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