COTA_BACIT
ID COTA_BACIT Reviewed; 510 AA.
AC A0A7T1FRB0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=Laccase {ECO:0000303|PubMed:33676982};
DE EC=1.10.3.2 {ECO:0000269|PubMed:33676982};
DE AltName: Full=BaCotA {ECO:0000303|PubMed:33676982};
GN Name=cotA {ECO:0000303|PubMed:33676982};
OS Bacillus stratosphericus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=293386;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=BCMC2;
RX PubMed=33676982; DOI=10.1016/j.ijbiomac.2021.02.205;
RA Xiao Y., Li J., Wu P., Ning N., Li J., Shen Y., Huang Q., Ni J.;
RT "An alkaline thermostable laccase from termite gut associated strain of
RT Bacillus stratosphericus.";
RL Int. J. Biol. Macromol. 179:270-278(2021).
CC -!- FUNCTION: Multicopper oxidase that catalyzes the oxidation of a variety
CC of substrates, including phenolic and non-phenolic compounds.
CC Substrates include 2,6-dimethoxyphenol (2,6-DMP) and the non-phenolic
CC compound 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS).
CC Cannot use guaiacol and catechol. {ECO:0000269|PubMed:33676982}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O;
CC Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2;
CC Evidence={ECO:0000269|PubMed:33676982};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P07788};
CC Note=Binds 4 copper ions per subunit. {ECO:0000250|UniProtKB:P07788};
CC -!- ACTIVITY REGULATION: Resistant to alkali and organic solvents such as
CC methanol, ethanol and acetone. Resistant to EDTA, which might be
CC explained by the spatial protection of copper ions in the active sites.
CC Inhibited by DMSO. Strongly inhibited by Fe(2+) and DTT.
CC {ECO:0000269|PubMed:33676982}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.278 mM for ABTS {ECO:0000269|PubMed:33676982};
CC Vmax=555 umol/min/mg enzyme with ABTS as substrate
CC {ECO:0000269|PubMed:33676982};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:33676982};
CC Temperature dependence:
CC Thermostable. Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:33676982};
CC -!- BIOTECHNOLOGY: Exhibits efficient decolorization ability towards indigo
CC and crystal violet, which are extensively used in textile industries
CC and biochemical study, suggesting a potential application of this
CC laccase in industrial processes. {ECO:0000269|PubMed:33676982}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; MW045312; QPM92784.1; -; Genomic_DNA.
DR SMR; A0A7T1FRB0; -.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR SUPFAM; SSF49503; SSF49503; 3.
PE 1: Evidence at protein level;
KW Copper; Metal-binding; Oxidoreductase; Repeat.
FT CHAIN 1..510
FT /note="Laccase"
FT /id="PRO_0000453717"
FT DOMAIN 45..79
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 99..174
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 242..317
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 372..506
FT /note="Plastocyanin-like 4"
FT /evidence="ECO:0000255"
FT BINDING 103
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 105
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 151
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 419
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 422
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 424
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 491
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 492
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 493
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 497
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT BINDING 502
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT SITE 114
FT /note="Plays a crucial role in the protonation steps"
FT /evidence="ECO:0000250|UniProtKB:P07788"
FT SITE 498
FT /note="Plays a crucial role in the protonation steps"
FT /evidence="ECO:0000250|UniProtKB:P07788"
SQ SEQUENCE 510 AA; 58673 MW; B0EC1A6A1D7C9265 CRC64;
MNLEKFVDEL PIPEVAEPVK KNPRQTYYEI AMEEVFLKVH RDLPPTKLWT YNGSLPGPTI
KANRNEKVKV KWMNKLPLKH FLPVDHTIHA GHHDEPEVKT VVHLHGGVTP ASSDGYPEAW
FSRDFEATGP FFEREVYEYP NHQQACTLWY HDHAMALTRL NVYAGLAGFY LISDAFEKSL
ELPKDEYDIP LMIMDRTFQE DGALFYPSRP NNTPEDSDLP DPSIVPFFCG ETILVNGKVW
PYLEVEPRKY RFRILNASNT RTYELHLDND ATILQIGSDG GFLPRPVHHQ SFSIAPAERF
DVIIDFSAYE NKTIVLKNSA GCGQDVNPET DANIMQFKVT RPLKGRAAKT LRPIFKPLPP
LRPSRADNER TLTLTGTQDK YGRPILLLDN QFWNDPVTEN PRLGSVEVWN IVNPTRGTHP
IHLHLVQFRV IDRRPFDTDI YQSTGEIVYT GPNEAPPLHE QGYKDTIQAH AGEVIRIIAR
FVPYSGRYVW HCHILEHEDY DMMRPMDIIQ
