CUTI1_HYPJQ
ID CUTI1_HYPJQ Reviewed; 248 AA.
AC G0RH85;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Cutinase {ECO:0000255|RuleBase:RU361263};
DE EC=3.1.1.74 {ECO:0000255|RuleBase:RU361263};
DE Flags: Precursor;
GN ORFNames=TRIREDRAFT_60489 {ECO:0000312|EMBL:EGR49371.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000312|Proteomes:UP000008984};
RN [1] {ECO:0000312|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000312|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (By similarity). Degrades cutin, a
CC macromolecule that forms the structure of the plant cuticle (By
CC similarity). {ECO:0000250|UniProtKB:A0A024SC78}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000255|RuleBase:RU361263};
CC -!- ACTIVITY REGULATION: Weakly inhibited by n-undecyl phosphonate (C11Y4)
CC (By similarity). Activity unaffected by paraoxon (By similarity).
CC {ECO:0000250|UniProtKB:A0A024SC78}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}.
CC -!- DOMAIN: In contract to classical cutinases, possesses a lid formed by
CC two N-terminal helices which covers its active site (By similarity).
CC The lid opens in the presence of surfactants to uncover the catalytic
CC crevice, allowing enzyme activity and inhibition (By similarity).
CC {ECO:0000250|UniProtKB:A0A024SC78}.
CC -!- SIMILARITY: Belongs to the cutinase family.
CC {ECO:0000255|RuleBase:RU361263}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGR49371.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GL985062; EGR49371.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006964533.1; XM_006964471.1.
DR SMR; G0RH85; -.
DR ESTHER; hypjq-g0rh85; Cutinase.
DR EnsemblFungi; EGR49371; EGR49371; TRIREDRAFT_60489.
DR GeneID; 18486631; -.
DR KEGG; tre:TRIREDRAFT_60489; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_60489; -.
DR eggNOG; ENOG502S3AW; Eukaryota.
DR HOGENOM; CLU_040058_2_2_1; -.
DR BRENDA; 3.1.1.3; 6451.
DR BRENDA; 3.1.1.74; 6451.
DR Proteomes; UP000008984; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR InterPro; IPR043580; CUTINASE_1.
DR InterPro; IPR043579; CUTINASE_2.
DR InterPro; IPR011150; Cutinase_monf.
DR Pfam; PF01083; Cutinase; 1.
DR PRINTS; PR00129; CUTINASE.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00155; CUTINASE_1; 1.
DR PROSITE; PS00931; CUTINASE_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..28
FT /evidence="ECO:0000250|UniProtKB:A0A024SC78"
FT /id="PRO_0000455278"
FT CHAIN 29..248
FT /note="Cutinase"
FT /id="PRO_0000455279"
FT REGION 31..70
FT /note="Lid covering the active site of the uncomplexed
FT enzyme"
FT /evidence="ECO:0000250|UniProtKB:A0A024SC78"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 216
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 229
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 90
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:A0A024SC78"
FT SITE 165
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:A0A024SC78"
FT DISULFID 55..91
FT /evidence="ECO:0000250|UniProtKB:A0A024SC78"
FT DISULFID 79..153
FT /evidence="ECO:0000250|UniProtKB:A0A024SC78"
FT DISULFID 212..219
FT /evidence="ECO:0000250|UniProtKB:A0A024SC78"
SQ SEQUENCE 248 AA; 25924 MW; 1FE2B82328641D42 CRC64;
MRSLAILTTL LAGHAFAYPK PAPQSVNRRD WPSINEFLSE LAKVMPIGDT ITAACDLISD
GEDAAASLFG ISETENDPCG DVTVLFARGT CDPGNVGVLV GPWFFDSLQT ALGSRTLGVK
GVPYPASVQD FLSGSVQNGI NMANQIKSVL QSCPNTKLVL GGYSQGSMVV HNAASNLDAA
TMSKISAVVL FGDPYYGKPV ANFDAAKTLV VCHDGDNICQ GGDIILLPHL TYAEDADTAA
AFVVPLVS
