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Database: UniProt
Entry: B4TPU7
LinkDB: B4TPU7
Original site: B4TPU7 
ID   GLPK_SALSV              Reviewed;         502 AA.
AC   B4TPU7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   01-OCT-2014, entry version 40.
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=SeSA_A4302;
OS   Salmonella schwarzengrund (strain CVM19633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=439843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM19633;
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(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: Activity of this regulatory enzyme is affected
CC       by several metabolites. Allosterically and non-competitively
CC       inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated
CC       phosphocarrier protein EIIA-Glc (III-Glc), an integral component
CC       of the bacterial phosphotransferase (PTS) system.
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   -!- SUBUNIT: Homotetramer and homodimer (in equilibrium). Heterodimer
CC       with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc
CC       dimer. The zinc ion is important for dimerization.
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; CP001127; ACF90443.1; -; Genomic_DNA.
DR   RefSeq; YP_002117007.1; NC_011094.1.
DR   ProteinModelPortal; B4TPU7; -.
DR   SMR; B4TPU7; 3-501.
DR   STRING; 439843.SeSA_A4302; -.
DR   EnsemblBacteria; ACF90443; ACF90443; SeSA_A4302.
DR   PATRIC; 32377167; VBISalEnt87589_4275.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   OMA; HFFGVEV; -.
DR   OrthoDB; EOG6RZB46; -.
DR   BioCyc; SENT439843:GHHR-1874-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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Allosteric enzyme; ATP-binding; Complete proteome;
KW   Glycerol metabolism; Kinase; Metal-binding; Nucleotide-binding;
KW   Transferase; Zinc.
FT   CHAIN         1    502       Glycerol kinase.
FT                                /FTId=PRO_1000098761.
FT   NP_BIND      14     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   NP_BIND     412    416       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   REGION       84     85       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   REGION      234    236       Allosteric FBP inhibitor binding.
FT   REGION      246    247       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   METAL       479    479       Zinc; shared with EIIA-Glc.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING      14     14       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING      18     18       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING     268    268       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     311    311       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     315    315       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     330    330       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
SQ   SEQUENCE   502 AA;  56052 MW;  A780A522CA16C1B4 CRC64;
     MTEKKYIVAL DQGTTSSRAV VMDHDANIVS VSQREFEQIY PKPGWVEHDP MEIWASQSST
     LVEVLAKADI SSDQIAAIGI TNQRETAIVW ERETGKPIYN AIVWQCRRTA DICEQLKRDG
     LEDYIRDNTG LVVDPYFSGT KVKWILDHVE GSRERAKRGE LLFGTVDTWL IWKMTQGRVH
     VTDYTNASRT MLFNIHDLDW DDKMLDVLDI PRAMLPQVRK SSEVYGQTNI GGKGGTRIPI
     AGIAGDQQAA LFGQLCVKEG MAKNTYGTGC FMLMNTGEKA VKSENGLLTT IACGPSGEVN
     YALEGAVFMA GASIQWLRDE MKLISDAFDS EYFATKVKDT NGVYVVPAFT GLGAPYWDPY
     ARGAIFGLTR GVNSNHIIRA TLESIAYQTR DVLEAMQADS GIRLHALRVD GGAVANNFLM
     QFQSDILGTR VERPEVREVT ALGAAYLAGL AVGYWQNLDE LQEKAVIERE FRPGIETTER
     NYRYSGWKKA VKRAMAWEEH DK
//
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