ID O15556_TRIVA Unreviewed; 324 AA.
AC O15556;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:AAC63597.1};
DE EC=1.2.1.12 {ECO:0000313|EMBL:AAC63597.1};
DE Flags: Fragment;
GN Name=gap2 {ECO:0000313|EMBL:AAC63597.1};
OS Trichomonas vaginalis.
OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC Trichomonas.
OX NCBI_TaxID=5722 {ECO:0000313|EMBL:AAC63597.1};
RN [1] {ECO:0000313|EMBL:AAC63597.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH-C1 ATCC 30001 {ECO:0000313|EMBL:AAC63597.1};
RX PubMed=9694668; DOI=10.1007/PL00006376;
RA Viscogliosi E., Muller M.;
RT "Phylogenetic relationships of the glycolytic enzyme, glyceraldehyde-3-
RT phosphate dehydrogenase, from parabasalid flagellates.";
RL J. Mol. Evol. 47:190-199(1998).
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; AF022414; AAC63597.1; -; Genomic_DNA.
DR AlphaFoldDB; O15556; -.
DR VEuPathDB; TrichDB:TVAG_347410; -.
DR VEuPathDB; TrichDB:TVAGG3_0358190; -.
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 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; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAC63597.1}.
FT DOMAIN 1..158
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 158
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 157..159
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 188
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 216..217
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 240
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT SITE 185
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAC63597.1"
FT NON_TER 324
FT /evidence="ECO:0000313|EMBL:AAC63597.1"
SQ SEQUENCE 324 AA; 34748 MW; 1EB0D19050B9720B CRC64;
GRLVFRACRK LYPKDVQVVA IHDLGDIKTN VYLLKYDTAH RAFPEPVTVD EEKQEFTVGE
GDDKWVVKSI GGRLGPSQLP WKELGIDVVL ESTGIFRSKA EVVDGKVTKD GYDGHIISGA
KKVVLSVPSA DEIECTLVLG VNDEDLKPET KCISNASCTT NCLGPVAKTL NNAFGIRNGF
MTTVHSYTND QVVADTMHKD LRRARAAGMN IIPTSTGAAI ALPKVCHGLP PKSLDGFALR
VPTITGSLVD LTVNVNAKVT KEEVNAALKK ATEEGSLKGI MTYVTDPIVS SDIIGCQYSS
IVDALSTKVL PNPEGQGTLV KVLS
//
