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Conserved domains on  [gi|18415888|ref|NP_567658|]
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Alternative oxidase family protein [Arabidopsis thaliana]

Protein Classification

alternative oxidase( domain architecture ID 10099399)

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
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
124-310 8.08e-98

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: 286.80  E-value: 8.08e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888 124 YRDRTYARFFVLETIARVPYFAFMSVLHMYETFGWWRRADYLKVHFAESWNEMHHLLIMEELGGNSWWFDRFLAQHIAtF 203
Cdd:cd01053   1 YEDRWLARFIFLETVARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEELGGPGWWFRRFVAQHQA-V 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888 204 YYFMTVFLYILSPRMAYHFSECVESHAYETYDKFLKASGEELK-NMPAPDIAVKYYTGGDlylfdefqtsrtpntrrpvI 282
Cdd:cd01053  80 FYNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKpDLPAPEIAIEYYRLGE-------------------D 140
                       170       180
                ....*....|....*....|....*...
gi 18415888 283 ENLYDVFVNIRDDEAEHCKTMRACQTLG 310
Cdd:cd01053 141 ATLYDVFVAIRADEAEHRKVNHACADLG 168
 
Name Accession Description Interval E-value
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
124-310 8.08e-98

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: 286.80  E-value: 8.08e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888 124 YRDRTYARFFVLETIARVPYFAFMSVLHMYETFGWWRRADYLKVHFAESWNEMHHLLIMEELGGNSWWFDRFLAQHIAtF 203
Cdd:cd01053   1 YEDRWLARFIFLETVARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEELGGPGWWFRRFVAQHQA-V 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888 204 YYFMTVFLYILSPRMAYHFSECVESHAYETYDKFLKASGEELK-NMPAPDIAVKYYTGGDlylfdefqtsrtpntrrpvI 282
Cdd:cd01053  80 FYNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKpDLPAPEIAIEYYRLGE-------------------D 140
                       170       180
                ....*....|....*....|....*...
gi 18415888 283 ENLYDVFVNIRDDEAEHCKTMRACQTLG 310
Cdd:cd01053 141 ATLYDVFVAIRADEAEHRKVNHACADLG 168
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
102-308 3.91e-57

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: 184.67  E-value: 3.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888   102 IKLEQGVNVFLTDSV----IKIL----DTLYR-----------DRTYARFFVLETIARVPYFAFMSVLHMYETFGWWRRA 162
Cdd:pfam01786   9 VKLTHREPKTFSDKVayglVKFLrwlfDLLTGykhppppemteRKWLHRAIFLETVAGVPGMVAGMLRHLRSLRLMKRDN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888   163 DYLKVHFAESWNEMHHLLIMEELgGNSWWFDRFLAQHIATFYYFMTVFLYILSPRMAYHFSECVESHAYETYDKFLKASG 242
Cdd:pfam01786  89 GWIHTLLEEAENERMHLLTFLKL-AKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYTHAIEDID 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888   243 ----EELKNMPAPDIAVKYYTGGDlylfdefqtSRTpntrrpvienLYDVFVNIRDDEAEHCKTMRACQT 308
Cdd:pfam01786 168 agklPNWENMPAPEIAIDYWGLPE---------DAT----------LRDLILAIRADEAKHRDVNHTLAN 218
PLN02478 PLN02478
alternative oxidase
71-299 3.93e-15

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 75.32  E-value: 3.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888   71 ESFKAETSTGTEPLEEPNmssSSTSAFETWIIKLeqgvnvfltdsvIKILDTLYRDRTYA-RFFVLETIARVPYFAFMSV 149
Cdd:PLN02478 106 ETYKADLSIDLKKHHVPK---TLLDKIAYWTVKS------------LRVPTDLFFQRRYGcRAMMLETVAAVPGMVGGML 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888  150 LHM-----YETFGWWrradyLKVHFAESWNEMHHLLIMEELGGNSWWfDR---FLAQHIATFYYFMtvfLYILSPRMAYH 221
Cdd:PLN02478 171 LHLkslrrFEHSGGW-----IKALLEEAENERMHLMTFMEVAKPKWY-ERalvIAVQGVFFNAYFL---GYLISPKFAHR 241
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18415888  222 FSECVESHAYETYDKFLKASGE-ELKNMPAPDIAVKYYtggdlylfdefqtsrtpntRRPVIENLYDVFVNIRDDEAEH 299
Cdd:PLN02478 242 IVGYLEEEAIHSYTEFLKDLDAgKIENVPAPAIAIDYW-------------------RLPADATLRDVVTVVRADEAHH 301
 
