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Q39219 (AOX1A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ubiquinol oxidase 1a, mitochondrial

EC=1.10.3.11
Alternative name(s):
Alternative oxidase 1a
Gene names
Name:AOX1A
Synonyms:AOX1, HSR3
Ordered Locus Names:At3g22370
ORF Names:MCB17.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length354 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. Increases respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures. Ref.6 Ref.9 Ref.19

Catalytic activity

2 ubiquinol + O2 = 2 ubiquinone + 2 H2O. Ref.9

Cofactor

Binds 2 iron ions per subunit. Ref.8 Ref.11 Ref.13

Enzyme regulation

When the two monomeric subunits are covalently linked by a S-S bond, the enzyme is essentially inactive. When the disulfide bond is reduced, its component sulfhydryls can associate with K-keto acids through formation of a thiohemiacetal, resulting in enzyme activation. Activated by glyoxylate, irrespective to the substitution found at Cys-127. That suggests the presence of a second activation site, possibly Cys-177. Ref.10 Ref.12

Subunit structure

Homodimer; disulfide-linked. Ref.10

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein Probable. Note: Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane. Ref.17

Tissue specificity

Expressed in roots, stems, cotyledons, leaves and flowers. High expression in sepals. Ref.1 Ref.20 Ref.21

Developmental stage

Expressed throughout development. Low expression during 48 hours after imbibition and then increases. Ref.14 Ref.20

Induction

Up-regulated by antimycin A, low-nitrogen and salt stresses, high light, H2O2, ethylene, paraquat, rotenone, salicylic acid, malonate,erythromycin and cold treatments. Ref.1 Ref.10 Ref.12 Ref.14 Ref.15 Ref.18 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.28

Disruption phenotype

No visible phenotype under normal growth conditions. Decreased operating efficiency of photosystem II and an enhanced activity of cyclic electron transport around photosystem I. Altered photosynthetic carbon metabolism when grown under high CO2 concentrations. Ref.23 Ref.25 Ref.27 Ref.29

Miscellaneous

Cys-127 is involved in the sulfhydryl/disulfide regulation system, but is not required for subunit dimerization. Presence of a positive charge at this residue 127 confers activity while an uncharged substitution creates an inactive enzyme (Ref.10, Ref.15).

Sequence similarities

Belongs to the alternative oxidase family.

Sequence caution

The sequence CAA10364.1 differs from that shown. Reason: Frameshift at position 6.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Mitochondrion Potential
Chain63 – 354292Ubiquinol oxidase 1a, mitochondrial
PRO_0000001731

Regions

Transmembrane179 – 19921Helical; Potential
Transmembrane241 – 26121Helical; Potential

Sites

Metal binding1831Iron Potential
Metal binding2221Iron Potential
Metal binding2251Iron Potential
Metal binding2741Iron Potential
Metal binding3241Iron Potential
Metal binding3271Iron Potential

Amino acid modifications

Disulfide bond127Interchain Ref.10

Experimental info

Mutagenesis1271C → A, L or Q: Loss of activity and stimulation by pyruvate. Ref.10 Ref.12 Ref.15
Mutagenesis1271C → E, D, R or K: Active enzyme insensitive to stimulation by pyruvate. Ref.10 Ref.12 Ref.15
Mutagenesis1271C → S: Loss of oxidative inactivation and stimulation by pyruvate, but can be activated by succinate. Ref.10 Ref.12 Ref.15
Mutagenesis1771C → A: No effect on stimulation by pyruvate. Ref.10
Mutagenesis2641F → L: Increased resistance to a substrate-analog inhibitor. Ref.9
Mutagenesis2681M → I or V: Increased resistance to a substrate-analog inhibitor. Ref.9
Mutagenesis3521G → E: Increased resistance to a substrate-analog inhibitor. Ref.9
Sequence conflict371A → R in CAA10364. Ref.2
Sequence conflict50 – 512IW → MD in AAA32870. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q39219 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 6DA19881E8BC9382

FASTA35439,980
        10         20         30         40         50         60 
MMITRGGAKA AKSLLVAAGP RLFSTVRTVS SHEALSASHI LKPGVTSAWI WTRAPTIGGM 

        70         80         90        100        110        120 
RFASTITLGE KTPMKEEDAN QKKTENESTG GDAAGGNNKG DKGIASYWGV EPNKITKEDG 

       130        140        150        160        170        180 
SEWKWNCFRP WETYKADITI DLKKHHVPTT FLDRIAYWTV KSLRWPTDLF FQRRYGCRAM 

