ID GLPO_STRP8 Reviewed; 612 AA. AC Q8NZX0; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 40. DE RecName: Full=Alpha-glycerophosphate oxidase; DE EC=1.1.3.21; DE AltName: Full=Glycerol-3-phosphate oxidase; GN Name=glpO; Synonyms=glpA; OrderedLocusNames=spyM18_1695; OS Streptococcus pyogenes serotype M18. OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=301451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGAS8232 / Serotype M18; RX MEDLINE=21927593; PubMed=11917108; DOI=10.1073/pnas.062526099; RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., RA Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., RA Kapur V., Daly J.A., Veasy L.G., Musser J.M.; RT "Genome sequence and comparative microarray analysis of serotype M18 RT group A Streptococcus strains associated with acute rheumatic fever RT outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002). CC -!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + O(2) = glycerone CC phosphate + H(2)O(2). CC -!- COFACTOR: FAD (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate CC dehydrogenase family. CC -!- CAUTION: As S.pyogenes is unable to produce acid from glycerol, CC the significance and/or function of the glpO gene in this organism CC is at present unknown. 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; AE009949; AAL98230.1; -; Genomic_DNA. DR RefSeq; NP_607731.1; -. DR GeneID; 994309; -. DR GenomeReviews; AE009949_GR; spyM18_1695. DR KEGG; spm:spyM18_1695; -. DR HOGENOM; Q8NZX0; -. DR OMA; Q8NZX0; KDIESSW. DR BioCyc; SPYO186103:SPYM18_1695-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:0004369; F:glycerol-3-phosphate oxidase activity; IEA:EC. 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; FALSE_NEG. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; KW Oxidoreductase. FT CHAIN 1 612 Alpha-glycerophosphate oxidase. FT /FTId=PRO_0000126113. FT NP_BIND 21 49 FAD (Potential). SQ SEQUENCE 612 AA; 67691 MW; 978A9017FE61779C CRC64; MEFSRETRRL ALQKMQERDL DLLIIGGGIT GAGVALQAAA SGLDTGLIEM QDFAQGTSSR STKLVHGGLR YLKQFDVEVV SDTVSERAVV QQIAPHIPKP DPMLLPVYDE PGSTFSMFRL KVAMDLYDLL AGVSNMPAAN KVLTKEEVLK REPDLKQEGL LGGGVYLDFR NNDARLVIEN IKRANRDGAL IASHVKAEDF LLDDNSKIIG VKARDLLSDQ EIIIKAKLVI NTTGPWSDEI RQFSHKGQPI HQMRPTKGVH LVVDRQKLPV SQPVYVDTGL NDGRMVFVLP REEKTYFGTT DTDYTGDLEH PQVTQEDVDY LLGVVNNRFP NANVTIDDIE SSWAGLRPLL SGNSASDYNG GNSGKVSDDS FDHLVDTVKA YINHEDSREA VEKAIKQVET STSEKELDPS AVSRGSSFDR DENGLFTLAG GKITDYRKMA EGALTGIIQI LKEEFGKSFK LINSKTYPVS GGEINPANVD SEIEAYAQLG TLSGLSMDDA RYLANLYGSN APKVFALTRQ LTAAEGLSLA ETLSLHYAMD YEMALKPTDY FLRRTNHLLF MRDSLDALID PVIKEMAKHF EWSDQERVAQ EDDLRRVIAD NDLSALKGQQ EG //