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Conserved domains on  [gi|2580096793|ref|WP_310782297|]
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cytochrome ubiquinol oxidase subunit I [Candidatus Palauibacter polyketidifaciens]

Protein Classification

cytochrome ubiquinol oxidase subunit I( domain architecture ID 941)

cytochrome ubiquinol oxidase subunit I is a component of the terminal oxidase enzyme that generates a proton motive force by utilizing protons and electrons from opposite sides of the membrane to generate water

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cyt_bd_oxida_I super family cl00562
Cytochrome bd terminal oxidase subunit I; This family are the alternative oxidases found in ...
57-290 5.08e-15

Cytochrome bd terminal oxidase subunit I; This family are the alternative oxidases found in many bacteria which oxidize ubiquinol and reduce oxygen as part of the electron transport chain. This family is the subunit I of the oxidase E. coli has two copies of the oxidase, bo and bd', both of which are represented here In some nitrogen fixing bacteria, e.g. Klebsiella pneumoniae this oxidase is responsible for removing oxygen in microaerobic conditions, making the oxidase required for nitrogen fixation. This subunit binds a single b-haem, through ligands at His186 and Met393 (using SW:P11026 numbering). In addition His19 is a ligand for the haem b found in subunit II


The actual alignment was detected with superfamily member pfam01654:

Pssm-ID: 469822  Cd Length: 428  Bit Score: 77.46  E-value: 5.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793  57 HLLFAAFVLGVPMFAVVIEAIGMFGGDEKYDKLAKEFTRLLLVAYSATAIWGAILVFFLSTLYPRFWAYLTAIFAPSMwV 136
Cdd:pfam01654  13 HILFVPLTIGLALLLAIMETLYLRTGDEVYLRLARFWGKLFAINFAVGVVTGIVMEFQFGTNWSGFSRFVGDVFGAPL-A 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 137 YAGL--FFLESFTLYLYYYGWDAWKkgaaKKVHWCLGIMLNIWGTIVMF---IANGWltymMSPPEG--LTADTAPQTVQ 209
Cdd:pfam01654  92 IEGLfaFFLEATFLGLMLFGWDRVS----PKLHLLATWLVALGTNLSAFwilAANSW----MQTPVGfeLNPDGRAELTD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 210 LWSAINNATWMPINIHRLLANVVFGGAIVGAYAAYRFLTSRtdeERAHYDWMGYTGNLIAIGALIVLPFAGYWLGREIYE 289
Cdd:pfam01654 164 FWAVIFNPSAPYRFVHTVLAAYLTGAFFVAGVSAWYLLRGR---DVEFARKSLKIALVVGLVAALLQALSGDLSGKNVAE 240

                  .
gi 2580096793 290 F 290
Cdd:pfam01654 241 H 241
 
Name Accession Description Interval E-value
Cyt_bd_oxida_I pfam01654
Cytochrome bd terminal oxidase subunit I; This family are the alternative oxidases found in ...
57-290 5.08e-15

Cytochrome bd terminal oxidase subunit I; This family are the alternative oxidases found in many bacteria which oxidize ubiquinol and reduce oxygen as part of the electron transport chain. This family is the subunit I of the oxidase E. coli has two copies of the oxidase, bo and bd', both of which are represented here In some nitrogen fixing bacteria, e.g. Klebsiella pneumoniae this oxidase is responsible for removing oxygen in microaerobic conditions, making the oxidase required for nitrogen fixation. This subunit binds a single b-haem, through ligands at His186 and Met393 (using SW:P11026 numbering). In addition His19 is a ligand for the haem b found in subunit II


Pssm-ID: 460282  Cd Length: 428  Bit Score: 77.46  E-value: 5.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793  57 HLLFAAFVLGVPMFAVVIEAIGMFGGDEKYDKLAKEFTRLLLVAYSATAIWGAILVFFLSTLYPRFWAYLTAIFAPSMwV 136
Cdd:pfam01654  13 HILFVPLTIGLALLLAIMETLYLRTGDEVYLRLARFWGKLFAINFAVGVVTGIVMEFQFGTNWSGFSRFVGDVFGAPL-A 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 137 YAGL--FFLESFTLYLYYYGWDAWKkgaaKKVHWCLGIMLNIWGTIVMF---IANGWltymMSPPEG--LTADTAPQTVQ 209
Cdd:pfam01654  92 IEGLfaFFLEATFLGLMLFGWDRVS----PKLHLLATWLVALGTNLSAFwilAANSW----MQTPVGfeLNPDGRAELTD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 210 LWSAINNATWMPINIHRLLANVVFGGAIVGAYAAYRFLTSRtdeERAHYDWMGYTGNLIAIGALIVLPFAGYWLGREIYE 289
Cdd:pfam01654 164 FWAVIFNPSAPYRFVHTVLAAYLTGAFFVAGVSAWYLLRGR---DVEFARKSLKIALVVGLVAALLQALSGDLSGKNVAE 240

