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Conserved domains on  [gi|1382516158|gb|PUX06373|]
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fumarate reductase subunit FrdD [Cronobacter malonaticus]

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 6.84e-67

fumarate reductase subunit FrdD;


:

Pssm-ID: 180105  Cd Length: 118  Bit Score: 197.10  E-value: 6.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   2 INQHPKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPEGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGLH 81
Cdd:PRK05470    1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPGDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1382516158  82 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVTLIGVATI 119
Cdd:PRK05470   81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
 
Name Accession Description Interval E-value
PRK05470 PRK05470
fumarate reductase subunit FrdD;
2-119 6.84e-67

fumarate reductase subunit FrdD;


Pssm-ID: 180105  Cd Length: 118  Bit Score: 197.10  E-value: 6.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   2 INQHPKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPEGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGLH 81
Cdd:PRK05470    1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPGDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1382516158  82 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVTLIGVATI 119
Cdd:PRK05470   81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
FrdD COG3080
Fumarate reductase subunit D [Energy production and conversion];
1-119 3.76e-52

Fumarate reductase subunit D [Energy production and conversion];


Pssm-ID: 442314  Cd Length: 120  Bit Score: 160.09  E-value: 3.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   1 MINQHPKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPEGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGL 80
Cdd:COG3080     1 MMNRNPKRSNEPIFWGLFGAGGMVSALVGPVLILITGILVPLGILPADALSYERVHAFAQNWLGKLVLLGVIALPLWHAA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1382516158  81 HRIHHGMHDLKIHVP-AGKWVFYGLAAILTVVTLIGVATI 119
Cdd:COG3080    81 HRIHHTLHDLGIHAGtAGKLVCYGVAALGSVLAAILLLTI 120
QFR_TypeD_subunitD cd00547
Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the ...
 6-119 5.44e-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: 159.43  E-value: 5.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   6 PKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPeGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGLHRIHH 85
Cdd:cd00547     2 PKRSDEPIFWGLFGAGGMWSAIVTPVLILLLGILLPLGLIP-AALSYDRIIAFAQSWIGKLFLLVLIILPMWHAMHRIHH 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1382516158  86 GMHDLKI-HVPAGKWVFYGLAAILTVVTLIGVATI 119
Cdd:cd00547    81 GLHDLKIhHVPAGKIIFYGLAALYSVLALFAVFTL 115
Fumarate_red_D pfam02313
Fumarate reductase subunit D; Fumarate reductase is a membrane-bound flavoenzyme consisting of ...
 5-116 9.71e-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: 153.56  E-value: 9.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   5 HPKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPEGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGLHRIH 84
Cdd:pfam02313   1 NPKRSNEPIFWLLFGAGGMLSALFGPVLILITGILLPLGLIPPDALSYEHLLAFATSWIGKLVLLVVIALPLWHAAHRIH 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1382516158  85 HGMHDLKIHVP-AGKWVFYGLAAILTVVTLIGV 116
Cdd:pfam02313  81 HGLHDLKIHVPrAGKLIFYGLAALGSVVALAAL 113
 
Name Accession Description Interval E-value
PRK05470 PRK05470
fumarate reductase subunit FrdD;
2-119 6.84e-67

fumarate reductase subunit FrdD;


Pssm-ID: 180105  Cd Length: 118  Bit Score: 197.10  E-value: 6.84e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   2 INQHPKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPEGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGLH 81
Cdd:PRK05470    1 INQNPKRSDEPVFWGLFGAGGMWSAIIAPVLILLVGILLPLGLFPGDALSYERVLAFAQSFIGKLFLLLMIVLPLWCGLH 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1382516158  82 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVTLIGVATI 119
Cdd:PRK05470   81 RIHHGMHDLKIHVPAGKWVFYGLAAILTVVALIGVLTI 118
FrdD COG3080
Fumarate reductase subunit D [Energy production and conversion];
1-119 3.76e-52

