G3P_CANAW
ID G3P_CANAW Reviewed; 335 AA.
AC Q92211; C4YP56;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
GN Name=TDH1; Synonyms=GAP, TDH3; ORFNames=CAWG_02997;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=9260938; DOI=10.1128/jb.179.16.4992-4999.1997;
RA Gil-Navarro I., Gil M.L., Casanova M., O'Connor J.E., Martinez J.P.,
RA Gozalbo D.;
RT "The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida
RT albicans is a surface antigen.";
RL J. Bacteriol. 179:4992-4999(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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. Secreted, cell wall.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U72203; AAC49800.1; -; Genomic_DNA.
DR EMBL; CM000310; EEQ44715.1; -; Genomic_DNA.
DR AlphaFoldDB; Q92211; -.
DR SMR; Q92211; -.
DR STRING; 5476.Q92211; -.
DR MoonDB; Q92211; Curated.
DR MoonProt; Q92211; -.
DR COMPLUYEAST-2DPAGE; Q92211; -.
DR PRIDE; Q92211; -.
DR EnsemblFungi; EEQ44715; EEQ44715; CAWG_02997.
DR VEuPathDB; FungiDB:CAWG_02997; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR OMA; NCVAPMA; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000001429; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0030312; C:external encapsulating structure; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 Cell wall; Cell wall biogenesis/degradation; Cytoplasm; Glycolysis; NAD;
KW Oxidoreductase; Secreted.
FT CHAIN 1..335
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145541"
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 104
FT /note="L -> V (in Ref. 1; AAC49800)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="V -> L (in Ref. 1; AAC49800)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="Q -> P (in Ref. 1; AAC49800)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="R -> K (in Ref. 1; AAC49800)"
FT /evidence="ECO:0000305"
FT CONFLICT 332..335
FT /note="Missing (in Ref. 1; AAC49800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 35833 MW; 24353A29CD3E332E CRC64;
MAIKIGINGF GRIGRLVLRV ALGRKDIEVV AVNDPFIAPD YAAYMFKYDS THGRYKGEVT
ASGDDLVIDG HKIKVFQERD PANIPWGKSG VDYVIESTGV FTKLEGAQKH IDAGAKKVII
TAPSADAPMF VVGVNEDKYT PDLKIISNAS CTTNCLAPLA KVVNDTFGIE EGLMTTVHSI
TATQKTVDGP SHKDWRGGRT ASGNIIPSST GAAKAVGKVI PELNGKLTGM SLRVPTTDVS
VVDLTVRLKK AASYEEIAQA IKKASEGPLK GVLGYTEDAV VSTDFLGSSY SSIFDEKAGI
LLSPTFVKLI SWYDNEYGYS TRVVDLLEHV AKASA
