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Protein

Laccase-1

Gene

LAC1

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

Functioni

Lignin degradation and detoxification of lignin-derived products.Curated1 Publication

Catalytic activityi

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

Cofactori

Cu cation2 PublicationsNote: Binds 4 Cu cations 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

Manual assertion based on experiment ini

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)DescriptionActionsGraphical viewLength
Metal bindingi143Copper 11 Publication1
Metal bindingi145Copper 21 Publication1
Metal bindingi188Copper 21 Publication1
Metal bindingi190Copper 31 Publication1
Metal bindingi481Copper 41 Publication1
Metal bindingi484Copper 11 Publication1
Metal bindingi486Copper 31 Publication1
Metal bindingi552Copper 31 Publication1
Metal bindingi553Copper 41 Publication1
Metal bindingi554Copper 21 Publication1
Metal bindingi558Copper 41 Publication1

GO - Molecular functioni

  • copper ion binding Source: UniProtKB
  • hydroquinone:oxygen oxidoreductase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin degradation

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BRENDAi1.10.3.2. 3208.

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

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

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000023582623 – 50Sequence analysis1 PublicationAdd BLAST28
ChainiPRO_000023582751 – 609Laccase-11 PublicationAdd BLAST559
PropeptideiPRO_0000235828610 – 6231 PublicationAdd BLAST14

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 621 Publication
Glycosylationi89N-linked (GlcNAc...)1 Publication1
Glycosylationi138N-linked (GlcNAc...)1 Publication1
Disulfide bondi164 ↔ 5901 Publication
Glycosylationi251N-linked (GlcNAc...)1 Publication1
Glycosylationi266N-linked (GlcNAc...)1 Publication1
Glycosylationi294N-linked (GlcNAc...)1 Publication1
Glycosylationi339N-linked (GlcNAc...)1 Publication1
Disulfide bondi348 ↔ 3821 Publication
Glycosylationi426N-linked (GlcNAc...)1 Publication1
Glycosylationi446N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Secreted protein; extracellular space.1 Publication

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1623
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 64Combined sources4
Turni73 – 75Combined sources3
Beta strandi83 – 97Combined sources15
Beta strandi103 – 110Combined sources8
Beta strandi113 – 115Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi126 – 134Combined sources9
Beta strandi142 – 145Combined sources4
Helixi153 – 155Combined sources3
Turni159 – 161Combined sources3
Turni168 – 170Combined sources3
Beta strandi171 – 178Combined sources8
Beta strandi183 – 189Combined sources7
Helixi194 – 197Combined sources4
Beta strandi200 – 206Combined sources7
Beta strandi214 – 225Combined sources12
Helixi230 – 237Combined sources8
Beta strandi245 – 250Combined sources6
Turni257 – 259Combined sources3
Beta strandi266 – 269Combined sources4
Beta strandi274 – 281Combined sources8
Beta strandi288 – 292Combined sources5
Beta strandi297 – 302Combined sources6
Beta strandi305 – 313Combined sources9
Beta strandi315 – 317Combined sources3
Beta strandi322 – 328Combined sources7
Beta strandi333 – 341Combined sources9
Helixi344 – 346Combined sources3
Beta strandi351 – 354Combined sources4
Beta strandi357 – 362Combined sources6
Beta strandi390 – 392Combined sources3
Beta strandi398 – 400Combined sources3
Helixi405 – 407Combined sources3
Beta strandi408 – 414Combined sources7
Beta strandi416 – 420Combined sources5
Beta strandi422 – 425Combined sources4
Beta strandi434 – 436Combined sources3
Helixi438 – 444Combined sources7
Helixi451 – 453Combined sources3
Beta strandi455 – 458Combined sources4
Beta strandi464 – 471Combined sources8
Beta strandi481 – 488Combined sources8
Beta strandi490 – 496Combined sources7
Helixi511 – 514Combined sources4
Helixi515 – 517Combined sources3
Beta strandi525 – 531Combined sources7
Beta strandi535 – 542Combined sources8
Beta strandi547 – 553Combined sources7
Helixi556 – 560Combined sources5
Beta strandi564 – 569Combined sources6
Helixi571 – 574Combined sources4
Helixi575 – 577Combined sources3
Helixi580 – 596Combined sources17
Helixi597 – 599Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
IPR033138. Cu_oxidase_CS.
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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ571698 Genomic DNA. Translation: CAE00180.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ571698 Genomic DNA. Translation: CAE00180.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA1. Auxiliary Activities 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.10.3.2. 3208.

Miscellaneous databases

EvolutionaryTraceiQ70KY3.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 70 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.