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Reviewed, UniProtKB/Swiss-Prot Q12737 (BLRO_MYRVE)

Last modified January 19, 2010. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Bilirubin oxidase
    EC=1.3.3.5
OrganismMyrothecium verrucaria
Taxonomic identifier5532 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › mitosporic Hypocreales › Myrothecium

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Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Oxidation of bilirubin and other tetrapyrroles.

Catalytic activity

2 bilirubin + O2 = 2 biliverdin + 2 H2O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 2 plastocyanin-like domains.

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Ontologies

Keywords
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMCleavage on pair of basic residues
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbilirubin oxidase activity

Inferred from electronic annotation. Source: EC

copper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Probable
Propeptide20 – 3819
PRO_0000002910
Chain39 – 572534Bilirubin oxidase
PRO_0000002911

Regions

Domain98 – 19497Plastocyanin-like 1
Domain404 – 526123Plastocyanin-like 2

Sites

Metal binding1321Copper 1; type 2 By similarity
Metal binding1341Copper 2; type 3 By similarity
Metal binding1721Copper 2; type 3 By similarity
Metal binding1741Copper 3; type 3 By similarity
Metal binding4361Copper 4; type 1 By similarity
Metal binding4391Copper 1; type 2 By similarity
Metal binding4411Copper 3; type 3 By similarity
Metal binding4941Copper 3; type 3 By similarity
Metal binding4951Copper 4; type 1 By similarity
Metal binding4961Copper 2; type 3 By similarity
Metal binding5001Copper 4; type 1 By similarity
Metal binding5051Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation5101N-linked (GlcNAc...) Potential
Glycosylation5201N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q12737-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5842D641303E5EFF

FASTA57263,948
        10         20         30         40         50         60 
MFKHTLGAAA LSLLFNSNAV QASPVPETSP ATGHLFKRVA QISPQYPMFT VPLPIPPVKQ 

        70         80         90        100        110        120 
PRLTVTNPVN GQEIWYYEVE IKPFTHQVYP DLGSADLVGY DGMSPGPTFQ VPRGVETVVR 

       130        140        150        160        170        180 
FINNAEAPNS VHLHGSFSRA AFDGWAEDIT EPGSFKDYYY PNRQSARTLW YHDHAMHITA 

       190        200        210        220        230        240 
ENAYRGQAGL YMLTDPAEDA LNLPSGYGEF DIPMILTSKQ YTANGNLVTT NGELNSFWGD 

       250        260        270        280        290        300 
VIHVNGQPWP FKNVEPRKYR FRFLDAAVSR SFGLYFADTD AIDTRLPFKV IASDSGLLEH 

       310        320        330        340        350        360 
PADTSLLYIS MAERYEVVFD FSDYAGKTIE LRNLGGSIGG IGTDTDYDNT DKVMRFVVAD 

       370        380        390        400        410        420 
DTTQPDTSVV PANLRDVPFP SPTTNTPRQF RFGRTGPTWT INGVAFADVQ NRLLANVPVG 

       430        440        450        460        470        480 
TVERWELINA GNGWTHPIHI HLVDFKVISR TSGNNARTVM PYESGLKDVV WLGRRETVVV 

       490        500        510        520        530        540 
EAHYAPFPGV YMFHCHNLIH EDHDMMAAFN ATVLPDYGYN ATVFVDPMEE LWQARPYELG 

       550        560        570 
EFQAQSGQFS VQAVTERIQT MAEYRPYAAA DE

« Hide

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References

[1]"Molecular cloning of the gene for bilirubin oxidase from Myrothecium verrucaria and its expression in yeast."
Koikeda S., Ando K., Kaji H., Inoue T., Murao S., Takeuchi K., Samejima T.
J. Biol. Chem. 268:18801-18809(1993) [PubMed: 8360171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: MT-1.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D14081 Genomic DNA. Translation: BAA03166.1.
D12579 mRNA. Translation: BAA02123.1.
PIRB48521.

3D structure databases

SMRQ12737. Positions 47-511, 105-542.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.3.5. 20939.

Family and domain databases

InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 3 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameBLRO_MYRVE
AccessionPrimary (citable) accession number: Q12737
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents