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Database: UniProt
Entry: Q1QR91
LinkDB: Q1QR91
Original site: Q1QR91 
ID   GLPK_NITHX              Reviewed;         503 AA.
AC   Q1QR91;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   26-NOV-2014, entry version 61.
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=Nham_0360;
OS   Nitrobacter hamburgensis (strain X14 / DSM 10229).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X14 / DSM 10229;
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., Ivanova N., Ward B.,
RA   Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L.,
RA   Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-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. {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; CP000319; ABE61256.1; -; Genomic_DNA.
DR   RefSeq; YP_575716.1; NC_007964.1.
DR   ProteinModelPortal; Q1QR91; -.
DR   SMR; Q1QR91; 5-492.
DR   STRING; 323097.Nham_0360; -.
DR   EnsemblBacteria; ABE61256; ABE61256; Nham_0360.
DR   GeneID; 4030246; -.
DR   KEGG; nha:Nham_0360; -.
DR   PATRIC; 22688099; VBINitHam61822_1087.
DR   eggNOG; COG0554; -.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; RRFAAHM; -.
DR   OrthoDB; EOG6RZB46; -.
DR   BioCyc; NHAM323097:GHP7-366-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; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glycerol metabolism; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    503       Glycerol kinase.
FT                                /FTId=PRO_1000020752.
FT   NP_BIND      12     14       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   NP_BIND     412    416       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   REGION       82     83       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00186}.
FT   REGION      243    244       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     265    265       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     308    308       ATP; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     312    312       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00186}.
FT   BINDING     327    327       ATP. {ECO:0000255|HAMAP-Rule:MF_00186}.
SQ   SEQUENCE   503 AA;  53996 MW;  E41C9C995FC5FCFD CRC64;
     MVTHVLAIDQ GTTSSRAILF RADTSIAAIA QQEFPQHFPA SGWVEHEPED IWTSTVATCR
     EAMNKAGVTP KDIAAIGITN QRETTVVWDR ATGQAMHRAV VWQDRRTADI CARLKAEGHE
     PAISAKTGLI VDPYFSGTKI AWILDSVPGA RARASRGDLL FGTVDCYLLW RLTGGKVHAT
     DATNASRTLL FDIHTGQWDE ELLKILRVPR AMLPEVKDSS AHFGDSVADL FGAPISIRGI
     AGDQQAAVVG QACFAPGMIK STYGTGCFAL LNTGATPVAS KNKLLTTIAY QLNGKRTYAL
     EGSIFVAGSA VQWLRDGLGL IKQASETGPL ADRSDATQSV YLVPAFVGMG APYWNPNVRG
     ALFGLTRNTG PAELAHAALE SVCYQTFDLW AAMRADWPDA AAAHTVLRVD GGMTASDWTM
     QRLADLLDAP VDRPVIQETT ALGAAYLAGL SAGVYPEPSK FADNWRLERR FKPAMSAATR
     TRKLKGWAAA VRGVLASDGG EGR
//
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