OTASE_ASPNG
ID OTASE_ASPNG Reviewed; 480 AA.
AC A0A075TJ05;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Ochratoxinase {ECO:0000303|PubMed:24947135};
DE Short=OTase {ECO:0000303|PubMed:24947135};
DE EC=3.4.17.- {ECO:0000269|PubMed:24947135};
DE AltName: Full=Amidohydrolase 2 {ECO:0000303|PubMed:24947135};
DE Short=Amidase 2 {ECO:0000303|PubMed:24947135};
DE AltName: Full=Carboxypeptidase Am2 {ECO:0000303|PubMed:33647354};
GN Name=Am2 {ECO:0000303|PubMed:24947135};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN,
RP COFACTOR, ACTIVE SITE, ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RC STRAIN=UVK143;
RX PubMed=24947135; DOI=10.1042/bj20140382;
RA Dobritzsch D., Wang H., Schneider G., Yu S.;
RT "Structural and functional characterization of ochratoxinase, a novel
RT mycotoxin-degrading enzyme.";
RL Biochem. J. 462:441-452(2014).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33647354; DOI=10.1016/j.jbiotec.2021.02.015;
RA Xiong K., Liu J., Wang X., Sun B., Zhang Y., Zhao Z., Pei P., Li X.;
RT "Engineering a carboxypeptidase from Aspergillus niger M00988 by mutation
RT to increase its ability in high Fischer ratio oligopeptide preparation.";
RL J. Biotechnol. 330:1-8(2021).
CC -!- FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal
CC amino acid with specific catalytic activity for aromatic amino acids
CC such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to
CC degrade ochratoxin A, one of the five major mycotoxins most harmful to
CC humans and animals that is produced by Aspergillus and Penicillium
CC species and occurs in a wide range of agricultural products
CC (PubMed:24947135). {ECO:0000269|PubMed:24947135,
CC ECO:0000269|PubMed:33647354}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24947135};
CC -!- ACTIVITY REGULATION: The Zn(2+)-specific chelator 1,10-phenanthroline
CC inhibits the enzyme activity. {ECO:0000269|PubMed:24947135}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:24947135};
CC Temperature dependence:
CC Optimum temperature is 66 degrees Celsius.
CC {ECO:0000269|PubMed:24947135};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:24947135}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}.
CC -!- DOMAIN: Each subunit of the homooctomeric enzyme folds into a two-
CC domain structure characteristic of a metal dependent amidohydrolase,
CC with a twisted TIM (triosephosphateisomerase)-barrel and a smaller
CC beta-sandwich domain. {ECO:0000269|PubMed:24947135}.
CC -!- BIOTECHNOLOGY: Detoxification of contaminated food is a challenging
CC health issue and ochratoxinase is a promising enzyme that hydrolyzes
CC ochrtoxin A, a mycotoxin demonstrated to have nephrotoxic, immunotoxic,
CC genotoxic, neurotoxic, and teratogenic properties; and that occurs in a
CC wide range of agricultural products (PubMed:24947135). Its
CC carboxypeptidase activity allows also to produce high Fischer ratio
CC (the ratio of moles of branched chain amino acid content to aromatic
CC amino acid content) oligopeptides, a kind of functional oligopeptides
CC that protect the liver, treat phenylketonuria, have anti-fatigue
CC properties, exhibits antioxidant properties, and support
CC anticoagulation of the blood (PubMed:33647354). Producing high Fischer
CC ratio oligopeptides using an enzymatic method is therefore of great
CC health significance and economic benefit (PubMed:33647354).
CC {ECO:0000269|PubMed:24947135, ECO:0000269|PubMed:33647354}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Ochratoxinase amidase 2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ854920; AIG55189.1; -; Genomic_DNA.
DR SMR; A0A075TJ05; -.
DR VEuPathDB; FungiDB:An14g02080; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1141547; -.
DR VEuPathDB; FungiDB:ATCC64974_1860; -.
DR VEuPathDB; FungiDB:M747DRAFT_291646; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Secreted; Zinc.
FT CHAIN 1..480
FT /note="Ochratoxinase"
FT /id="PRO_0000453665"
FT ACT_SITE 246
FT /evidence="ECO:0000250|UniProtKB:A2R2V4"
FT ACT_SITE 378
FT /evidence="ECO:0000250|UniProtKB:A2R2V4"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A2R2V4"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A2R2V4"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A2R2V4"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A2R2V4"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A2R2V4"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A2R2V4"
SQ SEQUENCE 480 AA; 51200 MW; 38F48AD24CCA5030 CRC64;
MVRRIASATP MVQSPMSPLG TTYCVRPNPV SLNLQRRPLV IASTDEAKVT IIYAGLLIPG
DGEPLRNAAL VISDKIIAFV GSEADIPKKY LRSTQSTHRV PVLMPGLWDC HMHFGGDDDY
YNDYTSGLAT HPASSGARLA RGCWEALQNG YTSYRDLAGY GCEVAKAIND GTIVGPNVYS
SGAALSQTAG HGDIFALPAG EVLGSYGVMN PRPGYWGAGP LCIADGVEEV RRAVRLQIRR
GAKVIKVMAS GGVMSRDDNP NFAQFSPEEL KVIVEEAARQ NRIVSAHVHG KAGIMAAIKA
GCKSLEHVSY ADEEVWELMK EKGILYVATR SVIEIFLASN GEGLVKESWA KLQALADSHL
KAYQGAIKAG VTIALGTDTA PGGPTALELQ FAVERGGMTP LEAIKAATAN APLSVGPQAP
LTGQLREGYE ADVIALEENP LEDIKVFQEP KAVTHVWKGG KLFKGPGIGP WGEDARNPFL
