ID Q5ISV0_9LECA Unreviewed; 279 AA.
AC Q5ISV0;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160};
DE Flags: Fragment;
GN Name=GAPD {ECO:0000313|EMBL:AAU14212.1};
OS Stictis radiata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Ostropomycetidae; Ostropales; Stictidaceae; Stictis.
OX NCBI_TaxID=38076 {ECO:0000313|EMBL:AAU14212.1};
RN [1] {ECO:0000313|EMBL:AAU14212.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MW6493 {ECO:0000313|EMBL:AAU14212.1};
RX AGRICOLA=IND43658945;
RA Wedin M., Doering H., Gilenstam G.;
RT "Saprotrophy and lichenization as options for the same fungal species on
RT different substrata: environmental plasticity and fungal lifestyles in the
RT Stictis-Conotrema complex.";
RL New Phytol. 164:459-465(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000256|RuleBase:RU361160};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869,
CC ECO:0000256|RuleBase:RU361160}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|RuleBase:RU361160}.
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; AY649852; AAU14212.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5ISV0; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
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, ECO:0000256|RuleBase:RU361160};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361160};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160}.
FT DOMAIN 2..131
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:AAU14212.1"
FT NON_TER 279
FT /evidence="ECO:0000313|EMBL:AAU14212.1"
SQ SEQUENCE 279 AA; 29820 MW; 1E4487922837A015 CRC64;
SIEHGAVNVV AVNDPFIEAH YAAYMLKYDS THGQFKGEIK VDGNDLIVNG QKVKFYQEKD
PANIPWSETG AYYVVESTGV FTTTDKAKAH LKGGAKKVVI SAPSADAPMF VMGVNEKSYK
SDIEVISNAS CTTNCLAPLA KVVHDNFTII EGLMTTIHSY TATQKTVDGP SAKDWRGGRT
AAQNIIPSST GAAKAVGKVI PSLNGKLTGM SMRVPTSNVS VVDLTCRLEK SVTYDQIKEA
IKKASDGELK GIMAYTEDEI VSTDLIGDNN SSIFDAKAG
//
