BLRO_ALBVE
ID BLRO_ALBVE Reviewed; 572 AA.
AC Q12737;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Bilirubin oxidase;
DE EC=1.3.3.5;
DE Flags: Precursor;
OS Albifimbria verrucaria (Myrothecium leaf spot and pod blight fungus)
OS (Myrothecium verrucaria).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Albifimbria.
OX NCBI_TaxID=1859699;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=MT-1;
RX PubMed=8360171; DOI=10.1016/s0021-9258(17)46699-3;
RA Koikeda S., Ando K., Kaji H., Inoue T., Murao S., Takeuchi K., 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:
CC Reaction=2 bilirubin IXalpha + O2 = 2 biliverdin IXalpha + 2 H2O;
CC Xref=Rhea:RHEA:20980, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57977, ChEBI:CHEBI:57991; EC=1.3.3.5;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; D14081; BAA03166.1; -; Genomic_DNA.
DR EMBL; D12579; BAA02123.1; -; mRNA.
DR PIR; B48521; B48521.
DR PDB; 2XLL; X-ray; 2.30 A; A/B/C/D=39-572.
DR PDB; 3ABG; X-ray; 2.30 A; A/B=39-572.
DR PDB; 6I3J; X-ray; 2.59 A; A/B=39-572.
DR PDB; 6I3K; X-ray; 1.60 A; A/B=39-572.
DR PDB; 6I3L; X-ray; 2.10 A; A/B=39-572.
DR PDB; 6IQX; X-ray; 1.43 A; A/B=39-572.
DR PDB; 6IQY; X-ray; 1.60 A; A/B=39-572.
DR PDB; 6IQZ; X-ray; 1.46 A; A=39-572.
DR PDBsum; 2XLL; -.
DR PDBsum; 3ABG; -.
DR PDBsum; 6I3J; -.
DR PDBsum; 6I3K; -.
DR PDBsum; 6I3L; -.
DR PDBsum; 6IQX; -.
DR PDBsum; 6IQY; -.
DR PDBsum; 6IQZ; -.
DR AlphaFoldDB; Q12737; -.
DR SMR; Q12737; -.
DR KEGG; ag:BAA03166; -.
DR BRENDA; 1.3.3.5; 3537.
DR EvolutionaryTrace; Q12737; -.
DR GO; GO:0047705; F:bilirubin oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Copper;
KW Direct protein sequencing; Glycoprotein; Metal-binding; Oxidoreductase;
KW Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000305"
FT PROPEP 20..38
FT /id="PRO_0000002910"
FT CHAIN 39..572
FT /note="Bilirubin oxidase"
FT /id="PRO_0000002911"
FT DOMAIN 98..194
FT /note="Plastocyanin-like 1"
FT DOMAIN 404..526
FT /note="Plastocyanin-like 2"
FT BINDING 132
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 436
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 505
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6IQX"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 73..86
FT /evidence="ECO:0007829|PDB:6IQX"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3ABG"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:3ABG"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3ABG"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:6IQX"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:6IQX"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3ABG"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6IQY"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:3ABG"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:6IQX"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 421..428
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3ABG"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 445..452
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:3ABG"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 476..484
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 506..512
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:6IQX"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:3ABG"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 539..544
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 551..563
FT /evidence="ECO:0007829|PDB:6IQX"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:6IQX"
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
