ID   Q2NQH1_SODGM            Unreviewed;       527 AA.
AC   Q2NQH1;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=SG2329 {ECO:0000313|EMBL:BAE75604.1};
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE75604.1, ECO:0000313|Proteomes:UP000001932};
RN   [1] {ECO:0000313|EMBL:BAE75604.1, ECO:0000313|Proteomes:UP000001932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans {ECO:0000313|Proteomes:UP000001932};
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE75604.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2NQH1; -.
DR   STRING; 343509.SG2329; -.
DR   KEGG; sgl:SG2329; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_0_6; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000001932; 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; 6.10.250.1890; -; 1.
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.
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          5..324
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          381..481
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          499..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  59126 MW;  B891222B55932E9A CRC64;
     METKDLIVIG GGINGTGIAS DAAGRGLSVL LLEAQDLACA TSSASSKLIH GGLRYLEHYE
     IRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRVGLFMYDH LGKRTSLPAS
     QSVRFGADSV LKPEIMRGFE YSDCWVDDAR LVVLNAQEVV AHGGEVKTRT QVTRAWRKNG
     LWQVEARDSL TGKQHRWHAK GLANATGPWA KHFIDESLHL PSQYGIRLIK GSHIVVPCVH
     HQPQAYILQN EDHRIVFVIP WMETFSIIGT TDVEYHGDPG EVHIDESEID YLLKVYNAHF
     QRPLGREDIV WTFSGVRPLC DDESNSPQAV TRDYTLSLSD ENGQAPLLSV FGGKLTTYRK
     LAEYALEKLA HYYPHAKGAW TSNAVLPGGD FAGTRDDYTA VLRRKFAFLP EALARRYSHT
     YGTRSEQLLA GVTGLADLGE DFGHGLYEAE LRYLVAQEWV VTLDDAIWRR TKLGMWLDEA
     QQTRITDWLV STSARRGCRW RPKPLPPAGS STGGRAPLSK SPWHIRG
//