ID E0YN95_9BASI Unreviewed; 220 AA.
AC E0YN95;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) {ECO:0000256|ARBA:ARBA00013119};
DE EC=1.2.1.12 {ECO:0000256|ARBA:ARBA00013119};
DE Flags: Fragment;
GN Name=GPD {ECO:0000313|EMBL:ADM18870.1};
OS Sporobolomyces johnsonii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Sporobolomyces.
OX NCBI_TaxID=5002 {ECO:0000313|EMBL:ADM18870.1};
RN [1] {ECO:0000313|EMBL:ADM18870.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYCC 4351 {ECO:0000313|EMBL:ADM18870.1};
RX PubMed=20700437;
RA Coelho M.A., Sampaio J.P., Goncalves P.;
RT "A deviation from the bipolar-tetrapolar mating paradigm in an early
RT diverged basidiomycete.";
RL PLoS Genet. 6:e1001052-e1001052(2010).
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HM133826; ADM18870.1; -; Genomic_DNA.
DR AlphaFoldDB; E0YN95; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..79
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADM18870.1"
FT NON_TER 220
FT /evidence="ECO:0000313|EMBL:ADM18870.1"
SQ SEQUENCE 220 AA; 22865 MW; CF955EA5D19208C4 CRC64;
IDVYNERDPA AIPWGKSGAD YVVESTGVFT TKEKAGLHLK GGAKKVVISA PSADAPMYVC
GVNLDKYNPA DTVISNASCT TNCLAPLAKV LNDKFGIVEA LMTTVHATTA TQKTVDGPSA
KDWRGGRGAA ANIIPSSTGA AKAVGKVIPE LNGKLTGMAF RVPTSDVSVV DLTARIEKGA
SYDQIKAAMK EASETYLKGI LDYTEDAVVS TDFVGCTASS
//
