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Conserved domains on  [gi|134074206|emb|CAM72948|]
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putative alternative oxidase [Leishmania infantum JPCM5]

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 super family cl47695
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 91-466 1.39e-37

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.


The actual alignment was detected with superfamily member pfam01786:

Pssm-ID: 460328  Cd Length: 218  Bit Score: 136.91  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206   91 AGITQLEREPLAHSTPGRINDHICIGMVKTLRWLADRAFRE-----------RYIHRATMLvtvaaaapaagsvaaylrm 159
Cdd:pfam01786   1 YTEEELESVKLTHREPKTFSDKVAYGLVKFLRWLFDLLTGYkhppppemterKWLHRAIFL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  160 lfrrsnsssactgdsqmpTTAEASSPFLAfggspsagaappippacrsfAMAR--PSLYMstssatMEgtgstPEHSYVd 237
Cdd:pfam01786  62 ------------------ETVAGVPGMVA--------------------GMLRhlRSLRL------MK-----RDNGWI- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  238 elRGLLAQCESHAVHYQVLSCMAEITLLERGLVLLLQAVHFTIYLALFLLYPRMGFRLMAYTAEESSVVWTQMVNDVDLG 317
Cdd:pfam01786  92 --HTLLEEAENERMHLLTFLKLAKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYTHAIEDIDAG 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  318 KIAEP---RVPQLALHYWGLEGvftaqaaplpktvapqeqeaalyktseglvteqipvtDApisgaspdggdnghraatp 394
Cdd:pfam01786 170 KLPNWenmPAPEIAIDYWGLPE-------------------------------------DA------------------- 193

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134074206  395 lsrsadhvpvpfaaagscddsavdskeseervittsdrgagpgasvlTLRDVALLIRSDEMIFRDLNHELAN 466
Cdd:pfam01786 194 -----------------------------------------------TLRDLILAIRADEAKHRDVNHTLAN 218
 
Name Accession Description Interval E-value
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 91-466 1.39e-37

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: 136.91  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206   91 AGITQLEREPLAHSTPGRINDHICIGMVKTLRWLADRAFRE-----------RYIHRATMLvtvaaaapaagsvaaylrm 159
Cdd:pfam01786   1 YTEEELESVKLTHREPKTFSDKVAYGLVKFLRWLFDLLTGYkhppppemterKWLHRAIFL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  160 lfrrsnsssactgdsqmpTTAEASSPFLAfggspsagaappippacrsfAMAR--PSLYMstssatMEgtgstPEHSYVd 237
Cdd:pfam01786  62 ------------------ETVAGVPGMVA--------------------GMLRhlRSLRL------MK-----RDNGWI- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  238 elRGLLAQCESHAVHYQVLSCMAEITLLERGLVLLLQAVHFTIYLALFLLYPRMGFRLMAYTAEESSVVWTQMVNDVDLG 317
Cdd:pfam01786  92 --HTLLEEAENERMHLLTFLKLAKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYTHAIEDIDAG 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  318 KIAEP---RVPQLALHYWGLEGvftaqaaplpktvapqeqeaalyktseglvteqipvtDApisgaspdggdnghraatp 394
Cdd:pfam01786 170 KLPNWenmPAPEIAIDYWGLPE-------------------------------------DA------------------- 193

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134074206  395 lsrsadhvpvpfaaagscddsavdskeseervittsdrgagpgasvlTLRDVALLIRSDEMIFRDLNHELAN 466
Cdd:pfam01786 194 -----------------------------------------------TLRDLILAIRADEAKHRDVNHTLAN 218
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
 274-334 1.00e-05

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: 45.66  E-value: 1.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134074206 274 QAVHFTIYLALFLLYPRMGFRLMAYTAEESSVVWTQMVNDVDLGKIAEPRVPQLALHYWGL 334
Cdd:cd01053   77 QAVFYNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKPDLPAPEIAIEYYRL 137
PLN02478 PLN02478
alternative oxidase
 272-335 1.06e-05

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 47.59  E-value: 1.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134074206 272 LLQAVHFTIYLALFLLYPRMGFRLMAYTAEESSVVWTQMVNDVDLGKIAEPRVPQLALHYWGLE 335
Cdd:PLN02478 219 AVQGVFFNAYFLGYLISPKFAHRIVGYLEEEAIHSYTEFLKDLDAGKIENVPAPAIAIDYWRLP 282
 
Name Accession Description Interval E-value
AOX pfam01786
Alternative oxidase; The alternative oxidase is used as a second terminal oxidase in the ...
 91-466 1.39e-37

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: 136.91  E-value: 1.39e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206   91 AGITQLEREPLAHSTPGRINDHICIGMVKTLRWLADRAFRE-----------RYIHRATMLvtvaaaapaagsvaaylrm 159
Cdd:pfam01786   1 YTEEELESVKLTHREPKTFSDKVAYGLVKFLRWLFDLLTGYkhppppemterKWLHRAIFL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  160 lfrrsnsssactgdsqmpTTAEASSPFLAfggspsagaappippacrsfAMAR--PSLYMstssatMEgtgstPEHSYVd 237
Cdd:pfam01786  62 ------------------ETVAGVPGMVA--------------------GMLRhlRSLRL------MK-----RDNGWI- 91

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  238 elRGLLAQCESHAVHYQVLSCMAEITLLERGLVLLLQAVHFTIYLALFLLYPRMGFRLMAYTAEESSVVWTQMVNDVDLG 317
Cdd:pfam01786  92 --HTLLEEAENERMHLLTFLKLAKPGWFERLLVLGAQGVFFNAFFLLYLISPRTCHRFVGYLEEEAVITYTHAIEDIDAG 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134074206  318 KIAEP---RVPQLALHYWGLEGvftaqaaplpktvapqeqeaalyktseglvteqipvtDApisgaspdggdnghraatp 394
Cdd:pfam01786 170 KLPNWenmPAPEIAIDYWGLPE-------------------------------------DA------------------- 193

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 134074206  395 lsrsadhvpvpfaaagscddsavdskeseervittsdrgagpgasvlTLRDVALLIRSDEMIFRDLNHELAN 466
Cdd:pfam01786 194 -----------------------------------------------TLRDLILAIRADEAKHRDVNHTLAN 218
AOX cd01053
Alternative oxidase, ferritin-like diiron-binding domain; Alternative oxidase (AOX) is a ...
 274-334 1.00e-05

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: 45.66  E-value: 1.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 134074206 274 QAVHFTIYLALFLLYPRMGFRLMAYTAEESSVVWTQMVNDVDLGKIAEPRVPQLALHYWGL 334
Cdd:cd01053   77 QAVFYNAYFLLYLISPRLAHRFVGYLEEEAVDTYTEFLKDIEEGLKPDLPAPEIAIEYYRL 137
PLN02478 PLN02478
alternative oxidase
 272-335 1.06e-05

alternative oxidase


Pssm-ID: 215265  Cd Length: 328  Bit Score: 47.59  E-value: 1.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134074206 272 LLQAVHFTIYLALFLLYPRMGFRLMAYTAEESSVVWTQMVNDVDLGKIAEPRVPQLALHYWGLE 335
Cdd:PLN02478 219 AVQGVFFNAYFLGYLISPKFAHRIVGYLEEEAIHSYTEFLKDLDAGKIENVPAPAIAIDYWRLP 282
 
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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