ID   GPDH_ENCCU              Reviewed;         614 AA.
AC   Q8SR40;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Probable glycerol-3-phosphate dehydrogenase;
DE            Short=GPDH;
DE            EC=1.1.5.3;
GN   OrderedLocusNames=ECU10_0870;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18318866; DOI=10.1111/j.1550-7408.2008.00315.x;
RA   Williams B.A.P., Cali A., Takvorian P.M., Keeling P.J.;
RT   "Distinct localization patterns of two putative mitochondrial proteins in
RT   the microsporidian Encephalitozoon cuniculi.";
RL   J. Eukaryot. Microbiol. 55:131-133(2008).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic
CC       route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18318866}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; AL590449; CAD25806.1; -; Genomic_DNA.
DR   RefSeq; NP_586202.1; NM_001042035.1.
DR   AlphaFoldDB; Q8SR40; -.
DR   SMR; Q8SR40; -.
DR   STRING; 284813.Q8SR40; -.
DR   PRIDE; Q8SR40; -.
DR   GeneID; 859851; -.
DR   KEGG; ecu:ECU10_0870; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_0870; -.
DR   HOGENOM; CLU_015740_4_1_1; -.
DR   InParanoid; Q8SR40; -.
DR   OMA; CIVNAAG; -.
DR   OrthoDB; 669193at2759; -.
DR   UniPathway; UPA00618; UER00673.
DR   Proteomes; UP000000819; Chromosome X.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..614
FT                   /note="Probable glycerol-3-phosphate dehydrogenase"
FT                   /id="PRO_0000383045"
FT   REGION          595..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57..85
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   614 AA;  68640 MW;  20942D4D6F7AC40E CRC64;
     MLVALVVLFL SVFMAMKFLY KRIFVASRLK MIEKPSEDWE PASREAMIER LRSEVFDLVV
     VGGGSTGAGC ALDGATRGLK VALVDAGDFG SGTSSKSTKL VHGGVRYLAK AVSNLDWSQY
     KLVWQALGER TTMFEISPYL TNSIKIMVPI YSKILIPYYY VGLKLYDWIS GFKSLGKSYF
     IDRKEAVDAF PHINKKNLCG AMVYFDGQQD DARNNVMIVM TAVCHGAVAA NHVSARSLMI
     EGGKIVGVRC RDEITGSEIE IRGTGVINST GNLADDLRRM DDADAREIIV QSSGTHIVIP
     KEYAPKEMGF LDPLTSDNRI AFFMPWMGKT IVGSTDIKTK TELSPSPTEE DLEFLIHEVQ
     AYTSMHPKLT RDEVSAVWTG IRPLVKDPDV SDTGSIVRKH FVRIEKNGLL TVTGGKWTIY
     RKMAEDAIDL AISAFSLKPS GPCVTKYVRI LGGDGYTKNT WASIQKELGV PKNVAERLAR
     SYGTRALRLS SYIKKNRKKV LSVKYSYLIE EVEYCIDNEM AVKVCDVLCN RLMIGLMDVK
     EAYQCIDKVL GVFKKKHGWD ADRCNREEAD AIRMLDKYGL QILRGCGQDA SSLQMECPEE
     KRHRGERRLP PQEK