ID   G3P1_AGABI              Reviewed;         337 AA.
AC   P32635;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-NOV-2008, entry version 54.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE            Short=GAPDH 1;
DE            EC=1.2.1.12;
GN   Name=gpd1;
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Horst U3;
RX   MEDLINE=93113715; PubMed=1473176; DOI=10.1007/BF00326409;
RA   Harmsen M.C., Schuren F.H.J., Moukha S.M., van Zuilen C.M., Punt P.J.,
RA   Wessels J.G.H.;
RT   "Sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase
RT   genes from the basidiomycetes Schizophyllum commune, Phanerochaete
RT   chrysosporium and Agaricus bisporus.";
RL   Curr. Genet. 22:447-454(1992).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; M81727; AAA32633.1; -; Genomic_DNA.
DR   PIR; S26975; S26975.
DR   HSSP; P56649; 1CRW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000173; GlycerAld_3-P_DHase.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DHase_1.
DR   PANTHER; PTHR10836; GAP_DH; 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   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN         1    337       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000145533.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      149    151       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      209    210       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    150    150       Nucleophile (By similarity).
FT   BINDING      33     33       NAD (By similarity).
FT   BINDING      78     78       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     180    180       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     232    232       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     318    318       NAD (By similarity).
FT   SITE        177    177       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   337 AA;  36749 MW;  FBA09EE1A75A4D3A CRC64;
     MVNVGINGFG RIGRLVLRNA LQMQILTVVA VNDPFLDVEY MAYLFKYDSV HGRYQGKVET
     KDGKLIIDGH KIAAFAEREP ANIKWADCGA EYIVESTGVF KTEELAKEHL KGGAKKVVIT
     APGSGVPTYV VGVNLDKYDP KEVVISNASC TTNCLAVLAK VINDKFGIVE GLMTTVHATT
     ATQKTVDAPA KKDWRSGRSV TNNIIPASTG AAKAVTKAIP DLEGKLTGLA FRVPTLDVSV
     VDLVVRLEKE TSYDDVKKAM RDAADGKHPG IEKGIVDYTE EDVVSTDFVG SNYSMIFDAK
     AGIALNSRFM KLVAWYDNEW GYARRVCDEV VYVAKKN
//