ID C4B671_9EUKA Unreviewed; 324 AA.
AC C4B671;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 22-FEB-2023, entry version 49.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000313|EMBL:BAH59459.1};
DE Flags: Fragment;
GN Name=gapdh 2 {ECO:0000313|EMBL:BAH59459.1};
OS Macrotrichomonas sp. GsMG10.
OC Eukaryota; Metamonada; Parabasalia; Cristamonadida; Macrotrichomonas.
OX NCBI_TaxID=561883 {ECO:0000313|EMBL:BAH59459.1};
RN [1] {ECO:0000313|EMBL:BAH59459.1}
RP NUCLEOTIDE SEQUENCE.
RA Noda S., Mantini C., Bordereau C., Kitade O., Dolan M.F., Viscogliosi E.,
RA Ohkuma M.;
RT "Molecular phylogeny of parabasalids with emphasis on the order
RT Cristamonadida and its complex morphological evolution.";
RL Mol. Phylogenet. Evol. 52:217-224(2009).
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; AB458883; BAH59459.1; -; mRNA.
DR AlphaFoldDB; C4B671; -.
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 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:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43148; 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 2: Evidence at transcript level;
KW NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..134
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 134
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 133..135
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 164
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 192..193
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 216
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 304
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 161
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAH59459.1"
SQ SEQUENCE 324 AA; 34887 MW; 1716013D9DF04856 CRC64;
LCPIQTNVHL LKFDTAHKIW PEEIRQRGDD EFQVGEGPNA WVVKNGGGRV NPSQLPWRDL
GVDVVLESTG IFRKKAVVEN GEVKTDGYDG HIIAGAKRVV LSVPSADEIE CTLVLGVNDE
DLKPDTKNIS NASCTTNCLG PVVKVLNEAF GVFSGFMTTV HSYTNDQVVS DVMHADLRRA
RAAGQNIIPT STGAAIALPK VVKGLTPKSL DGLSLRVPTL TGSLVDLTVN LKKTVTVDDV
NNALIAATKR PELKGILVFS TDPLVSSDIV DNPASSIVDG LSTKVINTDG TSGSLVKVLS
WYDNEWMYSC RCADIFQKLG TFLK
//