ID   B8DL64_DESVM            Unreviewed;       542 AA.
AC   B8DL64;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=DvMF_0811 {ECO:0000313|EMBL:ACL07767.1};
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=883 {ECO:0000313|EMBL:ACL07767.1};
RN   [1] {ECO:0000313|EMBL:ACL07767.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Miyazaki F {ECO:0000313|EMBL:ACL07767.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-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; CP001197; ACL07767.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8DL64; -.
DR   STRING; 883.DvMF_0811; -.
DR   KEGG; dvm:DvMF_0811; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_4_1_7; -.
DR   OrthoDB; 9766796at2; -.
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.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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          17..378
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          401..522
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   542 AA;  59308 MW;  C9B822C8533F91FB CRC64;
     MNRSGLLERL KSGREFDLLV IGGGATGCGV AVDAATRGLD VALVDRADFA QGTSSRSTKL
     VHGGVRYLEK AVLQCDREQF GLVREGLRER GFLLANAPHL AHAVRLLTPV PTWKDAGYMF
     AGLTLYDLLA GRLGLGHSKF VGKRAAERMF PTLRMGDYKA AVTYWDGQFN DARMAVALAR
     TANAHGATCC NHVEVTHLIK EGGRLRGAEL RDMLTGETWT LRARGIINAT GPMADTVRRM
     DDPGADEILK VSSGIHIVLE AGFTPPDLSL MIPKTEDGRV LFMIPWQNHV VFGTTDEHAN
     PEHDPVPDVA DIDYLLRYAS KYLSRPVTRG DVRAVWSGLR PLVFAPGKGS TQELARTHVI
     EVSPAGLLTI AGGKWTSYRM MAQDTVDRAD VAFGLNLTRP CVTRHLKVVG ARGFIPGGYT
     EIAREYGVPV ELAKALHGTY GDETGQVLTI ARDENLGDRV HPDHPHIMAE VAFIVRNEMA
     MRLVDVLVRR LPMGLLDVEH TLQAAPGVAR IMAAELGWDA ARTDAELQYL ETYLSGWRAP
     RD
//