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Protein

Bilirubin oxidase

Gene
N/A
Organism
Myrothecium verrucaria
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Oxidation of bilirubin and other tetrapyrroles.

Catalytic activityi

2 bilirubin + O2 = 2 biliverdin + 2 H2O.

Cofactori

Cu cationBy similarityNote: Binds 4 Cu cations per monomer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi132 – 1321Copper 1; type 2By similarity
Metal bindingi134 – 1341Copper 2; type 3By similarity
Metal bindingi172 – 1721Copper 2; type 3By similarity
Metal bindingi174 – 1741Copper 3; type 3By similarity
Metal bindingi436 – 4361Copper 4; type 1By similarity
Metal bindingi439 – 4391Copper 1; type 2By similarity
Metal bindingi441 – 4411Copper 3; type 3By similarity
Metal bindingi494 – 4941Copper 3; type 3By similarity
Metal bindingi495 – 4951Copper 4; type 1By similarity
Metal bindingi496 – 4961Copper 2; type 3By similarity
Metal bindingi500 – 5001Copper 4; type 1By similarity
Metal bindingi505 – 5051Copper 4; type 1By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BRENDAi1.3.3.5. 3537.

Names & Taxonomyi

Protein namesi
Recommended name:
Bilirubin oxidase (EC:1.3.3.5)
OrganismiMyrothecium verrucaria
Taxonomic identifieri5532 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesStachybotriaceaeMyrothecium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919CuratedAdd
BLAST
Propeptidei20 – 3819PRO_0000002910Add
BLAST
Chaini39 – 572534Bilirubin oxidasePRO_0000002911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence analysis
Glycosylationi520 – 5201N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Structurei

Secondary structure

1
572
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi62 – 665Combined sources
Beta strandi70 – 723Combined sources
Beta strandi75 – 828Combined sources
Turni90 – 923Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi104 – 1129Combined sources
Beta strandi117 – 1237Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi131 – 1344Combined sources
Turni140 – 1445Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1736Combined sources
Helixi179 – 1846Combined sources
Beta strandi188 – 1947Combined sources
Turni196 – 2005Combined sources
Helixi207 – 2104Combined sources
Beta strandi214 – 2196Combined sources
Beta strandi223 – 2253Combined sources
Beta strandi240 – 2445Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi256 – 26510Combined sources
Beta strandi272 – 2765Combined sources
Beta strandi279 – 2813Combined sources
Beta strandi288 – 2936Combined sources
Beta strandi296 – 30510Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi314 – 3207Combined sources
Helixi321 – 3244Combined sources
Beta strandi327 – 3326Combined sources
Beta strandi337 – 3404Combined sources
Beta strandi345 – 3473Combined sources
Turni348 – 3503Combined sources
Beta strandi351 – 3577Combined sources
Beta strandi388 – 3914Combined sources
Beta strandi398 – 4014Combined sources
Turni409 – 4113Combined sources
Beta strandi413 – 4186Combined sources
Beta strandi422 – 4298Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi438 – 4425Combined sources
Beta strandi445 – 4528Combined sources
Beta strandi455 – 4573Combined sources
Helixi462 – 4643Combined sources
Beta strandi467 – 4704Combined sources
Beta strandi474 – 48310Combined sources
Beta strandi489 – 4968Combined sources
Helixi498 – 5025Combined sources
Beta strandi506 – 5116Combined sources
Turni519 – 5224Combined sources
Beta strandi525 – 5295Combined sources
Helixi530 – 5323Combined sources
Helixi539 – 5435Combined sources
Beta strandi549 – 5546Combined sources
Helixi568 – 5703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XLLX-ray2.30A/B/C/D39-572[»]
3ABGX-ray2.30A/B39-572[»]
ProteinModelPortaliQ12737.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12737.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 19497Plastocyanin-like 1Add
BLAST
Domaini404 – 526123Plastocyanin-like 2Add
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 2 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.

Sequencei

Sequence statusi: Complete.

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

Q12737-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKHTLGAAA LSLLFNSNAV QASPVPETSP ATGHLFKRVA QISPQYPMFT
60 70 80 90 100
VPLPIPPVKQ PRLTVTNPVN GQEIWYYEVE IKPFTHQVYP DLGSADLVGY
110 120 130 140 150
DGMSPGPTFQ VPRGVETVVR FINNAEAPNS VHLHGSFSRA AFDGWAEDIT
160 170 180 190 200
EPGSFKDYYY PNRQSARTLW YHDHAMHITA ENAYRGQAGL YMLTDPAEDA
210 220 230 240 250
LNLPSGYGEF DIPMILTSKQ YTANGNLVTT NGELNSFWGD VIHVNGQPWP
260 270 280 290 300
FKNVEPRKYR FRFLDAAVSR SFGLYFADTD AIDTRLPFKV IASDSGLLEH
310 320 330 340 350
PADTSLLYIS MAERYEVVFD FSDYAGKTIE LRNLGGSIGG IGTDTDYDNT
360 370 380 390 400
DKVMRFVVAD DTTQPDTSVV PANLRDVPFP SPTTNTPRQF RFGRTGPTWT
410 420 430 440 450
INGVAFADVQ NRLLANVPVG TVERWELINA GNGWTHPIHI HLVDFKVISR
460 470 480 490 500
TSGNNARTVM PYESGLKDVV WLGRRETVVV EAHYAPFPGV YMFHCHNLIH
510 520 530 540 550
EDHDMMAAFN ATVLPDYGYN ATVFVDPMEE LWQARPYELG EFQAQSGQFS
560 570
VQAVTERIQT MAEYRPYAAA DE
Length:572
Mass (Da):63,948
Last modified:November 1, 1996 - v1
Checksum:i5842D641303E5EFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14081 Genomic DNA. Translation: BAA03166.1.
D12579 mRNA. Translation: BAA02123.1.
PIRiB48521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14081 Genomic DNA. Translation: BAA03166.1.
D12579 mRNA. Translation: BAA02123.1.
PIRiB48521.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XLLX-ray2.30A/B/C/D39-572[»]
3ABGX-ray2.30A/B39-572[»]
ProteinModelPortaliQ12737.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.3.3.5. 3537.

Miscellaneous databases

EvolutionaryTraceiQ12737.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: MT-1.

Entry informationi

Entry nameiBLRO_MYRVE
AccessioniPrimary (citable) accession number: Q12737
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 16, 2015
This is version 71 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.