Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q70KY3

- LAC1_MELAO

UniProt

Q70KY3 - LAC1_MELAO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Laccase-1

Gene

LAC1

Organism
Melanocarpus albomyces
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Lignin degradation and detoxification of lignin-derived products.1 PublicationCurated

Catalytic activityi

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.1 Publication

Cofactori

Binds 4 copper ions per monomer.2 Publications

Absorptioni

Abs(max)=280 nm2 Publications

Exhibits a shoulder at 360 nm, a smaller absorption peak at 450 nm, and a second, larger peak at 590 nm.1 Publication

pH dependencei

Optimum pH is 3.5 with 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) as substrate, 5.0-7.5 with guiacol as substrate, and 6.0-7.0 with syringaldazine as substrate.2 Publications

Temperature dependencei

Optimum temperature is 60-70 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi143 – 1431Copper 11 Publication
Metal bindingi145 – 1451Copper 21 Publication
Metal bindingi188 – 1881Copper 21 Publication
Metal bindingi190 – 1901Copper 31 Publication
Metal bindingi481 – 4811Copper 41 Publication
Metal bindingi484 – 4841Copper 11 Publication
Metal bindingi486 – 4861Copper 31 Publication
Metal bindingi552 – 5521Copper 31 Publication
Metal bindingi553 – 5531Copper 41 Publication
Metal bindingi554 – 5541Copper 21 Publication
Metal bindingi558 – 5581Copper 41 Publication

GO - Molecular functioni

  1. copper ion binding Source: UniProtKB
  2. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB
  2. lignin catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Laccase-1 (EC:1.10.3.2)
Alternative name(s):
Benzenediol:oxygen oxidoreductase 1
Diphenol oxidase 1
Ligninolytic phenoloxidase
Urishiol oxidase 1
Gene namesi
Name:LAC1
OrganismiMelanocarpus albomyces
Taxonomic identifieri204285 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariales incertae sedisMelanocarpus

Subcellular locationi

GO - Cellular componenti

  1. extraorganismal space Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 50281 PublicationSequence AnalysisPRO_0000235826Add
BLAST
Chaini51 – 609559Laccase-11 PublicationPRO_0000235827Add
BLAST
Propeptidei610 – 623141 PublicationPRO_0000235828Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 621 Publication
Glycosylationi89 – 891N-linked (GlcNAc...)1 Publication
Glycosylationi138 – 1381N-linked (GlcNAc...)1 Publication
Disulfide bondi164 ↔ 5901 Publication
Glycosylationi251 – 2511N-linked (GlcNAc...)1 Publication
Glycosylationi266 – 2661N-linked (GlcNAc...)1 Publication
Glycosylationi294 – 2941N-linked (GlcNAc...)1 Publication
Glycosylationi339 – 3391N-linked (GlcNAc...)1 Publication
Disulfide bondi348 ↔ 3821 Publication
Glycosylationi426 – 4261N-linked (GlcNAc...)1 Publication
Glycosylationi446 – 4461N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Secreted protein; extracellular space.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 644
Turni73 – 753
Beta strandi83 – 9715
Beta strandi103 – 1108
Beta strandi113 – 1153
Beta strandi119 – 1224
Beta strandi126 – 1349
Beta strandi142 – 1454
Helixi153 – 1553
Turni159 – 1613
Turni168 – 1703
Beta strandi171 – 1788
Beta strandi183 – 1897
Helixi194 – 1974
Beta strandi200 – 2067
Beta strandi214 – 22512
Helixi230 – 2378
Beta strandi245 – 2506
Turni257 – 2593
Beta strandi266 – 2694
Beta strandi274 – 2818
Beta strandi288 – 2925
Beta strandi297 – 3026
Beta strandi305 – 3139
Beta strandi315 – 3173
Beta strandi322 – 3287
Beta strandi333 – 3419
Helixi344 – 3463
Beta strandi351 – 3544
Beta strandi357 – 3626
Beta strandi390 – 3923
Beta strandi398 – 4003
Helixi405 – 4073
Beta strandi408 – 4147
Beta strandi416 – 4205
Beta strandi422 – 4254
Beta strandi434 – 4363
Helixi438 – 4447
Helixi451 – 4533
Beta strandi455 – 4584
Beta strandi464 – 4718
Beta strandi481 – 4888
Beta strandi490 – 4967
Helixi511 – 5144
Helixi515 – 5173
Beta strandi525 – 5317
Beta strandi535 – 5428
Beta strandi547 – 5537
Helixi556 – 5605
Beta strandi564 – 5696
Helixi571 – 5744
Helixi575 – 5773
Helixi580 – 59617
Helixi597 – 5993

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GW0X-ray2.40A/B51-609[»]
2IH8X-ray2.00A/B51-609[»]
2IH9X-ray2.00A/B51-609[»]
2Q9OX-ray1.30A/B51-609[»]
3DKHX-ray2.40A/B51-609[»]
3FU7X-ray1.67A/B51-609[»]
3FU8X-ray1.80A/B51-609[»]
3FU9X-ray2.00A/B51-609[»]
3QPKX-ray1.90A/B51-609[»]
ProteinModelPortaliQ70KY3.
SMRiQ70KY3. Positions 51-609.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ70KY3.

