ID GLPD_STAEQ Reviewed; 557 AA. AC Q5HPP0; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 16-JUN-2009, entry version 33. DE RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase; DE EC=1.1.5.3; GN Name=glpD; OrderedLocusNames=SERP0868; OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=176279; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005; RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C., RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., RA Hance I.R., Nelson K.E., Fraser C.M.; RT "Insights on evolution of virulence and resistance from the complete RT genome analysis of an early methicillin-resistant Staphylococcus RT aureus strain and a biofilm-producing methicillin-resistant RT Staphylococcus epidermidis strain."; RL J. Bacteriol. 187:2426-2438(2005). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + a quinone = CC glycerone phosphate + a quinol. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol CC kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate CC (aerobic route): step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate CC dehydrogenase 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; CP000029; AAW54267.1; -; Genomic_DNA. DR RefSeq; YP_188450.1; -. DR GeneID; 3240419; -. DR GenomeReviews; CP000029_GR; SERP0868. DR KEGG; ser:SERP0868; -. DR TIGR; SERP0868; -. DR HOGENOM; Q5HPP0; -. DR OMA; Q5HPP0; DSIRKMD. DR BioCyc; SEPI176279:SERP0868-MON; -. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase activity; IEA:InterPro. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000447; FAD-dep_Gly3P_DH. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR Pfam; PF01266; DAO; 1. DR PRINTS; PR01001; FADG3PDH. DR PROSITE; PS00977; FAD_G3PDH_1; 1. DR PROSITE; PS00978; FAD_G3PDH_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; KW Oxidoreductase. FT CHAIN 1 557 Aerobic glycerol-3-phosphate FT dehydrogenase. FT /FTId=PRO_0000270065. FT NP_BIND 21 49 FAD (Potential). SQ SEQUENCE 557 AA; 62276 MW; 6F6044C656324F7C CRC64; MSLSTLKRDH IKKNLRDTEY DVVIVGGGIT GAGIALDASN RGMKVALVEM QDFAQGTSSR STKLVHGGLR YLKQLQVGVV AETGKERAIV YENGPHVTTP EWMLLPMHKG GTFGKFSTSI GLAMYDRLAG VKKSERKKML SKQETLNKEP LVKRDGLKGG GYYVEYRTDD ARLTIEVMKK AAENGAEILN YTKSEHFTYD SNKKVNGIEV LDMIDGETYA IKAKKVINAS GPWVDEVRSG DYARNNKQLR LTKGVHVVID QSKFPLGQAV YFDTEKDGRM IFAIPREGKA YVGTTDTFYD NEKATPLTTQ EDRDYLINAI NYMFPTVNVK DEDIESTWAG IRPLILEKGK DPSEISRKDE VWEGESGLLT IAGGKLTGYR HMALEIVDLL AKRLKQEYGL KFESCATKNL KISGGDVGGS KNFEHFVEQK VDAAKGFGID EDVARRLASK YGSNVDQLFN IAQTAPYHDS KLPLEIYVEL VYSIQQEMVY KPTDFLVRRS GKLYFNIQDV LDYKNAVIDV MADMLNYSET QKEAYTEEVE VAIDEARTGN DQPATKA //