ID   G3P_PHACH      STANDARD;      PRT;   337 AA.
AC   Q01982;
DT   01-APR-1993 (Rel. 25, Created)
DT   01-APR-1993 (Rel. 25, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) (GAPDH).
GN   Name=GPD;
OS   Phanerochaete chrysosporium.
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Aphyllophorales; Corticiaceae; Phanerochaete.
OX   NCBI_TaxID=5306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=93113715; PubMed=1473176;
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: Second phase of glycolysis; first step.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M81754; AAA33732.1; -.
DR   HSSP; P56649; 1CRW.
DR   InterPro; IPR000173; GAP_dhdrogenase.
DR   InterPro; IPR006424; GAPDH-I.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
KW   Glycolysis; NAD; Oxidoreductase.
FT   BINDING     151    151       Glyceraldehyde 3-phosphate.
FT   ACT_SITE    178    178       Activates thiol group during catalysis.
SQ   SEQUENCE   337 AA;  36259 MW;  5428354147659F09 CRC64;
     MPVKAGINGF GRIGRIVLRN ALLHGDIDVV AVNDPFIDLE YMVYMFKYDS VHGRFKGSVE
     AKDGKLYVEG KPIHVFAEKD PANIPWGSVG AEYIVESTGV FTTTEKASAH LKGVCKKVII
     SAPSADAPMF VCGVNLDAYD SKYKVISNAS CTTNCLAPLA KVIHDKFGIV QGLMTSVHAT
     TATQKTVDGP SNKDWLGGRS VGNNIIPSST GAAKAVGKVI PSLNGKLNGL AFRVPTVDVS
     VVDLVVRLEK PASYDEIKQA IKEASETTHK GILGYTEEKV VSTDFTGNDN SSIFDRDAGI
     ALNKTFVKLI SWYDNEWGYS RRCCDLLGYA AKVDGAL
//