ID   G3P1_TRIKO     STANDARD;      PRT;   335 AA.
AC   P17729;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   04-APR-2006, entry version 52.
DE   Glyceraldehyde-3-phosphate dehydrogenase 1 (EC 1.2.1.12) (GAPDH1).
GN   Name=gpd1;
OS   Trichoderma koningii.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea.
OX   NCBI_TaxID=55202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=M3947;
RX   MEDLINE=93176825; PubMed=8439569; DOI=10.1016/0167-4781(93)90267-H;
RA   Watanabe H., Hasumi K., Fukushima Y., Sakai K., Endo A.;
RT   "Cloning of two isozymes of Trichoderma koningii
RT   glyceraldehyde-3-phosphate dehydrogenase with different sensitivity to
RT   koningic acid.";
RL   Biochim. Biophys. Acta 1172:43-48(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-31.
RC   STRAIN=M3947;
RX   MEDLINE=91031446; PubMed=2226438;
RA   Sakai K., Hasumi K., Endo A.;
RT   "Two glyceraldehyde-3-phosphate dehydrogenase isozymes from the
RT   koningic acid (heptelidic acid) producer Trichoderma koningii.";
RL   Eur. J. Biochem. 193:195-202(1990).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC   -!- ENZYME REGULATION: Inhibited by koningic acid through the
CC       interaction of cysteine residues with koningic acid even at very
CC       low concentrations.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from
CC       D-glyceraldehyde 3-phosphate: step 1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: This protein is a koningic acid (antibiotic)-
CC       resistant GAPDH isozyme. It is present under antibiotic
CC       production.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; D14519; BAA03392.1; -; mRNA.
DR   PIR; S13205; S13205.
DR   HSSP; P56649; 1IHX.
DR   SMR; P17729; 3-334.
DR   InterPro; IPR000173; GAP_DH.
DR   InterPro; IPR006424; GAPDH_I.
DR   InterPro; IPR011596; GAPDH_like.
DR   PANTHER; PTHR10836; GAP_dhdrogenase; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   ProDom; PD007761; GAPDH_like; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
KW   Direct protein sequencing; Glycolysis; NAD; Oxidoreductase.
FT   INIT_MET      0      0
FT   CHAIN         1    335       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000145585.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      148    150       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      208    209       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    149    149       Nucleophile (By similarity).
FT   BINDING      33     33       NAD (By similarity).
FT   BINDING      78     78       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     179    179       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     231    231       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     313    313       NAD (By similarity).
FT   SITE        176    176       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   335 AA;  36121 MW;  D3F9A01754281A22 CRC64;
     VPKVGINGFG RIGRVVLRNA LETGAVEVVA LNDPFIEPHY AEYMFKYDST HGRFKGDIKV
     DGKDLVIDGK RIKFYQERDP ANIPWKDSGA EYIVESTGVF TTTEKASAHF KGGAKKVIIS
     APSADAPMYV MGVNEDTYAG ANVISNASCT TNCLAPLAKT LNDKFTIVEG LMTAIHAYTA
     SQKTVDGPSS KDWRGGRAAA QNLIPSSTGA AKAVGKVIPE LAGKVTGMSV RVPTVNVSLV
     DFTVRFAKDV TYDEVKAAIK EASEGPLKGI LAYTEDDIVS TDILTDPHSS TFDAKAGIAL
     NKNFVKVMSW YDNEYGYSRR VVDLIVYVSK KDAGQ
//