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Conserved domains on  [gi|578263618|gb|EUM23640|]
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fumarate reductase subunit C [Enterobacter sp. BIDMC 27]

Protein Classification

fumarate reductase subunit C( domain architecture ID 10012241)

quinol:fumarate reductase transmembrane subunit C, together with the D 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
PRK04987 PRK04987
fumarate reductase subunit FrdC;
1-130 1.42e-77

fumarate reductase subunit FrdC;


:

Pssm-ID: 235327  Cd Length: 130  Bit Score: 225.25  E-value: 1.42e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618   1 MTTKRKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAA 80
Cdd:PRK04987   1 MTTKRKPYVRPMTPTWWKKLPFYRFYMLREATAVPAVWFSLVLIYGLFALKNGPEAWAGFVSFLQNPIVVILNIITLAAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 578263618  81 LLHTKTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVALF 130
Cdd:PRK04987  81 LLHTKTWFEMAPKAANIIVKDEKMGPEPIIKALWAVTAVVSLVILVVALL 130
 
Name Accession Description Interval E-value
PRK04987 PRK04987
fumarate reductase subunit FrdC;
1-130 1.42e-77

fumarate reductase subunit FrdC;


Pssm-ID: 235327  Cd Length: 130  Bit Score: 225.25  E-value: 1.42e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618   1 MTTKRKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAA 80
Cdd:PRK04987   1 MTTKRKPYVRPMTPTWWKKLPFYRFYMLREATAVPAVWFSLVLIYGLFALKNGPEAWAGFVSFLQNPIVVILNIITLAAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 578263618  81 LLHTKTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVALF 130
Cdd:PRK04987  81 LLHTKTWFEMAPKAANIIVKDEKMGPEPIIKALWAVTAVVSLVILVVALL 130
FrdC COG3029
Fumarate reductase subunit C [Energy production and conversion];
2-129 1.72e-65

Fumarate reductase subunit C [Energy production and conversion];


Pssm-ID: 442265  Cd Length: 128  Bit Score: 194.73  E-value: 1.72e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618   2 TTKRKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAAL 81
Cdd:COG3029    1 MSKRKPYVREMKATWWKKLPFYRFYMLREGTAVFVAWFSLVLLYGLFALSQGPEAWAGFVAFLQNPLVLLLNLIALAAAL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578263618  82 LHTKTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVAL 129
Cdd:COG3029   81 LHTVTWFELAPKAMNIIIGGERVPPKPIVAGLWAATAVVSVVILALAL 128
QFR_TypeD_subunitC cd00546
Quinol:fumarate reductase (QFR) Type D subfamily, 15kD hydrophobic subunit C; QFR couples the ...
 5-128 3.43e-63

Quinol:fumarate reductase (QFR) Type D subfamily, 15kD hydrophobic subunit C; 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: 238306  Cd Length: 124  Bit Score: 188.69  E-value: 3.43e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618   5 RKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAALLHT 84
Cdd:cd00546    1 RKPYVRPMTPTWWKKLDFYRFYMLREATAVPTVWFSLVLLYGLFALGSGPESWAGFVSFLQNPIVVLLNIIALAAALLHA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578263618  85 KTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVA 128
Cdd:cd00546   81 KTWFEMAPKVMNIIVKGERVPPEAITKALWAVTAVVSVVALVLV 124
Fumarate_red_C pfam02300
Fumarate reductase subunit C; Fumarate reductase is a membrane-bound flavoenzyme consisting of ...
 3-129 1.65e-62

Fumarate reductase subunit C; 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 15kD hydrophobic subunit C.


Pssm-ID: 426709  Cd Length: 127  Bit Score: 187.07  E-value: 1.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618    3 TKRKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAALL 82
Cdd:pfam02300   1 SKRKPYVRPMTPTWWKKLPFYRFYMLREGTAVFVAWFALVLLYGLLALAQGPAAWEGWLGFLQNPLVILLNLIALAAALL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578263618   83 HTKTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVAL 129
Cdd:pfam02300  81 HAVTWFQLAPKAMNIVVGGERVPPRPIVAGLWAATAVVSLILLVIVL 127
 
Name Accession Description Interval E-value
PRK04987 PRK04987
fumarate reductase subunit FrdC;
1-130 1.42e-77

fumarate reductase subunit FrdC;


