CUTI2_EMENI
ID CUTI2_EMENI Reviewed; 255 AA.
AC Q5AVY9; C8VBM7; Q1HFR3;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cutinase 2 {ECO:0000303|PubMed:30863878};
DE EC=3.1.1.74 {ECO:0000269|PubMed:22238011, ECO:0000269|PubMed:28124733};
DE AltName: Full=Ancut2 {ECO:0000303|PubMed:22238011};
DE AltName: Full=Cutin hydrolase 2;
DE Flags: Precursor;
GN Name=cut2 {ECO:0000303|PubMed:22238011}; ORFNames=AN7541;
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 FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=22238011; DOI=10.1007/s12010-011-9513-7;
RA Castro-Ochoa D., Pena-Montes C., Gonzalez-Canto A., Alva-Gasca A.,
RA Esquivel-Bautista R., Navarro-Ocana A., Farres A.;
RT "ANCUT2, an extracellular cutinase from Aspergillus nidulans induced by
RT olive oil.";
RL Appl. Biochem. Biotechnol. 166:1275-1290(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, AND BIOTECHNOLOGY.
RX PubMed=28124733; DOI=10.1007/s12010-016-2378-z;
RA Bermudez-Garcia E., Pena-Montes C., Castro-Rodriguez J.A.,
RA Gonzalez-Canto A., Navarro-Ocana A., Farres A.;
RT "ANCUT2, a Thermo-alkaline Cutinase from Aspergillus nidulans and Its
RT Potential Applications.";
RL Appl. Biochem. Biotechnol. 182:1014-1036(2017).
RN [6]
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, PubMed:22238011,
CC PubMed:28124733). Degrades cutin, a macromolecule that forms the
CC structure of the plant cuticle (PubMed:22238011, PubMed:28124733). Also
CC degrades suberin, a specialized macromolecule found in the cell wall of
CC various plant tissues (By similarity). {ECO:0000250|UniProtKB:Q5B2C1,
CC ECO:0000269|PubMed:16844780, ECO:0000269|PubMed:22238011,
CC ECO:0000269|PubMed:28124733}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000269|PubMed:22238011, ECO:0000269|PubMed:28124733};
CC -!- ACTIVITY REGULATION: Partially inhibited by the serine protease
CC inhibitor phenylmethanesulfonyl fluoride (PubMed:28124733). Inhibited
CC by various ions, including copper, iron, sodium, potassium, magnesium
CC and calcium (PubMed:28124733). Inhibited by the chelating agent EDTA
CC (ethylenediaminetetraacetic acid) (PubMed:28124733). Inhibited by the
CC surfactants sodium dodecyl sulfate and polysorbate 80
CC (PubMed:28124733). {ECO:0000269|PubMed:28124733}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.88 mM for p-nitrophenyl acetate (at pH 9 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:28124733};
CC Note=kcat is 242 sec(-1) with p-nitrophenyl acetate as substrate (at
CC pH 9 and 37 degrees Celsius). {ECO:0000269|PubMed:28124733};
CC pH dependence:
CC Optimum pH is 9-10.;
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:28124733};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
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 olive oil (PubMed:30863878, PubMed:22238011). Not induced
CC during growth on the lipidic carbon sources 16-hydroxyhexadecanoic acid
CC and propyl ricinoleate (synthetic cutin monomers), or triacetin and
CC triesterate (triglycerides) (PubMed:30863878). Repressed during growth
CC on glucose and on starch (PubMed:30863878, PubMed:22238011).
CC {ECO:0000269|PubMed:22238011, ECO:0000269|PubMed:30863878}.
CC -!- BIOTECHNOLOGY: May be exploited in the production of biodiesel.
CC {ECO:0000269|PubMed:28124733}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF79598.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA62121.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490511; ABF50887.1; -; mRNA.
DR EMBL; AACD01000129; EAA62121.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001304; CBF79598.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_680810.1; XM_675718.1.
DR AlphaFoldDB; Q5AVY9; -.
DR SMR; Q5AVY9; -.
DR CLAE; CUT5B_EMENI; -.
DR ESTHER; emeni-q5avy9; Cutinase.
DR EnsemblFungi; EAA62121; EAA62121; AN7541.2.
DR GeneID; 2869670; -.
DR KEGG; ani:AN7541.2; -.
DR VEuPathDB; FungiDB:AN7541; -.
DR eggNOG; ENOG502SI38; Eukaryota.
DR HOGENOM; CLU_040058_2_0_1; -.
DR InParanoid; Q5AVY9; -.
DR OrthoDB; 1227171at2759; -.
DR BioCyc; MetaCyc:MON-17223; -.
DR BRENDA; 3.1.1.74; 517.
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 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..255
FT /note="Cutinase 2"
FT /id="PRO_0000395261"
FT REGION 219..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 185
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 198
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 51
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 131
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 40..119
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 66..80
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 181..188
FT /evidence="ECO:0000250|UniProtKB:P52956"
SQ SEQUENCE 255 AA; 26074 MW; 581932254FF32B8A CRC64;
MHFKLLSLAA LAGLSVASPL NLDERQLGSS SGNDLRDGDC KPVTFIFARA STEPGLLGMS
TGPAVCNDLK ADASLGGVAC QGVGPKYTAG LAENALPQGT SSAAINEAKE LFELAASKCP
DTRIVAGGYS QGTAVMHGAI PDLSDEIKDK IAGVVLFGDT RNKQDGGQIK NFPKDKIKIY
CATGDLVCDG TLVVTAAHFT YVANTGEASK WLEQQLASMP ASTSTSSSSS SSSSAPASQT
SQSSGLSSWF SGLGN
