CUTI3_EMENI
ID CUTI3_EMENI Reviewed; 221 AA.
AC Q5AX00; C8VD42; Q1HFR8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Cutinase 3 {ECO:0000303|PubMed:30863878};
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE AltName: Full=Ancut3 {ECO:0000303|PubMed:30863878};
DE AltName: Full=Cutin hydrolase 3;
DE Flags: Precursor;
GN Name=cut3 {ECO:0000303|PubMed:30863878}; ORFNames=AN7180;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP INDUCTION.
RX PubMed=30863878; DOI=10.1007/s00253-019-09712-3;
RA Bermudez-Garcia E., Pena-Montes C., Martins I., Pais J., Pereira C.S.,
RA Sanchez S., Farres A.;
RT "Regulation of the cutinases expressed by Aspergillus nidulans and
RT evaluation of their role in cutin degradation.";
RL Appl. Microbiol. Biotechnol. 103:3863-3874(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (PubMed:16844780). Degrades cutin, a
CC macromolecule that forms the structure of the plant cuticle (By
CC similarity). Also degrades suberin, a specialized macromolecule found
CC in the cell wall of various plant tissues (By similarity).
CC {ECO:0000250|UniProtKB:Q5AVY9, ECO:0000250|UniProtKB:Q5B2C1,
CC ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-
CC ProRule:PRU10109};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC -!- INDUCTION: Constitutively expressed in a manner dependent on
CC transcription factor FarB: levels are unaffected by varying lipidic or
CC non-lipidic carbon source, or by oxidative stress.
CC {ECO:0000269|PubMed:30863878}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; DQ490506; ABF50882.1; -; mRNA.
DR EMBL; AACD01000122; EAA61432.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF78915.1; -; Genomic_DNA.
DR RefSeq; XP_664784.1; XM_659692.1.
DR AlphaFoldDB; Q5AX00; -.
DR SMR; Q5AX00; -.
DR CLAE; CUT5C_EMENI; -.
DR ESTHER; emeni-CUTI3; Cutinase.
DR EnsemblFungi; CBF78915; CBF78915; ANIA_07180.
DR EnsemblFungi; EAA61432; EAA61432; AN7180.2.
DR GeneID; 2869828; -.
DR KEGG; ani:AN7180.2; -.
DR VEuPathDB; FungiDB:AN7180; -.
DR eggNOG; ENOG502SI38; Eukaryota.
DR HOGENOM; CLU_040058_2_0_1; -.
DR InParanoid; Q5AX00; -.
DR OMA; VIGPPLC; -.
DR OrthoDB; 1227171at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050525; F:cutinase activity; IDA:UniProtKB.
DR GO; GO:0044275; P:cellular carbohydrate catabolic process; IDA:UniProtKB.
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 PANTHER; PTHR33630; PTHR33630; 1.
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 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..221
FT /note="Cutinase 3"
FT /id="PRO_0000395262"
FT ACT_SITE 133
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 188
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 201
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 55
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 134
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 44..122
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 70..84
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 184..191
FT /evidence="ECO:0000250|UniProtKB:P52956"
SQ SEQUENCE 221 AA; 23074 MW; 851820532CD96475 CRC64;
MRFHTILLAA LASLVIATPL PSDTDVSLER RQSMNSNDLE KGDCKSVAFI FARGSTEIGN
MGFVVGPGVC SNLKSTLGSD KVACQGVGGA YTAGLIQNAL PANTDSGSIK EAVKMFDLAA
KCPDTQIVAG GYSQGSAVID NAIQKLDDST RDRVKGVVLF GFTRNLQDKG QIPGYPKDQT
KVYCAVGDLV CSGTLIITAS HMTYGLNAGD AAKFLASQVS V