Pssm-ID: 235327  Cd Length: 130  Bit Score: 225.25  E-value: 1.42e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618   1 MTTKRKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAA 80
Cdd:PRK04987   1 MTTKRKPYVRPMTPTWWKKLPFYRFYMLREATAVPAVWFSLVLIYGLFALKNGPEAWAGFVSFLQNPIVVILNIITLAAA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 578263618  81 LLHTKTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVALF 130
Cdd:PRK04987  81 LLHTKTWFEMAPKAANIIVKDEKMGPEPIIKALWAVTAVVSLVILVVALL 130
FrdC COG3029
Fumarate reductase subunit C [Energy production and conversion];
2-129 1.72e-65

Fumarate reductase subunit C [Energy production and conversion];


Pssm-ID: 442265  Cd Length: 128  Bit Score: 194.73  E-value: 1.72e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618   2 TTKRKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAAL 81
Cdd:COG3029    1 MSKRKPYVREMKATWWKKLPFYRFYMLREGTAVFVAWFSLVLLYGLFALSQGPEAWAGFVAFLQNPLVLLLNLIALAAAL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 578263618  82 LHTKTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVAL 129
Cdd:COG3029   81 LHTVTWFELAPKAMNIIIGGERVPPKPIVAGLWAATAVVSVVILALAL 128
QFR_TypeD_subunitC cd00546
Quinol:fumarate reductase (QFR) Type D subfamily, 15kD hydrophobic subunit C; QFR couples the ...
 5-128 3.43e-63

Quinol:fumarate reductase (QFR) Type D subfamily, 15kD hydrophobic subunit C; 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: 238306  Cd Length: 124  Bit Score: 188.69  E-value: 3.43e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618   5 RKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAALLHT 84
Cdd:cd00546    1 RKPYVRPMTPTWWKKLDFYRFYMLREATAVPTVWFSLVLLYGLFALGSGPESWAGFVSFLQNPIVVLLNIIALAAALLHA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578263618  85 KTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVA 128
Cdd:cd00546   81 KTWFEMAPKVMNIIVKGERVPPEAITKALWAVTAVVSVVALVLV 124
Fumarate_red_C pfam02300
Fumarate reductase subunit C; Fumarate reductase is a membrane-bound flavoenzyme consisting of ...
 3-129 1.65e-62

Fumarate reductase subunit C; 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 15kD hydrophobic subunit C.


Pssm-ID: 426709  Cd Length: 127  Bit Score: 187.07  E-value: 1.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618    3 TKRKAYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAALL 82
Cdd:pfam02300   1 SKRKPYVRPMTPTWWKKLPFYRFYMLREGTAVFVAWFALVLLYGLLALAQGPAAWEGWLGFLQNPLVILLNLIALAAALL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 578263618   83 HTKTWFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVAL 129
Cdd:pfam02300  81 HAVTWFQLAPKAMNIVVGGERVPPRPIVAGLWAATAVVSLILLVIVL 127
PRK13603 PRK13603
fumarate reductase subunit C; Provisional
 7-129 1.67e-16

fumarate reductase subunit C; Provisional


Pssm-ID: 172166  Cd Length: 126  Bit Score: 70.08  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618   7 AYVRPMPSTWWKKLPFYRFYMLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAALLHTKT 86
Cdd:PRK13603   3 AYRQPVERYWWARRRSYLRFMLREISCIFVAWFVLYLVLVLRAVGAGGNSYQRFLDFSANPVVVVLNVVALSFLLLHAVT 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578263618  87 WFELAPKAANIIVKGEKMGPEPVIKGLWAVTAVVSVVILFVAL 129
Cdd:PRK13603  83 WFGSAPRAMVIQVRGRRVPARAVLAGHYAAWLVVSVIVAWMVL 125
SQR_QFR_TM cd03493
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 27-126 2.45e-06

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: 43.04  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578263618  27 MLREGTAVPAVWFSLELLYGVYALKHGPEAWASFVGFLQNPIIVVLNLIVLAAALLHTKTWFELAPKAANIIVkgEKMGP 106
Cdd:cd03493    1 ILHRITGVALLLFLPLHLLGLLALLGGPYAFAEVVAFLSSPLGKLLYLLLLLALLYHALNGIRHLIWDYGKGL--ELKLR 78

                         90       100
                 ....*....|....*....|
gi 578263618 107 EPVIKGLWAVTAVVSVVILF 126
Cdd:cd03493   79 KALGYAVLALSVLLTVLLLF 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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