NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1905876045|ref|WP_188658040|]
View 

succinate dehydrogenase, cytochrome b556 subunit [Sphingomonas metalli]

Protein Classification

SdhC family protein( domain architecture ID 10005170)

SdhC family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SdhC COG2009
Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and ...
 2-135 1.54e-37

Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and conversion];


:

Pssm-ID: 441612  Cd Length: 128  Bit Score: 124.12  E-value: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   2 ASRNPARPLSPHLTIWRWGPHMLVSILHRVTGSGMAtVGAGLLVWFLAALAGGEESYATFVDTFTvesgklNVLGYIVGI 81
Cdd:COG2009     1 AEVKKNRPLSPHLQIYRLPLTMIVSILHRITGVALF-LGLPLLVWWLAASASSPEAFAAVQAFLG------SPLGKLVLL 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1905876045  82 GLTLSLFQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAFWLYLGM 135
Cdd:COG2009    74 GLTWALLYHLLAGIRHLLWDFGYGFELETARRSAWVVLVLSVVLTVLLGVVLWG 127
 
Name Accession Description Interval E-value
SdhC COG2009
Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and ...
 2-135 1.54e-37

Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and conversion];


Pssm-ID: 441612  Cd Length: 128  Bit Score: 124.12  E-value: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   2 ASRNPARPLSPHLTIWRWGPHMLVSILHRVTGSGMAtVGAGLLVWFLAALAGGEESYATFVDTFTvesgklNVLGYIVGI 81
Cdd:COG2009     1 AEVKKNRPLSPHLQIYRLPLTMIVSILHRITGVALF-LGLPLLVWWLAASASSPEAFAAVQAFLG------SPLGKLVLL 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1905876045  82 GLTLSLFQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAFWLYLGM 135
Cdd:COG2009    74 GLTWALLYHLLAGIRHLLWDFGYGFELETARRSAWVVLVLSVVLTVLLGVVLWG 127
SQR_TypeC_SdhC cd03499
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) ...
 8-131 3.05e-31

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) subunit; composed of bacterial SdhC and eukaryotic large cytochrome b binding (CybL) proteins. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this family reduce high potential quinones such as ubiquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Proteins in this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. The heme and quinone binding sites reside in the transmembrane subunits. The SdhC or CybL protein is one of the two transmembrane subunits of bacterial and eukaryotic SQRs. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.


Pssm-ID: 239579  Cd Length: 117  Bit Score: 107.62  E-value: 3.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   8 RPLSPHLTIWRWGPHMLVSILHRVTGSGMAtVGAGLLVWFLAALAGGEESYATFVDTFTvesgklNVLGYIVGIGLTLSL 87
Cdd:cd03499     1 RPLSPHLTIYRPPLTAILSILHRITGVALF-LGLPLLLWWLLASLSSPESFESVSALLG------SWLGKLVLFGLTWAL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1905876045  88 FQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAFWL 131
Cdd:cd03499    74 FYHLLNGIRHLIWDLGKGLELKTVYKSGYAVLVLSVVLTVLLGI 117
succ_dehyd_cytB TIGR02970
succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two ...
 8-132 7.62e-27

succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two small, hydrophobic, mutually homologous subunits of succinate dehydrogenase, a TCA cycle enzyme, are SdhC and SdhD. This family is the SdhC, the cytochrome b subunit, called b556 in bacteria and b560 in mitochondria. SdhD (see TIGR02968) is called the hydrophobic membrane anchor subunit, although both SdhC and SdhD participate in anchoring the complex. In some bacteria, this cytochrome b subunit is replaced my a member of the cytochrome b558 family (see TIGR02046). [Energy metabolism, TCA cycle]


Pssm-ID: 274370  Cd Length: 120  Bit Score: 96.48  E-value: 7.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   8 RPLSPHLTIWRWGPHMLVSILHRVTGSGMaTVGAGLLVWFLAALAGGEESYATFVDTFTVESGKLnvlgyiVGIGLTLSL 87
Cdd:TIGR02970   3 RPLSPHLQIYRFPITAILSILHRITGVLL-FFGLPFLLWWLSLSLSSPESFATVHALLSSPLGKL------ILWGLLWAL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1905876045  88 FQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAFWLY 132
Cdd:TIGR02970  76 LYHLLAGIRHLLWDLGYGLELKSARISAWVVLVLSLVLTILAGIW 120
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 4-129 1.51e-20

Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a transmembrane protein from both the Succinate dehydrogenase and Fumarate reductase complexes.


