ID   B0CJ57_BRUSI            Unreviewed;       503 AA.
AC   B0CJ57;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   Name=glpD {ECO:0000313|EMBL:ABY37301.1};
GN   OrderedLocusNames=BSUIS_A0201 {ECO:0000313|EMBL:ABY37301.1};
OS   Brucella suis (strain ATCC 23445 / NCTC 10510).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=470137 {ECO:0000313|EMBL:ABY37301.1, ECO:0000313|Proteomes:UP000008545};
RN   [1] {ECO:0000313|EMBL:ABY37301.1, ECO:0000313|Proteomes:UP000008545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23445 / NCTC 10510 {ECO:0000313|Proteomes:UP000008545};
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361217};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU361217};
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; CP000911; ABY37301.1; -; Genomic_DNA.
DR   RefSeq; WP_006072021.1; NC_010169.1.
DR   AlphaFoldDB; B0CJ57; -.
DR   KEGG; bmt:BSUIS_A0201; -.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   Proteomes; UP000008545; Chromosome I.
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:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 6.10.250.1890; -; 1.
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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217}.
FT   DOMAIN          8..336
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          388..494
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   503 AA;  56344 MW;  8FF44671A162D5DA CRC64;
     MVQEKQFDIF IIGGGINGCG IARDAVGRGF TVGLAEMNDL ANGTSSRATK LIHGGLRYLE
     HYEFRLVREA LMEREVLWAN APHIIHPMRF VLPYHKGGLR PAWLLRLGLF LYDHLGGRKK
     LPATRTLNMR TDKAGEPLKP LFTKAFEYSD CWVDDARFVA LTARDAADRG AKIATRTSVV
     AASRDGQGWT ITLEDTGTGR RENVHARLLV NAAGPWADKV LQGVEGDRQL HNIRLVQGSH
     IVVRRKFSDP RAYFFQNNDG RIIFAIPYED DFTLIGTTDQ DYKGDPAKVA ITDSETDYLC
     QAASEYFREP VRREDIVWTY SGVRPLYDDG ASKAQEATRD YVLKEDAPDG LAPLINVFGG
     KLTTARKLAE HMLQKIEHRL GRKGAPWTHA APLPGGDFED VAFETELKKL EAAYPFLDAR
     HARRLFRLYG TRAYKLLGQA SSLGDLGRHF GSDLYEAEVR YLVENEWARS AEDILWRRTK
     LGLRLTAAEV AAVQGFVEPA IAA
//