Fumarate reductase subunit D [Energy production and conversion];


Pssm-ID: 442314  Cd Length: 120  Bit Score: 160.09  E-value: 3.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   1 MINQHPKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPEGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGL 80
Cdd:COG3080     1 MMNRNPKRSNEPIFWGLFGAGGMVSALVGPVLILITGILVPLGILPADALSYERVHAFAQNWLGKLVLLGVIALPLWHAA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1382516158  81 HRIHHGMHDLKIHVP-AGKWVFYGLAAILTVVTLIGVATI 119
Cdd:COG3080    81 HRIHHTLHDLGIHAGtAGKLVCYGVAALGSVLAAILLLTI 120
QFR_TypeD_subunitD cd00547
Quinol:fumarate reductase (QFR) Type D subfamily, 13kD hydrophobic subunit D; QFR couples the ...
 6-119 5.44e-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: 159.43  E-value: 5.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   6 PKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPeGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGLHRIHH 85
Cdd:cd00547     2 PKRSDEPIFWGLFGAGGMWSAIVTPVLILLLGILLPLGLIP-AALSYDRIIAFAQSWIGKLFLLVLIILPMWHAMHRIHH 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1382516158  86 GMHDLKI-HVPAGKWVFYGLAAILTVVTLIGVATI 119
Cdd:cd00547    81 GLHDLKIhHVPAGKIIFYGLAALYSVLALFAVFTL 115
Fumarate_red_D pfam02313
Fumarate reductase subunit D; Fumarate reductase is a membrane-bound flavoenzyme consisting of ...
 5-116 9.71e-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: 153.56  E-value: 9.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158   5 HPKRSDEPVFWGLFGAGGMWCAIIAPVIILLVGILLPLGMAPEGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGLHRIH 84
Cdd:pfam02313   1 NPKRSNEPIFWLLFGAGGMLSALFGPVLILITGILLPLGLIPPDALSYEHLLAFATSWIGKLVLLVVIALPLWHAAHRIH 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1382516158  85 HGMHDLKIHVP-AGKWVFYGLAAILTVVTLIGV 116
Cdd:pfam02313  81 HGLHDLKIHVPrAGKLIFYGLAALGSVVALAAL 113
SQR_QFR_TM cd03493
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 32-114 2.93e-03

Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, transmembrane subunits; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol, while QFR catalyzes the reverse reaction. SQR, also called succinate dehydrogenase or Complex II, is part of the citric acid cycle and the aerobic respiratory chain, while QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQRs may reduce either high or low potential quinones while QFRs oxidize only low potential quinols. 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. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit(s) containing the electron donor/acceptor (quinol or quinone). The reversible reduction of quinone is an essential feature of respiration, allowing the transfer of electrons between respiratory complexes. SQRs and QFRs can be classified into five types (A-E) according to the number of their hydrophobic subunits and heme groups. This classification is consistent with the characteristics and phylogeny of the catalytic and iron-sulfur subunits. Type E proteins, e.g. non-classical archael SQRs, contain atypical transmembrane subunits and are not included in this hierarchy. The heme and quinone binding sites reside in the transmembrane subunits. Although succinate oxidation and fumarate reduction are carried out by separate enzymes in most organisms, some bifunctional enzymes that exhibit both SQR and QFR activities exist.


Pssm-ID: 239573  Cd Length: 98  Bit Score: 34.56  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1382516158  32 IILLVGILLPLGMAPEGAFSYERVLAFAQSWVGRLFLFLMIVLPLWCGLHRIHHGMHDL-----KIHVPAGKWVFYGLAA 106
Cdd:cd03493    11 LLFLPLHLLGLLALLGGPYAFAEVVAFLSSPLGKLLYLLLLLALLYHALNGIRHLIWDYgkgleLKLRKALGYAVLALSV 90


                  ....*...
gi 1382516158 107 ILTVVTLI 114
Cdd:cd03493    91 LLTVLLLF 98
 
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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