LACC_HALVD
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 03-AUG-2022, entry version 56.
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}.
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DR EMBL; CP001953; ADE01515.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GPK6; -.
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; LLPKQWG; -.
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_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11709; PTHR11709; 1.
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 BINDING 145
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 513
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 518
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
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
