CUTI1_ASPOR
ID CUTI1_ASPOR Reviewed; 213 AA.
AC P52956; Q2UTG4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cutinase 1;
DE EC=3.1.1.74 {ECO:0000255|PROSITE-ProRule:PRU10108, ECO:0000255|PROSITE-ProRule:PRU10109, ECO:0000305|PubMed:15968570, ECO:0000305|PubMed:19810726};
DE AltName: Full=Cutin hydrolase 1;
DE Short=L1;
DE Flags: Precursor;
GN Name=cutL; Synonyms=CutL1 {ECO:0000303|PubMed:15968570};
GN ORFNames=AO090005000029;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=NBRC 4202;
RX PubMed=7705606; DOI=10.1111/j.1574-6968.1995.tb07408.x;
RA Ohnishi K., Toida J., Nakazawa H., Sekiguchi J.;
RT "Genome structure and nucleotide sequence of a lipolytic enzyme gene of
RT Aspergillus oryzae.";
RL FEMS Microbiol. Lett. 126:145-150(1995).
RN [2]
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).
RN [3]
RP PROTEIN SEQUENCE OF 104-113, FUNCTION, ACTIVITY REGULATION, CATALYTIC
RP ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=15968570; DOI=10.1007/s00253-004-1853-6;
RA Maeda H., Yamagata Y., Abe K., Hasegawa F., Machida M., Ishioka R.,
RA Gomi K., Nakajima T.;
RT "Purification and characterization of a biodegradable plastic-degrading
RT enzyme from Aspergillus oryzae.";
RL Appl. Microbiol. Biotechnol. 67:778-788(2005).
RN [4] {ECO:0007744|PDB:3GBS}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 17-213, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
RX PubMed=19810726; DOI=10.1021/ja9046697;
RA Liu Z., Gosser Y., Baker P.J., Ravee Y., Lu Z., Alemu G., Li H.,
RA Butterfoss G.L., Kong X.P., Gross R., Montclare J.K.;
RT "Structural and functional studies of Aspergillus oryzae cutinase: enhanced
RT thermostability and hydrolytic activity of synthetic ester and polyester
RT degradation.";
RL J. Am. Chem. Soc. 131:15711-15716(2009).
RN [5] {ECO:0007744|PDB:3QPD}
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 26-212.
RA Lu A., Gosser Y., Montclare J.K., Liu Z., Kong X.;
RT "Structure of Aspergillus oryzae cutinase expressed in Pichia pastoris,
RT crystallized in the presence of Paraoxon.";
RL Submitted (FEB-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters
CC found in the cell wall of plants (PubMed:19810726, PubMed:15968570).
CC Degrades cutin, a macromolecule that forms the structure of the plant
CC cuticle (PubMed:19810726, PubMed:15968570).
CC {ECO:0000269|PubMed:15968570, ECO:0000269|PubMed:19810726}.
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, ECO:0000305|PubMed:15968570,
CC ECO:0000305|PubMed:19810726};
CC -!- ACTIVITY REGULATION: Competitively inhibited by the carboxylic acids
CC butyric acid, valeric acid and hexanoic acid (PubMed:15968570).
CC Competitively inhibited by the dicarboxylic acid succinic acid
CC (PubMed:15968570). Competitively inhibited by the alcohols propan-1-ol,
CC butan-1-ol, hexan-1-ol, octan-1-ol, and butane-1,4-diol
CC (PubMed:15968570). {ECO:0000269|PubMed:15968570}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.96 uM for p-nitrophenyl acetate (at pH 7.5)
CC {ECO:0000269|PubMed:19810726};
CC KM=1100 uM for p-nitrophenyl propionate (at pH 8.0 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:15968570};
CC KM=0.21 uM for p-nitrophenyl butyrate (at pH 7.5)
CC {ECO:0000269|PubMed:19810726};
CC KM=220 uM for p-nitrophenyl butyrate (at pH 8.0 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:15968570};
CC KM=0.04 uM for p-nitrophenyl valerate (at pH 7.5)
CC {ECO:0000269|PubMed:19810726};
CC KM=44 uM for p-nitrophenyl valerate (at pH 8.0 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:15968570};
CC KM=0.29 uM for p-nitrophenyl hexanoate (at pH 7.5)
CC {ECO:0000269|PubMed:19810726};
CC Note=kcat is 11 sec(-1) with p-nitrophenyl propionate as substrate
CC (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). kcat is 18
CC sec(-1) with p-nitrophenyl butyrate as substrate (at pH 8.0 and 37
CC degrees Celsius) (PubMed:15968570). kcat is 14 sec(-1) with p-
CC nitrophenyl valerate as substrate (at pH 8.0 and 37 degrees Celsius)
CC (PubMed:15968570). {ECO:0000269|PubMed:15968570};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:15968570};
CC Temperature dependence:
CC Optimum temperature is 25-40 degrees Celsius (PubMed:19810726).
