Ubiquinol oxidase 1, mitochondrial precursor - Typhonium venosum (Voodoo lily)

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P22185 (AOX1_TYPVN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ubiquinol oxidase 1, mitochondrial
EC=1.10.3.11

Alternative name(s):
Alternative oxidase 1

Gene names

Name:

AOX1

Organism

Typhonium venosum (Voodoo lily) (Sauromatum guttatum)

Taxonomic identifier

4463 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Araceae › Aroideae › Areae › Typhonium

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW respiratory gaseous exchange Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	alternative oxidase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 63

Mitochondrion Potential

Chain

64 – 349

286

Ubiquinol oxidase 1, mitochondrial

PRO_0000001736

Regions

Transmembrane

174 – 194

Helical; Potential

Transmembrane

236 – 256

Helical; Potential

Sites

Metal binding

178

Iron 1 Potential

Metal binding

217

Iron 1 Potential

Metal binding

217

Iron 2 Potential

Metal binding

220

Iron 1 Potential

Metal binding

269

Iron 2 Potential

Metal binding

319

Iron 1 Potential

Metal binding

319

Iron 2 Potential

Metal binding

322

Iron 2 Potential

Amino acid modifications

Disulfide bond

122

Interchain Potential

Experimental info

Mutagenesis

172

C → A: No effect. Ref.7

Mutagenesis

217

E → A: Loss of activity. Ref.7

Mutagenesis

253

Y → F: No effect. Ref.7

Mutagenesis

270

E → N: Loss of activity. Ref.5

Mutagenesis

275

Y → F: Loss of activity. Ref.7

Sequence conflict

M → I in CAA78823. Ref.2

Sequence conflict

V → A in CAA78823. Ref.2

Sequence conflict

G → R in CAA78823. Ref.2

Sequence conflict

P → R in CAA78823. Ref.2

Sequence conflict

284

S → N in CAA78823. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P22185 [UniParc].

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

349

38,931

        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

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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.
PIR	A39158. S30143.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-10382.
Family and domain databases
InterPro	IPR002680. AOX. [Graphical view]
Pfam	PF01786. AOX. 1 hit. [Graphical view]
PIRSF	PIRSF005229. AOX. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AOX1_TYPVN

Accession

Primary (citable) accession number: P22185

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents