G3PG_CRIFA
ID G3PG_CRIFA Reviewed; 361 AA.
AC O96423; Q9UAM2;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, glycosomal;
DE Short=GAPDH;
DE EC=1.2.1.12;
GN Name=GAPDG;
OS Crithidia fasciculata.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Crithidia.
OX NCBI_TaxID=5656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11745;
RX PubMed=9847415; DOI=10.1007/pl00006432;
RA Hannaert V., Opperdoes F.R., Michels P.A.M.;
RT "Comparison and evolutionary analysis of the glycosomal glyceraldehyde-3-
RT phosphate dehydrogenase from different Kinetoplastida.";
RL J. Mol. Evol. 47:728-738(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-347.
RA Robello C.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AF047493; AAD02465.1; -; Genomic_DNA.
DR EMBL; AF053739; AAD17497.1; -; Genomic_DNA.
DR AlphaFoldDB; O96423; -.
DR SMR; O96423; -.
DR VEuPathDB; TriTrypDB:CFAC1_260054400; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0020015; C:glycosome; 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 3: Inferred from homology;
KW Glycolysis; Glycosome; NAD; Oxidoreductase; Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..361
FT /note="Glyceraldehyde-3-phosphate dehydrogenase,
FT glycosomal"
FT /id="PRO_0000145527"
FT MOTIF 359..361
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 167
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 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 166..168
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 227..228
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 92
FT /note="D -> E (in Ref. 2; AAD17497)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="A -> G (in Ref. 2; AAD17497)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="F -> L (in Ref. 2; AAD17497)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="F -> Y (in Ref. 2; AAD17497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 39088 MW; C96C5A4566429334 CRC64;
MAPIKVGING FGRIGRMVFQ SMCEDNVLGT ELDVVAVVDM STDAEYFAYQ MKFDTVHGRP
KYTVEVAKSS PSAKKPDVLV VNGHRILCVK ADRNPADLPW GKLGVDYVIE STGLFTDKAK
AEGHVKGGAK KVVISAPASG GAKTIVMGVN QHEYNPATHH VVSNASCTTN CLAPIVHVLT
KENFGIETGL MTTIHSYTAT QKTVDGVSIK DWRGGRAAAV NIIPSTTGAA KAVGMVIPST
KGKLTGMSFR VPTPDVSVVD LTFRATRDTS IQEIDAALKK ASQTYMKGIL GFTDEELVSS
DFINDARSSI YDSKATLQNN LPGEKRFFKV VSWYDNEWGY SHRVVDLVRF MGAKDRSSSK
L
