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Database: UniProt
Entry: C4B671_9EUKA
LinkDB: C4B671_9EUKA
Original site: C4B671_9EUKA 
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
//
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