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Conserved domains on  [gi|307109615|gb|EFN57853|]
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hypothetical protein CHLNCDRAFT_143310 [Chlorella variabilis]

Protein Classification

alternative oxidase( domain architecture ID 10484894)

alternative oxidase from plant mitochondria, some fungi, and protists, is a terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force; may function to reoxidize reducing equivalents produced by glycolysis such as ubiquinol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 52-271 5.86e-76

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: 230.90  E-value: 5.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615   52 YTSEYLESVQPAH-------EYAAWYWHVAARTLVGLLTGTLGAPADRLTERSLGKRILCFTSVGTVSGLAGkpwgrgAV 124
Cdd:pfam01786   1 YTEEELESVKLTHrepktfsDKVAYGLVKFLRWLFDLLTGYKHPPPPEMTERKWLHRAIFLETVAGVPGMVA------GM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615  125 FNHVRSILFNKPDNGWVHTAAANAECVRAHAGIVANTtwtpAQPPLWARLFHLMFQArvVMFLQILPVYFFLPSAAYAYD 204
Cdd:pfam01786  75 LRHLRSLRLMKRDNGWIHTLLEEAENERMHLLTFLKL----AKPGWFERLLVLGAQG--VFFNAFFLLYLISPRTCHRFV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307109615  205 AFRAEEQV--YSQAISLIGSGRFKTWKSTRAPGLGVSYYALPEGAMLRDALLRMRADEACIHQLNIVLA 271
Cdd:pfam01786 149 GYLEEEAVitYTHAIEDIDAGKLPNWENMPAPEIAIDYWGLPEDATLRDLILAIRADEAKHRDVNHTLA 217
 
Name Accession Description Interval E-value
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 52-271 5.86e-76

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: 230.90  E-value: 5.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615   52 YTSEYLESVQPAH-------EYAAWYWHVAARTLVGLLTGTLGAPADRLTERSLGKRILCFTSVGTVSGLAGkpwgrgAV 124
Cdd:pfam01786   1 YTEEELESVKLTHrepktfsDKVAYGLVKFLRWLFDLLTGYKHPPPPEMTERKWLHRAIFLETVAGVPGMVA------GM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615  125 FNHVRSILFNKPDNGWVHTAAANAECVRAHAGIVANTtwtpAQPPLWARLFHLMFQArvVMFLQILPVYFFLPSAAYAYD 204
Cdd:pfam01786  75 LRHLRSLRLMKRDNGWIHTLLEEAENERMHLLTFLKL----AKPGWFERLLVLGAQG--VFFNAFFLLYLISPRTCHRFV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307109615  205 AFRAEEQV--YSQAISLIGSGRFKTWKSTRAPGLGVSYYALPEGAMLRDALLRMRADEACIHQLNIVLA 271
Cdd:pfam01786 149 GYLEEEAVitYTHAIEDIDAGKLPNWENMPAPEIAIDYWGLPEDATLRDLILAIRADEAKHRDVNHTLA 217
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
 115-262 6.92e-14

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: 68.00  E-value: 6.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615 115 AGKPWGRGAVFNHVRSILFNKPDNGWVHTAAANAECVRAHAGIVANTtwtpAQPPLWARLFHLMFQArvVMFLQILPVYF 194
Cdd:cd01053   16 ARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEEL----GGPGWWFRRFVAQHQA--VFYNAYFLLYL 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615 195 FLPSAAYAYDAFRAEEQV--YSQAISLIGSGRFKTwksTRAPGLGVSYYALPEGAMLRDALLRMRADEAC 262
Cdd:cd01053   90 ISPRLAHRFVGYLEEEAVdtYTEFLKDIEEGLKPD---LPAPEIAIEYYRLGEDATLYDVFVAIRADEAE 156
PLN02478 PLN02478
alternative oxidase
 85-261 1.10e-08

