ID   D2SRN5_9AGAR            Unreviewed;       144 AA.
AC   D2SRN5;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:ACN38767.1};
DE   Flags: Fragment;
GN   Name=gpd {ECO:0000313|EMBL:ACN38767.1};
OS   Armillaria heimii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=108573 {ECO:0000313|EMBL:ACN38767.1};
RN   [1] {ECO:0000313|EMBL:ACN38767.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K59 {ECO:0000313|EMBL:ACN38767.1};
RA   Stefani F.O.P., Berube J.A., Hamelin R.C.;
RT   "Phylogeny and phylogeography of Armillaria related-species inferred from
RT   four coding genes.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406}.
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DR   EMBL; FJ618687; ACN38767.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2SRN5; -.
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   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..143
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02800"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACN38767.1"
FT   NON_TER         144
FT                   /evidence="ECO:0000313|EMBL:ACN38767.1"
SQ   SEQUENCE   144 AA;  15122 MW;  67CAE98F149BC46D CRC64;
     ALMSTIHATT ATQKTVDGPS NKDWRGGRGV NNNIIPSSTG AAKAVGKVIP SLNGKLTGLA
     FRVPTSDVSV VDLVARIEKE ASYDDIKAAI KEAASSGPLK GIIEYTEDAV VSTDFVGHSA
     SSIFDAKAGI QLNKNFVKLV SWYD
//