ID   G9FQL4_9PEZI            Unreviewed;       144 AA.
AC   G9FQL4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:AEJ91744.1};
DE   Flags: Fragment;
GN   Name=GPD {ECO:0000313|EMBL:AEJ91744.1};
OS   Verticillium isaacii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=1051614 {ECO:0000313|EMBL:AEJ91744.1};
RN   [1] {ECO:0000313|EMBL:AEJ91744.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PD437 {ECO:0000313|EMBL:AEJ91744.1};
RX   PubMed=22174791; DOI=10.1371/journal.pone.0028341;
RA   Inderbitzin P., Bostock R.M., Davis R.M., Usami T., Platt H.W.,
RA   Subbarao K.V.;
RT   "Phylogenetics and taxonomy of the fungal vascular wilt pathogen
RT   verticillium, with the descriptions of five new species.";
RL   PLoS ONE 6:E28341-E28341(2011).
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; JN188159; AEJ91744.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9FQL4; -.
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   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; 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; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 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          1..129
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:AEJ91744.1"
FT   NON_TER         144
FT                   /evidence="ECO:0000313|EMBL:AEJ91744.1"
SQ   SEQUENCE   144 AA;  15474 MW;  A6F94F49941217BB CRC64;
     EHSDVEIVAV NDPFIETKYA AYMLKYDSTH GVFKGEITED GSSLTVNGKK VKFYQERDPA
     SIPWSETGAD YVVESTGVFT TTDKASAHIK GGAKKVIISA PSADAPMYVM GVNEKTYDGK
     ADVISNASCT TNCLAPLAKV INDK
//