       190        200        210        220        230        240 
MLETVAAVPG MVGGMLLHCK SLRRFEQSGG WIKALLEEAE NERMHLMTFM EVAKPKWYER 

       250        260        270        280        290        300 
ALVITVQGVF FNAYFLGYLI SPKFAHRMVG YLEEEAIHSY TEFLKELDKG NIENVPAPAI 

       310        320        330        340        350 
AIDYWRLPAD ATLRDVVMVV RADEAHHRDV NHFASDIHYQ GRELKEAPAP IGYH 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the gene family for alternative oxidase from Arabidopsis thaliana."
Saisho D., Nambara E., Naito S., Tsutsumi N., Hirai A., Nakazono M.
Plant Mol. Biol. 35:585-596(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY ANTIMYCIN A, TISSUE SPECIFICITY.
Strain: cv. Columbia.
Tissue: Leaf and Stem.
[2]"Identification of new early markers of the hypersensitive response in Arabidopsis thaliana."
Lacomme C.J., Roby D.
FEBS Lett. 459:149-153(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Arabidopsis alternative oxidase sustains Escherichia coli respiration."
Kumar A.M., Soell D.
Proc. Natl. Acad. Sci. U.S.A. 89:10842-10846(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-354, FUNCTION.
[7]Johnson Potter F., Wiskich J.T.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-354.
[8]"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.
[9]"Isolation of mutants of the Arabidopsis thaliana alternative oxidase (ubiquinol:oxygen oxidoreductase) resistant to salicylhydroxamic acid."
Berthold D.A.
Biochim. Biophys. Acta 1364:73-83(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-264; MET-268 AND GLY-352.
[10]"Regulation of the cyanide-resistant alternative oxidase of plant mitochondria. Identification of the cysteine residue involved in alpha-keto acid stimulation and intersubunit disulfide bond formation."
Rhoads D.M., Umbach A.L., Sweet C.R., Lennon A.M., Rauch G.S., Siedow J.N.
J. Biol. Chem. 273:30750-30756(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-127 AND CYS-177, SUBUNIT, DISULFIDE BOND, ENZYME REGULATION.
[11]"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, COFACTOR.
[12]"A single amino acid change in the plant alternative oxidase alters the specificity of organic acid activation."
Djajanegara I., Holtzapffel R., Finnegan P.M., Hoefnagel M.H., Berthold D.A., Wiskich J.T., Day D.A.
FEBS Lett. 454:220-224(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-127, ENZYME REGULATION.
[13]"New insight into the structure and function of the alternative oxidase."
Berthold D.A., Andersson M.E., Nordlund P.
Biochim. Biophys. Acta 1460:241-254(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IRON-BINDING SITES, COFACTOR.
[14]"The gene for alternative oxidase-2 (AOX2) from Arabidopsis thaliana consists of five exons unlike other AOX genes and is transcribed at an early stage during germination."
Saisho D., Nakazono M., Lee K.-H., Tsutsumi N., Akita S., Hirai A.
Genes Genet. Syst. 76:89-97(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, INDUCTION BY ANTIMYCIN A.
Strain: cv. Columbia GL1.
[15]"Activation of the plant mitochondrial alternative oxidase: insights from site-directed mutagenesis."
Umbach A.L., Gonzalez-Meler M.A., Sweet C.R., Siedow J.N.
Biochim. Biophys. Acta 1554:118-128(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-127, INDUCTION BY GLYOXLATE.
[16]"EPR studies of the mitochondrial alternative oxidase. Evidence for a diiron carboxylate center."
Berthold D.A., Voevodskaya N., Stenmark P., Graslund A., Nordlund P.
J. Biol. Chem. 277:43608-43614(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: EPR SPECTROSCOPY.
[17]"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Landsberg erecta.
[18]"Stress-induced co-expression of alternative respiratory chain components in Arabidopsis thaliana."
Clifton R., Lister R., Parker K.L., Sappl P.G., Elhafez D., Millar A.H., Day D.A., Whelan J.
Plant Mol. Biol. 58:193-212(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ABIOTIC STRESSES.
[19]"The alternative oxidase of plant mitochondria is involved in the acclimation of shoot growth at low temperature. A study of Arabidopsis AOX1a transgenic plants."
Fiorani F., Umbach A.L., Siedow J.N.
Plant Physiol. 139:1795-1805(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"Alternative oxidases in Arabidopsis: a comparative analysis of differential expression in the gene family provides new insights into function of non-phosphorylating bypasses."
Clifton R., Millar A.H., Whelan J.
