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Protein
Submitted name:

Aryl-alcohol oxidase

Gene

aao

Organism
Pleurotus eryngii (Boletus of the steppes)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881FADCombined sources
Binding sitei114 – 1141FADCombined sources
Binding sitei258 – 2581FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei528 – 5281FADCombined sources
Binding sitei563 – 5631FAD; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 402FADCombined sources
Nucleotide bindingi60 – 612FADCombined sources
Nucleotide bindingi118 – 1214FADCombined sources
Nucleotide bindingi574 – 5752FADCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseImported

Keywords - Ligandi

FADUniRule annotationCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17609.
BRENDAi1.1.3.7. 4910.
SABIO-RKO94219.

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.
mycoCLAPiAAO3A_PLEER.

Names & Taxonomyi

Protein namesi
Submitted name:
Aryl-alcohol oxidaseImported (EC:1.1.3.7Imported)
Gene namesi
Name:aaoImported
OrganismiPleurotus eryngii (Boletus of the steppes)Imported
Taxonomic identifieri5323 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesPleurotaceaePleurotus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 593572Sequence analysisPRO_5004161117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi275 ↔ 290Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FIMX-ray2.55B28-593[»]
ProteinModelPortaliO94219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini300 – 31415GMC_OxRdtase_NInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00624. GMC_OXRED_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O94219-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFGALRQLL LIACLALPSL AATNLPTADF DYVVVGAGNA GNVVAARLTE
60 70 80 90 100
DPDVSVLVLE AGVSDENVLG AEAPLLAPGL VPNSIFDWNY TTTAQAGYNG
110 120 130 140 150
RSIAYPRGRM LGGSSSVHYM VMMRGSTEDF DRYAAVTGDE GWNWDNIQQF
160 170 180 190 200
VRKNEMVVPP ADNHNTSGEF IPAVHGTNGS VSISLPGFPT PLDDRVLATT
210 220 230 240 250
QEQSEEFFFN PDMGTGHPLG ISWSIASVGN GQRSSSSTAY LRPAQSRPNL
260 270 280 290 300
SVLINAQVTK LVNSGTTNGL PAFRCVEYAE QEGAPTTTVC AKKEVVLSAG
310 320 330 340 350
SVGTPILLQL SGIGDENDLS SVGIDTIVNN PSVGRNLSDH LLLPAAFFVN
360 370 380 390 400
SNQTFDNIFR DSSEFNVDLD QWTNTRTGPL TALIANHLAW LRLPSNSSIF
410 420 430 440 450
QTFPDPAAGP NSAHWETIFS NQWFHPAIPR PDTGSFMSVT NALISPVARG
460 470 480 490 500
DIKLATSNPF DKPLINPQYL STEFDIFTMI QAVKSNLRFL SGQAWADFVI
510 520 530 540 550
RPFDPRLRDP TDDAAIESYI RDNANTIFHP VGTASMSPRG ASWGVVDPDL
560 570 580 590
KVKGVDGLRI VDGSILPFAP NAHTQGPIYL VGKQGADLIK ADQ
Length:593
Mass (Da):63,709
Last modified:May 1, 1999 - v1
Checksum:i5FCB95CD2E4A5422
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064069 Genomic DNA. Translation: AAC72747.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064069 Genomic DNA. Translation: AAC72747.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FIMX-ray2.55B28-593[»]
ProteinModelPortaliO94219.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiAA3. Auxiliary Activities 3.
mycoCLAPiAAO3A_PLEER.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17609.
BRENDAi1.1.3.7. 4910.
SABIO-RKO94219.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Substrate specificity and properties of the aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryngii."
    Guillen F., Martinez A.T., Martinez M.J.
    Eur. J. Biochem. 209:603-611(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC90787Imported.
    Tissue: Mycelium sampleImported.
  2. "Description of a new gene coding the aryl-alcohol oxidase of Pleurotus eryngii."
    Varela E., Martinez A.T., Martinez M.J.
    (In) Martin, J.F. and Gutierrez, S. (eds.); FUNGAL GENETICS, pp.220-0, Unknown Publisher (1998)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC90787Imported.
    Tissue: Mycelium sampleImported.
  3. "Molecular characterization of a new gene coding the aryl-alcohol oxidase of Pleurotus eryngii."
    Varela E., Martinez A.T., Martinez M.J.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC90787Imported.
    Tissue: Mycelium sampleImported.
  4. "In vitro activation, purification, and characterization of Escherichia coli expressed aryl-alcohol oxidase, a unique H2O2-producing enzyme."
    Ruiz-Duenas F.J., Ferreira P., Martinez M.J., Martinez A.T.
    Protein Expr. Purif. 45:191-199(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC90787Imported.
    Tissue: Mycelium sampleImported.
  5. "Novel structural features in the GMC family of oxidoreductases revealed by the crystal structure of fungal aryl-alcohol oxidase."
    Fernandez I.S., Ruiz-Duenas F.J., Santillana E., Ferreira P., Martinez M.J., Martinez A.T., Romero A.
    Acta Crystallogr. D 65:1196-1205(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 28-593 IN COMPLEX WITH FAD, DISULFIDE BONDS.

Entry informationi

Entry nameiO94219_PLEER
AccessioniPrimary (citable) accession number: O94219
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.