ID   ARI1_YEAST              Reviewed;         347 AA.
AC   P53111; D6VTZ4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=NADPH-dependent aldehyde reductase ARI1;
DE            EC=1.1.1.-;
GN   Name=ARI1; OrderedLocusNames=YGL157W; ORFNames=G1857;
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].
RX   PubMed=8585324; DOI=10.1002/yea.320111409;
RA   James C.M., Indge K.J., Oliver S.G.;
RT   "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT   chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT   PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL   Yeast 11:1413-1419(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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.
RX   PubMed=14574691; DOI=10.1002/bit.10824;
RA   Katz M., Frejd T., Hahn-Hagerdal B., Gorwa-Grauslund M.F.;
RT   "Efficient anaerobic whole cell stereoselective bioreduction with
RT   recombinant Saccharomyces cerevisiae.";
RL   Biotechnol. Bioeng. 84:573-582(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
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).
RN   [7]
RP   INDUCTION, FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19577617; DOI=10.1016/j.gene.2009.06.018;
RA   Liu Z.L., Moon J.;
RT   "A novel NADPH-dependent aldehyde reductase gene from Saccharomyces
RT   cerevisiae NRRL Y-12632 involved in the detoxification of aldehyde
RT   inhibitors derived from lignocellulosic biomass conversion.";
RL   Gene 446:1-10(2009).
RN   [8]
RP   FUNCTION, AND COFACTOR.
RX   PubMed=20525870; DOI=10.1128/aem.00542-10;
RA   Bowman M.J., Jordan D.B., Vermillion K.E., Braker J.D., Moon J., Liu Z.L.;
RT   "Stereochemistry of furfural reduction by a Saccharomyces cerevisiae
RT   aldehyde reductase that contributes to in situ furfural detoxification.";
RL   Appl. Environ. Microbiol. 76:4926-4932(2010).
CC   -!- FUNCTION: NADPH-dependent aldehyde reductase involved in the
CC       detoxification of aldehyde inhibitors derived from lignocellulosic
CC       biomass conversion. Reduces commonly detected inhibitors in biomass
CC       conversion hydrolysates such as furfural, 5-hydroxymethylfurfural
CC       (HMF), cinnamic aldehyde, benzaldehyde, phenylacetaldehyde, and
CC       anisaldehyde. {ECO:0000269|PubMed:14574691,
CC       ECO:0000269|PubMed:19577617, ECO:0000269|PubMed:20525870}.
CC   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC         Evidence={ECO:0000269|PubMed:19577617, ECO:0000269|PubMed:20525870};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:19577617};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:19577617};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: By furfural and 5-hydroxymethylfurfural (HMF).
CC       {ECO:0000269|PubMed:19577617}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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   EMBL; Z48618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z72679; CAA96869.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07955.1; -; Genomic_DNA.
DR   PIR; S60428; S60428.
DR   RefSeq; NP_011358.3; NM_001181022.3.
DR   AlphaFoldDB; P53111; -.
DR   SMR; P53111; -.
DR   BioGRID; 33097; 61.
DR   DIP; DIP-5112N; -.
DR   IntAct; P53111; 8.
DR   MINT; P53111; -.
DR   STRING; 4932.YGL157W; -.
DR   iPTMnet; P53111; -.
DR   MaxQB; P53111; -.
DR   PaxDb; 4932-YGL157W; -.
DR   PeptideAtlas; P53111; -.
DR   EnsemblFungi; YGL157W_mRNA; YGL157W; YGL157W.
DR   GeneID; 852720; -.
DR   KEGG; sce:YGL157W; -.
DR   AGR; SGD:S000003125; -.
DR   SGD; S000003125; ARI1.
DR   VEuPathDB; FungiDB:YGL157W; -.
DR   eggNOG; KOG1502; Eukaryota.
DR   GeneTree; ENSGT00940000176317; -.
DR   HOGENOM; CLU_007383_9_2_1; -.
DR   InParanoid; P53111; -.
DR   OMA; HFNVQDP; -.
DR   OrthoDB; 1200131at2759; -.
DR   BioCyc; YEAST:G3O-30646-MONOMER; -.
DR   BioGRID-ORCS; 852720; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53111; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53111; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; IDA:SGD.
DR   GO; GO:0016491; F:oxidoreductase activity; IDA:SGD.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   CDD; cd05227; AR_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR   PANTHER; PTHR10366:SF853; NADPH-DEPENDENT ALDEHYDE REDUCTASE ARI1-RELATED; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; NADP; Nucleus; Oxidoreductase; Reference proteome.
FT   CHAIN           1..347
FT                   /note="NADPH-dependent aldehyde reductase ARI1"
FT                   /id="PRO_0000215578"
FT   BINDING         40
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   BINDING         169
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ   SEQUENCE   347 AA;  38083 MW;  51035AD526E418AD CRC64;
     MTTDTTVFVS GATGFIALHI MNDLLKAGYT VIGSGRSQEK NDGLLKKFNN NPKLSMEIVE
     DIAAPNAFDE VFKKHGKEIK IVLHTASPFH FETTNFEKDL LTPAVNGTKS ILEAIKKYAA
     DTVEKVIVTS STAALVTPTD MNKGDLVITE ESWNKDTWDS CQANAVAAYC GSKKFAEKTA
     WEFLKENKSS VKFTLSTINP GFVFGPQMFA DSLKHGINTS SGIVSELIHS KVGGEFYNYC
     GPFIDVRDVS KAHLVAIEKP ECTGQRLVLS EGLFCCQEIV DILNEEFPQL KGKIATGEPA
     TGPSFLEKNS CKFDNSKTKK LLGFQFYNLK DCIVDTAAQM LEVQNEA
//