ID   I7CDH2_9PEZI            Unreviewed;       256 AA.
AC   I7CDH2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) {ECO:0000256|ARBA:ARBA00013119};
DE            EC=1.2.1.12 {ECO:0000256|ARBA:ARBA00013119};
DE   Flags: Fragment;
GN   Name=gpd {ECO:0000313|EMBL:AFO66540.1};
OS   Phyllosticta hubeiensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Phyllostictaceae;
OC   Phyllosticta.
OX   NCBI_TaxID=1214783 {ECO:0000313|EMBL:AFO66540.1};
RN   [1] {ECO:0000313|EMBL:AFO66540.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LC1654 {ECO:0000313|EMBL:AFO66540.1};
RA   Zhang K., Su Y.Y., Cai L.;
RT   "Morphological and phylogenetic characterization of two new species of
RT   Phyllosticta from China.";
RL   Mycol. Prog. 12:547-556(2013).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; JX025029; AFO66540.1; -; Genomic_DNA.
DR   AlphaFoldDB; I7CDH2; -.
DR   UniPathway; UPA00109; UER00184.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..109
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFO66540.1"
FT   NON_TER         256
FT                   /evidence="ECO:0000313|EMBL:AFO66540.1"
SQ   SEQUENCE   256 AA;  27196 MW;  620D548254378070 CRC64;
     AYMLKYDSTH GQFKGEVKVE GSDLLINGKK VRFYQERDPA SIPWAETGAY YIVESTGVFT
     TTEKASAHLK GGAKKVVISA PSADAPMFVM GVNNETYTSD INVLSNASCT TNCLAPLAKV
     INDKYTIIEG LMTTVHSYTA TQKTVDGPSA KDWRGGRTAA TNIIPSSTGA AKAVGKVIPN
     LNGKLTGMAF RVPTSNVSVV DLTARIEKGA SYDEIKQTIK AAAEGPLKGI LAYTEDEVVS
     SDMNGDVHSS IFDAKA
//