ID   C0RGQ2_BRUMB            Unreviewed;       500 AA.
AC   C0RGQ2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=BMEA_A0209 {ECO:0000313|EMBL:ACO00010.1};
OS   Brucella melitensis biotype 2 (strain ATCC 23457).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=546272 {ECO:0000313|EMBL:ACO00010.1, ECO:0000313|Proteomes:UP000001748};
RN   [1] {ECO:0000313|Proteomes:UP000001748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23457 {ECO:0000313|Proteomes:UP000001748};
RA   Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA   Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA   Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA   Han C., Detter J.C., Bruce D., Brettin T.S.;
RT   "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL   Submitted (MAR-2009) 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; CP001488; ACO00010.1; -; Genomic_DNA.
DR   RefSeq; WP_004686639.1; NC_012441.1.
DR   AlphaFoldDB; C0RGQ2; -.
DR   KEGG; bmi:BMEA_A0209; -.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   Proteomes; UP000001748; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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..491
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   500 AA;  55983 MW;  DA5ADF0E51413C17 CRC64;
     MVQEKQFDIF IIGGGINGCG IARDAVGRGF TVGLAEMNDL ASGTSSRATK LIHGGLRYLE
     HYEFRLVREA LMEREVLWAN APHIIHPMRF VLPYHKGGLR PAWLLRLGLF LYDHLGGRKK
     LPATRTLNMR TDKAGEPLKP LFTKAFEYSD CWVDDARFVA LTARDAADRG AKIATRTSVV
     AASRDGQGWT ITLEDTGTGR RENVHARLLV NAAGPWADKV LQSVEGDRQL HNIRLVQGSH
     IVVRRKFSDP RAYFFQNNDG RIIFAIPYED DFTLIGTTDQ DYKGDPAKVA ITDSETDYLC
     QAASEYFREP VRREDIVWTY SGVRPLYDDG ASKAQEATRD YVLKEDAPDG LAPLINVFGG
     KLTTARKLAE HMLQKIEHRL GRKGAPWTHA APLPGGDFED VAFETELKKL EAAYPFLDAR
     RLFRLYGTRA YKLLGQASSL GDLGRHFGSD LYEAEVRYLV ENEWARSAED ILWRRTKLGL
     RLTAAEVAAV QGFVEPAIAA
//