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Database: UniProt
Entry: E2RZM8_TRITO
LinkDB: E2RZM8_TRITO
Original site: E2RZM8_TRITO 
ID   E2RZM8_TRITO            Unreviewed;       152 AA.
AC   E2RZM8;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 35.
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:BAJ23019.1};
OS   Trichophyton tonsurans (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34387 {ECO:0000313|EMBL:BAJ23019.1};
RN   [1] {ECO:0000313|EMBL:BAJ23019.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KMU 4872 {ECO:0000313|EMBL:BAJ23019.1};
RA   Kawasaki M., Anzawa K.;
RT   "Dermatophytes glyceraldehyde-3-phosphate gene partial cds.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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; AB573053; BAJ23019.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2RZM8; -.
DR   VEuPathDB; FungiDB:TESG_06829; -.
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; 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..117
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:BAJ23019.1"
FT   NON_TER         152
FT                   /evidence="ECO:0000313|EMBL:BAJ23019.1"
SQ   SEQUENCE   152 AA;  16722 MW;  1F6E1FDEFCDFC714 CRC64;
     PFIETKYAEY MLKYDSQHGQ FKDEISHEES SLVVGGKHIK FYAERDPANI KWSETGAEYI
     VESTGVFTTT EKASAHLKGG AKKVIISAPS ADAPMFVMGV NEEKYTADIQ VLSNASCTTN
     CLAPLAKVVH KNWGLKEGLM TTVHSYTATQ KT
//
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