(data stored in ACNUC7421 zone)

SWISSPROT: GLPK_SHESH

ID   GLPK_SHESH              Reviewed;         495 AA.
AC   A8FQ89;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 62.
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=Ssed_0399;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000821; ABV35012.1; -; Genomic_DNA.
DR   RefSeq; WP_012140749.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ89; -.
DR   SMR; A8FQ89; -.
DR   STRING; 425104.Ssed_0399; -.
DR   EnsemblBacteria; ABV35012; ABV35012; Ssed_0399.
DR   KEGG; sse:Ssed_0399; -.
DR   eggNOG; ENOG4108JQ0; Bacteria.
DR   eggNOG; COG0554; LUCA.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; WQDTRTQ; -.
DR   OrthoDB; POG091H02FA; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
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; A8FQ89.
DR   SWISS-2DPAGE; A8FQ89.
KW   ATP-binding; Complete proteome; Glycerol metabolism; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    495       Glycerol kinase.
FT                                /FTId=PRO_1000077431.
FT   NP_BIND      13     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   NP_BIND     410    414       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   REGION       83     84       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   REGION      244    245       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING      13     13       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING      17     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     135    135       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING     266    266       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     309    309       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     313    313       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     328    328       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
SQ   SEQUENCE   495 AA;  54105 MW;  E69A88331F74860D CRC64;
     MAKKYVVALD QGTTSSRAII FDHDANIVSV SQREFPQIYP QAGWVEHDPM EIWASQSSTL
     IELLARSGIH GSEVAAIGIT NQRETTVIWD KLTGKPVYNA IVWQCRRSSH ICDELKAQGL
     EDYVRETTGL LLDPYFSGTK IKWILDNVAG VRERAEKGEL LFGTIDTWLV WKLTEGKVHV
     TDPTNASRTL LFNIHTQQWD SKLLEALNIP ESLLPEVKPS CAVYGKTRIA GEGGEISIAG
     IAGDQQSALF GQLCIDEGMA KNTYGTGCFL LMNTGKQAVK STHGLLTTVA IGADCEVNYA
     LEGAVFMGGA TIQWLRDELG LIRDAQDTEY FASKVEDTNG VYLVPAFVGL GAPYWDPNAR
     GALVGLTRGS NRNHIIRAAL EAIAYQSRDL LDAMAKDSGV MLKQLKVDGG AVSNDFLMQF
     QADITNVEVQ RPAITETTAM GAAFLAGLAV GFWSSTSELK HKADIERTFI PSISAEKCDE
     LYCGWNRAVT QTIKS
//

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