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Database: UniProt
Entry: Q92BH6
LinkDB: Q92BH6
Original site: Q92BH6 
ID   GLPK_LISIN              Reviewed;         497 AA.
AC   Q92BH6;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   19-FEB-2014, entry version 73.
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=lin1573;
OS   Listeria innocua serovar 6a (strain CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA   Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA   Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA   Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA   Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA   Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL596169; CAC96804.1; -; Genomic_DNA.
DR   PIR; AD1629; AD1629.
DR   RefSeq; NP_470909.1; NC_003212.1.
DR   ProteinModelPortal; Q92BH6; -.
DR   SMR; Q92BH6; 5-490.
DR   STRING; 272626.lin1573; -.
DR   EnsemblBacteria; CAC96804; CAC96804; CAC96804.
DR   GeneID; 1130190; -.
DR   KEGG; lin:lin1573; -.
DR   PATRIC; 20299883; VBILisInn102668_1608.
DR   GenoList; LIN1573; -.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; ALYGQLC; -.
DR   OrthoDB; EOG6RZB46; -.
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; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glycerol metabolism; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1    497       Glycerol kinase.
FT                                /FTId=PRO_0000059463.
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   497 AA;  55436 MW;  D4126042AD2F6F74 CRC64;
     MEKKYILALD QGTTSSRAMI IDEEGEVIGV AQEEFDQIFP KPGWVEHSAN EIWASILAVI
     AGVLLKTNIS SKEIAGIGIT NQRETTVIWD KESGNPIYNA IVWQSRQTED ICKQLRKDGY
     EDTIRSKTGL LIDPYFAGTK ARWILDHVDG AQERAEKGEL LFGTIDTWLV WKLTGGRAHI
     TDYSNASRTL LYNIYDLEWD DELLKMLNIP RAMLPEVRPS SEVYADTVPY HFFGEEVPVA
     GIAGDQQAAL FGQGCFEKGM AKNTYGTGCF LLMNTGEKAV RSENGLLTTL AWGLDGKVEY
     ALEGSIFVAG SAIQWLRDGL RMVRQSSDSE NYASRIESSD GVYVVPAFVG LGAPYWDSDV
     RGAVFGLTRG TEKEQFIRAT LESLAYQTRD VLYAMEQDSG ISLKTLRVDG GASANNFLMQ
     FQSDILGVPV ERPENKETTV LGAAFLAGLA VGVWKDKNEI KKHWKLDKRF EVEMKDDQRE
     DLYEGWHKAV KAAQAFK
//
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