ID   C6E1L9_GEOSM            Unreviewed;       537 AA.
AC   C6E1L9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-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=GM21_0871 {ECO:0000313|EMBL:ACT16938.1};
OS   Geobacter sp. (strain M21).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT16938.1};
RN   [1] {ECO:0000313|EMBL:ACT16938.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21 {ECO:0000313|EMBL:ACT16938.1};
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., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) 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; CP001661; ACT16938.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6E1L9; -.
DR   STRING; 443144.GM21_0871; -.
DR   KEGG; gem:GM21_0871; -.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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;  59093 MW;  CE7BAD0384AACE8F CRC64;
     MTDRKERLDR LKSGEIFDLL VVGGGATGCG IALDAASRGL KVALAERRDF AGGTSGRSTK
     LLHGGVRYLE AAVLHRDKVQ FNLVRDALHE RGVLLKIAPH LCQRLTLVSP LYRLAQVPYI
     WAGLKFYDLL ARRAGLGHSR YLSPSEMLWR FPQIKAEGLK GGVLYYDGQF NDARMNVALA
     QTALREGAAL SNYLEVVGLV REKGRVAGAL VRDPLGGASW QIRARCVVNA CGPSADLVRR
     MDDPTAAPLL RVSRGSHIVL PGRFAPADAG IMIPKTEDGR VIFILPWQGM CLVGTTEEPA
     LPGTPPVVDD KDVDYLLRHL RRYFNITVDE GDIMARWAGL RPLVHDPFTA DTAELARDHV
     ISCSPTGLVT IVGGKWTTYR KMALDTVDYA VATLGLATSC ECRTDRIVLH GGEGFQEQGA
     TELAKRFRLP PDIALHLHGS YGSLAADVAE FCQGELRDRL VPPHPYLKGE VLYAVRYEMA
     LSPLDFLERR IHLALLDQRG AQVAAPVVLE MMAEELGWSQ ARVAHERAQM QERFSNV
//