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Database: UniProt
Entry: Q6X8M8_9LECA
LinkDB: Q6X8M8_9LECA
Original site: Q6X8M8_9LECA 
ID   Q6X8M8_9LECA            Unreviewed;       278 AA.
AC   Q6X8M8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 72.
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;
OS   Everniastrum sp. Feuerer s.n.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Parmeliaceae;
OC   Everniastrum.
OX   NCBI_TaxID=235859 {ECO:0000313|EMBL:AAP83270.1};
RN   [1] {ECO:0000313|EMBL:AAP83270.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Thell A., Feuerer T., Kaernefelt I., Myllys L., Stenroos S.;
RT   "Monphyletic groups within the Parmeliaceae identified by ITS rDNA,
RT   betatubulin and GAPDH sequences.";
RL   Mycol. Prog. 3:297-314(2004).
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; AY249613; AAP83270.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6X8M8; -.
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..130
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:AAP83270.1"
FT   NON_TER         278
FT                   /evidence="ECO:0000313|EMBL:AAP83270.1"
SQ   SEQUENCE   278 AA;  29873 MW;  8BADE4A894150FEB CRC64;
     VEHGEVKVVA VNDPFIEPHY AAYMLKYDSQ HGQFKGTIEV KGSDLVVNGQ TVKFYTEKDP
     ANIPWKDTGA YYIVESTGVF TTTEKAKAHL KGGAKKVVIS APSADAAMFV MGVNEKEYKS
     DIEVISNASC TTNCLAPLAK VMHDNYTIIE GLMTTIHSYT ATQKTVDGPS AKDWRGGRTA
     AQNIIPSSTG AAKAVGKVIP SLNGKLTGMS MRVPTSNVSV VDLTCRLEKS VTYDQIKETM
     KKASEGELKG IMSYSEDALV STDLNGDNHS CIFDATAG
//
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