ID   E8WMH3_GEOS8            Unreviewed;       537 AA.
AC   E8WMH3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=GM18_3456 {ECO:0000313|EMBL:ADW14890.1};
OS   Geobacter sp. (strain M18).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW14890.1, ECO:0000313|Proteomes:UP000001442};
RN   [1] {ECO:0000313|EMBL:ADW14890.1, ECO:0000313|Proteomes:UP000001442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18 {ECO:0000313|EMBL:ADW14890.1,
RC   ECO:0000313|Proteomes:UP000001442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA   Aklujkar M., Lovley D., Woyke T.;
RT   "Complete sequence of Geobacter sp. M18.";
RL   Submitted (JAN-2011) 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; CP002479; ADW14890.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8WMH3; -.
DR   STRING; 443143.GM18_3456; -.
DR   KEGG; geb:GM18_3456; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_4_1_7; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000001442; Chromosome.
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          18..380
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          402..522
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   537 AA;  58579 MW;  CFA1852BACD42409 CRC64;
     MTDRNANLEI LKSGQTFDML VIGGGATGCG IAVDAANRGL SVALVERGDF GCGTSSKSTK
     LVHGGVRYLE AALLHMDRVQ FNLVRDGLHE RSVLLKIAPH LCHRLTLVTP LYGLAQVPYV
     WSGLKLYDIL AAEAGLGPSR FVRRREMLSR FPMIRKEGLK GGVQYYDGQF NDMRMNVALA
     QTAAREGAVV CNYLEVAGLM REKGRVAGAL VRDPLAGVSW QIRARCVVNA CGPSSDLVRR
     MDDPTAAPLL RVSRGVHIVL PGRFAPKEGG IMIPKTEDGR VAFILPWEGA CLVGTTEEPA
     APGDAPVADA RDIEFLLRHL RRYFNLDVNS GDITASWAGL RPLVHDPFTA DTAELARDHV
     ISCSATGLIT IVGGKWTTYR KMALDTVEFA VNNAGLTPQH PCRTDRIILE GGENFTEEMG
     AELARQYGFP PDVTQHLHRS YGDRSFDVAE MCHGAMGGRL VQGHPYLKGE VLYAVRHEMA
     LRALDFLERR IPLALLDRKG VLAAAPAVVE LMAAELGWNP SRQSRELEEV ADTLGVD
//