ID   BLRO_MYRVE              Reviewed;         572 AA.
AC   Q12737;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-NOV-2008, entry version 43.
DE   RecName: Full=Bilirubin oxidase;
DE            EC=1.3.3.5;
DE   Flags: Precursor;
OS   Myrothecium verrucaria.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales;
OC   mitosporic Hypocreales; Myrothecium.
OX   NCBI_TaxID=5532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN
RP   SEQUENCE.
RC   STRAIN=MT-1;
RX   MEDLINE=93366794; PubMed=8360171;
RA   Koikeda S., Ando K., Kaji H., Inoue T., Murao S., Takeuchi K.,
RA   Samejima T.;
RT   "Molecular cloning of the gene for bilirubin oxidase from Myrothecium
RT   verrucaria and its expression in yeast.";
RL   J. Biol. Chem. 268:18801-18809(1993).
CC   -!- FUNCTION: Oxidation of bilirubin and other tetrapyrroles.
CC   -!- CATALYTIC ACTIVITY: 2 bilirubin + O(2) = 2 biliverdin + 2 H(2)O.
CC   -!- COFACTOR: Binds 4 copper ions per monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 2 plastocyanin-like domains.
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DR   EMBL; D14081; BAA03166.1; -; Genomic_DNA.
DR   EMBL; D12579; BAA02123.1; -; mRNA.
DR   PIR; B48521; B48521.
DR   HSSP; P36649; 1KV7.
DR   GO; GO:0047705; F:bilirubin oxidase activity; IEA:EC.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011706; Cu-oxidase_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR008972; Cupredoxin.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 3.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Copper; Direct protein sequencing;
KW   Glycoprotein; Metal-binding; Oxidoreductase; Repeat; Signal.
FT   SIGNAL        1     19       Probable.
FT   PROPEP       20     38
FT                                /FTId=PRO_0000002910.
FT   CHAIN        39    572       Bilirubin oxidase.
FT                                /FTId=PRO_0000002911.
FT   DOMAIN       98    194       Plastocyanin-like 1.
FT   DOMAIN      404    526       Plastocyanin-like 2.
FT   METAL       132    132       Copper 1; type 2 (By similarity).
FT   METAL       134    134       Copper 2; type 3 (By similarity).
FT   METAL       172    172       Copper 2; type 3 (By similarity).
FT   METAL       174    174       Copper 3; type 3 (By similarity).
FT   METAL       436    436       Copper 4; type 1 (By similarity).
FT   METAL       439    439       Copper 1; type 2 (By similarity).
FT   METAL       441    441       Copper 3; type 3 (By similarity).
FT   METAL       494    494       Copper 3; type 3 (By similarity).
FT   METAL       495    495       Copper 4; type 1 (By similarity).
FT   METAL       496    496       Copper 2; type 3 (By similarity).
FT   METAL       500    500       Copper 4; type 1 (By similarity).
FT   METAL       505    505       Copper 4; type 1 (By similarity).
FT   CARBOHYD    510    510       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    520    520       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   572 AA;  63948 MW;  5842D641303E5EFF CRC64;
     MFKHTLGAAA LSLLFNSNAV QASPVPETSP ATGHLFKRVA QISPQYPMFT VPLPIPPVKQ
     PRLTVTNPVN GQEIWYYEVE IKPFTHQVYP DLGSADLVGY DGMSPGPTFQ VPRGVETVVR
     FINNAEAPNS VHLHGSFSRA AFDGWAEDIT EPGSFKDYYY PNRQSARTLW YHDHAMHITA
     ENAYRGQAGL YMLTDPAEDA LNLPSGYGEF DIPMILTSKQ YTANGNLVTT NGELNSFWGD
     VIHVNGQPWP FKNVEPRKYR FRFLDAAVSR SFGLYFADTD AIDTRLPFKV IASDSGLLEH
     PADTSLLYIS MAERYEVVFD FSDYAGKTIE LRNLGGSIGG IGTDTDYDNT DKVMRFVVAD
     DTTQPDTSVV PANLRDVPFP SPTTNTPRQF RFGRTGPTWT INGVAFADVQ NRLLANVPVG
     TVERWELINA GNGWTHPIHI HLVDFKVISR TSGNNARTVM PYESGLKDVV WLGRRETVVV
     EAHYAPFPGV YMFHCHNLIH EDHDMMAAFN ATVLPDYGYN ATVFVDPMEE LWQARPYELG
     EFQAQSGQFS VQAVTERIQT MAEYRPYAAA DE
//