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Database: UniProt
Entry: A0A0R1QFD5_9LACO
LinkDB: A0A0R1QFD5_9LACO
Original site: A0A0R1QFD5_9LACO 
ID   A0A0R1QFD5_9LACO        Unreviewed;       567 AA.
AC   A0A0R1QFD5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ORFNames=FD29_GL001073 {ECO:0000313|EMBL:KRL43249.1};
OS   Companilactobacillus mindensis DSM 14500.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Companilactobacillus.
OX   NCBI_TaxID=1423770 {ECO:0000313|EMBL:KRL43249.1, ECO:0000313|Proteomes:UP000050872};
RN   [1] {ECO:0000313|EMBL:KRL43249.1, ECO:0000313|Proteomes:UP000050872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14500 {ECO:0000313|EMBL:KRL43249.1,
RC   ECO:0000313|Proteomes:UP000050872};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + sn-glycerol 3-phosphate = 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:ARBA00000275};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRL43249.1}.
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DR   EMBL; AZEZ01000091; KRL43249.1; -; Genomic_DNA.
DR   RefSeq; WP_057888456.1; NZ_AZEZ01000091.1.
DR   AlphaFoldDB; A0A0R1QFD5; -.
DR   STRING; 1423770.FD29_GL001073; -.
DR   PATRIC; fig|1423770.3.peg.1106; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000050872; Unassembled WGS sequence.
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; 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; 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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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.
DR   PROSITE; PS00978; FAD_G3PDH_2; 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}.
FT   DOMAIN          22..350
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          409..535
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   567 AA;  63965 MW;  4B0336492E7291BB CRC64;
     MTEFSDKTRS KNLQAMQDQV LDLLVIGGGI TGSGIALDAQ TRNIQTGLIE MRDFASGTSS
     RSTKLVHGGL RYLKQAAVKE VHEVGSERAI VYNNAPQITT PLKMMLPFYE DGTFGPFTTA
     IGLDVYDRLA QVKPAERKYM LNAHDALERE PYIKGENLKG AGVYVEYRTD DARLTLEVLK
     KAHEEGALIA NYVKATGLLY DSSNKVCGVT FNDSVTGKIG EIHAKKVINA SGPWVDEIRD
     IDHSNKDKHL HLTKGVHLVI DQEKFPISNS IYFDTPFHDN RMMFAIPREG KTYVGTTDTT
     WTKDPAEPNI TATDVTYILS AVNEMFDLPQ YLTPKDVESG WSGVRPLIQE EGKAPSEISR
     KDEIFQSDSG LLSIAGGKLT GYRKMAEKIV DRVSQQLAFE TNYEFQPART KDLPLSGGDV
     GGDSGWMEFY DKMVHEGIIN YVLEREDSEK LVQRYGSNVE DVFKLLPDTK TKARLPRVDW
     AMLTYGLENE MVEHPIDYLL RRSSQMLFDI THMKTIKTPV IEYMAKFYDW DDETKQKLTD
     EVNEKLALTD LSDIKKQYAD FVLKKNN
//
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