Pssm-ID: 426067  Cd Length: 122  Bit Score: 80.50  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   4 RNPARPLSPHLTIWRWGPHMLVSILHRVTGSGMATVGAGLLVWFLAALA--GGEESYATFVDTFTvesgklNVLGYIVGI 81
Cdd:pfam01127   1 MRKNRPLSPHLGLYRAHLTTWLSILHRITGVALAVLGLIFLLLWLLLLLslLGPESYATVVAWLA------SPVKLILLL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1905876045  82 GLTLSLFQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAF 129
Cdd:pfam01127  75 LLLLALFYHAANGIRHLIWDVGFGLELKTVRKSGAAVLALSVVLVIVL 122
sdhC PRK09487
succinate dehydrogenase cytochrome b556 subunit;
8-103 7.15e-05

succinate dehydrogenase cytochrome b556 subunit;


Pssm-ID: 181900  Cd Length: 129  Bit Score: 39.74  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   8 RPLSPHLTIWRWGPHMLVSILHRVTGSgMATVGAGLLVWFLAALAGGEESY---ATFVDTFTVEsgklnvlgyIVGIGLT 84
Cdd:PRK09487    9 RPVNLDLQTIRFPITAIASILHRVSGV-ITFVAVGILLWLLGTSLSSPEGFeqaAAIMDSFFVK---------FIMWGIL 78

                          90
                  ....*....|....*....
gi 1905876045  85 LSLFQHMMTGIRHLVLDTG 103
Cdd:PRK09487   79 TALAYHVVVGIRHLLMDFG 97
 
Name Accession Description Interval E-value
SdhC COG2009
Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and ...
 2-135 1.54e-37

Succinate dehydrogenase/fumarate reductase, cytochrome b subunit [Energy production and conversion];


Pssm-ID: 441612  Cd Length: 128  Bit Score: 124.12  E-value: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   2 ASRNPARPLSPHLTIWRWGPHMLVSILHRVTGSGMAtVGAGLLVWFLAALAGGEESYATFVDTFTvesgklNVLGYIVGI 81
Cdd:COG2009     1 AEVKKNRPLSPHLQIYRLPLTMIVSILHRITGVALF-LGLPLLVWWLAASASSPEAFAAVQAFLG------SPLGKLVLL 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1905876045  82 GLTLSLFQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAFWLYLGM 135
Cdd:COG2009    74 GLTWALLYHLLAGIRHLLWDFGYGFELETARRSAWVVLVLSVVLTVLLGVVLWG 127
SQR_TypeC_SdhC cd03499
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) ...
 8-131 3.05e-31

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase C (SdhC) subunit; composed of bacterial SdhC and eukaryotic large cytochrome b binding (CybL) proteins. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this family reduce high potential quinones such as ubiquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Proteins in this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. The heme and quinone binding sites reside in the transmembrane subunits. The SdhC or CybL protein is one of the two transmembrane subunits of bacterial and eukaryotic SQRs. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.


Pssm-ID: 239579  Cd Length: 117  Bit Score: 107.62  E-value: 3.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   8 RPLSPHLTIWRWGPHMLVSILHRVTGSGMAtVGAGLLVWFLAALAGGEESYATFVDTFTvesgklNVLGYIVGIGLTLSL 87
Cdd:cd03499     1 RPLSPHLTIYRPPLTAILSILHRITGVALF-LGLPLLLWWLLASLSSPESFESVSALLG------SWLGKLVLFGLTWAL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1905876045  88 FQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAFWL 131
Cdd:cd03499    74 FYHLLNGIRHLIWDLGKGLELKTVYKSGYAVLVLSVVLTVLLGI 117
succ_dehyd_cytB TIGR02970
succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two ...
 8-132 7.62e-27

succinate dehydrogenase, cytochrome b556 subunit; In E. coli and many other bacteria, two small, hydrophobic, mutually homologous subunits of succinate dehydrogenase, a TCA cycle enzyme, are SdhC and SdhD. This family is the SdhC, the cytochrome b subunit, called b556 in bacteria and b560 in mitochondria. SdhD (see TIGR02968) is called the hydrophobic membrane anchor subunit, although both SdhC and SdhD participate in anchoring the complex. In some bacteria, this cytochrome b subunit is replaced my a member of the cytochrome b558 family (see TIGR02046). [Energy metabolism, TCA cycle]


