ID   A2S8R5_BURM9            Unreviewed;       510 AA.
AC   A2S8R5;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
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:ABN00805.1};
GN   OrderedLocusNames=BMA10229_A2372 {ECO:0000313|EMBL:ABN00805.1};
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022 {ECO:0000313|EMBL:ABN00805.1, ECO:0000313|Proteomes:UP000002283};
RN   [1] {ECO:0000313|EMBL:ABN00805.1, ECO:0000313|Proteomes:UP000002283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229 {ECO:0000313|EMBL:ABN00805.1,
RC   ECO:0000313|Proteomes:UP000002283};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (JAN-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; CP000546; ABN00805.1; -; Genomic_DNA.
DR   RefSeq; WP_004189374.1; NC_008836.1.
DR   AlphaFoldDB; A2S8R5; -.
DR   GeneID; 56596616; -.
DR   KEGG; bml:BMA10229_A2372; -.
DR   HOGENOM; CLU_015740_5_0_4; -.
DR   Proteomes; UP000002283; 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; 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..329
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          386..487
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   510 AA;  56452 MW;  6D4E03B7F9D8C003 CRC64;
     MTQQNRYDLL VVGGGINGAG IARDAAGRGL SVLLCEQDDL ASHTSSSSTK LIHGGLRYLE
     YKEFGLVRKA LQERETLLRA APHIMWPLRF VMPHMPNLRP AWLIRIGLFL YDHLAKRELL
     PGSRGIDMRR HPAGAPLVDS IKRGFVYSDG WVDDARLVVL NALDAQERGA RILTRTKLVS
     AERRDGQWHA RLQRADGSTL DVRARAIANA AGPWVGEVLH GALGRGAQHS VRLVKGSHII
     TPRLFDHDHA YIFQNPDKRI IFAIPYERDF TLIGTTDVEY RDDPSRVAID RDETRYLCES
     INRYFKRKIS PADVCWTYSG VRPLLEDENA DNPSAVTRDY RLELDDGEGA PLLSVFGGKI
     TTFRKLAEEA TDMLGGALGA ARGAWTAGVP LPGGDIANAR FAPFAEAFAK RHPWLPAALA
     RRYARAYGTR AERVIGRARS HAELGVQLAP GLYEAELRYL RDVEWAGCAD DVLWRRSKLG
     LHVAPGTLEP VTAALDAWFG AAREAASAAH
//