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 02-JUN-2021, entry version 52. 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 14742 / OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii). OG Plasmid pHV3. OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales; OC Haloferacaceae; 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 / VKM RC 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., Madupu R., RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., 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, AND RP ACTIVITY 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 into RT 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-di- CC (3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and dimethoxyphenol CC (DMP). No oxidation of Fe(2+) or guaiacol. CC {ECO:0000269|PubMed:19966030}. 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: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 -!- ACTIVITY 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 acid CC {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-ethylbenzothiazoline)- CC 6-sulfonic acid as substrate. Kcat is 21.7 sec(-1) with CC syringaldazine as substrate. Optimal activity at 200 mM salt, with CC 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 of CC syringaldazine. {ECO:0000269|PubMed:19966030}; CC Temperature dependence: CC Optimum temperature is 45-50 degrees Celsius. Highly thermostable. CC {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. {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 STRING; 309800.C498_02605; -. DR EnsemblBacteria; ADE01515; ADE01515; HVO_B0205. DR KEGG; hvo:HVO_B0205; -. DR eggNOG; arCOG03914; Archaea. DR HOGENOM; CLU_009100_4_0_2; -. DR OMA; PHNFHVH; -. DR BRENDA; 1.10.3.2; 2561. DR SABIO-RK; D4GPK6; -. 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; 2. DR PROSITE; PS51318; TAT; 1. PE 1: Evidence at protein level; KW Copper; Direct protein sequencing; Glycoprotein; Metal-binding; KW Oxidoreductase; Plasmid; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..31 FT /note="Tat-type signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, FT ECO:0000269|PubMed:19966030" FT CHAIN 32..579 FT /note="Laccase" FT /id="PRO_0000428861" FT DOMAIN 82..214 FT /note="Plastocyanin-like 1" FT DOMAIN 423..530 FT /note="Plastocyanin-like 2" FT REGION 372..401 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 380..395 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 145 FT /note="Copper 1; type 2" FT /evidence="ECO:0000250" FT METAL 147 FT /note="Copper 2; type 3" FT /evidence="ECO:0000250" FT METAL 192 FT /note="Copper 2; type 3" FT /evidence="ECO:0000250" FT METAL 194 FT /note="Copper 3; type 3" FT /evidence="ECO:0000250" FT METAL 455 FT /note="Copper 4; type 1" FT /evidence="ECO:0000250" FT METAL 458 FT /note="Copper 1; type 2" FT /evidence="ECO:0000250" FT METAL 460 FT /note="Copper 3; type 3" FT /evidence="ECO:0000250" FT METAL 512 FT /note="Copper 3; type 3" FT /evidence="ECO:0000250" FT METAL 513 FT /note="Copper 4; type 1" FT /evidence="ECO:0000250" FT METAL 514 FT /note="Copper 2; type 3" FT /evidence="ECO:0000250" FT METAL 518 FT /note="Copper 4; type 1" FT /evidence="ECO:0000250" FT METAL 523 FT /note="Copper 4; type 1" FT /evidence="ECO:0000250" FT CARBOHYD 449 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 557 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="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 //