ID   ALDH3_YEAST             Reviewed;         506 AA.
AC   P54114; D6VZZ1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Aldehyde dehydrogenase [NAD(P)+] 2 {ECO:0000305};
DE            EC=1.2.1.3 {ECO:0000269|PubMed:10407263, ECO:0000269|PubMed:12586697};
GN   Name=ALD3; Synonyms=ALD4; OrderedLocusNames=YMR169C;
GN   ORFNames=YM8520.18C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=10407263;
RX   DOI=10.1002/(sici)1097-0061(199907)15:10a<829::aid-yea423>3.0.co;2-9;
RA   Navarro-Avino J.P., Prasad R., Miralles V.J., Benito R.M., Serrano R.;
RT   "A proposal for nomenclature of aldehyde dehydrogenases in Saccharomyces
RT   cerevisiae and characterization of the stress-inducible ALD2 and ALD3
RT   genes.";
RL   Yeast 15:829-842(1999).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12586697; DOI=10.1093/genetics/163.1.69;
RA   White W.H., Skatrud P.L., Xue Z., Toyn J.H.;
RT   "Specialization of function among aldehyde dehydrogenases: the ALD2 and
RT   ALD3 genes are required for beta-alanine biosynthesis in Saccharomyces
RT   cerevisiae.";
RL   Genetics 163:69-77(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Cytoplasmic aldehyde dehydrogenase involved in ethanol
CC       oxidation. Involved in pantothenic acid production through the
CC       conversion of 3-aminopropanal to beta-alanine, an intermediate in
CC       pantothenic acid (vitamin B5) and coenzyme A (CoA) biosynthesis.
CC       {ECO:0000269|PubMed:10407263, ECO:0000269|PubMed:12586697}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:10407263,
CC         ECO:0000269|PubMed:12586697};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966,
CC         ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:10407263,
CC         ECO:0000269|PubMed:12586697};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696;
CC         Evidence={ECO:0000305|PubMed:12586697};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Expression is under the control of MSN2 and MSN4, and is
CC       induced during diauxic shift and osmotic stress.
CC       {ECO:0000269|PubMed:10407263}.
CC   -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; Z49705; CAA89805.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10065.1; -; Genomic_DNA.
DR   PIR; S54527; S54527.
DR   RefSeq; NP_013892.1; NM_001182673.1.
DR   AlphaFoldDB; P54114; -.
DR   SMR; P54114; -.
DR   BioGRID; 35347; 47.
DR   MINT; P54114; -.
DR   STRING; 4932.YMR169C; -.
DR   iPTMnet; P54114; -.
DR   MaxQB; P54114; -.
DR   PaxDb; 4932-YMR169C; -.
DR   PeptideAtlas; P54114; -.
DR   EnsemblFungi; YMR169C_mRNA; YMR169C; YMR169C.
DR   GeneID; 855205; -.
DR   KEGG; sce:YMR169C; -.
DR   AGR; SGD:S000004779; -.
DR   SGD; S000004779; ALD3.
DR   VEuPathDB; FungiDB:YMR169C; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   GeneTree; ENSGT00940000176434; -.
DR   HOGENOM; CLU_005391_0_1_1; -.
DR   InParanoid; P54114; -.
DR   OMA; GTYAINW; -.
DR   OrthoDB; 216092at2759; -.
DR   BioCyc; MetaCyc:YMR169C-MONOMER; -.
DR   BioCyc; YEAST:YMR169C-MONOMER; -.
DR   BioGRID-ORCS; 855205; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P54114; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P54114; Protein.
DR   GO; GO:0005737; C:cytoplasm; ISS:SGD.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:SGD.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019483; P:beta-alanine biosynthetic process; IMP:SGD.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006598; P:polyamine catabolic process; IMP:SGD.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR43720; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43720:SF2; 2-AMINOMUCONIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; NAD; Oxidoreductase; Pantothenate biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..506
FT                   /note="Aldehyde dehydrogenase [NAD(P)+] 2"
FT                   /id="PRO_0000056440"
FT   ACT_SITE        268
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        302
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   SITE            169
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   506 AA;  55385 MW;  11687E520B7E97DD CRC64;
     MPTLYTDIEI PQLKISLKQP LGLFINNEFC PSSDGKTIET VNPATGEPIT SFQAANEKDV
     DKAVKAARAA FDNVWSKTSS EQRGIYLSNL LKLIEEEQDT LAALETLDAG KPFHSNAKQD
     LAQIIELTRY YAGAVDKFNM GETIPLTFNK FAYTLKVPFG VVAQIVPWNY PLAMACRKMQ
     GALAAGNTVI IKPAENTSLS LLYFATLIKK AGFPPGVVNV IPGYGSVVGK ALGTHMDIDK
     ISFTGSTKVG GSVLEASGQS NLKDITLECG GKSPALVFED ADLDKAIEWV ANGIFFNSGQ
     ICTANSRVYV QSSIYDKFVE KFKETAKKEW DVAGKFDPFD EKCIVGPVIS STQYDRIKSY
     IERGKKEEKL DMFQTSEFPI GGAKGYFIPP TIFTDVPETS KLLRDEIFGP VVVVSKFTNY
     DDALKLANDT CYGLASAVFT KDVKKAHMFA RDIKAGTVWI NQTNQEEAKV PFGGFKMSGI
     GRESGDTGVD NYLQIKSVHV DLSLDK
//