CUTI4_EMENI
ID CUTI4_EMENI Reviewed; 223 AA.
AC C8VJF5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Cutinase 4 {ECO:0000303|PubMed:30863878};
DE EC=3.1.1.74 {ECO:0000255|RuleBase:RU361263};
DE AltName: Full=Ancut4 {ECO:0000303|PubMed:30863878};
DE Flags: Precursor;
GN Name=cut4 {ECO:0000303|PubMed:30863878};
GN ORFNames=ANIA_10346 {ECO:0000312|EMBL:CBF83913.1};
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 {ECO:0000312|Proteomes:UP000000560};
RN [1] {ECO:0000312|Proteomes:UP000000560}
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] {ECO:0000312|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000312|Proteomes:UP000000560};
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 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q5AVY9, ECO:0000250|UniProtKB:Q5B2C1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000255|RuleBase:RU361263};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|RuleBase:RU361263}.
CC -!- INDUCTION: Induced by oxidative stress, in a manner dependent on
CC transcription factor napA. {ECO:0000269|PubMed:30863878}.
CC -!- PTM: The 2 disulfide bonds play a critical role in holding the
CC catalytic residues in juxta-position; reduction of the disulfide
CC bridges results in the complete inactivation of the enzyme.
CC {ECO:0000250|UniProtKB:P11373}.
CC -!- SIMILARITY: Belongs to the cutinase family.
CC {ECO:0000255|RuleBase:RU361263}.
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DR EMBL; BN001306; CBF83913.1; -; Genomic_DNA.
DR ESTHER; emeni-q5b9e7; Cutinase.
DR EnsemblFungi; CBF83913; CBF83913; ANIA_10346.
DR VEuPathDB; FungiDB:AN10346; -.
DR eggNOG; ENOG502S3AW; Eukaryota.
DR HOGENOM; CLU_040058_2_2_1; -.
DR InParanoid; C8VJF5; -.
DR OMA; GAMVTHA; -.
DR OrthoDB; 1193797at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
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 PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF01083; Cutinase; 1.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00155; CUTINASE_1; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..223
FT /note="Cutinase 4"
FT /evidence="ECO:0000255"
FT /id="PRO_5005125857"
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 191
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 203
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 71
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 145
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 60..133
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 187..194
FT /evidence="ECO:0000250|UniProtKB:P00590"
SQ SEQUENCE 223 AA; 22699 MW; F3969F2139C579AE CRC64;
MPLPLLPPLL LPLEALLDLA LHLVDSTGVA YSARQVTPTA PLPRLRGSST SNDVTDNSGC
KELTFIFARG TTEIGNMGTV VGPKVGEALK SLTGNKAAIQ GVDYPADAAG NAALGGSGGP
KMASLVETAL KQCPDTKIVL GGYSQGAMVV HNAASKLSSG QVVGAVTFGD PFKSQKPDNI
DQFKTFCASG DPVCLNGANV MAHLSYGNDA QTAAQFLVSA AGL
