ID K9M963_9TRYP Unreviewed; 293 AA.
AC K9M963;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glycosomal glyceraldehyde 3-phosphate dehydrogenase {ECO:0000313|EMBL:AFT63961.1};
DE Flags: Fragment;
GN Name=gGAPDH {ECO:0000313|EMBL:AFT63961.1};
OS Herpetomonas samuelpessoai.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Herpetomonas.
OX NCBI_TaxID=5715 {ECO:0000313|EMBL:AFT63961.1};
RN [1] {ECO:0000313|EMBL:AFT63961.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TCC005E {ECO:0000313|EMBL:AFT63961.1};
RX PubMed=22938923; DOI=10.1016/j.protis.2012.06.001;
RA Borghesan T.C., Ferreira R.C., Takata C.S., Campaner M., Borda C.C.,
RA Paiva F., Milder R.V., Teixeira M.M., Camargo E.P.;
RT "Molecular phylogenetic redefinition of herpetomonas (kinetoplastea,
RT trypanosomatidae), a genus of insect parasites associated with flies.";
RL Protist 164:129-152(2013).
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; JQ359743; AFT63961.1; -; Genomic_DNA.
DR AlphaFoldDB; K9M963; -.
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 1..136
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 136
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 8
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 135..137
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 167
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 196..197
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 219
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT SITE 164
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFT63961.1"
FT NON_TER 293
FT /evidence="ECO:0000313|EMBL:AFT63961.1"
SQ SEQUENCE 293 AA; 31408 MW; 9179322209F194EC CRC64;
FDVVAVVDMS TDAEYFAYQM KYDSVHGKPK YTVEVAKSSP SVKKPDVLVV NGHRIQCVKA
QRNPADLPWS KLGVEYVIES TGLFTNKAKA EGHLKGGAKK VIISAPASGG AKTIVMGVNN
QEYNPSSHSV VSNASCTTNC LAPLVHVLLK EGFGVETGLM TTIHSYTATQ KTVDGVSLKD
WRGGRAAAMN IIPSTTGAAK AVGEVLPVTK GKLTGMSFRV PTPDVSVVDL TFTAAKDTSI
KEIDEAFKRA SKTYMKGILS YTDEELVSSD FYNNNNSSIY DSKATLQNNL PGE
//