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 55.29  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615  85 TLGAPADRLTERSLGKRILCFTSVGTVSGLAGkpwgrGAVFnHVRSILFNKPDNGWVHTAAANAECVRAHAgivaNTTWT 164
Cdd:PLN02478 136 SLRVPTDLFFQRRYGCRAMMLETVAAVPGMVG-----GMLL-HLKSLRRFEHSGGWIKALLEEAENERMHL----MTFME 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615 165 PAQPPLWARLfhLMFQARVVMFLQILPVYFFLPSAAYAYDAFRAEEQV--YSQAISLIGSGRFKtwkSTRAPGLGVSYYA 242
Cdd:PLN02478 206 VAKPKWYERA--LVIAVQGVFFNAYFLGYLISPKFAHRIVGYLEEEAIhsYTEFLKDLDAGKIE---NVPAPAIAIDYWR 280

                        170
                 ....*....|....*....
gi 307109615 243 LPEGAMLRDALLRMRADEA 261
Cdd:PLN02478 281 LPADATLRDVVTVVRADEA 299
 
Name Accession Description Interval E-value
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 52-271 5.86e-76

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: 230.90  E-value: 5.86e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615   52 YTSEYLESVQPAH-------EYAAWYWHVAARTLVGLLTGTLGAPADRLTERSLGKRILCFTSVGTVSGLAGkpwgrgAV 124
Cdd:pfam01786   1 YTEEELESVKLTHrepktfsDKVAYGLVKFLRWLFDLLTGYKHPPPPEMTERKWLHRAIFLETVAGVPGMVA------GM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615  125 FNHVRSILFNKPDNGWVHTAAANAECVRAHAGIVANTtwtpAQPPLWARLFHLMFQArvVMFLQILPVYFFLPSAAYAYD 204
Cdd:pfam01786  75 LRHLRSLRLMKRDNGWIHTLLEEAENERMHLLTFLKL----AKPGWFERLLVLGAQG--VFFNAFFLLYLISPRTCHRFV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307109615  205 AFRAEEQV--YSQAISLIGSGRFKTWKSTRAPGLGVSYYALPEGAMLRDALLRMRADEACIHQLNIVLA 271
Cdd:pfam01786 149 GYLEEEAVitYTHAIEDIDAGKLPNWENMPAPEIAIDYWGLPEDATLRDLILAIRADEAKHRDVNHTLA 217
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
 115-262 6.92e-14

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: 68.00  E-value: 6.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615 115 AGKPWGRGAVFNHVRSILFNKPDNGWVHTAAANAECVRAHAGIVANTtwtpAQPPLWARLFHLMFQArvVMFLQILPVYF 194
Cdd:cd01053   16 ARVPGMVAGMLLHLYSLRGMWRDGGWIKTLLEEAENERMHLLIFEEL----GGPGWWFRRFVAQHQA--VFYNAYFLLYL 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615 195 FLPSAAYAYDAFRAEEQV--YSQAISLIGSGRFKTwksTRAPGLGVSYYALPEGAMLRDALLRMRADEAC 262
Cdd:cd01053   90 ISPRLAHRFVGYLEEEAVdtYTEFLKDIEEGLKPD---LPAPEIAIEYYRLGEDATLYDVFVAIRADEAE 156
PLN02478 PLN02478
alternative oxidase
 85-261 1.10e-08

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 55.29  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615  85 TLGAPADRLTERSLGKRILCFTSVGTVSGLAGkpwgrGAVFnHVRSILFNKPDNGWVHTAAANAECVRAHAgivaNTTWT 164
Cdd:PLN02478 136 SLRVPTDLFFQRRYGCRAMMLETVAAVPGMVG-----GMLL-HLKSLRRFEHSGGWIKALLEEAENERMHL----MTFME 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307109615 165 PAQPPLWARLfhLMFQARVVMFLQILPVYFFLPSAAYAYDAFRAEEQV--YSQAISLIGSGRFKtwkSTRAPGLGVSYYA 242
Cdd:PLN02478 206 VAKPKWYERA--LVIAVQGVFFNAYFLGYLISPKFAHRIVGYLEEEAIhsYTEFLKDLDAGKIE---NVPAPAIAIDYWR 280

                        170
                 ....*....|....*....
gi 307109615 243 LPEGAMLRDALLRMRADEA 261
Cdd:PLN02478 281 LPADATLRDVVTVVRADEA 299
 
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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