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Database: UniProt
Entry: Q5ZPH1_9TRYP
LinkDB: Q5ZPH1_9TRYP
Original site: Q5ZPH1_9TRYP 
ID   Q5ZPH1_9TRYP            Unreviewed;       304 AA.
AC   Q5ZPH1;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Glycosomal glyceraldehyde phosphate dehydrogenase {ECO:0000313|EMBL:CAF04217.1};
DE   Flags: Fragment;
GN   Name=gGAPDH {ECO:0000313|EMBL:CAF04217.1};
OS   Trypanosoma mega.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=71805 {ECO:0000313|EMBL:CAF04217.1};
RN   [1] {ECO:0000313|EMBL:CAF04217.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC30038 {ECO:0000313|EMBL:CAF04217.1};
RX   PubMed=15542100; DOI=10.1016/j.ijpara.2004.08.011;
RA   Hamilton P.B., Stevens J.R., Gaunt M.W., Gidley J., Gibson W.C.;
RT   "Trypanosomes are monophyletic: evidence from genes for glyceraldehyde
RT   phosphate dehydrogenase and small subunit ribosomal RNA.";
RL   Int. J. Parasitol. 34:1393-1404(2004).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; AJ620253; CAF04217.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5ZPH1; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          6..145
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        145
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         71
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         144..146
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         176
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         205..206
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         228
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   SITE            173
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAF04217.1"
FT   NON_TER         304
FT                   /evidence="ECO:0000313|EMBL:CAF04217.1"
SQ   SEQUENCE   304 AA;  32591 MW;  4299BEEBFA33BDD0 CRC64;
     RIHGLLGTEI DVVAVVDMNT DAEYFAYQMK YDTVHGKFKY TVSTTKTDAS AAKDDTLVVN
     GHRILCVKAQ RNPADLPWGK LGVEYVIEST GLFTLKSAAE GHLKGGARKV VISAPASGGA
     KTLVMGVNHN EYNPSEHHVV SNASCTTNCL APIVHVMVKE GFGVQTGLMT TIHSYTATQK
     TVDGVSVKDW RGGRAAAVNI IPSTTGAAKA VGMVIPSTQG KLTGMSFRVP TPDVSVVDLT
     FTTTRDTSIK EIDAALKRAS ATYMKGILGY TDEELVSTDF INDNRSSIYD SKATLQNKGE
     FQHT
//
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