                  .
gi 2580096793 290 F 290
Cdd:pfam01654 241 H 241
AppC COG1271
Cytochrome bd-type quinol oxidase, subunit 1 [Energy production and conversion];
57-289 2.52e-13

Cytochrome bd-type quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440882  Cd Length: 442  Bit Score: 72.43  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793  57 HLLFAAFVLGVPMFAVVIEAIGMFGGDEKYDKLAKEFTRLLLVAYSATAIWGAILVFFLSTLYPRFWAYLTAIFAPSMwV 136
Cdd:COG1271    18 HILFVPLTIGLALLLAIMETLWLRTGDEVYLRLTRFWGKLFAINFAVGVVTGIVMEFQFGTNWSGFSRFVGDVFGAPL-A 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 137 YAGL--FFLESFTLYLYYYGWDAWKkgaaKKVHWCLGIMLNIWGTIVMF---IANGWltymMSPPEGLTADTA-PQTVQL 210
Cdd:COG1271    97 YEGLtaFFLEATFLGIMLFGWDRVS----PKLHLLATWLVALGTNLSAFwilAANSW----MQTPVGFEIVDGrAELTDF 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2580096793 211 WSAINNATWMPINIHRLLANVVFGGAIVGAYAAYRFLTSRtdeERAHYDWMGYTGNLIAIGALIVLPFAGYWLGREIYE 289
Cdd:COG1271   169 WAVIFNPSFPYRFVHMVLAAYLTGAFFVAGVSAWYLLRGR---HVEFARKSLKIALVFALIAAPLQAVSGDLSGLNVAE 244
PRK15035 PRK15035
cytochrome bd-II oxidase subunit 1; Provisional
52-253 1.42e-06

cytochrome bd-II oxidase subunit 1; Provisional


Pssm-ID: 184995  Cd Length: 514  Bit Score: 51.19  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793  52 IAAQLHLLFAAFVLGVPMFAVVIEAIGMFGGDEKYDKLAKEFTRLLLVAYSATAIWGAILVFFLSTLYPRFWAYLTAIFA 131
Cdd:PRK15035   14 LTALYHFLFVPLTLGLIFLLAIMETIYVVTGKTIYRDMTRFWGKLFGINFALGVATGLTMEFQFGTNWSFYSNYVGDIFG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 132 PSMWVYAGL-FFLESFTLYLYYYGWDAWKKGAAKKVHWCLGIMLNIwGTIVMFIANGWLTYmmspPEGLTADTAPQTVQL 210
Cdd:PRK15035   94 APLAMEALMaFFLESTFVGLFFFGWQRLNKYQHLLVTWLVAFGSNL-SALWILNANGWMQY----PTGAHFDIDTLRMEM 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2580096793 211 wSAINNATWMPIN----IHRLLANVVFGGAIVGAYAAYRFLTSRTDE 253
Cdd:PRK15035  169 -TSFSELVFNPVSqvkfVHTVMAGYVTGAMFIMAISAWYLLRGRERD 214
 
Name Accession Description Interval E-value
Cyt_bd_oxida_I pfam01654
Cytochrome bd terminal oxidase subunit I; This family are the alternative oxidases found in ...
57-290 5.08e-15

Cytochrome bd terminal oxidase subunit I; This family are the alternative oxidases found in many bacteria which oxidize ubiquinol and reduce oxygen as part of the electron transport chain. This family is the subunit I of the oxidase E. coli has two copies of the oxidase, bo and bd', both of which are represented here In some nitrogen fixing bacteria, e.g. Klebsiella pneumoniae this oxidase is responsible for removing oxygen in microaerobic conditions, making the oxidase required for nitrogen fixation. This subunit binds a single b-haem, through ligands at His186 and Met393 (using SW:P11026 numbering). In addition His19 is a ligand for the haem b found in subunit II


Pssm-ID: 460282  Cd Length: 428  Bit Score: 77.46  E-value: 5.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793  57 HLLFAAFVLGVPMFAVVIEAIGMFGGDEKYDKLAKEFTRLLLVAYSATAIWGAILVFFLSTLYPRFWAYLTAIFAPSMwV 136
Cdd:pfam01654  13 HILFVPLTIGLALLLAIMETLYLRTGDEVYLRLARFWGKLFAINFAVGVVTGIVMEFQFGTNWSGFSRFVGDVFGAPL-A 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 137 YAGL--FFLESFTLYLYYYGWDAWKkgaaKKVHWCLGIMLNIWGTIVMF---IANGWltymMSPPEG--LTADTAPQTVQ 209
Cdd:pfam01654  92 IEGLfaFFLEATFLGLMLFGWDRVS----PKLHLLATWLVALGTNLSAFwilAANSW----MQTPVGfeLNPDGRAELTD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 210 LWSAINNATWMPINIHRLLANVVFGGAIVGAYAAYRFLTSRtdeERAHYDWMGYTGNLIAIGALIVLPFAGYWLGREIYE 289
Cdd:pfam01654 164 FWAVIFNPSAPYRFVHTVLAAYLTGAFFVAGVSAWYLLRGR---DVEFARKSLKIALVVGLVAALLQALSGDLSGKNVAE 240

