G3P_PHARH
ID G3P_PHARH Reviewed; 338 AA.
AC O13507; Q9UVD2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
GN Name=GPD;
OS Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Cystofilobasidiales; Mrakiaceae; Phaffia.
OX NCBI_TaxID=264483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96594 / BCRC 22365 / CBS 6938 / JCM 9684 / VKM Y-2793;
RX PubMed=9364747;
RX DOI=10.1002/(sici)1097-0061(199710)13:13<1231::aid-yea171>3.0.co;2-q;
RA Verdoes J.C., Wery J., Boekhout T., van Ooyen A.J.J.;
RT "Molecular characterization of the glyceraldehyde-3-phosphate dehydrogenase
RT gene of Phaffia rhodozyma.";
RL Yeast 13:1231-1242(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=67-385;
RA Choi E.S., Nam S.G., Kim I.G., Rhee S.K.;
RT "Isolation and characterization of the gene encoding glyceraldehyde-3-
RT phosphate dehydrogenase Of Phaffia rhodozyma.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Y08366; CAA69652.1; -; Genomic_DNA.
DR EMBL; AF006483; AAF21599.1; -; Genomic_DNA.
DR AlphaFoldDB; O13507; -.
DR SMR; O13507; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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 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 3: Inferred from homology;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT CHAIN 1..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145568"
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 316
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 160
FT /note="G -> A (in Ref. 2; AAF21599)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="G -> A (in Ref. 2; AAF21599)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="G -> A (in Ref. 2; AAF21599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36083 MW; 871FDB51D48B7F43 CRC64;
MAVKVGINGF GRIGRIVLRN AIIHGDIDVV AINDPFIDLE YMVYMFKYDS THGVFKGSVE
IKDGKLVIEG KPIVVYGERD PANIQWGAAG ADYVVESTGV FTTQEKAELH LKGGAKKVVI
SAPSADAPMF VCGVNLDKYD PKYTVVSNAS CTTNCLAPLG KVIHDNYTIV EGLMTTVHAT
TATQKTVDGP SNKDWRGGRG AGANIIPSST GAAKAVGKVI PSLNGKLTGM AFRVPTPDVS
VVDLVVRIEK GASYEEIKET IKKASQTPEL KGILNYTDDQ VVSTDFTGDS ASSTFDAQGG
ISLNGNFVKL VSWYDNEWGY SARVCDLVSY IAAQDAKA
