IED ID | IndEnz0015000009 |
Enzyme Type ID | laccase000009 |
Protein Name |
Laccase EC 1.10.3.2 LccA multicopper oxidase |
Gene Name | lccA HVO_B0205 |
Organism | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Halobacteria Haloferacales Haloferacaceae Haloferax Haloferax volcanii (Halobacterium volcanii) Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
Enzyme Sequence | MTDWSRRRFLQTGAALGIAGTLPQTTTEVSAASPTLEKFVQPLPIPSVREPDGQRDGADAYEIAVTEFTQQLHPDLPETTVWGFDGSYPGPTIEADAGSPVHVRFDNSGLPSEHLFPVDDRLGGTTAENHPGYDGPVPEVRTVTHFHGLELDPANDGQSDMWTSPGGVEGPRFDSAWQELPMEQGRTTSTYHDHTLGITRLNAYAGLLGLYSITTDAERELGLPSGDYDIPLLLQDKEFNDDGSLHYPEEFVSAFLGDTAVVNGAVWPYVEVEPRRYRFRILNGANHRSFDLQLESESGSGVPTMYQFAPGHGFLESVVPIGPNGDLDSLLLTPFERGELVVDFSDHAGETLTLANGADMGPELTDLVEFRVSDPSTPPEDASADPTSLSLPTPASYDESDARVTREMTLGTEVRNGLITHTLNGHVFGDEDAPVYPQLGATEIWELQNESGGRHPIHLHLVTFRVIGRGPDGTQPPDPNELGPKDTVRVDPGERVRILVTFEGYTGQFPWHCHMLEHEDNKMMIPFVVENPVADYANEENVVDATGLTDAVGDWRNETLETEVLLEVIDQWRSGDEVA |
Enzyme Length | 579 |
Uniprot Accession Number | D4GPK6 |
Absorption | BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=605 nm {ECO:0000269|PubMed:19966030}; |
Active Site | |
Activity Regulation | ACTIVITY 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}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O; Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2; Evidence={ECO:0000269|PubMed:19966030}; |
DNA Binding | |
EC Number | 1.10.3.2 |
Enzyme Function | 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}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-50 degrees Celsius. Highly thermostable. {ECO:0000269|PubMed:19966030}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: 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}; |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Compositional bias (1); Domain (2); Glycosylation (2); Metal binding (12); Region (1); Signal peptide (1) |
Keywords | Copper;Direct protein sequencing;Glycoprotein;Metal-binding;Oxidoreductase;Plasmid;Reference proteome;Repeat;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19966030}. |
Modified Residue | |
Post Translational Modification | PTM: Exported by the Tat system.; PTM: Glycosylated. {ECO:0000269|PubMed:19966030}. |
Signal Peptide | SIGNAL 1..31; /note="Tat-type signal"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|PubMed:19966030" |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | Plasmid pHV3 |
Mass | 63,442 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: 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.; |
Metal Binding | METAL 145; /note=Copper 1; type 2; /evidence=ECO:0000250; METAL 147; /note=Copper 2; type 3; /evidence=ECO:0000250; METAL 192; /note=Copper 2; type 3; /evidence=ECO:0000250; METAL 194; /note=Copper 3; type 3; /evidence=ECO:0000250; METAL 455; /note=Copper 4; type 1; /evidence=ECO:0000250; METAL 458; /note=Copper 1; type 2; /evidence=ECO:0000250; METAL 460; /note=Copper 3; type 3; /evidence=ECO:0000250; METAL 512; /note=Copper 3; type 3; /evidence=ECO:0000250; METAL 513; /note=Copper 4; type 1; /evidence=ECO:0000250; METAL 514; /note=Copper 2; type 3; /evidence=ECO:0000250; METAL 518; /note=Copper 4; type 1; /evidence=ECO:0000250; METAL 523; /note=Copper 4; type 1; /evidence=ECO:0000250 |
Rhea ID | RHEA:11276 |
Cross Reference Brenda | 1.10.3.2; |