ID   B1JY42_BURO0            Unreviewed;       507 AA.
AC   B1JY42;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=Bcenmc03_2706 {ECO:0000313|EMBL:ACA91866.1};
OS   Burkholderia orbicola (strain MC0-3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex;
OC   Burkholderia orbicola.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA91866.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL   Submitted (FEB-2008) 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; CP000958; ACA91866.1; -; Genomic_DNA.
DR   RefSeq; WP_012329185.1; NC_010508.1.
DR   AlphaFoldDB; B1JY42; -.
DR   GeneID; 83049491; -.
DR   KEGG; bcm:Bcenmc03_2706; -.
DR   HOGENOM; CLU_015740_5_0_4; -.
DR   Proteomes; UP000002169; Chromosome 1.
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..496
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   507 AA;  55913 MW;  B651446A4F29D6A5 CRC64;
     MTQPNRYDLL VVGGGINGAG IARDAAGRGL SVMLCEQDDL ASHTSSSSTK LIHGGLRYLE
     YNEFGLVRKA LQERETLLRA APHIMWPLRF VMPHMPNLRP AWLIRIGLFL YDHLAKRELL
     PGSRGIDMRR HAAGAPLIDS IKRGFVYSDG WVDDARLVVL NAMDAKERGA EILTRTKLVS
     AERRGDEWEA RLQHPDGSIR VVHARAIANA AGPWVGEVLH GALGRGAHHS VRLVKGSHII
     TRRLFDHDHA YIFQNPDKRI IFAIPYEHDF TLIGTTDVEY TNDPAKVAID RDETQYLCDS
     INRYFKRKIS PADVHWTYSG VRPLLEDENA ANASAVTRDY RLELDDGAGA PLLSVFGGKI
     TTFRKLAEEA GDMLCRALGR DAKTWTAGVA LPGGDIADAK FDGFASAFAK RHPWLPAALA
     RRYARAYGTR AERVVDGAKS LADLGAEIAP GIHDAELRYL RDAEWATCAQ DVLWRRSKLG
     LHVAPGTLDA VTAAVDAWFA AAHAPHA
//