ID R9QSN8_9AGAR Unreviewed; 184 AA.
AC R9QSN8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glyceraldehyde 3 phosphate dehydrogenase {ECO:0000313|EMBL:AGB76073.1};
DE Flags: Fragment;
GN Name=gpd {ECO:0000313|EMBL:AGB76073.1};
OS Tricholoma flavovirens.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Tricholomataceae;
OC Tricholoma.
OX NCBI_TaxID=80606 {ECO:0000313|EMBL:AGB76073.1};
RN [1] {ECO:0000313|EMBL:AGB76073.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=613 {ECO:0000313|EMBL:AGB76073.1}, and 614
RC {ECO:0000313|EMBL:AGB76074.1};
RX PubMed=22684294; DOI=10.3852/12-068;
RA Ota Y., Yamanaka T., Murata H., Neda H., Ohta A., Kawai M., Konno M.,
RA Tanaka C.;
RT "Phylogenetic relationship and species delimitation of matsutake and allied
RT species based on multilocus phylogeny and haplotype analyses.";
RL Mycologia 104:1369-1380(2012).
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; JQ697034; AGB76073.1; -; Genomic_DNA.
DR EMBL; JQ697035; AGB76074.1; -; Genomic_DNA.
DR AlphaFoldDB; R9QSN8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 50..182
FT /note="Glyceraldehyde 3-phosphate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF02800"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGB76073.1"
FT NON_TER 184
FT /evidence="ECO:0000313|EMBL:AGB76073.1"
SQ SEQUENCE 184 AA; 19151 MW; 8A97A872C13C819C CRC64;
RAAAHLNGGA KKVIISAPSA DAPMYVCGVN LDTYDSKHTI SNASCTTNCL APIAKVIHDK
FGIVEGLMST IHATTATQKT VDGPSNKDWR GGRSVNNNII PSSTGAAKAV GKVIPSLNGK
LTGLSFRVPT LDVSVVDLVV RLEKSASYDE IKAAVQEAAN GPFKGIIEYT DEAVVSADFV
GHTA
//