IAH1_YEAST
ID IAH1_YEAST Reviewed; 238 AA.
AC P41734; D6W2I4; Q92313;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Isoamyl acetate-hydrolyzing esterase {ECO:0000303|Ref.2};
DE EC=3.1.1.112 {ECO:0000269|PubMed:10855721, ECO:0000269|PubMed:21069734, ECO:0000269|Ref.2};
GN Name=IAH1 {ECO:0000303|PubMed:10855721, ECO:0000312|EMBL:CAA63350.1};
GN Synonyms=EST2 {ECO:0000303|Ref.2};
GN OrderedLocusNames=YOR126C {ECO:0000312|EMBL:CAA99325.1,
GN ECO:0000312|EMBL:DAA10900.1};
GN ORFNames=O3287 {ECO:0000312|EMBL:CAA62126.1},
GN YOR3287C {ECO:0000312|EMBL:CAA64045.1};
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].
RA Proft M.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 204510 / AB320;
RA Fukuda K., Kuwahata O., Kiyokawa Y., Yanagiuchi T., Wakai Y., Kitamoto K.,
RA Inoue Y., Kimura A.;
RT "Molecular cloning and nucleotide sequence of the isoamyl acetate-
RT hydrolyzing esterase gene (EST2) from Saccharomyces cerevisiae.";
RL J. Ferment. Bioeng. 82:8-15(1996).
RN [3]
RP SEQUENCE REVISION.
RA Fukuda K.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=10855721; DOI=10.1007/s002530051662;
RA Fukuda K., Kiyokawa Y., Yanagiuchi T., Wakai Y., Kitamoto K., Inoue Y.,
RA Kimura A.;
RT "Purification and characterization of isoamyl acetate-hydrolyzing esterase
RT encoded by the IAH1 gene of Saccharomyces cerevisiae from a recombinant
RT Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 53:596-600(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, SUBUNIT, AND MUTAGENESIS OF 220-GLN--SER-238.
RX PubMed=21069734; DOI=10.1002/prot.22865;
RA Ma J., Lu Q., Yuan Y., Ge H., Li K., Zhao W., Gao Y., Niu L., Teng M.;
RT "Crystal structure of isoamyl acetate-hydrolyzing esterase from
RT Saccharomyces cerevisiae reveals a novel active site architecture and the
RT basis of substrate specificity.";
RL Proteins 79:662-668(2011).
CC -!- FUNCTION: Plays a crucial role in the hydrolysis of isoamyl acetate in
CC sake mash (Ref.2). Hydrolyzes short chain esters from acetate (C2) to
CC hexanoate (C6), showing more specificity for shorter chain exters. No
CC activity for decanoate (C10) esters (PubMed:21069734).
CC {ECO:0000269|PubMed:21069734, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutyl acetate + H2O = 3-methylbutanol + acetate +
CC H(+); Xref=Rhea:RHEA:60436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15837, ChEBI:CHEBI:30089, ChEBI:CHEBI:31725;
CC EC=3.1.1.112; Evidence={ECO:0000269|PubMed:10855721,
CC ECO:0000269|PubMed:21069734, ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40.3 mM for 3-mehtylbutyl acetate {ECO:0000269|PubMed:10855721};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:10855721};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10855721,
CC ECO:0000269|PubMed:21069734}.
CC -!- DISRUPTION PHENOTYPE: Accumulates approximately 19 times higher amounts
CC of isoamyl acetate compared to wild-type in laboratory scale sake
CC brewing. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. IAH1
CC subfamily. {ECO:0000305}.
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DR EMBL; X82930; CAA58104.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64045.1; -; Genomic_DNA.
DR EMBL; X92662; CAA63350.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62126.1; -; Genomic_DNA.
DR EMBL; Z75034; CAA99325.1; -; Genomic_DNA.
DR EMBL; AY557754; AAS56080.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10900.1; -; Genomic_DNA.
DR PIR; S49911; S49911.
DR RefSeq; NP_014769.3; NM_001183545.3.
DR PDB; 3MIL; X-ray; 1.60 A; A/B=1-238.
DR PDBsum; 3MIL; -.
DR AlphaFoldDB; P41734; -.
DR SMR; P41734; -.
DR BioGRID; 34521; 67.
DR STRING; 4932.YOR126C; -.
DR MaxQB; P41734; -.
DR PaxDb; P41734; -.
DR PRIDE; P41734; -.
DR EnsemblFungi; YOR126C_mRNA; YOR126C; YOR126C.
DR GeneID; 854293; -.
DR KEGG; sce:YOR126C; -.
DR SGD; S000005652; IAH1.
DR VEuPathDB; FungiDB:YOR126C; -.
DR eggNOG; KOG3035; Eukaryota.
DR GeneTree; ENSGT00390000008069; -.
DR HOGENOM; CLU_051989_0_3_1; -.
DR InParanoid; P41734; -.
DR OMA; FANGGWG; -.
DR BioCyc; MetaCyc:YOR126C-MON; -.
DR BioCyc; YEAST:YOR126C-MON; -.
DR BRENDA; 3.1.1.112; 984.
DR SABIO-RK; P41734; -.
DR EvolutionaryTrace; P41734; -.
DR PRO; PR:P41734; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P41734; protein.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:SGD.
DR GO; GO:0006083; P:acetate metabolic process; IDA:SGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR045136; Iah1-like.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR14209; PTHR14209; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..238
FT /note="Isoamyl acetate-hydrolyzing esterase"
FT /id="PRO_0000084126"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:21069734"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:21069734"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21069734"
FT SITE 53
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:21069734"
FT SITE 83
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:21069734"
FT MUTAGEN 220..238
FT /note="Missing: Hydrolyzes decanoate (C10) esters in
FT contrast to wild-type. Active also on short chain esters
FT from acetate (C2) to hexanoate (C6), but the catalytic
FT efficiency is lower than that of wild-type."
FT /evidence="ECO:0000269|PubMed:21069734"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:3MIL"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:3MIL"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:3MIL"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:3MIL"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:3MIL"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:3MIL"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:3MIL"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:3MIL"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3MIL"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3MIL"
FT TURN 234..238
FT /evidence="ECO:0007829|PDB:3MIL"
SQ SEQUENCE 238 AA; 27346 MW; 8C86C0B4CF49C50B CRC64;
MDYEKFLLFG DSITEFAFNT RPIEDGKDQY ALGAALVNEY TRKMDILQRG FKGYTSRWAL
KILPEILKHE SNIVMATIFL GANDACSAGP QSVPLPEFID NIRQMVSLMK SYHIRPIIIG
PGLVDREKWE KEKSEEIALG YFRTNENFAI YSDALAKLAN EEKVPFVALN KAFQQEGGDA
WQQLLTDGLH FSGKGYKIFH DELLKVIETF YPQYHPKNMQ YKLKDWRDVL DDGSNIMS
