ID   C0RM12_BRUMB            Unreviewed;       502 AA.
AC   C0RM12;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=BMEA_B0844 {ECO:0000313|EMBL:ACO02645.1};
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:ACO02645.1, 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; CP001489; ACO02645.1; -; Genomic_DNA.
DR   RefSeq; WP_004682238.1; NC_012442.1.
DR   AlphaFoldDB; C0RM12; -.
DR   GeneID; 29595453; -.
DR   KEGG; bmi:BMEA_B0844; -.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   PRO; PR:C0RM12; -.
DR   Proteomes; UP000001748; Chromosome II.
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; 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..333
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          386..482
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   502 AA;  56139 MW;  4A5361379A5C53B3 CRC64;
     MAEPETCDLF VIGGGINGAG VARDAAGRGL KVVLAEKDDL AQGTSSRSGK LVHGGLRYLE
     YYEFRLVREA LIEREVLLNA APHIIWPMRF VLPHSPQDRP AWLVRLGLFL YDHLGGRKKL
     PGTRTLDLKR DPEGTPILDQ YTKGFEYSDC WVDDARLVAL NAVGAAEKGA TILTRTPVVS
     ARRENGGWIV ETRNSDTGET HTFRARCIVN CAGPWVTDVI HNVAASTSSR NVRLVKGSHI
     IVPKFWSGAN AYLVQNHDKR VIFINPYEGD KALIGTTDIA YEGRAEDVAA DEKEIDYLIT
     AVNRYFKEKL RREDVLHSFS GVRPLFDDGK GNPSAVTRDY VFDLDETGGA PLLNVFGGKI
     TTFRELAERG VHRLKHIFPQ MGGDWTHDAP LPGGEIANAD YETFANTLRD TYPWMPRTLV
     HHYGRLYGAR TKDVVAGAQN LEGLGRHFGG DFHEAEVRYL VAREWAKTAE DILYRRTKHY
     LHLTEAERAA FVEWFDNANL VA
//