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Conserved domains on  [gi|16131976|ref|NP_418575|]
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fumarate reductase membrane protein FrdD [Escherichia coli str. K-12 substr. MG1655]

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;
2-119 1.77e-68

fumarate reductase subunit FrdD;


:

Pssm-ID: 180105  Cd Length: 118  Bit Score: 201.34  E-value: 1.77e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976    2 INPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLH 81
Cdd:PRK05470   1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPGDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16131976   82 RMHHAMHDLKIHVPAGKWVFYGLAAILTVVTLIGVVTI 119
Cdd:PRK05470  81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
 
Name Accession Description Interval E-value
PRK05470 PRK05470
fumarate reductase subunit FrdD;
2-119 1.77e-68

fumarate reductase subunit FrdD;


Pssm-ID: 180105  Cd Length: 118  Bit Score: 201.34  E-value: 1.77e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976    2 INPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLH 81
Cdd:PRK05470   1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPGDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16131976   82 RMHHAMHDLKIHVPAGKWVFYGLAAILTVVTLIGVVTI 119
Cdd:PRK05470  81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
FrdD COG3080
Fumarate reductase subunit D [Energy production and conversion];
1-119 3.37e-53

Fumarate reductase subunit D [Energy production and conversion];


Pssm-ID: 442314  Cd Length: 120  Bit Score: 162.79  E-value: 3.37e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976   1 MINPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGL 80
Cdd:COG3080   1 MMNRNPKRSNEPIFWGLFGAGGMVSALVGPVLILITGILVPLGILPADALSYERVHAFAQNWLGKLVLLGVIALPLWHAA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 16131976  81 HRMHHAMHDLKIHVP-AGKWVFYGLAAILTVVTLIGVVTI 119
Cdd:COG3080  81 HRIHHTLHDLGIHAGtAGKLVCYGVAALGSVLAAILLLTI 120
QFR_TypeD_subunitD cd00547
Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the ...
 5-119 6.55e-53

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: 161.74  E-value: 6.55e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976   5 NPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGdALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLHRMH 84
Cdd:cd00547   1 SPKRSDEPIFWGLFGAGGMWSAIVTPVLILLLGILLPLGLIPA-ALSYDRIIAFAQSWIGKLFLLVLIILPMWHAMHRIH 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131976  85 HAMHDLKI-HVPAGKWVFYGLAAILTVVTLIGVVTI 119
Cdd:cd00547  80 HGLHDLKIhHVPAGKIIFYGLAALYSVLALFAVFTL 115
Fumarate_red_D pfam02313
Fumarate reductase subunit D; Fumarate reductase is a membrane-bound flavoenzyme consisting of ...
 5-117 2.31e-50

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: 155.49  E-value: 2.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976     5 NPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLHRMH 84
Cdd:pfam02313   1 NPKRSNEPIFWLLFGAGGMLSALFGPVLILITGILLPLGLIPPDALSYEHLLAFATSWIGKLVLLVVIALPLWHAAHRIH 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 16131976    85 HAMHDLKIHVP-AGKWVFYGLAAILTVVTLIGVV 117
Cdd:pfam02313  81 HGLHDLKIHVPrAGKLIFYGLAALGSVVALAALL 114
 
Name Accession Description Interval E-value
PRK05470 PRK05470
fumarate reductase subunit FrdD;
2-119 1.77e-68

fumarate reductase subunit FrdD;


Pssm-ID: 180105  Cd Length: 118  Bit Score: 201.34  E-value: 1.77e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976    2 INPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLH 81
Cdd:PRK05470   1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPGDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 16131976   82 RMHHAMHDLKIHVPAGKWVFYGLAAILTVVTLIGVVTI 119
Cdd:PRK05470  81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
FrdD COG3080
Fumarate reductase subunit D [Energy production and conversion];
1-119 3.37e-53

Fumarate reductase subunit D [Energy production and conversion];


Pssm-ID: 442314  Cd Length: 120  Bit Score: 162.79  E-value: 3.37e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976   1 MINPNPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGL 80
Cdd:COG3080   1 MMNRNPKRSNEPIFWGLFGAGGMVSALVGPVLILITGILVPLGILPADALSYERVHAFAQNWLGKLVLLGVIALPLWHAA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 16131976  81 HRMHHAMHDLKIHVP-AGKWVFYGLAAILTVVTLIGVVTI 119
Cdd:COG3080  81 HRIHHTLHDLGIHAGtAGKLVCYGVAALGSVLAAILLLTI 120
QFR_TypeD_subunitD cd00547
Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the ...
 5-119 6.55e-53

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: 161.74  E-value: 6.55e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976   5 NPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGdALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLHRMH 84
Cdd:cd00547   1 SPKRSDEPIFWGLFGAGGMWSAIVTPVLILLLGILLPLGLIPA-ALSYDRIIAFAQSWIGKLFLLVLIILPMWHAMHRIH 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16131976  85 HAMHDLKI-HVPAGKWVFYGLAAILTVVTLIGVVTI 119
Cdd:cd00547  80 HGLHDLKIhHVPAGKIIFYGLAALYSVLALFAVFTL 115
Fumarate_red_D pfam02313
Fumarate reductase subunit D; Fumarate reductase is a membrane-bound flavoenzyme consisting of ...
 5-117 2.31e-50

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: 155.49  E-value: 2.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131976     5 NPKRSDEPVFWGLFGAGGMWSAIIAPVMILLVGILLPLGLFPGDALSYERVLAFAQSFIGRVFLFLMIVLPLWCGLHRMH 84
Cdd:pfam02313   1 NPKRSNEPIFWLLFGAGGMLSALFGPVLILITGILLPLGLIPPDALSYEHLLAFATSWIGKLVLLVVIALPLWHAAHRIH 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 16131976    85 HAMHDLKIHVP-AGKWVFYGLAAILTVVTLIGVV 117
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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