Biochim. Biophys. Acta 1757:730-741(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[21]"Characterization of mitochondrial alternative NAD(P)H dehydrogenases in Arabidopsis: intraorganelle location and expression."
Elhafez D., Murcha M.W., Clifton R., Soole K.L., Day D.A., Whelan J.
Plant Cell Physiol. 47:43-54(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[22]"Alternative oxidase involvement in cold stress response of Arabidopsis thaliana fad2 and FAD3+ cell suspensions altered in membrane lipid composition."
Matos A.R., Hourton-Cabassa C., Cicek D., Reze N., Arrabaca J.D., Zachowski A., Moreau F.
Plant Cell Physiol. 48:856-865(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY COLD.
[23]"Induction of the AOX1D isoform of alternative oxidase in A. thaliana T-DNA insertion lines lacking isoform AOX1A is insufficient to optimize photosynthesis when treated with antimycin A."
Strodtkoetter I., Padmasree K., Dinakar C., Speth B., Niazi P.S., Wojtera J., Voss I., Do P.T., Nunes-Nesi A., Fernie A.R., Linke V., Raghavendra A.S., Scheibe R.
Mol. Plant 2:284-297(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[24]"Differential gene expression profiles of the mitochondrial respiratory components in illuminated Arabidopsis leaves."
Yoshida K., Noguchi K.
Plant Cell Physiol. 50:1449-1462(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY HIGH LIGHT.
[25]"Effects of AOX1a deficiency on plant growth, gene expression of respiratory components and metabolic profile under low-nitrogen stress in Arabidopsis thaliana."
Watanabe C.K., Hachiya T., Takahara K., Kawai-Yamada M., Uchimiya H., Uesono Y., Terashima I., Noguchi K.
Plant Cell Physiol. 51:810-822(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY LOW-NITROGEN STRESS, DISRUPTION PHENOTYPE.
[26]"Involvement of ethylene and hydrogen peroxide in induction of alternative respiratory pathway in salt-treated Arabidopsis calluses."
Wang H., Liang X., Huang J., Zhang D., Lu H., Liu Z., Bi Y.
Plant Cell Physiol. 51:1754-1765(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY SALT STRESS; H(2)O(2) AND ETHYLENE.
[27]"Physiological impact of mitochondrial alternative oxidase on photosynthesis and growth in Arabidopsis thaliana."
Yoshida K., Watanabe C.K., Terashima I., Noguchi K.
Plant Cell Environ. 34:1890-1899(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[28]"Involvement of hydrogen peroxide, calcium, and ethylene in the induction of the alternative pathway in chilling-stressed Arabidopsis callus."
Wang H., Huang J., Liang X., Bi Y.
Planta 235:53-67(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY COLD AND ETHYLENE.
[29]"The absence of alternative oxidase AOX1A results in altered response of photosynthetic carbon assimilation to increasing CO2 in Arabidopsis thaliana."
Gandin A., Duffes C., Day D.A., Cousins A.B.
Plant Cell Physiol. 53:1627-1637(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89875 Genomic DNA. Translation: BAA22625.1.
AJ131392 mRNA. Translation: CAA10364.1. Frameshift.
AB022215 Genomic DNA. Translation: BAB01775.1.
CP002686 Genomic DNA. Translation: AEE76627.1.
AF370166 mRNA. Translation: AAK43981.1.
AY059128 mRNA. Translation: AAL15234.1.
M96417 mRNA. Translation: AAA32870.1.
U85244 Genomic DNA. Translation: AAB49302.1.
PIRA46364.
T51615.
RefSeqNP_188876.1. NM_113135.3.
UniGeneAt.23475.

3D structure databases

ProteinModelPortalQ39219.
SMRQ39219. Positions 145-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ39219. 1 interaction.
STRING3702.AT3G22370.1-P.

Proteomic databases

PaxDbQ39219.
PRIDEQ39219.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G22370.1; AT3G22370.1; AT3G22370.
GeneID821806.
KEGGath:AT3G22370.

Organism-specific databases

GeneFarm1749. 131.
TAIRAT3G22370.

Phylogenomic databases

eggNOGNOG80852.
HOGENOMHOG000178442.
InParanoidQ39219.
KOK17893.
OMAKEEDANQ.
PhylomeDBQ39219.
ProtClustDBPLN02478.

Enzyme and pathway databases

BioCycMetaCyc:AT3G22370-MONOMER.

Gene expression databases

GenevestigatorQ39219.

Family and domain databases

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

Entry information

Entry nameAOX1A_ARATH
AccessionPrimary (citable) accession number: Q39219
Secondary accession number(s): O23914, P93734, Q9ZRT8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: March 19, 2014
This is version 117 of the entry and version 2 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names