ID   Q2YP39_BRUA2            Unreviewed;       503 AA.
AC   Q2YP39;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
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:CAJ10156.1};
GN   OrderedLocusNames=BAB1_0200 {ECO:0000313|EMBL:CAJ10156.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ10156.1, ECO:0000313|Proteomes:UP000002719};
RN   [1] {ECO:0000313|EMBL:CAJ10156.1, ECO:0000313|Proteomes:UP000002719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308 {ECO:0000313|EMBL:CAJ10156.1,
RC   ECO:0000313|Proteomes:UP000002719};
RX   PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG   Microbial Genomics Group;
RG   Lawrence Livermore National Laboratory;
RG   and the Genome Analysis Group;
RG   Oak Ridge National Laboratory;
RA   Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ10156.1; -; Genomic_DNA.
DR   RefSeq; WP_002969529.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YP39; -.
DR   STRING; 359391.BAB1_0200; -.
DR   GeneID; 3788729; -.
DR   KEGG; bmf:BAB1_0200; -.
DR   PATRIC; fig|359391.11.peg.1623; -.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   Proteomes; UP000002719; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002719}.
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;  56275 MW;  E5BBFCF085BEFA19 CRC64;
     MVQEKQFDIF IIGGGINGCG IARDAVGRGF TVGLAEMNDL ASGTSSRATK LIHGGLRYLE
     HYEFRLVREA LMEREVLWAN ALHIIHPMRF VLPYHKGGLR PAWLLRLGLF LYDHLGGRKK
     LPATRTLNMR TDKAGEPLKP LFTKAFEYSD CWVDDARFVA LTARDAADRG AKIATRTSVV
     AASRGGQGWT 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
//