G3P_NEUCR
ID G3P_NEUCR Reviewed; 338 AA.
AC P54118; Q7RV61; Q8WZR2; Q92255;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
DE AltName: Full=Clock-controlled protein 7;
GN Name=gpd-1; Synonyms=ccg-7; ORFNames=B9G16.70, NCU01528;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sahni M., Kinsey J.A.;
RT "Identification and cloning of the Neurospora crassa glyceraldehyde-3-
RT phosphate dehydrogenase gene, gpd-1.";
RL Fungal Genet. Newsl. 44:47-49(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9417102; DOI=10.1074/jbc.273.1.446;
RA Shinohara M.L., Loros J.J., Dunlap J.C.;
RT "Glyceraldehyde-3-phosphate dehydrogenase is regulated on a daily basis by
RT the circadian clock.";
RL J. Biol. Chem. 273:446-452(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Clock-regulated. The peak of GAPDH activity lags
CC several hours behind the peak in mRNA accumulation in the late night.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U56397; AAB00570.1; -; mRNA.
DR EMBL; U67457; AAB95425.1; -; Genomic_DNA.
DR EMBL; AL670003; CAD21242.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA27741.1; -; Genomic_DNA.
DR PIR; T47218; T47218.
DR RefSeq; XP_956977.1; XM_951884.3.
DR AlphaFoldDB; P54118; -.
DR SMR; P54118; -.
DR STRING; 5141.EFNCRP00000001688; -.
DR PRIDE; P54118; -.
DR EnsemblFungi; EAA27741; EAA27741; NCU01528.
DR GeneID; 3873099; -.
DR KEGG; ncr:NCU01528; -.
DR VEuPathDB; FungiDB:NCU01528; -.
DR HOGENOM; CLU_030140_0_1_1; -.
DR InParanoid; P54118; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; IBA:GO_Central.
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 PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145563"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 150..152
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 210..211
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 178
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 78..79
FT /note="ER -> DA (in Ref. 1; AAB00570)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="A -> S (in Ref. 2; AAB95425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36292 MW; 07C6858F67C05F59 CRC64;
MVVKVGINGF GRIGRIVFRN AIEHDDIHIV AVNDPFIEPK YAAYMLRYDT THGNFKGTIE
VDGADLVVNG KKVKFYTERD PAAIPWSETG ADYIVESTGV FTTTEKASAH LKGGAKKVII
SAPSADAPMY VMGVNNETYD GSADVISNAS CTTNCLAPLA KVIHDNFTIV EGLMTTVHSY
TATQKTVDGP SAKDWRGGRT AAQNIIPSST GAAKAVGKVI PDLNGKLTGM AMRVPTANVS
VVDLTARIEK GATYDEIKEV IKKASEGPLA GILAYTEDEV VSSDMNGNPA SSIFDAKAGI
SLNKNFVKLV SWYDNEWGYS RRVLDLISYI SKVDAKKA