Family & Domainsi

Sequence similaritiesi

Belongs to the multicopper oxidase family.Sequence Analysis

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q70KY3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTFTSALAL VVGMLAPGAV VAAPPSTPAQ RDLVELREAR QEGGKDLRPR
60 70 80 90 100
EPTCNTPSNR ACWSDGFDIN TDYEVSTPDT GVTQSYVFNL TEVDNWMGPD
110 120 130 140 150
GVVKEKVMLI NGNIMGPNIV ANWGDTVEVT VINNLVTNGT SIHWHGIHQK
160 170 180 190 200
DTNLHDGANG VTECPIPPKG GQRTYRWRAR QYGTSWYHSH FSAQYGNGVV
210 220 230 240 250
GTIQINGPAS LPYDIDLGVF PITDYYYRAA DDLVHFTQNN APPFSDNVLI
260 270 280 290 300
NGTAVNPNTG EGQYANVTLT PGKRHRLRIL NTSTENHFQV SLVNHTMTVI
310 320 330 340 350
AADMVPVNAM TVDSLFLAVG QRYDVVIDAS RAPDNYWFNV TFGGQAACGG
360 370 380 390 400
SLNPHPAAIF HYAGAPGGLP TDEGTPPVDH QCLDTLDVRP VVPRSVPVNS
410 420 430 440 450
FVKRPDNTLP VALDLTGTPL FVWKVNGSDI NVDWGKPIID YILTGNTSYP
460 470 480 490 500
VSDNIVQVDA VDQWTYWLIE NDPEGPFSLP HPMHLHGHDF LVLGRSPDVP
510 520 530 540 550
AASQQRFVFD PAVDLARLNG DNPPRRDTTM LPAGGWLLLA FRTDNPGAWL
560 570 580 590 600
FHCHIAWHVS GGLSVDFLER PADLRQRISQ EDEDDFNRVC DEWRAYWPTN
610 620
PYPKIDSGLK RRRWVEESEW LVR
Length:623
Mass (Da):68,958
Last modified:July 5, 2004 - v1
Checksum:iA322F89B438784E1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ571698 Genomic DNA. Translation: CAE00180.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ571698 Genomic DNA. Translation: CAE00180.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GW0 X-ray 2.40 A/B 51-609 [» ]
2IH8 X-ray 2.00 A/B 51-609 [» ]
2IH9 X-ray 2.00 A/B 51-609 [» ]
2Q9O X-ray 1.30 A/B 51-609 [» ]
3DKH X-ray 2.40 A/B 51-609 [» ]
3FU7 X-ray 1.67 A/B 51-609 [» ]
3FU8 X-ray 1.80 A/B 51-609 [» ]
3FU9 X-ray 2.00 A/B 51-609 [» ]
3QPK X-ray 1.90 A/B 51-609 [» ]
ProteinModelPortali Q70KY3.
SMRi Q70KY3. Positions 51-609.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q70KY3.

Family and domain databases

Gene3Di 2.60.40.420. 3 hits.
InterProi IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view ]
Pfami PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 3 hits.
PROSITEi PS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and expression in Saccharomyces cerevisiae of a laccase gene from the ascomycete Melanocarpus albomyces."
    Kiiskinen L.-L., Saloheimo M.
    Appl. Environ. Microbiol. 70:137-144(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces."
    Kiiskinen L.-L., Viikari L., Kruus K.
    Appl. Microbiol. Biotechnol. 59:198-204(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-78; 214-228 AND 507-517, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Strain: VTT D-964901 Publication.
  3. "Laccase from Melanocarpus albomyces binds effectively to cellulose."
    Kiiskinen L.-L., Palonen H., Linder M., Viikari L., Kruus K.
    FEBS Lett. 576:251-255(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE FUNCTION.
  4. "Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site."
    Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., Koivula A., Rouvinen J.
    Nat. Struct. Biol. 9:601-605(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 51-609 IN COMPLEX WITH COFACTOR AND OXYGEN, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION AT ASN-89; ASN-138; ASN-251; ASN-266; ASN-294; ASN-339; ASN-426 AND ASN-446, DISULFIDE BONDS.

Entry informationi

Entry nameiLAC1_MELAO
AccessioniPrimary (citable) accession number: Q70KY3
Secondary accession number(s): Q7SIE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: July 5, 2004
Last modified: October 1, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3