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Database: UniProt
Entry: A1TGD7
LinkDB: A1TGD7
Original site: A1TGD7 
ID   GLPK_MYCVP              Reviewed;         505 AA.
AC   A1TGD7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   19-FEB-2014, entry version 53.
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=Mvan_5467;
OS   Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3-
CC       phosphate.
CC   -!- ENZYME REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP)
CC       (By similarity).
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
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DR   EMBL; CP000511; ABM16237.1; -; Genomic_DNA.
DR   RefSeq; YP_956243.1; NC_008726.1.
DR   ProteinModelPortal; A1TGD7; -.
DR   SMR; A1TGD7; 2-505.
DR   STRING; 350058.Mvan_5467; -.
DR   EnsemblBacteria; ABM16237; ABM16237; Mvan_5467.
DR   GeneID; 4645206; -.
DR   KEGG; mva:Mvan_5467; -.
DR   PATRIC; 18189353; VBIMycVan31953_5569.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; AMEGSVF; -.
DR   OrthoDB; EOG6RZB46; -.
DR   ProtClustDB; PRK00047; -.
DR   BioCyc; MVAN350058:GIWR-5518-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; Transferase.
FT   CHAIN         1    505       Glycerol kinase.
FT                                /FTId=PRO_1000020749.
FT   NP_BIND      12     14       ATP (By similarity).
FT   NP_BIND     416    420       ATP (By similarity).
FT   REGION       82     83       Substrate binding (By similarity).
FT   REGION      249    250       Substrate binding (By similarity).
FT   BINDING      12     12       Substrate (By similarity).
FT   BINDING      16     16       ATP (By similarity).
FT   BINDING     134    134       Substrate (By similarity).
FT   BINDING     271    271       ATP (By similarity).
FT   BINDING     315    315       ATP; via carbonyl oxygen (By similarity).
FT   BINDING     319    319       ATP; via amide nitrogen (By similarity).
FT   BINDING     334    334       ATP (By similarity).
SQ   SEQUENCE   505 AA;  54920 MW;  9F313CD8F573FFFE CRC64;
     MADFVAAIDQ GTTSTRCMIF DHDGAEVGRH QLEHEQILPR AGWVEHNPVE IWERTGSVLA
     TALNKTKLST SDLVALGITN QRETSLVWNR HTGRPYYNAI VWQDTRTDRI ASALDRDGRG
     DVIRQKAGLP PATYFSGGKL QWLLENVDGL RADAEKGDAL FGTTDTWVLW NLTGGHRGGV
     HVTDVTNASR TMLMNLETLD WDDELLGFFD IPRQMLPEIR PSSSPEPHGV TVDWGPADGE
     IPVTGILGDQ QAAMVGQVCL DAGEAKNTYG TGNFLLLNTG ENIVRSKNGL LTTVCYQFGD
     AKPVYALEGS IAVTGSAVQW LRDQLGIISG AAQSESLARQ VEDNGGVYFV PAFSGLFAPY
     WRSDARGAIV GLSRFNTNAH VARATLEAIC YQSRDVVDAM AADSGVHLEV LKVDGGITAN
     DLCMQIQADV LGVDVVRPVV AETTALGAAY AAGLAVGFWD GADDLRANWQ EDKRWSPTWS
     DDQRAAGYAG WRKAVQRTMD WVDVD
//
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