ID   GPD_COLGL               Reviewed;         420 AA.
AC   Q7Z8E7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   22-FEB-2023, entry version 85.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)];
DE            EC=1.1.1.8;
OS   Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=474922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14563847; DOI=10.1074/jbc.m308363200;
RA   Wei Y., Shen W., Dauk M., Wang F., Selvaraj G., Zou J.;
RT   "Targeted gene disruption of glycerol-3-phosphate dehydrogenase in
RT   Colletotrichum gloeosporioides reveals evidence that glycerol is a
RT   significant transferred nutrient from host plant to fungal pathogen.";
RL   J. Biol. Chem. 279:429-435(2004).
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}.
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DR   EMBL; AY331190; AAP94992.1; -; mRNA.
DR   AlphaFoldDB; Q7Z8E7; -.
DR   SMR; Q7Z8E7; -.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00957; NAD_G3PDH; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..420
FT                   /note="Glycerol-3-phosphate dehydrogenase [NAD(+)]"
FT                   /id="PRO_0000138089"
FT   REGION          190..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        278
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         16..21
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         344..345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         344
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
FT   BINDING         373
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P21695"
SQ   SEQUENCE   420 AA;  45278 MW;  ECCB6A3D3D1DF128 CRC64;
     MASLGADKKH KVTVVGSGNW GSTICKIVAE NTKANPDLFE EAVHMWVFEE DVVIDKSSPY
     YDPAVGDAPQ KLTGVINKYH ENTKYLPGIK LPDNIIANPS LQDAVKDSTI LVFNLPHQFI
     GNVCKQLRGH IMPFARGISC IKGVNVSDDG ISLFSEWIGD GLGIYCGALS GANIASEIAA
     EKWSETTIAY DPPPMDNSRA PTPRSNSPAN GNGIAPLTPV EMQHKDARGR TSKTKLTPVP
     AEYPPLDHQI FKQLFHRPYF HVRMVSDVAG VSLGGALKNI VALAAGFVDG RGWGDNAKAA
     IMRVGLLEMV NFGKEFFGQT VHTGTFTEES AGVADLITSC SGGRNFRCAK MAVAEGLSVE
     EIEKRELNGQ LLQGTSTAKE VNSFLKARGL EKDYPLFTAV HGILEGRHSV DDIPSLVSDS
//