFFGVEV; -.
DR   OrthoDB; EOG6RZB46; -.
DR   UniPathway; UPA00618; UER00672.
DR   PRO; PR:Q8FWK8; -.
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; Transferase.
FT   CHAIN         1    498       Glycerol kinase.
FT                                /FTId=PRO_0000059441.
FT   NP_BIND      12     14       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   NP_BIND     411    415       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   REGION       82     83       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   REGION      243    244       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING      12     12       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING      16     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     134    134       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING     265    265       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     308    308       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     312    312       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
SQ   SEQUENCE   498 AA;  54795 MW;  B356F6A4418B51D3 CRC64;
     MSGYILAIDQ GTTSTRSMLF DRNMRVVGLG QQEFTQHFPS SGWVEHDAEE IWKSVQSTIR
     IALAQAGISA ADVAAIGITN QRETTVVWDR ISGKPVHRAI VWQDRRTAQF CDELKRRNLE
     PLFTEKTGLL LDPYFSGTKL AWLLNHVPGL RERAQKGQVC FGTIDSWLIY KLTGGKAHVT
     DATNASRTLI YHIGENRWDD ELLDILGIPA AMLPEVKDCA ADFGMTDPAL FGVSIPILGV
     AGDQQTAVIG NACFEPGMMK STYGTGCFAL LNTGTDRVTS SNRLLTTIAY RLDGVTTYAL
     EGSIFIAGAA VQWLRDEMGF ISVVSEVSAL AEKADPNQRI YLVPAFTGLG APYWDAEARG
     AIFGLTRGTG RAEFARAALE SVAYQTFDLL EAMQGDWKGA TNHTVLRVDG GMVASDWTMQ
     RLADILNAPV DRPVFLETTV LGAAWLAASR AGIWPDRKGF SERWQRDCRF EPAMPEKERE
     SAIAGWRDSV SRCLTRPQ
//
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