CUTI1_EMENI
ID CUTI1_EMENI Reviewed; 213 AA.
AC Q5B2C1; C8VGW9;
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 1 {ECO:0000303|PubMed:30863878};
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE AltName: Full=Ancut1 {ECO:0000303|PubMed:30863878};
DE AltName: Full=Cutin hydrolase 1;
DE Flags: Precursor;
GN Name=cut1 {ECO:0000303|PubMed:30863878}; ORFNames=AN5309;
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 [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 [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=25043916; DOI=10.1186/1471-2164-15-613;
RA Martins I., Hartmann D.O., Alves P.C., Martins C., Garcia H.,
RA Leclercq C.C., Ferreira R., He J., Renaut J., Becker J.D.,
RA Silva Pereira C.;
RT "Elucidating how the saprophytic fungus Aspergillus nidulans uses the plant
RT polyester suberin as carbon source.";
RL BMC Genomics 15:613-613(2014).
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 (By similarity). 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 (Probable).
CC {ECO:0000250|UniProtKB:Q5AVY9, ECO:0000305|PubMed:25043916}.
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:0000269|PubMed:25043916}.
CC -!- INDUCTION: Induced during growth on cutin, in a manner dependent on
CC transcription factors FarA and FarB (PubMed:30863878). Induced during
CC growth on suberin (PubMed:25043916). Induced during growth on the
CC lipidic carbon sources 16-hydroxyhexadecanoic acid and propyl
CC ricinoleate (synthetic cutin monomers), triacetin and triesterate
CC (triglycerides), and olive oil (PubMed:30863878). Repressed during
CC growth on glucose (PubMed:30863878). {ECO:0000269|PubMed:25043916,
CC ECO:0000269|PubMed:30863878}.
CC -!- SIMILARITY: Belongs to the cutinase family. {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; AACD01000093; EAA62469.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF82125.1; -; Genomic_DNA.
DR RefSeq; XP_662913.1; XM_657821.1.
DR AlphaFoldDB; Q5B2C1; -.
DR SMR; Q5B2C1; -.
DR ESTHER; emeni-q5b2c1; Cutinase.
DR EnsemblFungi; CBF82125; CBF82125; ANIA_05309.
DR EnsemblFungi; EAA62469; EAA62469; AN5309.2.
DR GeneID; 2871597; -.
DR KEGG; ani:AN5309.2; -.
DR VEuPathDB; FungiDB:AN5309; -.
DR eggNOG; ENOG502SI38; Eukaryota.
DR HOGENOM; CLU_040058_2_0_1; -.
DR InParanoid; Q5B2C1; -.
DR OMA; KIFCLPT; -.
DR OrthoDB; 1227171at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR GO; GO:0050525; F:cutinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044275; P:cellular carbohydrate catabolic process; IBA:GO_Central.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..213
FT /note="Cutinase 1"
FT /id="PRO_0000395260"
FT ACT_SITE 127
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 182
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 195
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 49
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 128
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 38..116
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 64..77
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 178..185
FT /evidence="ECO:0000250|UniProtKB:P52956"
SQ SEQUENCE 213 AA; 22413 MW; 731FB1B4E3F6DB2C CRC64;
MKLQLHLALS LLAAIVAANP IRLDQRQITG NELRDGSCHD VTFIFARGST ELGYLGSTVG
PATCNVLKLR KPGQVACQGV APAYIADLAS NFLPQGTNQI AINEAKSLFE LAASKCPNTK
IVAGGYSQGA AVMHAAISTL SSTVQDQIKG VVLFGDTRNK QDGGRIPNFP TDKTKIICAF
GDLVCEGTLV ITAAHLSYID DVPDAADFLV GKL
