sujigwak/NVAR huggingface dataset:
UniProt ID: P24752
Variant: N -> S at position 93-93
Variant annotation: in 3KTD; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074145
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: G -> A at position 152-152
Variant annotation: in 3KTD; dbSNP:rs762991875
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: N -> D at position 158-158
Variant annotation: in 3KTD; loss of acetyl-CoAC-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
Effect: loss
Target: acetylcoacacyltransferase activity
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: G -> R at position 183-183
Variant annotation: in 3KTD; no activity; dbSNP:rs120074141
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: T -> M at position 297-297
Variant annotation: in 3KTD; decreased protein abundance; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: A -> P at position 301-301
Variant annotation: in 3KTD; loss of acetyl-CoAC-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
Effect: loss
Target: acetylcoacacyltransferase activity
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: I -> T at position 312-312
Variant annotation: in 3KTD; decreased protein stability; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: A -> P at position 333-333
Variant annotation: in 3KTD; loss of protein solubility; loss of acetyl-CoAC-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
Effect: loss
Target: protein solubility
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: G -> V at position 379-379
Variant annotation: in 3KTD; dbSNP:rs120074143
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24752
Variant: A -> T at position 380-380
Variant annotation: in 3KTD; decreased protein stability; dbSNP:rs120074140
Protein function: This is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA . Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms . The activity of the enzyme is reversible and it can also catalyze the condensation of two acetyl-CoA molecules into acetoacetyl-CoA . Thereby, it plays a major role in ketone body metabolism .
Reference sequence:
MAVLAALLRSGARSRSPLLRRLVQEIRYVERSYVSKPTLKEVVIVSATRTPIGSFLGSLSLLPATKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMGSCAENTAKKLNIARNEQDAYAINSYTRSKAAWEAGKFGNEVIPVTVTVKGQPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTVTAANASTLNDGAAALVLMTADAAKRLNVTPLARIVAFADAAVEPIDFPIAPVYAASMVLKDVGLKKEDIAMWEVNEAFSLVVLANIKMLEIDPQKVNINGGAVSLGHPIGMSGARIVGHLTHALKQGEYGLASICNGGGGASAMLIQKL
UniProt ID: P24777
Variant: F -> Y at position 10-10
Variant annotation: in toxin 11A
Protein function: This protein lyses red blood cells and has cardiotoxic and hypotensive activities.
Reference sequence:
LKCHNKLVPFLSKTCPDGKNLCYKMSMEVTPMIPIKRGCTDTCPKSSLLVKVVCCKTDKCN
UniProt ID: P24778
Variant: K -> R at position 37-37
Variant annotation: in toxin 9BB
Protein function: This toxin has a very low toxicity.
Reference sequence:
LICHNRPLPFLHKTCPEGQNICYKMTLKKTPMKLSVKRGCAATCPSERPLVQVECCKTDKCNW
UniProt ID: P24789
Variant: S -> SS at position 43-43
Variant annotation: in vim2
Protein function: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
Reference sequence:
MATTKSSYRRIFGGNPRSSSSGNRYATSSTRYTLGSAMRPSTSSRMVYSTSSSPAVFKSSSVRLRSSLPPARMADSVDFALADAVNLEFKANRTNEKAEMIELNDRFANFIDKVRFLEQQNKILVAELEQLKGKGTSRIGDLYEEEMRELRRQLDQATNDKARVEVDRDNLADDLQRLREKLQDEMIQKEEAEGNLQSFRQDVDNASLARIDLERKVESLQEEIAFLKKLHDEEIRELQLQIQESHIQVDMDVSKPDLTAALRDVRQQYENVAAKNLSDAEEWYKSKFADLSEAANRNNDALRQAKQETSDFRRQIQTLTCEIDAMKGSNESYERQMREMEENFAIEAANYQDTIQRLQEEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPVHSFSTMSLRETNLDSHPAETHSKRTVLIKTVETRDGQVVNESSQHHDDFE
UniProt ID: P24891
Variant: G -> W at position 185-185
Variant annotation: in strain: PB306
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MFHNFHILSLSSYAYNLFFASAGMLSSLVMFFKFGLYELFIFTLFSVLFISFAWGKDIAMEGLSGYHNFFVMDGFKFGVILFVFSEFMFFFCIFCTFFDAALVPVHELGETWSPFGMHLVNPFGVPLLNTIILLSSGVTVTWAHHSLLSNKSCTNSMILTCLLAAYFTGIQLMEYMEASFSIADGVFGSIFYLSTGFHGIHVLCGGLFLAFNFLRLLKNHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY
UniProt ID: P24891
Variant: F -> L at position 187-187
Variant annotation: in strain: PB306
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MFHNFHILSLSSYAYNLFFASAGMLSSLVMFFKFGLYELFIFTLFSVLFISFAWGKDIAMEGLSGYHNFFVMDGFKFGVILFVFSEFMFFFCIFCTFFDAALVPVHELGETWSPFGMHLVNPFGVPLLNTIILLSSGVTVTWAHHSLLSNKSCTNSMILTCLLAAYFTGIQLMEYMEASFSIADGVFGSIFYLSTGFHGIHVLCGGLFLAFNFLRLLKNHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY
UniProt ID: P24891
Variant: N -> S at position 222-222
Variant annotation: in strain: CB4854
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MFHNFHILSLSSYAYNLFFASAGMLSSLVMFFKFGLYELFIFTLFSVLFISFAWGKDIAMEGLSGYHNFFVMDGFKFGVILFVFSEFMFFFCIFCTFFDAALVPVHELGETWSPFGMHLVNPFGVPLLNTIILLSSGVTVTWAHHSLLSNKSCTNSMILTCLLAAYFTGIQLMEYMEASFSIADGVFGSIFYLSTGFHGIHVLCGGLFLAFNFLRLLKNHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY
UniProt ID: P24891
Variant: Y -> N at position 235-235
Variant annotation: in strain: CB4856
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MFHNFHILSLSSYAYNLFFASAGMLSSLVMFFKFGLYELFIFTLFSVLFISFAWGKDIAMEGLSGYHNFFVMDGFKFGVILFVFSEFMFFFCIFCTFFDAALVPVHELGETWSPFGMHLVNPFGVPLLNTIILLSSGVTVTWAHHSLLSNKSCTNSMILTCLLAAYFTGIQLMEYMEASFSIADGVFGSIFYLSTGFHGIHVLCGGLFLAFNFLRLLKNHFNYNHHLGLEFAILYWHFVDVVWLFLFVFVYWWSY
UniProt ID: P24892
Variant: W -> G at position 11-11
Variant annotation: in strain: AB1
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: L -> W at position 20-20
Variant annotation: in strain: PB306
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: S -> G at position 26-26
Variant annotation: in strain: PB306
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: F -> C at position 30-30
Variant annotation: in strain: PB306
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: Y -> C at position 45-45
Variant annotation: in strain: CB4856
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: I -> S at position 51-51
Variant annotation: in strain: PB306
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY