ID   F8B2L7_9ACTN            Unreviewed;       570 AA.
AC   F8B2L7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   02-SEP-2026, entry version 69.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=FsymDg_1332 {ECO:0000313|EMBL:AEH08812.1};
OS   Candidatus Protofrankia datiscae.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
OC   Frankiaceae; Protofrankia.
OX   NCBI_TaxID=2716812 {ECO:0000313|EMBL:AEH08812.1, ECO:0000313|Proteomes:UP000001549};
RN   [1] {ECO:0000313|EMBL:AEH08812.1, ECO:0000313|Proteomes:UP000001549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4085684 {ECO:0000313|Proteomes:UP000001549};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Chertkov O., Teshima H., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Berry A.,
RA   Pawlowski K., Persson T., Vanden Heuvel B., Benson D., Woyke T.;
RT   "Complete sequence of chromosome of Frankia symbiont of Datisca
RT   glomerata.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = dihydroxyacetone
CC         phosphate + a quinol; 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; CP002801; AEH08812.1; -; Genomic_DNA.
DR   RefSeq; WP_013872786.1; NC_015656.1.
DR   AlphaFoldDB; F8B2L7; -.
DR   STRING; 656024.FsymDg_1332; -.
DR   KEGG; fsy:FsymDg_1332; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_11; -.
DR   Proteomes; UP000001549; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase (FAD) complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:TreeGrafter.
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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR   PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU361217};
KW   Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001549}.
FT   DOMAIN          82..439
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          460..564
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..62
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  59382 MW;  03C5F999574B5F7E CRC64;
     MSSQRHRDNH HDTLDAPPRR RSAAGRTATP SRLPPPSHQA TASHQATAPR RPTARPASST
     ASLNRRQRER DLAELADGAV VDVLVIGGGV TGAGVALDAA SRGLSVALVE AHDLAFGTSR
     WSSKLVHGGL RYLASGDLAL AHESARERAV LLGTTAPHLV RPLPMLLPLA AGFPISTALA
     ANAGLRVADI LRRAAGTPRT VLPGPRRLTA VEARHMVPAL RAPGLRGGLL TWDGQLVDDA
     RLVVAIARTA ARHGTRVITR CRVREADGSG ATAVDTVSNS PVILRSRSVV NATGVWAGDL
     CADARLRPSR GTHLVVAGSA LDGLRTAIII PVPGERNRYV FALPQPGGHV YVGITDEPVD
     TVVDVPVPTA AELDFLLGVL SSVLTVPVGR ADVLGAFAGL RPLLASAAGR TADLSRRHAV
     ITSSDGMVTV VGGKLTTYRR MAADAVDTLV RAGGLDAGPC RTRRLPLVGA ASWSQLATVD
     APPRLVARYG AEAPAVVAGT HGDPGLLLPL CDGVEVTGAE LLFALRHEGA LDADDLLDRR
     TRIGLVPADR QAALPAAEAL VRQTLTMIDT
//