AAD16_YEAST
ID AAD16_YEAST Reviewed; 342 AA.
AC Q02895; D6W3S9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative aryl-alcohol dehydrogenase AAD16 {ECO:0000303|PubMed:10581269};
DE EC=1.1.1.-;
GN Name=AAD16 {ECO:0000303|PubMed:10581269};
GN OrderedLocusNames=YPL088W {ECO:0000312|SGD:S000006009};
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 GENE NAME.
RX PubMed=10581269; DOI=10.1093/genetics/153.4.1591;
RA Delneri D., Gardner D.C.J., Oliver S.G.;
RT "Analysis of the seven-member AAD gene set demonstrates that genetic
RT redundancy in yeast may be more apparent than real.";
RL Genetics 153:1591-1600(1999).
RN [4]
RP INDUCTION.
RX PubMed=11909958; DOI=10.1128/mcb.22.8.2642-2649.2002;
RA Le Crom S., Devaux F., Marc P., Zhang X., Moye-Rowley W.S., Jacq C.;
RT "New insights into the pleiotropic drug resistance network from genome-wide
RT characterization of the YRR1 transcription factor regulation system.";
RL Mol. Cell. Biol. 22:2642-2649(2002).
RN [5]
RP INDUCTION.
RX PubMed=15116342; DOI=10.1002/yea.1109;
RA Boorsma A., de Nobel H., ter Riet B., Bargmann B., Brul S.,
RA Hellingwerf K.J., Klis F.M.;
RT "Characterization of the transcriptional response to cell wall stress in
RT Saccharomyces cerevisiae.";
RL Yeast 21:413-427(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Putative aryl-alcohol dehydrogenase. {ECO:0000250}.
CC -!- INDUCTION: By cell wall stress and the YRR1 transcription factor.
CC {ECO:0000269|PubMed:11909958, ECO:0000269|PubMed:15116342}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; U43281; AAB68211.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11345.1; -; Genomic_DNA.
DR PIR; S61978; S61978.
DR RefSeq; NP_015237.1; NM_001183902.1.
DR AlphaFoldDB; Q02895; -.
DR SMR; Q02895; -.
DR BioGRID; 36093; 43.
DR DIP; DIP-4021N; -.
DR IntAct; Q02895; 11.
DR MINT; Q02895; -.
DR STRING; 4932.YPL088W; -.
DR PaxDb; Q02895; -.
DR PRIDE; Q02895; -.
DR EnsemblFungi; YPL088W_mRNA; YPL088W; YPL088W.
DR GeneID; 856017; -.
DR KEGG; sce:YPL088W; -.
DR SGD; S000006009; YPL088W.
DR VEuPathDB; FungiDB:YPL088W; -.
DR eggNOG; KOG1575; Eukaryota.
DR GeneTree; ENSGT01000000220103; -.
DR HOGENOM; CLU_023205_2_0_1; -.
DR InParanoid; Q02895; -.
DR OMA; VDLWQVH; -.
DR BioCyc; YEAST:G3O-33993-MON; -.
DR PRO; PR:Q02895; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02895; protein.
DR GO; GO:0047681; F:aryl-alcohol dehydrogenase (NADP+) activity; ISS:SGD.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:SGD.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..342
FT /note="Putative aryl-alcohol dehydrogenase AAD16"
FT /id="PRO_0000238634"
SQ SEQUENCE 342 AA; 39683 MW; E99B1EB62FC880B1 CRC64;
MVLVKQVRLG NSGLKISPIV IGCMSYGSKK WADWVIEDKT QIFKIMKHCY DKGLRTFDTA
DFYSNGLSER IIKEFLEYYS IKRETVVIMT KIYFPVDETL DLHHNFTLNE FEELDLSNQR
GLSRKHIIAG VENSVKRLGT YIDLLQIHRL DHETPMKEIM KALNDVVEAG HVRYIGASSM
LATEFAELQF TADKYGWFQF ISSQSYYNLL YREDERELIP FAKRHNIGLL PWSPNARGML
TRPLNQSTDR IKSDPTFKSL HLDNLEEEQK EIINRVEKVS KDKKVSMAML SIAWVLHKGC
HPIVGLNTTA RVDEAIAALQ VTLTEEEIKY LEEPYKPQRQ RC