Name Accession Description Interval E-value
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
124-310 8.08e-98

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: 286.80  E-value: 8.08e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888 124 YRDRTYARFFVLETIARVPYFAFMSVLHMYETFGWWRRADYLKVHFAESWNEMHHLLIMEELGGNSWWFDRFLAQHIAtF 203
Cdd:cd01053   1 YEDRWLARFIFLETVARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEELGGPGWWFRRFVAQHQA-V 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888 204 YYFMTVFLYILSPRMAYHFSECVESHAYETYDKFLKASGEELK-NMPAPDIAVKYYTGGDlylfdefqtsrtpntrrpvI 282
Cdd:cd01053  80 FYNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKpDLPAPEIAIEYYRLGE-------------------D 140
                       170       180
                ....*....|....*....|....*...
gi 18415888 283 ENLYDVFVNIRDDEAEHCKTMRACQTLG 310
Cdd:cd01053 141 ATLYDVFVAIRADEAEHRKVNHACADLG 168
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
102-308 3.91e-57

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: 184.67  E-value: 3.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888   102 IKLEQGVNVFLTDSV----IKIL----DTLYR-----------DRTYARFFVLETIARVPYFAFMSVLHMYETFGWWRRA 162
Cdd:pfam01786   9 VKLTHREPKTFSDKVayglVKFLrwlfDLLTGykhppppemteRKWLHRAIFLETVAGVPGMVAGMLRHLRSLRLMKRDN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888   163 DYLKVHFAESWNEMHHLLIMEELgGNSWWFDRFLAQHIATFYYFMTVFLYILSPRMAYHFSECVESHAYETYDKFLKASG 242
Cdd:pfam01786  89 GWIHTLLEEAENERMHLLTFLKL-AKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYTHAIEDID 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888   243 ----EELKNMPAPDIAVKYYTGGDlylfdefqtSRTpntrrpvienLYDVFVNIRDDEAEHCKTMRACQT 308
Cdd:pfam01786 168 agklPNWENMPAPEIAIDYWGLPE---------DAT----------LRDLILAIRADEAKHRDVNHTLAN 218
PLN02478 PLN02478
alternative oxidase
71-299 3.93e-15

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 75.32  E-value: 3.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888   71 ESFKAETSTGTEPLEEPNmssSSTSAFETWIIKLeqgvnvfltdsvIKILDTLYRDRTYA-RFFVLETIARVPYFAFMSV 149
Cdd:PLN02478 106 ETYKADLSIDLKKHHVPK---TLLDKIAYWTVKS------------LRVPTDLFFQRRYGcRAMMLETVAAVPGMVGGML 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415888  150 LHM-----YETFGWWrradyLKVHFAESWNEMHHLLIMEELGGNSWWfDR---FLAQHIATFYYFMtvfLYILSPRMAYH 221
Cdd:PLN02478 171 LHLkslrrFEHSGGW-----IKALLEEAENERMHLMTFMEVAKPKWY-ERalvIAVQGVFFNAYFL---GYLISPKFAHR 241
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18415888  222 FSECVESHAYETYDKFLKASGE-ELKNMPAPDIAVKYYtggdlylfdefqtsrtpntRRPVIENLYDVFVNIRDDEAEH 299
Cdd:PLN02478 242 IVGYLEEEAIHSYTEFLKDLDAgKIENVPAPAIAIDYW-------------------RLPADATLRDVVTVVRADEAHH 301
 
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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