G3P2_TRIKO
ID G3P2_TRIKO Reviewed; 338 AA.
AC P17730;
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 2;
DE Short=GAPDH2;
DE EC=1.2.1.12;
GN Name=gpd2;
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)-sensitive
CC GAPDH isozyme. It is present only when no antibiotic is produced.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; D14518; BAA03391.1; -; mRNA.
DR AlphaFoldDB; P17730; -.
DR SMR; P17730; -.
DR PRIDE; P17730; -.
DR SABIO-RK; P17730; -.
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..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000145586"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 151..153
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 25
FT /note="H -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36106 MW; 5D054CB198A78514 CRC64;
MAPIKVGING FGRIGRIVFR NAVEHPDIEV VAVNDPFIET TYAAYMLKYD SSHGLFKGEV
EVDGKDLVVN GKKVRFYTER NPADIKWSET GAEYVVESTG VFTTTEKAKA HLVGGAKKVI
ISAPSADAPM YVMGVNESDY DGSADVISNA SCTTNCLAPL AKVINDNYGI VEGLMTTVHS
YTATQKTVDG PSAKDWRGGR GAAQNIIPSS TGAAKAVGKV IPALNGKLTG MSIRVPTANV
SVVDLTVRIE KGASYEEITE TIKKAADGPL KGVLAYTGDD VVSSDMLGNT NSSIFDIKAG
ISLNKNFVKL VSWYDNEWGY SRRVLDLLAH VAKVDASK
