ID   A9WZF1_BRUSI            Unreviewed;       502 AA.
AC   A9WZF1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=BSUIS_B0858 {ECO:0000313|EMBL:ABY39817.1};
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:ABY39817.1, ECO:0000313|Proteomes:UP000008545};
RN   [1] {ECO:0000313|EMBL:ABY39817.1, 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; CP000912; ABY39817.1; -; Genomic_DNA.
DR   RefSeq; WP_002965781.1; NC_010167.1.
DR   AlphaFoldDB; A9WZF1; -.
DR   SMR; A9WZF1; -.
DR   GeneID; 3827518; -.
DR   KEGG; bmt:BSUIS_B0858; -.
DR   PATRIC; fig|359391.4.peg.2665; -.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   PRO; PR:A9WZF1; -.
DR   Proteomes; UP000008545; 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;  56191 MW;  F3D0FAE51B352540 CRC64;
     MAEPETCDLF VIGGGINGAG VARDAAGRGL KVVLAEKDDL AQGTSSRSGK LVHGGLRYLE
     YYEFRLVREA LIEREVLLNA APHIIWPMRF VLPHSPQDRP AWLVRLGLFL YDHLGGRKKL
     PGTRTLDLKR DPEGTPILDQ YTKGFEYSDC WVDDARLVAL NAVGAAEKGA TILTRTPVVS
     ARRENGGWIV ETRNSDTGET RTFRARCIVN CAGPWVTDVI HNVAASTSSR NVRLVKGSHI
     IVPKFWSGAN AYLVQNHDKR VIFINPYEGD KALIGTTDIA YEGRAEDVAA DEKEIDYLIT
     AVNRYFKEKL RREDVLHSFS GVRPLFDDGK GNPSAVTRDY VFDLDETGGA PLLNVFGGKI
     TTFRELAERG MHRLKHIFPQ MGGDWTHDAP LPGGEIANAD YETFANTLRD TYPWMPRTLV
     HHYGRLYGAR TKDVVAGAQN LEGLGRHFGG DFHEAEVRYL VAREWAKTAE DILYRRTKHY
     LHLTEAERAA FVEWFDNANL VA
//