ID   G3P2_AGABI              Reviewed;         338 AA.
AC   P32636;
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 2;
DE            Short=GAPDH 2;
DE            EC=1.2.1.12;
GN   Name=gpd2;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M81728; AAA32634.1; -; Genomic_DNA.
DR   PIR; S26976; S26976.
DR   HSSP; P00357; 4GPD.
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    338       Glyceraldehyde-3-phosphate dehydrogenase
FT                                2.
FT                                /FTId=PRO_0000145534.
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     314    314       NAD (By similarity).
FT   SITE        177    177       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   338 AA;  36570 MW;  3381DBBF73B84469 CRC64;
     MVKVGINGFG RIGRIVLRNA LQFQDIEVVA VNDPFIDLEY MAYMFKYDSV HGRFKGTVEV
     KNGSFVVDGR PMKVFAERDP AAIPWGSVGA DYVVESTGVF TTIDKASAHL KGGAKKVVIS
     APSADAPMYV CGVNLDKYNP KDTIISNASC TTNCLATLAK VIHDNFGIVE GLMTTVHATT
     ATQKTVDGPS HKDWRGGRGV GNNIIPSSTG AAKAVGKVIP SLNGKLTGLS MRVPTQDVSV
     VDLVVRLEKP ASYEQIKEVM RKAAEGEYKG IIAYTDEDVV STDFISDNNS CVFDAKAGIQ
     LSPNFVKLIA WYDNEWGYSR RVCNLLQYVA KEDAKAGI
//