G3P3_KLUMA
ID G3P3_KLUMA Reviewed; 331 AA.
AC P84999;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 3;
DE Short=GAPDH 3;
DE EC=1.2.1.12;
GN Name=GAP3 {ECO:0000303|PubMed:7668042};
OS Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=4911;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665
RC {ECO:0000269|PubMed:7668042};
RX PubMed=7668042; DOI=10.1002/yea.320110804;
RA Fernandes P.A., Sena-Esteves M., Moradas-Ferreira P.;
RT "Characterization of the glyceraldehyde-3-phosphate dehydrogenase gene
RT family from Kluyveromyces marxianus -- polymerase chain reaction-single-
RT strand conformation polymorphism as a tool for the study of multigenic
RT families.";
RL Yeast 11:725-733(1995).
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 ECO:0000269|PubMed:7668042};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:7668042}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P22513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00359}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S57281; S57281.
DR AlphaFoldDB; P84999; -.
DR SMR; P84999; -.
DR PRIDE; P84999; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0030312; C:external encapsulating structure; IEA:UniProt.
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 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.
FT CHAIN 1..331
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 3"
FT /id="PRO_0000253991"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P22513,
FT ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 148..150
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 179
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 208..209
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 231
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT SITE 176
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00359"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00359"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00359"
SQ SEQUENCE 331 AA; 35524 MW; 5E09084264795F01 CRC64;
MVRIAINGFG RIGRLVLRIA LSRKNIEVVA INDPFITVDY AAYMFKYDST HGRFDGEVSH
DGKALIIDGK KVLVFQERDP ATLPWGAEKI DIAIDSTGIF KELDSAQKHI DAGAKKVVIT
APSSTAPMFV VGVNEDKYAG QTIVSNASCT TNCLAPLAKI INNAFGIEEG LMTTVHSITA
TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTVDVSVV
DLTVKLAKPA TYEEIKAVVK KASENELKGV MGYTEDAVVS SDFLGDTHSS IFDAAAGIQL
SPQFVKLVSW YDNEFGYSTR VVDLVELVAK N
