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Database: UniProt
Entry: A4T5Y1
LinkDB: A4T5Y1
Original site: A4T5Y1 
ID   GLPK_MYCGI              Reviewed;         505 AA.
AC   A4T5Y1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   26-NOV-2014, entry version 60.
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=Mflv_1327;
OS   Mycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens
OS   (strain ATCC 700033 / PYR-GCK)).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-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}.
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DR   EMBL; CP000656; ABP43809.1; -; Genomic_DNA.
DR   RefSeq; YP_001132597.1; NC_009338.1.
DR   ProteinModelPortal; A4T5Y1; -.
DR   SMR; A4T5Y1; 2-503.
DR   STRING; 350054.Mflv_1327; -.
DR   EnsemblBacteria; ABP43809; ABP43809; Mflv_1327.
DR   GeneID; 4972653; -.
DR   KEGG; mgi:Mflv_1327; -.
DR   PATRIC; 18030696; VBIMycGil17082_1355.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; HSSKITE; -.
DR   OrthoDB; EOG6RZB46; -.
DR   BioCyc; MGIL350054:GHK8-1337-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_1000077422.
FT   NP_BIND      12     14       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   NP_BIND     416    420       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   REGION       82     83       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   REGION      249    250       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING      12     12       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING      16     16       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     134    134       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING     271    271       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     315    315       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     319    319       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     334    334       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
SQ   SEQUENCE   505 AA;  54768 MW;  906FB1A394DD126A CRC64;
     MADFVAAIDQ GTTSTRCMIF DHDGAEVGRH QLEHEQILPK AGWVEHNPVE IWERTGSVLA
     TALNATKLAT TDLAALGITN QRETSLVWNR HTGRPYYNAI VWQDTRTDRI ASALDRDGRG
     DVIRRKAGLP PATYFSGGKL QWLLENVDGL RADAANGDAL FGTTDTWVLW NLTGGHRGGV
     HVTDVTNASR TMLMNLETLD WDDELLGFFD IPRQMLPEIR PSSSPQPYGV TVETGPADGE
     IPITGILGDQ QAAMVGQVCL DVGEAKNTYG TGNFLLLNTG EKIVRSDNGL LTTVCYQFGD
     SKPVYALEGS IAVTGSAVQW LRDQLGIISG ASQSESLARQ VDDNGGVYFV PAFSGLFAPY
     WRSDARGAIV GLSRFNTNAH VARATLEAIC YQSRDVVDAM AADSGVPLEV LKVDGGITAN
     DLCMQIQADV LGVDVVKPVV AETTALGAAY AAGLAVGFWE GADDLRANWQ EGRRWSPQWS
     DEQRAEGYAG WQKAVHRTLD WVDVE
//
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