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Database: UniProt
Entry: Q99YI7
LinkDB: Q99YI7
Original site: Q99YI7 
ID   GLPK_STRP1              Reviewed;         508 AA.
AC   Q99YI7; Q48XC6;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   14-MAY-2014, entry version 85.
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=SPy_1684, M5005_Spy1381;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J.,
RA   Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J.,
RA   Hoe N.P., Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of
RT   serotype M1 group A Streptococcus involved multiple horizontal gene
RT   transfer events.";
RL   J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34440.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51999.1; -; Genomic_DNA.
DR   RefSeq; NP_269719.1; NC_002737.1.
DR   RefSeq; YP_282744.1; NC_007297.1.
DR   ProteinModelPortal; Q99YI7; -.
DR   SMR; Q99YI7; 6-491.
DR   STRING; 160490.SPy_1684; -.
DR   EnsemblBacteria; AAK34440; AAK34440; SPy_1684.
DR   EnsemblBacteria; AAZ51999; AAZ51999; M5005_Spy1381.
DR   GeneID; 3571496; -.
DR   GeneID; 901930; -.
DR   KEGG; spy:SPy_1684; -.
DR   KEGG; spz:M5005_Spy_1381; -.
DR   PATRIC; 19716826; VBIStrPyo79812_1465.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; MAKYVMA; -.
DR   OrthoDB; EOG6RZB46; -.
DR   BioCyc; SPYO160490:GJ81-1391-MONOMER; -.
DR   BioCyc; SPYO293653:GHFC-1452-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; Phosphoprotein; Transferase.
FT   CHAIN         1    508       Glycerol kinase.
FT                                /FTId=PRO_0000059507.
FT   NP_BIND      14     16       ATP (By similarity).
FT   NP_BIND     412    416       ATP (By similarity).
FT   REGION       84     85       Substrate binding (By similarity).
FT   REGION      246    247       Substrate binding (By similarity).
FT   BINDING      14     14       Substrate (By similarity).
FT   BINDING      18     18       ATP (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     268    268       ATP (By similarity).
FT   BINDING     311    311       ATP; via carbonyl oxygen (By similarity).
FT   BINDING     315    315       ATP; via amide nitrogen (By similarity).
FT   BINDING     330    330       ATP (By similarity).
FT   MOD_RES     232    232       Phosphohistidine; by HPr (By similarity).
SQ   SEQUENCE   508 AA;  56053 MW;  8DCF3FFA86252114 CRC64;
     MSQEKYIMAI DQGTTSSRAI IFNQKGEKVS SSQKEFPQIF PHAGWVEHNA NQIWNSVQSV
     IAGAFIESSI KPSQIEAIGI TNQRETTVVW DKKTGVPIYN AIVWQSRQTA PIAEQLKQDG
     HTKMIHEKTG LVIDAYFSAT KIRWILDHVP GAQERAEKGE LLFGTIDTWL VWKLTDGAVH
     VTDYSNAART MLYNIKDLTW DDEILELLNI PKDMLPEVKS NSEIYGKTAA FHFYGGEVPI
     SGMAGDQQAA LFGQLAFEPG MVKNTYGTGS FIIMNTGDEM QLSSNNLLTT IGYGINGKVH
     YALEGSIFIA GSAIQWLRDG LKMIETSPES EQFALASTSD DEVYVVPAFT GLGAPYWDSN
     ARGSVFGLTR GTSKEDFVKA TLQSIAYQVR DVIDTMQVDS GIDIQQLRVD GGAAMNNMLM
     QFQADILGID IARAKNLETT ALGAAFLAGL AVGYWEDMDA LKELNATGQL FKASMNESRK
     EKLYKGWKRA VKATQVFTQE EDADDDAK
//
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