G3PG_TRYCR
ID G3PG_TRYCR Reviewed; 359 AA.
AC P22513;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, glycosomal;
DE Short=GAPDH;
DE EC=1.2.1.12;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=X10/6;
RX PubMed=2167831; DOI=10.1002/j.1460-2075.1990.tb07462.x;
RA Kendall G., Wilderspin A.F., Ashall F., Miles M.A., Kelly J.M.;
RT "Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase does
RT not conform to the 'hotspot' topogenic signal model.";
RL EMBO J. 9:2751-2758(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH CHALEPIN, AND
RP SUBUNIT.
RX PubMed=12044862; DOI=10.1016/s0014-5793(02)02700-x;
RA Pavao F., Castilho M.S., Pupo M.T., Dias R.L.A., Correa A.G.,
RA Fernandes J.B., da Silva M.F.G.F., Mafezoli J., Vieira P.C., Oliva G.;
RT "Structure of Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate
RT dehydrogenase complexed with chalepin, a natural product inhibitor, at 1.95
RT A resolution.";
RL FEBS Lett. 520:13-17(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOG, AND SUBUNIT.
RX PubMed=12795610; DOI=10.1021/bi0206107;
RA Castilho M.S., Pavao F., Oliva G., Ladame S., Willson M., Perie J.;
RT "Evidence for the two phosphate binding sites of an analogue of the
RT thioacyl intermediate for the Trypanosoma cruzi glyceraldehyde-3-phosphate
RT dehydrogenase-catalyzed reaction, from its crystal structure.";
RL Biochemistry 42:7143-7151(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOG, AND SUBUNIT.
RX PubMed=14622286; DOI=10.1046/j.1432-1033.2003.03857.x;
RA Ladame S., Castilho M.S., Silva C.H.T.P., Denier C., Hannaert V., Perie J.,
RA Oliva G., Willson M.;
RT "Crystal structure of Trypanosoma cruzi glyceraldehyde-3-phosphate
RT dehydrogenase complexed with an analogue of 1,3-bisphospho-d-glyceric
RT acid.";
RL Eur. J. Biochem. 270:4574-4586(2003).
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. {ECO:0000269|PubMed:12044862,
CC ECO:0000269|PubMed:12795610, ECO:0000269|PubMed:14622286}.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- MISCELLANEOUS: There are two identical genes that code for glycosomal
CC GAPDH.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X52898; CAA37080.1; -; Genomic_DNA.
DR EMBL; X52898; CAA37079.1; -; Genomic_DNA.
DR PIR; S12565; DEUT1C.
DR PDB; 1K3T; X-ray; 1.95 A; A/B/C/D=1-359.
DR PDB; 1ML3; X-ray; 2.50 A; A/B/C/D=1-359.
DR PDB; 1QXS; X-ray; 2.75 A; A/B/C/D=1-359.
DR PDB; 3DMT; X-ray; 2.30 A; A/B/C/D=1-359.
DR PDB; 3IDS; X-ray; 1.80 A; A/B/C/D=1-359.
DR PDBsum; 1K3T; -.
DR PDBsum; 1ML3; -.
DR PDBsum; 1QXS; -.
DR PDBsum; 3DMT; -.
DR PDBsum; 3IDS; -.
DR AlphaFoldDB; P22513; -.
DR SMR; P22513; -.
DR BindingDB; P22513; -.
DR ChEMBL; CHEMBL5926; -.
DR DrugBank; DB02205; (+)-Rutamarin alcohol.
DR DrugBank; DB03211; (3-Formyl-but-3-Enyl)-Phosphonic Acid.
DR DrugBank; DB11820; Nifurtimox.
DR PRIDE; P22513; -.
DR VEuPathDB; TriTrypDB:BCY84_01123; -.
DR VEuPathDB; TriTrypDB:BCY84_01124; -.
DR VEuPathDB; TriTrypDB:BCY84_03946; -.
DR VEuPathDB; TriTrypDB:BCY84_03947; -.
DR VEuPathDB; TriTrypDB:BCY84_03948; -.
DR VEuPathDB; TriTrypDB:C3747_28g40; -.
DR VEuPathDB; TriTrypDB:C4B63_18g232; -.
DR VEuPathDB; TriTrypDB:C4B63_18g233; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_2044; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0027980; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM01054; -.
DR VEuPathDB; TriTrypDB:TcCLB.506943.60; -.
DR VEuPathDB; TriTrypDB:TcCLB.509065.60; -.
DR VEuPathDB; TriTrypDB:TCDM_02134; -.
DR VEuPathDB; TriTrypDB:TcG_01020; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_003325; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_003326; -.
DR VEuPathDB; TriTrypDB:TcYC6_0098240; -.
DR BRENDA; 1.2.1.12; 6524.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P22513; -.
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 1: Evidence at protein level;
KW 3D-structure; Glycolysis; Glycosome; NAD; Oxidoreductase; Peroxisome.
FT CHAIN 1..359
FT /note="Glyceraldehyde-3-phosphate dehydrogenase,
FT glycosomal"
FT /id="PRO_0000145532"
FT MOTIF 357..359
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 166
FT /note="Nucleophile"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12795610,
FT ECO:0000269|PubMed:14622286"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12795610,
FT ECO:0000269|PubMed:14622286"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12795610,
FT ECO:0000269|PubMed:14622286"
FT BINDING 134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12795610,
FT ECO:0000269|PubMed:14622286"
FT BINDING 165..167
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT BINDING 197
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT BINDING 226..227
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT BINDING 249
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT BINDING 335
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12795610,
FT ECO:0000269|PubMed:14622286"
FT SITE 194
FT /note="Activates thiol group during catalysis"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3IDS"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:3IDS"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1ML3"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3IDS"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3IDS"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3IDS"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:3IDS"
FT TURN 283..288
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:3IDS"
FT STRAND 324..333
FT /evidence="ECO:0007829|PDB:3IDS"
FT HELIX 337..356
FT /evidence="ECO:0007829|PDB:3IDS"
SQ SEQUENCE 359 AA; 39061 MW; 741ED29A4426453B CRC64;
MPIKVGINGF GRIGRMVFQA LCEDGLLGTE IDVVAVVDMN TDAEYFAYQM RYDTVHGKFK
YEVTTTKSSP SVAKDDTLVV NGHRILCVKA QRNPADLPWG KLGVEYVIES TGLFTAKAAA
EGHLRGGARK VVISAPASGG AKTLVMGVNH HEYNPSEHHV VSNASCTTNC LAPIVHVLVK
EGFGVQTGLM TTIHSYTATQ KTVDGVSVKD WRGGRAAAVN IIPSTTGAAK AVGMVIPSTQ
GKLTGMSFRV PTPDVSVVDL TFTAARDTSI QEIDAALKRA SKTYMKGILG YTDEELVSAD
FINDNRSSIY DSKATLQNNL PKERRFFKIV SWYDNEWGYS HRVVDLVRHM ASKDRSARL
