CUTI3_ASPOR
ID CUTI3_ASPOR Reviewed; 224 AA.
AC Q2U199;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable cutinase 3;
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109};
DE AltName: Full=Cutin hydrolase 3;
DE Flags: Precursor;
GN ORFNames=AO090011000113;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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:P00590}.
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 -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; AP007171; BAE64666.1; -; Genomic_DNA.
DR RefSeq; XP_001825799.1; XM_001825747.1.
DR AlphaFoldDB; Q2U199; -.
DR SMR; Q2U199; -.
DR ESTHER; aspor-q2u199; Cutinase.
DR EnsemblFungi; BAE64666; BAE64666; AO090011000113.
DR GeneID; 5997902; -.
DR KEGG; aor:AO090011000113; -.
DR VEuPathDB; FungiDB:AO090011000113; -.
DR HOGENOM; CLU_040058_2_0_1; -.
DR OMA; VIGPPLC; -.
DR Proteomes; UP000006564; Chromosome 7.
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 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 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..224
FT /note="Probable cutinase 3"
FT /id="PRO_0000395254"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 190
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT ACT_SITE 203
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 56
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 136
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 45..124
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 71..85
FT /evidence="ECO:0000250|UniProtKB:P52956"
FT DISULFID 186..193
FT /evidence="ECO:0000250|UniProtKB:P52956"
SQ SEQUENCE 224 AA; 23075 MW; AF09EA2AA627362B CRC64;
MVMLRSLLVS ALAALAAGSP IAEPADQSLE ARQLGSSNDL TNGACKDVTL IFARGSTEMG
NMGTVIGPPL CSSLKSKLGA DKVACQGVGG LYTGGLMQNA LPQNTDPGAI STAKSLFEQA
STKCPNTQIV AGGYSQGSAV IDNAVQQLSA EVKDKVKGVV FFGFTRNLQD KGQIPNYPKD
NVKVFCAMGD LVCDGTLIVT AAHLTYTINA PEAASFLASK VQSA