Pssm-ID: 274370  Cd Length: 120  Bit Score: 96.48  E-value: 7.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   8 RPLSPHLTIWRWGPHMLVSILHRVTGSGMaTVGAGLLVWFLAALAGGEESYATFVDTFTVESGKLnvlgyiVGIGLTLSL 87
Cdd:TIGR02970   3 RPLSPHLQIYRFPITAILSILHRITGVLL-FFGLPFLLWWLSLSLSSPESFATVHALLSSPLGKL------ILWGLLWAL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1905876045  88 FQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAFWLY 132
Cdd:TIGR02970  76 LYHLLAGIRHLLWDLGYGLELKSARISAWVVLVLSLVLTILAGIW 120
Sdh_cyt pfam01127
Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a ...
 4-129 1.51e-20

Succinate dehydrogenase/Fumarate reductase transmembrane subunit; This family includes a transmembrane protein from both the Succinate dehydrogenase and Fumarate reductase complexes.


Pssm-ID: 426067  Cd Length: 122  Bit Score: 80.50  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   4 RNPARPLSPHLTIWRWGPHMLVSILHRVTGSGMATVGAGLLVWFLAALA--GGEESYATFVDTFTvesgklNVLGYIVGI 81
Cdd:pfam01127   1 MRKNRPLSPHLGLYRAHLTTWLSILHRITGVALAVLGLIFLLLWLLLLLslLGPESYATVVAWLA------SPVKLILLL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1905876045  82 GLTLSLFQHMMTGIRHLVLDTGAGYELRRNKLGALATMLASVTLTAAF 129
Cdd:pfam01127  75 LLLLALFYHAANGIRHLIWDVGFGLELKTVRKSGAAVLALSVVLVIVL 122
SQR_QFR_TM cd03493
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 27-131 2.71e-08

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: 48.43  E-value: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045  27 ILHRVTGSGMAtVGAGLLVWFLAALAGGEESYATFVDTFTvesgklNVLGYIVGIGLTLSLFQHMMTGIRHLVLDTGAGY 106
Cdd:cd03493     1 ILHRITGVALL-LFLPLHLLGLLALLGGPYAFAEVVAFLS------SPLGKLLYLLLLLALLYHALNGIRHLIWDYGKGL 73

                          90       100
                  ....*....|....*....|....*
gi 1905876045 107 ELRRNKLGALATMLASVTLTAAFWL 131
Cdd:cd03493    74 ELKLRKALGYAVLALSVLLTVLLLF 98
sdhC PRK09487
succinate dehydrogenase cytochrome b556 subunit;
8-103 7.15e-05

succinate dehydrogenase cytochrome b556 subunit;


Pssm-ID: 181900  Cd Length: 129  Bit Score: 39.74  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   8 RPLSPHLTIWRWGPHMLVSILHRVTGSgMATVGAGLLVWFLAALAGGEESY---ATFVDTFTVEsgklnvlgyIVGIGLT 84
Cdd:PRK09487    9 RPVNLDLQTIRFPITAIASILHRVSGV-ITFVAVGILLWLLGTSLSSPEGFeqaAAIMDSFFVK---------FIMWGIL 78

                          90
                  ....*....|....*....
gi 1905876045  85 LSLFQHMMTGIRHLVLDTG 103
Cdd:PRK09487   79 TALAYHVVVGIRHLLMDFG 97
PLN00127 PLN00127
succinate dehydrogenase (ubiquinone) cytochrome b subunit; Provisional
 8-128 2.36e-04

succinate dehydrogenase (ubiquinone) cytochrome b subunit; Provisional


Pssm-ID: 177738  Cd Length: 178  Bit Score: 39.09  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905876045   8 RPLSPHL-------TIWRWGPHMLVSILHRVTGSGMATVGAGLLVwflAALAGGEESYATFVDTFTVESGklnVLGYIVG 80
Cdd:PLN00127   52 RPLSPDVmdidgksTHYKFPVVALSSITNRVTGCVLSGGAAGGGV---LALVGGSEAVPATMEGFKSGGP---LIVFPAK 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1905876045  81 IGLTLSLFQHMMTGIRHLVLD-TGAGYELRRNKLGALATMLASVTLTAA 128
Cdd:PLN00127  126 FAVSFPFVYHTLGGLRHLVWDkTTEGLDNPSVEASSYGLFGASAALSAA 174
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH