ID   Q03DS7_PEDPA            Unreviewed;       605 AA.
AC   Q03DS7;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=Alpha-glycerophosphate oxidase {ECO:0000256|ARBA:ARBA00021658};
DE            EC=1.1.3.21 {ECO:0000256|ARBA:ARBA00013104};
DE   AltName: Full=Glycerol-3-phosphate oxidase {ECO:0000256|ARBA:ARBA00032349};
GN   OrderedLocusNames=PEPE_1624 {ECO:0000313|EMBL:ABJ68645.1};
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197 {ECO:0000313|EMBL:ABJ68645.1, ECO:0000313|Proteomes:UP000000773};
RN   [1] {ECO:0000313|EMBL:ABJ68645.1, ECO:0000313|Proteomes:UP000000773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w
RC   {ECO:0000313|Proteomes:UP000000773};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sn-glycerol 3-phosphate + O2 = dihydroxyacetone phosphate +
CC         H2O2; Xref=Rhea:RHEA:18369, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642; EC=1.1.3.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00049503};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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DR   EMBL; CP000422; ABJ68645.1; -; Genomic_DNA.
DR   RefSeq; WP_002832952.1; NC_008525.1.
DR   AlphaFoldDB; Q03DS7; -.
DR   SMR; Q03DS7; -.
DR   STRING; 278197.PEPE_1624; -.
DR   GeneID; 33061787; -.
DR   KEGG; ppe:PEPE_1624; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000000773; Chromosome.
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:0046168; P:glycerol-3-phosphate catabolic process; IEA:TreeGrafter.
DR   Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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   NCBIfam; NF033461; glycerol3P_ox_1; 1.
DR   PANTHER; PTHR11985:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABJ68645.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000773}.
FT   DOMAIN          23..353
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          463..585
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   605 AA;  67065 MW;  A9BD955FF6DFBE0B CRC64;
     MSFSLISRKQ DIERLKNETL DLLTIGGGIT GAGVAIQASA MGMNNALIEM QDFAEGTSSR
     STKLVHGGIR YLKNFDVEVV SDTVKERAVV QGIAPHIPRP DPMLLPIYDE PGSTFDMFSV
     KIAMNLYDQL AGVTDPKYTN YTISKDEVLQ REPQLNPEGL LGGGVYLDFR NNDARLVIEN
     IKKAHENGGL MVSHIKAQHI LHDENGRVNG VNVKDLLTGE EFDIHAKLVI NTTGPWSDFI
     REMDDKEEVV PQMRPTKGVH LVVDRSRLNV PQPTYFDSGK QDGRMIFAIP REGKTYFGTT
     DTDYKGDFLH PRVEQEDVDY LLSIINKHYP EAKITIDDIE ASWAGLRPLI SSNGSSDYNG
     GNSGKITSDS FDEVIDIVNK YENKEADRVD VEDVLNNLES TLSEKNPSAV SRGSALDVAN
     DGLITLAGGK ITDYRKMAAG AIALITKVLK EDFNETFNEI DSKHLQVSGG DIDPNNVDAT
     LSFFAKQGIE SGLSKAEAEQ IANLFGSNAA RVFSQIGKIE AAPGLTLAET ISLHYSMNEE
     MTLTPVDYLL RRTNHLLFHH DTIDDVKKGV INEMARYFEW SDEEREAQAK KLQETIDEAS
     LTYLK
//