ID GLPK_CLOP1 Reviewed; 500 AA. AC Q0TMA0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 26. 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=CPF_2876; OS Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=195103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and CC metabolism. CC -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3- CC phosphate. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000246; ABG82764.1; -; Genomic_DNA. DR RefSeq; YP_697240.1; -. DR SMR; Q0TMA0; 3-496. DR GeneID; 4200961; -. DR GenomeReviews; CP000246_GR; CPF_2876. DR KEGG; cpf:CPF_2876; -. DR TIGR; CPF_2876; -. DR HOGENOM; Q0TMA0; -. DR OMA; Q0TMA0; IAQREFT. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004370; F:glycerol kinase activity; IEA:HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:HAMAP. DR HAMAP; MF_00186; -; 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 PANTHER; PTHR10196; FGGY_kin; 1. DR PANTHER; PTHR10196:SF9; Glycerol_kin; 1. 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 1 500 Glycerol kinase. FT /FTId=PRO_1000020722. FT NP_BIND 411 415 ATP (By similarity). FT BINDING 12 12 Substrate (By similarity). FT BINDING 16 16 ATP (By similarity). FT BINDING 82 82 Substrate (By similarity). FT BINDING 135 135 Substrate (By similarity). FT BINDING 245 245 Substrate (By similarity). FT BINDING 267 267 ATP (By similarity). FT BINDING 310 310 ATP; via carbonyl oxygen (By similarity). SQ SEQUENCE 500 AA; 56003 MW; 75EF0EF894CACF57 CRC64; MKKYIVALDQ GTTSSRAIIF DKEQNIIGVS QKEFNQIYPR EGWVEHDPME IWATQYSVLQ EVMAKCNITQ ENIAAIGITN QRETTIVWDK NTGVPIYNAI VWQCRRTADI CDELKERDGL VDYIRENTGL VLDAYFSGTK IKWILDNVEG AREKAEKGEL LFGTVDSWLV WKLTNGKVHV TDYTNASRTM IFNIKNLEWD ERMLKELDIP RSMLPEVKNS SEIYGYANLG AKGGIRVPIA GIAGDQQAAL FGQAAFNKGD VKNTYGTGCF LLMNTGEELV KSKSGLLTTI AIGLHGKVQY ALEGSVFVGG AVIQWLRDEL RIISDSSDTE YFATKVEDNG GVYVVPAFVG LGAPYWDMYA RGTIVGLTRG TNRNHIIRAA LESIAYQTRD VLEAMINDVG YDINCIKVDG GASRNNFLMQ FQSDLVGKKV IKPIITETTA LGAAYLAGLA VGYWSDKEEI AKLWFASEEF EPTISEERRN KYHKKWKKAV ERSKGWALED //