CUTI_KINRD
ID CUTI_KINRD Reviewed; 294 AA.
AC A6WFI5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cutinase {ECO:0000303|PubMed:34705546};
DE EC=3.1.1.74 {ECO:0000269|PubMed:34705546};
DE AltName: Full=KrCUT {ECO:0000303|PubMed:34705546};
DE Flags: Precursor;
GN Name=cut {ECO:0000303|PubMed:34705546};
GN OrderedLocusNames=Krad_4111 {ECO:0000312|EMBL:ABS05574.1},
GN YP_001363838.1 {ECO:0000303|PubMed:34705546};
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX NCBI_TaxID=266940 {ECO:0000312|Proteomes:UP000001116};
RN [1] {ECO:0000312|Proteomes:UP000001116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC {ECO:0000312|Proteomes:UP000001116};
RX PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT "Survival in nuclear waste, extreme resistance, and potential applications
RT gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL PLoS ONE 3:e3878-e3878(2008).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND BIOTECHNOLOGY.
RX PubMed=34705546; DOI=10.1128/aem.01522-21;
RA Abokitse K., Grosse S., Leisch H., Corbeil C.R., Perrin-Sarazin F.,
RA Lau P.C.K.;
RT "A Novel Actinobacterial Cutinase Containing a Non-Catalytic Polymer-
RT Binding Domain.";
RL Appl. Environ. Microbiol. 88:AEM0152221-AEM0152221(2021).
CC -!- FUNCTION: Catalyzes the hydrolysis of cutin, a polyester that forms the
CC structure of plant cuticle (PubMed:34705546). Shows esterase activity
CC towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters)
CC (PubMed:34705546). Can depolymerize synthetic polyesters such as
CC poly(epsilon-caprolactone) (PCL) and poly(1,3-propylene adipate) (PPA)
CC (PubMed:34705546). Exhibits some activity on poly(lactic acid) (PLA)
CC (PubMed:34705546). Can bind but not hydrolyze poly(hydroxybutyrate)
CC (PHB) (PubMed:34705546). {ECO:0000269|PubMed:34705546}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000269|PubMed:34705546};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:34705546};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47389;
CC Evidence={ECO:0000269|PubMed:34705546};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoate ester = an aliphatic alcohol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:47392, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25835; Evidence={ECO:0000269|PubMed:34705546};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47393;
CC Evidence={ECO:0000269|PubMed:34705546};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:34705546};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:34705546};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC Evidence={ECO:0000269|PubMed:34705546};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:34705546};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34705546}.
CC -!- BIOTECHNOLOGY: Shows promising applications in improving the surface
CC properties of natural textile fibers. {ECO:0000269|PubMed:34705546}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; CP000750; ABS05574.1; -; Genomic_DNA.
DR STRING; 266940.Krad_4111; -.
DR ESTHER; kinrd-a6wfi5; Cutinase.
DR EnsemblBacteria; ABS05574; ABS05574; Krad_4111.
DR KEGG; kra:Krad_4111; -.
DR eggNOG; ENOG5030I1N; Bacteria.
DR HOGENOM; CLU_040058_3_1_11; -.
DR OMA; CAKGLYM; -.
DR Proteomes; UP000001116; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0050525; F:cutinase activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF01083; Cutinase; 1.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000305|PubMed:34705546"
FT CHAIN 34..294
FT /note="Cutinase"
FT /evidence="ECO:0000255"
FT /id="PRO_5002704814"
FT REGION 222..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..294
FT /note="May be involved in substrate binding"
FT /evidence="ECO:0000269|PubMed:34705546"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT ACT_SITE 184
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT ACT_SITE 198
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT SITE 119
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00590"
FT DISULFID 36..107
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT DISULFID 180..187
FT /evidence="ECO:0000250|UniProtKB:O53581"
SQ SEQUENCE 294 AA; 29136 MW; 030B7765EBDDC238 CRC64;
MLRARPSHRL ASAAAVVAAT GAALLAGSSP AAAATCSDVD VVFARGTGET PGLGVVGGPF
VRSLTGELSD RTVTSHAVDY AASSSQASAG PGATAMSAHV REVAAACPST RFVLGGYSQG
ATVTDIALGI RTGTTTGTPV PAELAGRVAA VVVFGNPLGL SGRTIATASS TYGPKSKDYC
NSSDSVCGSA PKTGTGGHLS YASNGSTTDG ARFAAGLVRA AGTPTTPTPT PTPTPVPTTC
VRDSTRDHVA ADRAVSLYGR AYARGSRDSL GATSSYNVVS LQQVEGGWRL VTAC