                  .
gi 2580096793 290 F 290
Cdd:pfam01654 241 H 241
AppC COG1271
Cytochrome bd-type quinol oxidase, subunit 1 [Energy production and conversion];
57-289 2.52e-13

Cytochrome bd-type quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440882  Cd Length: 442  Bit Score: 72.43  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793  57 HLLFAAFVLGVPMFAVVIEAIGMFGGDEKYDKLAKEFTRLLLVAYSATAIWGAILVFFLSTLYPRFWAYLTAIFAPSMwV 136
Cdd:COG1271    18 HILFVPLTIGLALLLAIMETLWLRTGDEVYLRLTRFWGKLFAINFAVGVVTGIVMEFQFGTNWSGFSRFVGDVFGAPL-A 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 137 YAGL--FFLESFTLYLYYYGWDAWKkgaaKKVHWCLGIMLNIWGTIVMF---IANGWltymMSPPEGLTADTA-PQTVQL 210
Cdd:COG1271    97 YEGLtaFFLEATFLGIMLFGWDRVS----PKLHLLATWLVALGTNLSAFwilAANSW----MQTPVGFEIVDGrAELTDF 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2580096793 211 WSAINNATWMPINIHRLLANVVFGGAIVGAYAAYRFLTSRtdeERAHYDWMGYTGNLIAIGALIVLPFAGYWLGREIYE 289
Cdd:COG1271   169 WAVIFNPSFPYRFVHMVLAAYLTGAFFVAGVSAWYLLRGR---HVEFARKSLKIALVFALIAAPLQAVSGDLSGLNVAE 244
PRK15035 PRK15035
cytochrome bd-II oxidase subunit 1; Provisional
52-253 1.42e-06

cytochrome bd-II oxidase subunit 1; Provisional


Pssm-ID: 184995  Cd Length: 514  Bit Score: 51.19  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793  52 IAAQLHLLFAAFVLGVPMFAVVIEAIGMFGGDEKYDKLAKEFTRLLLVAYSATAIWGAILVFFLSTLYPRFWAYLTAIFA 131
Cdd:PRK15035   14 LTALYHFLFVPLTLGLIFLLAIMETIYVVTGKTIYRDMTRFWGKLFGINFALGVATGLTMEFQFGTNWSFYSNYVGDIFG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 132 PSMWVYAGL-FFLESFTLYLYYYGWDAWKKGAAKKVHWCLGIMLNIwGTIVMFIANGWLTYmmspPEGLTADTAPQTVQL 210
Cdd:PRK15035   94 APLAMEALMaFFLESTFVGLFFFGWQRLNKYQHLLVTWLVAFGSNL-SALWILNANGWMQY----PTGAHFDIDTLRMEM 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2580096793 211 wSAINNATWMPIN----IHRLLANVVFGGAIVGAYAAYRFLTSRTDE 253
Cdd:PRK15035  169 -TSFSELVFNPVSqvkfVHTVMAGYVTGAMFIMAISAWYLLRGRERD 214
PRK15097 PRK15097
cytochrome bd-I ubiquinol oxidase subunit CydA;
52-189 4.40e-06

cytochrome bd-I ubiquinol oxidase subunit CydA;


Pssm-ID: 185052  Cd Length: 522  Bit Score: 49.45  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793  52 IAAQLHLLFAAFVLGVPMFAVVIEAIGMFGGDEKYDKLAKEFTRLLLVAYSATAIWGAILVFFLSTLYPRFWAYLTAIFA 131
Cdd:PRK15097   14 LTAMYHFLFVPLTLGMAFLLAIMETVYVLSGKQIYKDMTKFWGKLFGINFALGVATGLTMEFQFGTNWSYYSHYVGDIFG 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2580096793 132 PSMWVyAGL--FFLESFTLYLYYYGWDAWKKGAAKKVHWCLGIMLNIwGTIVMFIANGWL 189
Cdd:PRK15097   94 APLAI-EGLmaFFLESTFVGLFFFGWDRLGKVQHMCVTWLVALGSNL-SALWILVANGWM 151
 
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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