IAH1_SCHPO
ID IAH1_SCHPO Reviewed; 246 AA.
AC O74648;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Isoamyl acetate-hydrolyzing esterase;
DE EC=3.1.1.112 {ECO:0000250|UniProtKB:P41734};
GN Name=iah1; ORFNames=SPCC126.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawamukai M.;
RT "S.pombe IAH1 homolog.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000250|UniProtKB:P41734};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. IAH1
CC 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; AB017605; BAA33369.1; -; mRNA.
DR EMBL; CU329672; CAA22479.1; -; Genomic_DNA.
DR PIR; T43421; T43421.
DR RefSeq; NP_588453.1; NM_001023444.2.
DR AlphaFoldDB; O74648; -.
DR SMR; O74648; -.
DR BioGRID; 275634; 4.
DR STRING; 4896.SPCC126.10.1; -.
DR MaxQB; O74648; -.
DR PaxDb; O74648; -.
DR EnsemblFungi; SPCC126.10.1; SPCC126.10.1:pep; SPCC126.10.
DR GeneID; 2539062; -.
DR KEGG; spo:SPCC126.10; -.
DR PomBase; SPCC126.10; iah1.
DR VEuPathDB; FungiDB:SPCC126.10; -.
DR eggNOG; KOG3035; Eukaryota.
DR HOGENOM; CLU_051989_0_0_1; -.
DR InParanoid; O74648; -.
DR OMA; FANGGWG; -.
DR PhylomeDB; O74648; -.
DR PRO; PR:O74648; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; ISO:PomBase.
DR GO; GO:0006083; P:acetate metabolic process; ISO:PomBase.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; NAS:PomBase.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..246
FT /note="Isoamyl acetate-hydrolyzing esterase"
FT /id="PRO_0000314106"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT SITE 78
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P41734"
FT SITE 108
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P41734"
SQ SEQUENCE 246 AA; 27991 MW; DBE6BFCD6359E78B CRC64;
MSDSQDKNYI SFEKTEIGQI VSEAPAEKYV SFQKKYFNRL TIIGDSITQK GFTPGGYCAE
LMNFYQRRLR VDVWGFSGYT SRHVLRYLPE IPLEIDSTKL LIVFLGTNDC QLTETGYMCP
VDEFKNNLLA LTRPFPHSKI IIVSPGICTK DICFKREQEP YVIAASETVN TLNKSKANSA
GLINLYEITK SYPTPELLFT DGLHFSSLGY SLLFNEIVAT ISKAWPELLP NNLPLQFPHW
SEILFT
