Alternative oxidase, mitochondrial precursor - Sauromatum guttatum (Voodoo lily)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P22185 (AOX1_SAUGU)

Last modified November 24, 2009. Version 71. History...

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

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
Alternative oxidase, mitochondrial
EC=1.-.-.-

Gene names

Name:

AOX1

Organism

Sauromatum guttatum (Voodoo lily) (Sauromatum venosum)

Taxonomic identifier

4463 [NCBI]

Taxonomic lineage

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

Hide | Top

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.

Hide | Top

General annotation (Comments)

Function	Catalyzes cyanide-resistant oxygen consumption. 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.
Cofactor	Binds 2 iron ions per subunit By similarity.
Enzyme regulation	Not sensitive to pyruvate. Is in a constitutively active state. Ref.6
Subunit structure	Homodimer; disulfide-linked Probable.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein. Note: Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane. Ref.3
Induction	By salicylic acid.
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.

Hide | Top

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane
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 transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

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

Alternative oxidase, mitochondrial

PRO_0000001736

Regions

Transmembrane

174 – 194

Potential

Transmembrane

236 – 256

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.5

Mutagenesis

217

E → A: Loss of activity. Ref.5

Mutagenesis

253

Y → F: No effect. Ref.5

Mutagenesis

270

E → N: Loss of activity. Ref.3

Mutagenesis

275

Y → F: Loss of activity. Ref.5

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

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P22185-1 [UniParc].

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

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

« Hide

Hide | Top

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: 1706518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 67-75.
[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: 8448361] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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: 9804791] [Abstract] Cited for: MUTAGENESIS OF GLU-270, SUBCELLULAR LOCATION.
[4]	"A revised model of the active site of alternative oxidase." Andersson M.E., Nordlund P. FEBS Lett. 449:17-22(1999) [PubMed: 10225419] [Abstract] Cited for: IRON-BINDING SITES.
[5]	"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: 11698414] [Abstract] Cited for: MUTAGENESIS OF CSY-172; GLU-217; TYR-253 AND TYR-275.
[6]	"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: 15642340] [Abstract] Cited for: ENZYME REGULATION.

Hide | Top

Web resources

Protein Spotlight

The beetle's brothel - Issue 107 of July 2009

Hide | Top

Cross-references

Sequence databases
	M60330 mRNA. Translation: AAA34048.1. Z15117 Genomic DNA. Translation: CAA78823.1.
PIR	A39158. S30143.
3D structure databases
ModBase	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...

Hide | Top

Entry information

Entry name

AOX1_SAUGU

Accession

Primary (citable) accession number: P22185

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	November 24, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

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

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents