(data stored in ACNUC7421 zone)

SWISSPROT: GLPK_POLNA

ID   GLPK_POLNA              Reviewed;         497 AA.
AC   A1VJ23;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   11-DEC-2019, entry version 79.
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}; OrderedLocusNames=Pnap_0328;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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:
CC       Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC         Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=2.7.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00186};
CC   -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP).
CC       {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       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}.
DR   EMBL; CP000529; ABM35651.1; -; Genomic_DNA.
DR   RefSeq; WP_011799758.1; NC_008781.1.
DR   SMR; A1VJ23; -.
DR   STRING; 365044.Pnap_0328; -.
DR   EnsemblBacteria; ABM35651; ABM35651; Pnap_0328.
DR   KEGG; pna:Pnap_0328; -.
DR   eggNOG; ENOG4108JQ0; Bacteria.
DR   eggNOG; COG0554; LUCA.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; FMLMNIG; -.
DR   OrthoDB; 233605at2; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000000644; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR   HAMAP; MF_00186; Glycerol_kin; 1.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
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   PIRSF; PIRSF000538; GlpK; 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;
DR   PRODOM; A1VJ23.
DR   SWISS-2DPAGE; A1VJ23.
KW   ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..497
FT                   /note="Glycerol kinase"
FT                   /id="PRO_1000098748"
FT   NP_BIND         11..13
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   NP_BIND         412..416
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   REGION          81..82
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   REGION          242..243
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         11
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         15
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         133
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         264
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         307
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         311
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   497 AA;  53154 MW;  8CFC3A7D9070E617 CRC64;
     MAYLLALDQG TSSSRSIVFD EEGRVVALAQ RELPQIYPRP GWVEHDPMEI WRGQLATARQ
     ALASVGLAAW DIRAMGITNQ RETTVLWNRR TGQPVHHAIV WQDRRAESTC AQLREQGHEA
     LIQAKTGLLI DAYFSGTKLK WLLDNVAGVR AQAERGELAF GTIDSWLIWQ LTGGTVHATD
     VSNASRTMLF NVRTNQWDAE LLDLLGIPAS LMPEVKPSSA HYGEVRPELL GHAIPIGGVA
     GDQQSALFGQ ACFRAGMAKN TYGTGCFLLM HTGAQFQASK NGLLTTSAAQ TTAQTEFALE
     GSVFVGGAVV QWLRDGLHAI QGSAEVEALA QSVPDSGGVM MVPAFTGLGA PYWKPEARGT
     ITGLTRGTTM AHIARAALES IAYQSAALLL AMSRDAVAAG AAPLAELRVD GGASSNDLLM
     QFQADLLGIP VIRPAVTETT ALGAAWLAGL SSGVYGSTDE LSSLWRAERT FLPTLSTGRA
     AELMAQWEHA VRQTVLA
//

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