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Database: UniProt
Entry: Q0VRN6
LinkDB: Q0VRN6
Original site: Q0VRN6 
ID   GLPK_ALCBS              Reviewed;         497 AA.
AC   Q0VRN6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   19-FEB-2014, entry version 59.
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=ABO_0714;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK2 / ATCC 700651 / DSM 11573;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL16162.1; -; Genomic_DNA.
DR   RefSeq; YP_692434.1; NC_008260.1.
DR   ProteinModelPortal; Q0VRN6; -.
DR   SMR; Q0VRN6; 3-490.
DR   STRING; 393595.ABO_0714; -.
DR   EnsemblBacteria; CAL16162; CAL16162; ABO_0714.
DR   GeneID; 4211193; -.
DR   KEGG; abo:ABO_0714; -.
DR   PATRIC; 20839103; VBIAlcBor124741_0751.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; VYGTTRG; -.
DR   OrthoDB; EOG6RZB46; -.
DR   BioCyc; ABOR393595:GHRI-732-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.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glycerol metabolism; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    497       Glycerol kinase.
FT                                /FTId=PRO_1000020695.
FT   NP_BIND      11     13       ATP (By similarity).
FT   NP_BIND     407    411       ATP (By similarity).
FT   REGION       81     82       Substrate binding (By similarity).
FT   REGION      242    243       Substrate binding (By similarity).
FT   BINDING      11     11       Substrate (By similarity).
FT   BINDING      15     15       ATP (By similarity).
FT   BINDING     133    133       Substrate (By similarity).
FT   BINDING     264    264       ATP (By similarity).
FT   BINDING     306    306       ATP; via carbonyl oxygen (By similarity).
FT   BINDING     310    310       ATP; via amide nitrogen (By similarity).
FT   BINDING     325    325       ATP (By similarity).
SQ   SEQUENCE   497 AA;  54056 MW;  B369FC409141A4DA CRC64;
     MPYILSIDQG TTSSRAIVFD ANGHACGQAQ KEFRQYFPED GWVEHDAMEI WNDTLAMCQQ
     ALRNARVEAQ QLVAIGITNQ RETTVLWDRE TGDPLARAIV WQDRRTASTC EALRDQGHEN
     QVRSKTGLLL DPYFSATKLA WLLDNVPNAR QRAEAGELAF GTIDSWLLWQ LTRGKVHATD
     ATNASRTLLF NIHEQCWDEE LLTLFNVPAS VLPDVRDSAA DFGTTCPELL GAAVPVTGIA
     GDQQAALVGQ ACFAPGMVKS TYGTGCFMVM NTGEAVESHN RLLTTVGYRL NGKTTYALEG
     SIFVAGAAIQ WLRDGLHLIR DARETEALAR RVGSAGGVYL VPAFTGLGAP WWDPHARGAL
     MGLTRDTGIA EVVTAGLEAV CYQSRDLLDA MAADCGTRPT TLRVDGGMVV NNWLSQTLSD
     VLGVCVDRPV VTETTALGAA YLAGLGVGLY ASLESIAEQW RCERGFSPAL AEPERQKRYQ
     GWRDAVARVC QTSRGAN
//
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