ALDH2_YEAST
ID ALDH2_YEAST Reviewed; 506 AA.
AC P47771; D6VZZ2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Aldehyde dehydrogenase [NAD(P)+] 1 {ECO:0000305};
DE EC=1.2.1.3 {ECO:0000269|PubMed:10407263, ECO:0000269|PubMed:12586697};
GN Name=ALD2; Synonyms=ALD5; OrderedLocusNames=YMR170C; ORFNames=YM8520.19C;
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 [GENOMIC DNA].
RC STRAIN=DBY939;
RX PubMed=8801420; DOI=10.1111/j.1365-2958.1995.mmi_17040653.x;
RA Miralles V.J., Serrano R.;
RT "A genomic locus in Saccharomyces cerevisiae with four genes up-regulated
RT by osmotic stress.";
RL Mol. Microbiol. 17:653-662(1995).
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [6]
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 [7]
RP INDUCTION.
RX PubMed=12794936; DOI=10.1002/yea.991;
RA Aranda A., del Olmo M.;
RT "Response to acetaldehyde stress in the yeast Saccharomyces cerevisiae
RT involves a strain-dependent regulation of several ALD genes and is mediated
RT by the general stress response pathway.";
RL Yeast 20:747-759(2003).
RN [8]
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. Required for 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:0000269|PubMed:11914276}.
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, ECO:0000269|PubMed:12794936}.
CC -!- MISCELLANEOUS: Present with 2070 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; X85987; CAA59975.1; -; Genomic_DNA.
DR EMBL; Z49705; CAA89806.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10066.1; -; Genomic_DNA.
DR PIR; S70189; S54615.
DR RefSeq; NP_013893.1; NM_001182674.1.
DR AlphaFoldDB; P47771; -.
DR SMR; P47771; -.
DR BioGRID; 35348; 53.
DR IntAct; P47771; 3.
DR MINT; P47771; -.
DR STRING; 4932.YMR170C; -.
DR MaxQB; P47771; -.
DR PaxDb; P47771; -.
DR PRIDE; P47771; -.
DR EnsemblFungi; YMR170C_mRNA; YMR170C; YMR170C.
DR GeneID; 855206; -.
DR KEGG; sce:YMR170C; -.
DR SGD; S000004780; ALD2.
DR VEuPathDB; FungiDB:YMR170C; -.
DR eggNOG; KOG2450; Eukaryota.
DR GeneTree; ENSGT00940000176434; -.
DR HOGENOM; CLU_005391_0_1_1; -.
DR InParanoid; P47771; -.
DR OMA; GDHTSYV; -.
DR BioCyc; MetaCyc:YMR170C-MON; -.
DR BioCyc; YEAST:YMR170C-MON; -.
DR PRO; PR:P47771; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P47771; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IMP:SGD.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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 Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 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)+] 1"
FT /id="PRO_0000056439"
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"
FT CONFLICT 23
FT /note="L -> C (in Ref. 1; CAA59975)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="S -> Q (in Ref. 1; CAA59975)"
FT /evidence="ECO:0000305"
FT CONFLICT 486..488
FT /note="QSG -> DNV (in Ref. 1; CAA59975)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> S (in Ref. 1; CAA59975)"
FT /evidence="ECO:0000305"
FT CONFLICT 500..501
FT /note="IN -> MD (in Ref. 1; CAA59975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 55188 MW; DD708CBD51BEAB39 CRC64;
MPTLYTDIEI PQLKISLKQP LGLFINNEFC PSSDGKTIET VNPATGEPIT SFQAANEKDV
DKAVKAARAA FDNVWSKTSS EQRGIYLSNL LKLIEEEQDT LAALETLDAG KPYHSNAKGD
LAQILQLTRY FAGSADKFDK GATIPLTFNK FAYTLKVPFG VVAQIVPWNY PLAMACWKLQ
GALAAGNTVI IKPAENTSLS LLYFATLIKK AGFPPGVVNI VPGYGSLVGQ ALASHMDIDK
ISFTGSTKVG GFVLEASGQS NLKDVTLECG GKSPALVFED ADLDKAIDWI AAGIFYNSGQ
NCTANSRVYV QSSIYDKFVE KFKETAKKEW DVAGKFDPFD EKCIVGPVIS STQYDRIKSY
IERGKREEKL DMFQTSEFPI GGAKGYFIPP TIFTDVPQTS KLLQDEIFGP VVVVSKFTNY
DDALKLANDT CYGLASAVFT KDVKKAHMFA RDIKAGTVWI NSSNDEDVTV PFGGFKMSGI
GRELGQSGVD TYLQTKAVHI NLSLDN
