ID H6W9R0_SCLSC Unreviewed; 234 AA.
AC H6W9R0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=g3pdh {ECO:0000313|EMBL:AEY84445.1};
OS Sclerotinia sclerotiorum (White mold) (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=5180 {ECO:0000313|EMBL:AEY84445.1};
RN [1] {ECO:0000313|EMBL:AEY84445.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1980 {ECO:0000313|EMBL:AEY84445.1}, LMK57
RC {ECO:0000313|EMBL:AEY84444.1}, and LMK754
RC {ECO:0000313|EMBL:AEY84443.1};
RX PubMed=22253834; DOI=10.1371/journal.pone.0029943;
RA Andrew M., Barua R., Short S.M., Kohn L.M.;
RT "Evidence for a common toolbox based on necrotrophy in a fungal lineage
RT spanning necrotrophs, biotrophs, endophytes, host generalists and
RT specialists.";
RL PLoS ONE 7:E29943-E29943(2012).
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 -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR EMBL; JQ036046; AEY84443.1; -; Genomic_DNA.
DR EMBL; JQ036047; AEY84444.1; -; Genomic_DNA.
DR EMBL; JQ036048; AEY84445.1; -; Genomic_DNA.
DR AlphaFoldDB; H6W9R0; -.
DR VEuPathDB; FungiDB:sscle_11g083230; -.
DR UniPathway; UPA00109; UER00184.
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 Pfam; PF00044; Gp_dh_N; 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..109
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:AEY84445.1"
FT NON_TER 234
FT /evidence="ECO:0000313|EMBL:AEY84445.1"
SQ SEQUENCE 234 AA; 24985 MW; EFD993D647B7BEB5 CRC64;
AYMLKYDSTH GQFKGDIKVL SDGLEVNGKK VKFYTERDPA NIPWAESEAY YVVESTGVFT
TTEKAKAHLK GGAKKVVISA PSADAPMYVM GVNNETYNGE ADVISNASCT TNCLAPLAKV
INDEFTIIEG LMTTIHSYTA TQKTVDGPSA KDWRGGRTAA QNIIPSSTGA AKAVGKVIPE
LNGKLTGMSM RVPTANVSVV DLTVRIEKAA SYDEIKEVIK KAANGPLKGI LAYT
//
