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Database: UniProt
Entry: Q99YI8
LinkDB: Q99YI8
Original site: Q99YI8 
ID   GLPO_STRP1              Reviewed;         612 AA.
AC   Q99YI8; Q48XC7;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   10-APR-2019, entry version 106.
DE   RecName: Full=Alpha-glycerophosphate oxidase;
DE            EC=1.1.3.21;
DE   AltName: Full=Glycerol-3-phosphate oxidase;
GN   Name=glpO; OrderedLocusNames=SPy_1683, M5005_Spy1380;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J.,
RA   Yuan X., Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J.,
RA   Hoe N.P., Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of
RT   serotype M1 group A Streptococcus involved multiple horizontal gene
RT   transfer events.";
RL   J. Infect. Dis. 192:771-782(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H2O2; Xref=Rhea:RHEA:18369, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642;
CC         EC=1.1.3.21;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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. {ECO:0000305}.
DR   EMBL; AE004092; AAK34439.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51998.1; -; Genomic_DNA.
DR   RefSeq; NP_269718.1; NC_002737.2.
DR   ProteinModelPortal; Q99YI8; -.
DR   SMR; Q99YI8; -.
DR   PaxDb; Q99YI8; -.
DR   PRIDE; Q99YI8; -.
DR   EnsemblBacteria; AAK34439; AAK34439; SPy_1683.
DR   EnsemblBacteria; AAZ51998; AAZ51998; M5005_Spy1380.
DR   GeneID; 901929; -.
DR   KEGG; spy:SPy_1683; -.
DR   KEGG; spz:M5005_Spy1380; -.
DR   PATRIC; fig|160490.10.peg.1464; -.
DR   eggNOG; ENOG4105C6V; Bacteria.
DR   eggNOG; COG0578; LUCA.
DR   HOGENOM; HOG000004812; -.
DR   KO; K00105; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR   GO; GO:0004369; F:glycerol-3-phosphate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.8.870; -; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
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_0000126110.
FT   NP_BIND      21     49       FAD. {ECO:0000255}.
SQ   SEQUENCE   612 AA;  67640 MW;  C5016720426C4BB4 CRC64;
     MEFSRETRRL ALQKMQERDL DLLIIGGGIT GAGVALQAAA SGLDTGLIEM QDFAQGTSSR
     STKLVHGGLR YLKQFDVEVV SDTVSERAVV QQIAPHIPKP DPMLLPVYDE PGSTFSMFRL
     KVAMDLYDLL AGVSNTPAAN KVLTKEEVLK REPDLKQEGL LGGGVYLDFR NNDARLVIEN
     IKRANRDGAL IASHVKAEDF LLDDNGKIIG VKARDLLSDQ EIIIKAKLVI NTTGPWSDEI
     RQFSHKGQPI HQMRPTKGVH LVVDRQKLPV SQPVYVDTGL NDGRMVFVLP REEKTYFGTT
     DTDYTGDLEH PQVTQEDVDY LLGVVNNRFP NANVTIDDIE SSWAGLRPLL SGNSASDYNG
     GNSGKVSDDS FDHLVDTVKA YINHEDSREA VEKAIKQVET STSEKELDPS AVSRGSSFER
     DENGLFTLAG GKITDYRKMA EGALTGIIQI LKEEFGKSFK LINSKTYPVS GGEINPANVD
     SEIEAYAQLG TLSGLSMDDA RYLANLYGSN APKVFALTRQ LTAAEGLSLA ETLSLHYAMD
     YEMALKPTDY FLRRTNHLLF MRDSLDALID PVINEMAKHF EWSDQERVAQ EDDLRRVIAD
     NDLSALKGHQ EG
//
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