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Conserved domains on  [gi|2087570955|gb|QZE48899|]
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fumarate reductase subunit FrdD [Citrobacter farmeri]

Protein Classification

fumarate reductase subunit D( domain architecture ID 10012426)

quinol:fumarate reductase transmembrane subunit D, together with the C subunit, acts to anchor the catalytic components of fumarate reductase to the cytoplasmic membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05470 PRK05470
fumarate reductase subunit FrdD;
2-118 4.11e-65

fumarate reductase subunit FrdD;


:

Pssm-ID: 180105  Cd Length: 118  Bit Score: 192.87  E-value: 4.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   2 INPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVP-DAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGLH 80
Cdd:PRK05470    1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPgDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2087570955  81 RMHHAMHDLKIHVPAGKWVFYGLAAILTVVTAIGILTI 118
Cdd:PRK05470   81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
 
Name Accession Description Interval E-value
PRK05470 PRK05470
fumarate reductase subunit FrdD;
2-118 4.11e-65

fumarate reductase subunit FrdD;


Pssm-ID: 180105  Cd Length: 118  Bit Score: 192.87  E-value: 4.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   2 INPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVP-DAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGLH 80
Cdd:PRK05470    1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPgDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2087570955  81 RMHHAMHDLKIHVPAGKWVFYGLAAILTVVTAIGILTI 118
Cdd:PRK05470   81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
QFR_TypeD_subunitD cd00547
Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the ...
 5-118 1.09e-52

Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, the opposite reaction to that catalyzed by the related protein, succinate:quinine oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and are involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type D as they contain two transmembrane subunits (C and D) and no heme groups. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron donor (quinol). The quinone binding site resides in the transmembrane subunits.


Pssm-ID: 238307  Cd Length: 115  Bit Score: 161.36  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   5 NPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVPDAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGLHRMHH 84
Cdd:cd00547     1 SPKRSDEPIFWGLFGAGGMWSAIVTPVLILLLGILLPLGLIPAALSYDRIIAFAQSWIGKLFLLVLIILPMWHAMHRIHH 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2087570955  85 AMHDLKI-HVPAGKWVFYGLAAILTVVTAIGILTI 118
Cdd:cd00547    81 GLHDLKIhHVPAGKIIFYGLAALYSVLALFAVFTL 115
FrdD COG3080
Fumarate reductase subunit D [Energy production and conversion];
1-118 1.30e-51

Fumarate reductase subunit D [Energy production and conversion];


Pssm-ID: 442314  Cd Length: 120  Bit Score: 158.55  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   1 MINPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVP-DAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGL 79
Cdd:COG3080     1 MMNRNPKRSNEPIFWGLFGAGGMVSALVGPVLILITGILVPLGILPaDALSYERVHAFAQNWLGKLVLLGVIALPLWHAA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2087570955  80 HRMHHAMHDLKIHVP-AGKWVFYGLAAILTVVTAIGILTI 118
Cdd:COG3080    81 HRIHHTLHDLGIHAGtAGKLVCYGVAALGSVLAAILLLTI 120
Fumarate_red_D pfam02313
Fumarate reductase subunit D; Fumarate reductase is a membrane-bound flavoenzyme consisting of ...
 5-116 3.59e-48

Fumarate reductase subunit D; Fumarate reductase is a membrane-bound flavoenzyme consisting of four subunits, A-B. A and B comprise the membrane-extrinsic catalytic domain and C and D link the catalytic centres to the electron-transport chain. This family consists of the 13kD hydrophobic subunit D.


Pssm-ID: 426714  Cd Length: 114  Bit Score: 149.71  E-value: 3.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   5 NPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVP-DAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGLHRMH 83
Cdd:pfam02313   1 NPKRSNEPIFWLLFGAGGMLSALFGPVLILITGILLPLGLIPpDALSYEHLLAFATSWIGKLVLLVVIALPLWHAAHRIH 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2087570955  84 HAMHDLKIHVP-AGKWVFYGLAAILTVVTAIGIL 116
Cdd:pfam02313  81 HGLHDLKIHVPrAGKLIFYGLAALGSVVALAALL 114
 
Name Accession Description Interval E-value
PRK05470 PRK05470
fumarate reductase subunit FrdD;
2-118 4.11e-65

fumarate reductase subunit FrdD;


Pssm-ID: 180105  Cd Length: 118  Bit Score: 192.87  E-value: 4.11e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   2 INPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVP-DAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGLH 80
Cdd:PRK05470    1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPgDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2087570955  81 RMHHAMHDLKIHVPAGKWVFYGLAAILTVVTAIGILTI 118
Cdd:PRK05470   81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
QFR_TypeD_subunitD cd00547
Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the ...
 5-118 1.09e-52

Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, the opposite reaction to that catalyzed by the related protein, succinate:quinine oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and are involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type D as they contain two transmembrane subunits (C and D) and no heme groups. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron donor (quinol). The quinone binding site resides in the transmembrane subunits.


Pssm-ID: 238307  Cd Length: 115  Bit Score: 161.36  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   5 NPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVPDAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGLHRMHH 84
Cdd:cd00547     1 SPKRSDEPIFWGLFGAGGMWSAIVTPVLILLLGILLPLGLIPAALSYDRIIAFAQSWIGKLFLLVLIILPMWHAMHRIHH 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2087570955  85 AMHDLKI-HVPAGKWVFYGLAAILTVVTAIGILTI 118
Cdd:cd00547    81 GLHDLKIhHVPAGKIIFYGLAALYSVLALFAVFTL 115
FrdD COG3080
Fumarate reductase subunit D [Energy production and conversion];
1-118 1.30e-51

Fumarate reductase subunit D [Energy production and conversion];


Pssm-ID: 442314  Cd Length: 120  Bit Score: 158.55  E-value: 1.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   1 MINPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVP-DAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGL 79
Cdd:COG3080     1 MMNRNPKRSNEPIFWGLFGAGGMVSALVGPVLILITGILVPLGILPaDALSYERVHAFAQNWLGKLVLLGVIALPLWHAA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2087570955  80 HRMHHAMHDLKIHVP-AGKWVFYGLAAILTVVTAIGILTI 118
Cdd:COG3080    81 HRIHHTLHDLGIHAGtAGKLVCYGVAALGSVLAAILLLTI 120
Fumarate_red_D pfam02313
Fumarate reductase subunit D; Fumarate reductase is a membrane-bound flavoenzyme consisting of ...
 5-116 3.59e-48

Fumarate reductase subunit D; Fumarate reductase is a membrane-bound flavoenzyme consisting of four subunits, A-B. A and B comprise the membrane-extrinsic catalytic domain and C and D link the catalytic centres to the electron-transport chain. This family consists of the 13kD hydrophobic subunit D.


Pssm-ID: 426714  Cd Length: 114  Bit Score: 149.71  E-value: 3.59e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2087570955   5 NPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGIMLPLGFVP-DAFSYERVLAFAQSFIGRAFLFLMIVLPLWCGLHRMH 83
Cdd:pfam02313   1 NPKRSNEPIFWLLFGAGGMLSALFGPVLILITGILLPLGLIPpDALSYEHLLAFATSWIGKLVLLVVIALPLWHAAHRIH 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2087570955  84 HAMHDLKIHVP-AGKWVFYGLAAILTVVTAIGIL 116
Cdd:pfam02313  81 HGLHDLKIHVPrAGKLIFYGLAALGSVVALAALL 114
 
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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