G3P1_TRIKO
ID G3P1_TRIKO Reviewed; 336 AA.
AC P17729;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE Short=GAPDH1;
DE EC=1.2.1.12;
GN Name=gpd1;
OS Trichoderma koningii (Hypocrea koningii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=97093;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=M3947;
RX 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 glyceraldehyde-3-phosphate
RT dehydrogenase with different sensitivity to koningic acid.";
RL Biochim. Biophys. Acta 1172:43-48(1993).
RN [2]
RP PROTEIN SEQUENCE OF 2-32.
RC STRAIN=M3947;
RX PubMed=2226438; DOI=10.1111/j.1432-1033.1990.tb19323.x;
RA Sakai K., Hasumi K., Endo A.;
RT "Two glyceraldehyde-3-phosphate dehydrogenase isozymes from the koningic
RT acid (heptelidic acid) producer Trichoderma koningii.";
RL Eur. J. Biochem. 193:195-202(1990).
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 -!- ACTIVITY REGULATION: Inhibited by koningic acid through the interaction
CC of cysteine residues with koningic acid even at very low
CC concentrations.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: This protein is a koningic acid (antibiotic)-resistant
CC GAPDH isozyme. It is present under antibiotic production.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; D14519; BAA03392.1; -; mRNA.
DR PIR; S13205; S13205.
DR AlphaFoldDB; P17729; -.
DR SMR; P17729; -.
DR PRIDE; P17729; -.
DR SABIO-RK; P17729; -.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2226438"
FT CHAIN 2..336
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1"
FT /id="PRO_0000145585"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 36252 MW; FC8C87E617297066 CRC64;
MVPKVGINGF GRIGRVVLRN ALETGAVEVV ALNDPFIEPH YAEYMFKYDS THGRFKGDIK
VDGKDLVIDG KRIKFYQERD PANIPWKDSG AEYIVESTGV FTTTEKASAH FKGGAKKVII
SAPSADAPMY VMGVNEDTYA GANVISNASC TTNCLAPLAK TLNDKFTIVE GLMTAIHAYT
ASQKTVDGPS SKDWRGGRAA AQNLIPSSTG AAKAVGKVIP ELAGKVTGMS VRVPTVNVSL
VDFTVRFAKD VTYDEVKAAI KEASEGPLKG ILAYTEDDIV STDILTDPHS STFDAKAGIA
LNKNFVKVMS WYDNEYGYSR RVVDLIVYVS KKDAGQ
