ID D0VB35_9AGAR Unreviewed; 177 AA.
AC D0VB35;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:ACY07004.1};
OS Tricholoma inocybeoides.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Tricholomataceae;
OC Tricholoma.
OX NCBI_TaxID=547464 {ECO:0000313|EMBL:ACY07004.1};
RN [1] {ECO:0000313|EMBL:ACY07004.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lille06.2 {ECO:0000313|EMBL:ACY07004.1};
RX PubMed=21044190; DOI=10.1111/j.1365-294X.2010.04863.x;
RA Jargeat P., Martos F., Carriconde F., Gryta H., Moreau P.A., Gardes M.;
RT "Phylogenetic species delimitation in ectomycorrhizal fungi and
RT implications for barcoding: the case of the Tricholoma scalpturatum complex
RT (Basidiomycota).";
RL Mol. Ecol. 19:5216-5230(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}.
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DR EMBL; GU060204; ACY07004.1; -; Genomic_DNA.
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 3..57
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:ACY07004.1"
FT NON_TER 177
FT /evidence="ECO:0000313|EMBL:ACY07004.1"
SQ SEQUENCE 177 AA; 18649 MW; 6418C2C1F6A7EEAD CRC64;
RTSRIFMLIS GDRAKGHLDG GAKKVIISAP SADAPMYVCG VNLDKYDSKH SISNASCTTN
CLAPIAKVIH DKFGIIEGLM STIHATTATQ KTVDGPSSKD WRGGRSVNNN IIPXSTGAAK
AVGKVIPSLN GKLTGLAFRV PTLDVSVVDL VVRLEKSATY DEIKTAVKEA SEGDLRG
//
