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Protein

Bilirubin oxidase

Gene
N/A
Organism
Myrothecium verrucaria (Myrothecium leaf spot and pod blight fungus) (Albifimbria 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)DescriptionActionsGraphical viewLength
Metal bindingi132Copper 1; type 2By similarity1
Metal bindingi134Copper 2; type 3By similarity1
Metal bindingi172Copper 2; type 3By similarity1
Metal bindingi174Copper 3; type 3By similarity1
Metal bindingi436Copper 4; type 1By similarity1
Metal bindingi439Copper 1; type 2By similarity1
Metal bindingi441Copper 3; type 3By similarity1
Metal bindingi494Copper 3; type 3By similarity1
Metal bindingi495Copper 4; type 1By similarity1
Metal bindingi496Copper 2; type 3By similarity1
Metal bindingi500Copper 4; type 1By similarity1
Metal bindingi505Copper 4; type 1By similarity1

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 (Myrothecium leaf spot and pod blight fungus) (Albifimbria verrucaria)
Taxonomic identifieri1859699 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesStachybotriaceaeAlbifimbria

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19CuratedAdd BLAST19
PropeptideiPRO_000000291020 – 38Add BLAST19
ChainiPRO_000000291139 – 572Bilirubin oxidaseAdd BLAST534

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi510N-linked (GlcNAc...)Sequence analysis1
Glycosylationi520N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Structurei

Secondary structure

1572
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi62 – 66Combined sources5
Beta strandi70 – 72Combined sources3
Beta strandi75 – 82Combined sources8
Turni90 – 92Combined sources3
Beta strandi98 – 100Combined sources3
Beta strandi104 – 112Combined sources9
Beta strandi117 – 123Combined sources7
Beta strandi125 – 127Combined sources3
Beta strandi131 – 134Combined sources4
Turni140 – 144Combined sources5
Beta strandi146 – 148Combined sources3
Beta strandi150 – 152Combined sources3
Beta strandi158 – 160Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi168 – 173Combined sources6
Helixi179 – 184Combined sources6
Beta strandi188 – 194Combined sources7
Turni196 – 200Combined sources5
Helixi207 – 210Combined sources4
Beta strandi214 – 219Combined sources6
Beta strandi223 – 225Combined sources3
Beta strandi240 – 244Combined sources5
Beta strandi247 – 249Combined sources3
Beta strandi251 – 254Combined sources4
Beta strandi256 – 265Combined sources10
Beta strandi272 – 276Combined sources5
Beta strandi279 – 281Combined sources3
Beta strandi288 – 293Combined sources6
Beta strandi296 – 305Combined sources10
Beta strandi307 – 309Combined sources3
Beta strandi314 – 320Combined sources7
Helixi321 – 324Combined sources4
Beta strandi327 – 332Combined sources6
Beta strandi337 – 340Combined sources4
Beta strandi345 – 347Combined sources3
Turni348 – 350Combined sources3
Beta strandi351 – 357Combined sources7
Beta strandi388 – 391Combined sources4
Beta strandi398 – 401Combined sources4
Turni409 – 411Combined sources3
Beta strandi413 – 418Combined sources6
Beta strandi422 – 429Combined sources8
Beta strandi431 – 433Combined sources3
Beta strandi438 – 442Combined sources5
Beta strandi445 – 452Combined sources8
Beta strandi455 – 457Combined sources3
Helixi462 – 464Combined sources3
Beta strandi467 – 470Combined sources4
Beta strandi474 – 483Combined sources10
Beta strandi489 – 496Combined sources8
Helixi498 – 502Combined sources5
Beta strandi506 – 511Combined sources6
Turni519 – 522Combined sources4
Beta strandi525 – 529Combined sources5
Helixi530 – 532Combined sources3
Helixi539 – 543Combined sources5
Beta strandi549 – 554Combined sources6
Helixi568 – 570Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XLLX-ray2.30A/B/C/D39-572[»]
3ABGX-ray2.30A/B39-572[»]
ProteinModelPortaliQ12737.
SMRiQ12737.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12737.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini98 – 194Plastocyanin-like 1Add BLAST97
Domaini404 – 526Plastocyanin-like 2Add BLAST123

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XLLX-ray2.30A/B/C/D39-572[»]
3ABGX-ray2.30A/B39-572[»]
ProteinModelPortaliQ12737.
SMRiQ12737.
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...

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: November 2, 2016
This is version 74 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.