CC Optimum temperature is 35-55 degrees Celsius (PubMed:15968570).
CC {ECO:0000269|PubMed:15968570, ECO:0000269|PubMed:19810726};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11373}.
CC -!- BIOTECHNOLOGY: This enzyme enables the fungus to utilize the
CC biodegradable plastics poly(butylene succinate) (PBS) and poly(butylene
CC succinate-co-butylene adipate) (PBSA) as sole carbon source and could
CC therefore be used in plastic recycling. {ECO:0000269|PubMed:15968570}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; D38311; BAA07428.1; -; Genomic_DNA.
DR EMBL; AP007151; BAE55151.1; -; Genomic_DNA.
DR RefSeq; XP_001817153.1; XM_001817101.2.
DR PDB; 3GBS; X-ray; 1.75 A; A=17-213.
DR PDB; 3QPD; X-ray; 1.57 A; A=26-212.
DR PDBsum; 3GBS; -.
DR PDBsum; 3QPD; -.
DR AlphaFoldDB; P52956; -.
DR SMR; P52956; -.
DR ESTHER; aspor-cutas; Cutinase.
DR EnsemblFungi; BAE55151; BAE55151; AO090005000029.
DR GeneID; 5989098; -.
DR KEGG; aor:AO090005000029; -.
DR VEuPathDB; FungiDB:AO090005000029; -.
DR HOGENOM; CLU_040058_2_0_1; -.
DR OMA; SCPKAIF; -.
DR BRENDA; 3.1.1.74; 522.
DR EvolutionaryTrace; P52956; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; TAS:AspGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0050525; F:cutinase activity; TAS:AspGD.
DR GO; GO:0016042; P:lipid catabolic process; TAS:AspGD.
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 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..213
FT /note="Cutinase 1"
FT /id="PRO_0000006434"
FT ACT_SITE 126
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:19810726,
FT ECO:0007744|PDB:3GBS"
FT ACT_SITE 181
FT /evidence="ECO:0000269|PubMed:19810726,
FT ECO:0007744|PDB:3GBS"
FT ACT_SITE 194
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:19810726,
FT ECO:0007744|PDB:3GBS"
FT SITE 48
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT SITE 127
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 37..115
FT /evidence="ECO:0000269|PubMed:19810726,
FT ECO:0007744|PDB:3GBS, ECO:0007744|PDB:3QPD"
FT DISULFID 63..76
FT /evidence="ECO:0000269|PubMed:19810726,
FT ECO:0007744|PDB:3GBS, ECO:0007744|PDB:3QPD"
FT DISULFID 177..184
FT /evidence="ECO:0000269|PubMed:19810726,
FT ECO:0007744|PDB:3GBS, ECO:0007744|PDB:3QPD"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:3QPD"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:3QPD"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:3QPD"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3GBS"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:3QPD"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:3QPD"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:3QPD"
FT TURN 156..163
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3QPD"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:3QPD"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:3QPD"
SQ SEQUENCE 213 AA; 22263 MW; 2213317B4A14A0CF CRC64;
MHLRNIVIAL AATAVASPVD LQDRQLTGGD ELRDGPCKPI TFIFARASTE PGLLGISTGP
AVCNRLKLAR SGDVACQGVG PRYTADLPSN ALPEGTSQAA IAEAQGLFEQ AVSKCPDTQI
VAGGYSQGTA VMNGAIKRLS ADVQDKIKGV VLFGYTRNAQ ERGQIANFPK DKVKVYCAVG
DLVCLGTLIV APPHFSYLSD TGDASDFLLS QLG
