ID   GPD_MAGO7               Reviewed;         433 AA.
AC   P0CT11; A4RGF7; G4NER8; Q5G5B9;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)];
DE            EC=1.1.1.8;
GN   ORFNames=MGG_00067;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.8;
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EHA49491.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM001235; EHA49491.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_003719075.1; XM_003719027.1.
DR   AlphaFoldDB; P0CT11; -.
DR   SMR; P0CT11; -.
DR   STRING; 318829.MGG_00067T0; -.
DR   GeneID; 2675060; -.
DR   KEGG; mgr:MGG_00067; -.
DR   eggNOG; KOG2711; Eukaryota.
DR   OrthoDB; 476066at2759; -.
DR   Proteomes; UP000009058; Chromosome 5.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..433
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)]"
FT                   /id="PRO_0000138091"
FT   REGION          187..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        283
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         17..22
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         49
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         117
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         173
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         349..350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         349
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         378
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
SQ   SEQUENCE   433 AA;  46756 MW;  AAFF086871BA1913 CRC64;
     MASLGSYAKK HKVTIIGSGN WGSTIAKIVA ESTREHKDVF EEDVQMWVFE EKVTIPKDSP
     YYESEEPQKL TEVINKHHEN VKYLPGIKLP SNIIANPSLT DAVRDSSVLV FNLPHEFLGK
     VCQQLNGHIV PFARGISCIK GVDVSGSGIN LFCEVIGEKL GIYCGALSGA NVASQIAAEE
     GVSETTIAYD PPPIDSSRAA TPRDRSPNYD STSANKLPDL TVTSADSNGK DDRGRRTKAK
     LTPVPESYPP LDHGTLQILF DRPYFSVSMV SDVAGVSLSG ALKNIVALAA GFVDGKGWGS
     NVQSAVIRVG LAEMLKFARE FFGESVDPFT ILLESAGVAD VITSCISGRN FRCASMAVKR
     GVSVAEIEEK ELNGQKLQGT STAKEVNSLL KARGREGDYP LFTTVNEILE GKARVDDLPK
     LVIRQKHTIE KSG