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Laccase (EC 1.10.3.2) (LccA multicopper oxidase)

 LACC_HALVD              Reviewed;         579 AA.
D4GPK6;
14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 1.
07-JUN-2017, entry version 41.
RecName: Full=Laccase;
EC=1.10.3.2;
AltName: Full=LccA multicopper oxidase;
Flags: Precursor;
Name=lccA; OrderedLocusNames=HVO_B0205;
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
Plasmid pHV3.
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=309800;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=20333302; DOI=10.1371/journal.pone.0009605;
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S.,
Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M.,
Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T.,
Eisen J.A.;
"The complete genome sequence of Haloferax volcanii DS2, a model
archaeon.";
PLoS ONE 5:E9605-E9605(2010).
[2]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, GLYCOSYLATION,
AND ENZYME REGULATION.
STRAIN=DS2 / DS70;
PubMed=19966030; DOI=10.1128/AEM.01757-09;
Uthandi S., Saad B., Humbard M.A., Maupin-Furlow J.A.;
"LccA, an archaeal laccase secreted as a highly stable glycoprotein
into the extracellular medium by Haloferax volcanii.";
Appl. Environ. Microbiol. 76:733-743(2010).
-!- FUNCTION: Catalyzes the oxidation of a wide variety of organic
substrates, including bilirubin, syringaldazine (SGZ), 2,2'-azino-
di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and
dimethoxyphenol (DMP). No oxidation of Fe(2+) or guaiacol.
{ECO:0000269|PubMed:19966030}.
-!- CATALYTIC ACTIVITY: 4 benzenediol + O(2) = 4 benzosemiquinone + 2
H(2)O. {ECO:0000269|PubMed:19966030}.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000305};
Note=Binds 4 copper ions per subunit. {ECO:0000305};
-!- ENZYME REGULATION: Inhibited by 1 mM NaN(3), 10 mM thiourea, 10 mM
1,10-phenanthroline, 0.1 mM DL-dithiothreitol (DTT) and 1 mM L-
cysteine. The inhibition by DTT and L-cysteine is likely caused by
reduction of the oxidized substrate and not by inhibition of the
enzyme. {ECO:0000269|PubMed:19966030}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=605 nm {ECO:0000269|PubMed:19966030};
Kinetic parameters:
KM=671 uM for 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic
acid {ECO:0000269|PubMed:19966030};
KM=35 uM for syringaldazine {ECO:0000269|PubMed:19966030};
Note=Kcat is 9.9 sec(-1) with 2,2'-azino-di-(3-
ethylbenzothiazoline)-6-sulfonic acid as substrate. Kcat is 21.7
sec(-1) with syringaldazine as substrate. Optimal activity at
200 mM salt, with 65% activity at 1 M NaCl.;
pH dependence:
Optimum pH is 6.0 for the oxidation of 2,2'-azino-di-(3-
ethylbenzothiazoline)-6-sulfonic acid and 8.4 for the oxidation
of syringaldazine. {ECO:0000269|PubMed:19966030};
Temperature dependence:
Optimum temperature is 45-50 degrees Celsius. Highly
thermostable. {ECO:0000269|PubMed:19966030};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19966030}.
-!- PTM: Exported by the Tat system.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:19966030}.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
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EMBL; CP001953; ADE01515.1; -; Genomic_DNA.
SMR; D4GPK6; -.
EnsemblBacteria; ADE01515; ADE01515; HVO_B0205.
KEGG; hvo:HVO_B0205; -.
HOGENOM; HOG000096435; -.
OMA; PHNFHVH; -.
OrthoDB; POG093Z00WW; -.
BRENDA; 1.10.3.2; 2561.
Proteomes; UP000008243; Plasmid pHV3.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
Gene3D; 2.60.40.420; -; 3.
InterPro; IPR011706; Cu-oxidase_2.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR006311; TAT_signal.
Pfam; PF07731; Cu-oxidase_2; 1.
Pfam; PF07732; Cu-oxidase_3; 1.
SUPFAM; SSF49503; SSF49503; 3.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
Complete proteome; Copper; Direct protein sequencing; Glycoprotein;
Metal-binding; Oxidoreductase; Plasmid; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 31 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648,
ECO:0000269|PubMed:19966030}.
CHAIN 32 579 Laccase.
/FTId=PRO_0000428861.
DOMAIN 82 214 Plastocyanin-like 1.
DOMAIN 423 530 Plastocyanin-like 2.
METAL 145 145 Copper 1; type 2. {ECO:0000250}.
METAL 147 147 Copper 2; type 3. {ECO:0000250}.
METAL 192 192 Copper 2; type 3. {ECO:0000250}.
METAL 194 194 Copper 3; type 3. {ECO:0000250}.
METAL 455 455 Copper 4; type 1. {ECO:0000250}.
METAL 458 458 Copper 1; type 2. {ECO:0000250}.
METAL 460 460 Copper 3; type 3. {ECO:0000250}.
METAL 512 512 Copper 3; type 3. {ECO:0000250}.
METAL 513 513 Copper 4; type 1. {ECO:0000250}.
METAL 514 514 Copper 2; type 3. {ECO:0000250}.
METAL 518 518 Copper 4; type 1. {ECO:0000250}.
METAL 523 523 Copper 4; type 1. {ECO:0000250}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 579 AA; 63442 MW; 567DF329448F0C06 CRC64;
MTDWSRRRFL QTGAALGIAG TLPQTTTEVS AASPTLEKFV QPLPIPSVRE PDGQRDGADA
YEIAVTEFTQ QLHPDLPETT VWGFDGSYPG PTIEADAGSP VHVRFDNSGL PSEHLFPVDD
RLGGTTAENH PGYDGPVPEV RTVTHFHGLE LDPANDGQSD MWTSPGGVEG PRFDSAWQEL
PMEQGRTTST YHDHTLGITR LNAYAGLLGL YSITTDAERE LGLPSGDYDI PLLLQDKEFN
DDGSLHYPEE FVSAFLGDTA VVNGAVWPYV EVEPRRYRFR ILNGANHRSF DLQLESESGS
GVPTMYQFAP GHGFLESVVP IGPNGDLDSL LLTPFERGEL VVDFSDHAGE TLTLANGADM
GPELTDLVEF RVSDPSTPPE DASADPTSLS LPTPASYDES DARVTREMTL GTEVRNGLIT
HTLNGHVFGD EDAPVYPQLG ATEIWELQNE SGGRHPIHLH LVTFRVIGRG PDGTQPPDPN
ELGPKDTVRV DPGERVRILV TFEGYTGQFP WHCHMLEHED NKMMIPFVVE NPVADYANEE
NVVDATGLTD AVGDWRNETL ETEVLLEVID QWRSGDEVA


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