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Database: UniProt/TrEMBL
Entry: A0A0B4S5T3_9BACI
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Original site: A0A0B4S5T3_9BACI 
ID   A0A0B4S5T3_9BACI        Unreviewed;       553 AA.
AC   A0A0B4S5T3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=QR42_04610 {ECO:0000313|EMBL:AIZ59565.1};
OS   Bacillus sp. WP8.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=756828 {ECO:0000313|EMBL:AIZ59565.1, ECO:0000313|Proteomes:UP000031306};
RN   [1] {ECO:0000313|EMBL:AIZ59565.1, ECO:0000313|Proteomes:UP000031306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP8 {ECO:0000313|EMBL:AIZ59565.1,
RC   ECO:0000313|Proteomes:UP000031306};
RX   PubMed=25614565;
RA   Kang Y., Shen M., Wang H., Zhao Q.;
RT   "Complete Genome Sequence of Bacillus pumilus Strain WP8, an Efficient
RT   Plant Growth-Promoting Rhizobacterium.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000153,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC       ECO:0000256|RuleBase:RU361217}.
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DR   EMBL; CP010075; AIZ59565.1; -; Genomic_DNA.
DR   RefSeq; WP_039177448.1; NZ_CP010075.1.
DR   AlphaFoldDB; A0A0B4S5T3; -.
DR   KEGG; bacw:QR42_04610; -.
DR   HOGENOM; CLU_015740_5_2_9; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000031306; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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; PS00977; FAD_G3PDH_1; 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   ECO:0000256|RuleBase:RU361217};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217}.
FT   DOMAIN          21..376
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          403..531
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   553 AA;  61820 MW;  FC9F4013F04109D5 CRC64;
     MTFSSLEREQ MLQEMTKKPY DVFIIGGGIT GAGTALDAAS RGMRVGLAEM QDFAAGTSSR
     STKLVHGGLR YLKQFEVKMV AEVGKERAIV YENGPHVTTP EWMLLPMHKG GTFGKFSTSI
     GLRVYDFLAG VKHSERRSML SAKETLAKEP LVKKDGLKGG GYYVEYRTDD ARLTIEVMKE
     AVKFGAEAVN YAKVKEFIYD KGKVVGVAIE DVMTKKTYDV YAKKIVNATG PWVDQLRDKD
     HSKEGKHLQH TKGIHLVFDQ SVFPLKQAIY FDTPDKRMVF AIPREGKTYV GTTDTVYKKQ
     LEHPRMTKAD RDYVIQAIQY MFPDLNITEK DVESNWAGLR PLIHEEGKDP SEISRKDEVW
     TSSSGLITIA GGKLTGYRKM AEHIVDLVRD GLKQETGKDY GPCKTKHMPI SGGHVGGSKN
     MAAFVQAKTA EGASVGLTEP IAQKLAEKYG SNVSSVYKRV EQLQGEADKR NIPAYVLAEL
     VYAIEEELAV TPVDFFLRRT GSLLFNINWA KKYAQPVVDY MAERFGWDEA AKQKHQTELD
     QLFHEAVVPL DAE
//
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