Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P22185 (AOX1_TYPVN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquinol oxidase 1, mitochondrial

EC=1.10.3.11
Alternative name(s):
Alternative oxidase 1
Gene names
Name:AOX1
OrganismTyphonium venosum (Voodoo lily) (Sauromatum guttatum)
Taxonomic identifier4463 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAraceaeAroideaeAreaeTyphonium

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures. In S.guttatum the alternative respiratory pathway is thermogenic. Ref.1 Ref.3

Catalytic activity

2 ubiquinol + O2 = 2 ubiquinone + 2 H2O.

Cofactor

Binds 2 iron ions per subunit. Ref.4

Enzyme regulation

Not sensitive to pyruvate. Is in a constitutively active state. When the two monomeric subunits are covalently linked by a S-S bond, the enzyme is essentially inactive. Ref.3 Ref.8

Subunit structure

Homodimer; disulfide-linked. Ref.3

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein. Note: Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane. Ref.5

Induction

By salicylic acid. Ref.2 Ref.3 Ref.8

Miscellaneous

The 3 alternative oxidase proteins detected in S.guttatum, with apparent MW of 35 kDa, 36 kDa and 37 kDa, may be post-translationally modified products of the same AOX1 gene.

Sequence similarities

Belongs to the alternative oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6363Mitochondrion Potential
Chain64 – 349286Ubiquinol oxidase 1, mitochondrial
PRO_0000001736

Regions

Transmembrane174 – 19421Helical; Potential
Transmembrane236 – 25621Helical; Potential

Sites

Metal binding1781Iron 1 Potential
Metal binding2171Iron 1 Potential
Metal binding2171Iron 2 Potential
Metal binding2201Iron 1 Potential
Metal binding2691Iron 2 Potential
Metal binding3191Iron 1 Potential
Metal binding3191Iron 2 Potential
Metal binding3221Iron 2 Potential

Amino acid modifications

Disulfide bond122Interchain Potential

Experimental info

Mutagenesis1721C → A: No effect. Ref.7
Mutagenesis2171E → A: Loss of activity. Ref.7
Mutagenesis2531Y → F: No effect. Ref.7
Mutagenesis2701E → N: Loss of activity. Ref.5
Mutagenesis2751Y → F: Loss of activity. Ref.7
Sequence conflict21M → I in CAA78823. Ref.2
Sequence conflict71V → A in CAA78823. Ref.2
Sequence conflict401G → R in CAA78823. Ref.2
Sequence conflict701P → R in CAA78823. Ref.2
Sequence conflict2841S → N in CAA78823. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P22185 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 6E70B2B7A858B273

FASTA34938,931
        10         20         30         40         50         60 
MMSSRLVGTA LCRQLSHVPV PQYLPALRPT ADTASSLLHG CSAAAPAQRA GLWPPSWFSP 

        70         80         90        100        110        120 
PRHASTLSAP AQDGGKEKAA GTAGKVPPGE DGGAEKEAVV SYWAVPPSKV SKEDGSEWRW 

       130        140        150        160        170        180 
TCFRPWETYQ ADLSIDLHKH HVPTTILDKL ALRTVKALRW PTDIFFQRRY ACRAMMLETV 

       190        200        210        220        230        240 
AAVPGMVGGV LLHLKSLRRF EHSGGWIRAL LEEAENERMH LMTFMEVAQP RWYERALVLA 

       250        260        270        280        290        300 
VQGVFFNAYF LGYLLSPKFA HRVVGYLEEE AIHSYTEFLK DIDSGAIQDC PAPAIALDYW 

       310        320        330        340 
RLPQGSTLRD VVTVVRADEA HHRDVNHFAS DVHYQDLELK TTPAPLGYH 

« Hide

References

[1]"Isolation and characterization of a cDNA clone encoding an alternative oxidase protein of Sauromatum guttatum (Schott)."
Rhoads D.M., McIntosh L.
Proc. Natl. Acad. Sci. U.S.A. 88:2122-2126(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 67-75, FUNCTION.
[2]"The salicylic acid-inducible alternative oxidase gene aox1 and genes encoding pathogenesis-related proteins share regions of sequence similarity in their promoters."
Rhoads D.M., McIntosh L.
Plant Mol. Biol. 21:615-624(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY SALICYLIC ACID.
[3]"Covalent and noncovalent dimers of the cyanide-resistant alternative oxidase protein in higher plant mitochondria and their relationship to enzyme activity."
Umbach A.L., Siedow J.N.
Plant Physiol. 103:845-854(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, ENZYME REGULATION.
[4]"The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center."
Siedow J.N., Umbach A.L., Moore A.L.
FEBS Lett. 362:10-14(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: IRON-BINDING SITES, COFACTOR, 3D-STRUCTURE MODELING.
[5]"A highly conserved glutamate residue (Glu-270) is essential for plant alternative oxidase activity."
Albury M.S., Affourtit C., Moore A.L.
J. Biol. Chem. 273:30301-30305(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-270, SUBCELLULAR LOCATION.
[6]"A revised model of the active site of alternative oxidase."
Andersson M.E., Nordlund P.
FEBS Lett. 449:17-22(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IRON-BINDING SITES.
[7]"Structure of the plant alternative oxidase. Site-directed mutagenesis provides new information on the active site and membrane topology."
Albury M.S., Affourtit C., Crichton P.G., Moore A.L.
J. Biol. Chem. 277:1190-1194(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CSY-172; GLU-217; TYR-253 AND TYR-275.
[8]"Constitutive activity of Sauromatum guttatum alternative oxidase in Schizosaccharomyces pombe implicates residues in addition to conserved cysteines in alpha-keto acid activation."
Crichton P.G., Affourtit C., Albury M.S., Carre J.E., Moore A.L.
FEBS Lett. 579:331-336(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.

Web resources

Protein Spotlight

The beetle's brothel - Issue 107 of July 2009

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60330 mRNA. Translation: AAA34048.1.
Z15117 Genomic DNA. Translation: CAA78823.1.
PIRA39158.
S30143.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-10382.

Family and domain databases

InterProIPR002680. AOX.
[Graphical view]
PfamPF01786. AOX. 1 hit.
[Graphical view]
PIRSFPIRSF005229. AOX. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAOX1_TYPVN
AccessionPrimary (citable) accession number: P22185
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries