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Conserved domains on  [gi|30697967|ref|NP_201226|]
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alternative oxidase 2 [Arabidopsis thaliana]

Protein Classification

alternative oxidase( domain architecture ID 10010803)

alternative oxidase, also called ubiquinol oxidase, 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; belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02478 PLN02478
alternative oxidase
19-353 0e+00

alternative oxidase


:

Pssm-ID: 215265  Cd Length: 328  Bit Score: 634.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   19 GNCNMFVSSVSSTSVMKSPYEITAPMRIHDWCGGFGDFKIGSKHVQGNFNLRWMGMSSASAMEKKDENLTVKKGQngggs 98
Cdd:PLN02478   1 GLCNRLVSSASSASHMKSPLFPAAPMRIGDRAPRFGGFRIGSKHAQEEKKLAEEEESSGKATENKDEGSTVKGGQ----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   99 VAVPSYWGIETAKmkITRKDGSDWPWNCFMPWETYQANLSIDLKKHHVPKNIADKVAYRIVKLLRIPTDIFFQRRYGCRA 178
Cdd:PLN02478  76 KAIVSYWGIEPAK--ITKEDGTEWKWNCFRPWETYKADLSIDLKKHHVPKTLLDKIAYWTVKSLRVPTDLFFQRRYGCRA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967  179 MMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWIKALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIFFNSFFVCYV 258
Cdd:PLN02478 154 MMLETVAAVPGMVGGMLLHLKSLRRFEHSGGWIKALLEEAENERMHLMTFMEVAKPKWYERALVIAVQGVFFNAYFLGYL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967  259 ISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKIENVAAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDVNHFASDIRN 338
Cdd:PLN02478 234 ISPKFAHRIVGYLEEEAIHSYTEFLKDLDAGKIENVPAPAIAIDYWRLPADATLRDVVTVVRADEAHHRDVNHFASDIHY 313
                        330
                 ....*....|....*
gi 30697967  339 QGKELREAAAPIGYH 353
Cdd:PLN02478 314 QGKELKEAPAPIGYH 328
 
Name Accession Description Interval E-value
PLN02478 PLN02478
alternative oxidase
19-353 0e+00

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 634.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   19 GNCNMFVSSVSSTSVMKSPYEITAPMRIHDWCGGFGDFKIGSKHVQGNFNLRWMGMSSASAMEKKDENLTVKKGQngggs 98
Cdd:PLN02478   1 GLCNRLVSSASSASHMKSPLFPAAPMRIGDRAPRFGGFRIGSKHAQEEKKLAEEEESSGKATENKDEGSTVKGGQ----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   99 VAVPSYWGIETAKmkITRKDGSDWPWNCFMPWETYQANLSIDLKKHHVPKNIADKVAYRIVKLLRIPTDIFFQRRYGCRA 178
Cdd:PLN02478  76 KAIVSYWGIEPAK--ITKEDGTEWKWNCFRPWETYKADLSIDLKKHHVPKTLLDKIAYWTVKSLRVPTDLFFQRRYGCRA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967  179 MMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWIKALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIFFNSFFVCYV 258
Cdd:PLN02478 154 MMLETVAAVPGMVGGMLLHLKSLRRFEHSGGWIKALLEEAENERMHLMTFMEVAKPKWYERALVIAVQGVFFNAYFLGYL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967  259 ISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKIENVAAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDVNHFASDIRN 338
Cdd:PLN02478 234 ISPKFAHRIVGYLEEEAIHSYTEFLKDLDAGKIENVPAPAIAIDYWRLPADATLRDVVTVVRADEAHHRDVNHFASDIHY 313
                        330
                 ....*....|....*
gi 30697967  339 QGKELREAAAPIGYH 353
Cdd:PLN02478 314 QGKELKEAPAPIGYH 328
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
143-335 7.33e-112

Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the mitochondria, electrons are transfered directly from reduced ubiquinol to oxygen forming water. This is not coupled to ATP synthesis and is not inhibited by cyanide, this pathway is a single step process. In rice the transcript levels of the alternative oxidase are increased by low temperature.


Pssm-ID: 460328  Cd Length: 218  Bit Score: 324.50  E-value: 7.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   143 KHHVPKNIADKVAYRIVKLLRIPTDIFF-----------QRRYGCRAMMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWI 211
Cdd:pfam01786  12 THREPKTFSDKVAYGLVKFLRWLFDLLTgykhppppemtERKWLHRAIFLETVAGVPGMVAGMLRHLRSLRLMKRDNGWI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   212 KALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIFFNSFFVCYVISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKI 291
Cdd:pfam01786  92 HTLLEEAENERMHLLTFLKLAKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYTHAIEDIDAGKL 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 30697967   292 EN---VAAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDVNHFASD 335
Cdd:pfam01786 172 PNwenMPAPEIAIDYWGLPEDATLRDLILAIRADEAKHRDVNHTLAN 218
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
170-336 4.45e-101

Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a mitochondrial ubiquinol oxidase found in plants and some fungi and protists. AOX is a member of the ferritin-like diiron-carboxylate superfamily. The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. AOX is a cyanide-resistant, salicylhydroxamic acid-sensitive oxidase that transfers electrons from ubiquinol to oxygen, bypassing the cytochrome chain. AOX has been proposed to contain a hydroxo-bridged diiron center within a four-helix bundle and a proximal redox-active tyrosine residue. AOX is proposed to be peripherally associated with the matrix side of the inner mitochondrial membrane. Fungal and protozoan AOXs generally exist as monomers. In plants, AOX is dimeric. Pyruvate is an allosteric activator of plant AOX involved in the reversible inactivation of the enzyme though the formation of an intermolecular disulfide bridge between monomeric subunits. The enzyme is non-proton-motive and does not contribute to the conservation of energy. The heat that dissipates from AOX activity is used in thermogenic plants to volatilize primary amines to attract pollinating insects. Other functions have been proposed: i) that the alternative oxidase allows Krebs-cycle turnover when the energy charge of the cell is high, and ii) that the enzyme protects against oxidative stress. The expression of AOX is induced when plants are exposed to a variety of stresses including chilling, pathogen attack, senescence and fruit ripening.


Pssm-ID: 153112  Cd Length: 168  Bit Score: 295.27  E-value: 4.45e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967 170 FQRRYGCRAMMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWIKALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIF 249
Cdd:cd01053   1 YEDRWLARFIFLETVARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEELGGPGWWFRRFVAQHQAVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967 250 FNSFFVCYVISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKIENVAAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDV 329
Cdd:cd01053  81 YNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKPDLPAPEIAIEYYRLGEDATLYDVFVAIRADEAEHRKV 160

                ....*..
gi 30697967 330 NHFASDI 336
Cdd:cd01053 161 NHACADL 167
 
Name Accession Description Interval E-value
PLN02478 PLN02478
alternative oxidase
19-353 0e+00

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 634.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   19 GNCNMFVSSVSSTSVMKSPYEITAPMRIHDWCGGFGDFKIGSKHVQGNFNLRWMGMSSASAMEKKDENLTVKKGQngggs 98
Cdd:PLN02478   1 GLCNRLVSSASSASHMKSPLFPAAPMRIGDRAPRFGGFRIGSKHAQEEKKLAEEEESSGKATENKDEGSTVKGGQ----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   99 VAVPSYWGIETAKmkITRKDGSDWPWNCFMPWETYQANLSIDLKKHHVPKNIADKVAYRIVKLLRIPTDIFFQRRYGCRA 178
Cdd:PLN02478  76 KAIVSYWGIEPAK--ITKEDGTEWKWNCFRPWETYKADLSIDLKKHHVPKTLLDKIAYWTVKSLRVPTDLFFQRRYGCRA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967  179 MMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWIKALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIFFNSFFVCYV 258
Cdd:PLN02478 154 MMLETVAAVPGMVGGMLLHLKSLRRFEHSGGWIKALLEEAENERMHLMTFMEVAKPKWYERALVIAVQGVFFNAYFLGYL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967  259 ISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKIENVAAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDVNHFASDIRN 338
Cdd:PLN02478 234 ISPKFAHRIVGYLEEEAIHSYTEFLKDLDAGKIENVPAPAIAIDYWRLPADATLRDVVTVVRADEAHHRDVNHFASDIHY 313
                        330
                 ....*....|....*
gi 30697967  339 QGKELREAAAPIGYH 353
Cdd:PLN02478 314 QGKELKEAPAPIGYH 328
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
143-335 7.33e-112

Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the mitochondria, electrons are transfered directly from reduced ubiquinol to oxygen forming water. This is not coupled to ATP synthesis and is not inhibited by cyanide, this pathway is a single step process. In rice the transcript levels of the alternative oxidase are increased by low temperature.


Pssm-ID: 460328  Cd Length: 218  Bit Score: 324.50  E-value: 7.33e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   143 KHHVPKNIADKVAYRIVKLLRIPTDIFF-----------QRRYGCRAMMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWI 211
Cdd:pfam01786  12 THREPKTFSDKVAYGLVKFLRWLFDLLTgykhppppemtERKWLHRAIFLETVAGVPGMVAGMLRHLRSLRLMKRDNGWI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967   212 KALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIFFNSFFVCYVISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKI 291
Cdd:pfam01786  92 HTLLEEAENERMHLLTFLKLAKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYTHAIEDIDAGKL 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 30697967   292 EN---VAAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDVNHFASD 335
Cdd:pfam01786 172 PNwenMPAPEIAIDYWGLPEDATLRDLILAIRADEAKHRDVNHTLAN 218
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
170-336 4.45e-101

Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a mitochondrial ubiquinol oxidase found in plants and some fungi and protists. AOX is a member of the ferritin-like diiron-carboxylate superfamily. The plant mitochondrial protein alternative oxidase catalyses dioxygen dependent ubiquinol oxidation to yield ubiquinone and water. AOX is a cyanide-resistant, salicylhydroxamic acid-sensitive oxidase that transfers electrons from ubiquinol to oxygen, bypassing the cytochrome chain. AOX has been proposed to contain a hydroxo-bridged diiron center within a four-helix bundle and a proximal redox-active tyrosine residue. AOX is proposed to be peripherally associated with the matrix side of the inner mitochondrial membrane. Fungal and protozoan AOXs generally exist as monomers. In plants, AOX is dimeric. Pyruvate is an allosteric activator of plant AOX involved in the reversible inactivation of the enzyme though the formation of an intermolecular disulfide bridge between monomeric subunits. The enzyme is non-proton-motive and does not contribute to the conservation of energy. The heat that dissipates from AOX activity is used in thermogenic plants to volatilize primary amines to attract pollinating insects. Other functions have been proposed: i) that the alternative oxidase allows Krebs-cycle turnover when the energy charge of the cell is high, and ii) that the enzyme protects against oxidative stress. The expression of AOX is induced when plants are exposed to a variety of stresses including chilling, pathogen attack, senescence and fruit ripening.


Pssm-ID: 153112  Cd Length: 168  Bit Score: 295.27  E-value: 4.45e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967 170 FQRRYGCRAMMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWIKALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIF 249
Cdd:cd01053   1 YEDRWLARFIFLETVARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEELGGPGWWFRRFVAQHQAVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967 250 FNSFFVCYVISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKIENVAAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDV 329
Cdd:cd01053  81 YNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKPDLPAPEIAIEYYRLGEDATLYDVFVAIRADEAEHRKV 160

                ....*..
gi 30697967 330 NHFASDI 336
Cdd:cd01053 161 NHACADL 167
Ferritin_like cd00657
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ...
206-328 6.47e-03

Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).


Pssm-ID: 153097  Cd Length: 130  Bit Score: 36.32  E-value: 6.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697967 206 HSGGWIKALLEEAENERMHLMTMMELVkpkwYERLLVMLVQGIFFNSFFVCYVISPRLAHRVVGYL--EEEAIHSYTEFL 283
Cdd:cd00657  25 PDPDLKDELLEIADEERRHADALAERL----RELGGTPPLPPAHLLAAYALPKTSDDPAEALRAALevEARAIAAYRELI 100
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30697967 284 KDIDngkienvaapaiaidywrlpkDATLKDVVTVIRADEAHHRD 328
Cdd:cd00657 101 EQAD---------------------DPELRRLLERILADEQRHAA 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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