ID   G3P_BOLED               Reviewed;         291 AA.
AC   Q00301;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE            Short=GAPDH;
DE            EC=1.2.1.12;
DE   Flags: Fragment;
GN   Name=GPD;
OS   Boletus edulis (King bolete).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Boletineae; Boletaceae; Boletoideae; Boletus.
OX   NCBI_TaxID=36056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8795234; DOI=10.1128/aem.62.9.3432-3438.1996;
RA   Kreuzinger N., Podeu R., Gruber F., Gobl F., Kubicek C.P.;
RT   "Identification of some ectomycorrhizal basidiomycetes by PCR amplification
RT   of their gpd (glyceraldehyde-3-phosphate dehydrogenase) genes.";
RL   Appl. Environ. Microbiol. 62:3432-3438(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; U30625; AAB38246.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q00301; -.
DR   SMR; Q00301; -.
DR   UniPathway; UPA00109; UER00184.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; PTHR10836; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN           <1..>291
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000145540"
FT   ACT_SITE        130
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..131
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..190
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   SITE            157
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         291
SQ   SEQUENCE   291 AA;  30895 MW;  B497315405D6D287 CRC64;
     LENPEINITA VNDPFIDLDY MVYMFKYDSV HGRFEGEVST KDGKLVINGK AITVFAERDP
     ANIPWGTVGA QYVVESTGVF TTIEKASAHL KGGAKKVIIS APSSDAPMFV CGVNLDAYDP
     KHTVISNASC TTNCLAPLAK VVNDKFGIVE GLMTTVHATT ATQKTVDGPS PKDWRGGRAV
     NNNIIPSSTG AAKAVGKVIP VLNGKLTGLA FRVPTLDVSV VDLVVRLAKP TSYEEIKTAF
     KEASESSELK GIVAYTEDAV VSTDFLGHHA SSIFDATGGI MLNDSFVKLI A