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Conserved domains on  [gi|1397983263]
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Chain G, fumarate reductase respiratory complex

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SQR_QFR_TM super family cl00881
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 20-212 1.35e-59

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.


The actual alignment was detected with superfamily member cd00581:

Pssm-ID: 469971  Cd Length: 206  Bit Score: 186.00  E-value: 1.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  20 MDFFQMVSGALLILFLWAHMMLVSSVILSPSLMNGIAWFFEA--------TYMAQIGGPAVFVLMVVHFILAARKMPFKQ 91
Cdd:cd00581     1 LDFLQSATGLFLALFMWAHMLFVSSILLGKEAMYWVARFFEGafffghgyPWVVSVVAAIVFALFVAHAFLALRKFPANY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  92 DEWKTFRVHACMLHHKDTTMWVVQVISAIFILVLGAVHMFVVLTDLP-ITAAKSAARLQSG-WLYLYLVLLPLAELHVGV 169
Cdd:cd00581    81 RQWRAFRRHMQLMKHGDTSLWWIQAVTGFVLFFLASAHLYEMLTNPEiIGPHTSAYRVVHGgWWLLYLALLPAVELHGGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1397983263 170 GFYRIGVKYGFVGRNKRKWFQKTENLMMIGFITIGLLTLVRFM 212
Cdd:cd00581   161 GLYRLAVKWGWFASESRKRLRRIKNVLSAFFLVLGLLTLLAYI 203
 
Name Accession Description Interval E-value
QFR_TypeB_TM cd00581
Quinol:fumarate reductase (QFR) Type B subfamily, transmembrane subunit; QFR couples the ...
 20-212 1.35e-59

Quinol:fumarate reductase (QFR) Type B subfamily, transmembrane subunit; 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:quinone oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and rhodoquinol 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 B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunit. 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 Type B enzyme from Desulfovibrio gigas is capable of fumarate reduction and succinate oxidation.


Pssm-ID: 238325  Cd Length: 206  Bit Score: 186.00  E-value: 1.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  20 MDFFQMVSGALLILFLWAHMMLVSSVILSPSLMNGIAWFFEA--------TYMAQIGGPAVFVLMVVHFILAARKMPFKQ 91
Cdd:cd00581     1 LDFLQSATGLFLALFMWAHMLFVSSILLGKEAMYWVARFFEGafffghgyPWVVSVVAAIVFALFVAHAFLALRKFPANY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  92 DEWKTFRVHACMLHHKDTTMWVVQVISAIFILVLGAVHMFVVLTDLP-ITAAKSAARLQSG-WLYLYLVLLPLAELHVGV 169
Cdd:cd00581    81 RQWRAFRRHMQLMKHGDTSLWWIQAVTGFVLFFLASAHLYEMLTNPEiIGPHTSAYRVVHGgWWLLYLALLPAVELHGGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1397983263 170 GFYRIGVKYGFVGRNKRKWFQKTENLMMIGFITIGLLTLVRFM 212
Cdd:cd00581   161 GLYRLAVKWGWFASESRKRLRRIKNVLSAFFLVLGLLTLLAYI 203
PRK13553 PRK13553
fumarate reductase cytochrome b subunit;
13-212 2.34e-36

fumarate reductase cytochrome b subunit;


Pssm-ID: 237423  Cd Length: 258  Bit Score: 128.20  E-value: 2.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  13 RSKIAGRMDFFQMVSGALLILFLWAHMMLVSSVILSPSLMNGIAWFFEATYMAQIGGPA--------VFVLMVVHFILAA 84
Cdd:PRK13553   17 KSRIPAKLDFLQSATGLFLGLFMWAHMFFVSTILISDDAMYKVAKFFEGSFFFKAGEPAlvsfvaagVILIFVVHAFLAM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  85 RKMPFKQDEWKTFRVHACMLHHKDTTMWVVQVISAIFILVLGAVHMFVVLTDLP-ITAAKSAARLQSGWLYLYLVLLPLA 163
Cdd:PRK13553   97 RKFPINYRQYQIFRTHKHLMKHGDTSLWFIQAFTGFAMFFLASVHLYVMLTNPDkIGPYGSSDRVVSQNMWLLYIVLLFA 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1397983263 164 -ELHVGVGFYRIGVKYG-FVGRN---KRKWFQKTENLMMIGFITIGLLTLVRFM 212
Cdd:PRK13553  177 vELHGSIGLYRLAVKWGwFEGKNpkeSRKKLKKVKWALSVFFLVLGLLTLAAYI 230
 
Name Accession Description Interval E-value
QFR_TypeB_TM cd00581
Quinol:fumarate reductase (QFR) Type B subfamily, transmembrane subunit; QFR couples the ...
 20-212 1.35e-59

Quinol:fumarate reductase (QFR) Type B subfamily, transmembrane subunit; 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:quinone oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and rhodoquinol 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 B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunit. 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 Type B enzyme from Desulfovibrio gigas is capable of fumarate reduction and succinate oxidation.


Pssm-ID: 238325  Cd Length: 206  Bit Score: 186.00  E-value: 1.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  20 MDFFQMVSGALLILFLWAHMMLVSSVILSPSLMNGIAWFFEA--------TYMAQIGGPAVFVLMVVHFILAARKMPFKQ 91
Cdd:cd00581     1 LDFLQSATGLFLALFMWAHMLFVSSILLGKEAMYWVARFFEGafffghgyPWVVSVVAAIVFALFVAHAFLALRKFPANY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  92 DEWKTFRVHACMLHHKDTTMWVVQVISAIFILVLGAVHMFVVLTDLP-ITAAKSAARLQSG-WLYLYLVLLPLAELHVGV 169
Cdd:cd00581    81 RQWRAFRRHMQLMKHGDTSLWWIQAVTGFVLFFLASAHLYEMLTNPEiIGPHTSAYRVVHGgWWLLYLALLPAVELHGGI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1397983263 170 GFYRIGVKYGFVGRNKRKWFQKTENLMMIGFITIGLLTLVRFM 212
Cdd:cd00581   161 GLYRLAVKWGWFASESRKRLRRIKNVLSAFFLVLGLLTLLAYI 203
PRK13553 PRK13553
fumarate reductase cytochrome b subunit;
13-212 2.34e-36

fumarate reductase cytochrome b subunit;


Pssm-ID: 237423  Cd Length: 258  Bit Score: 128.20  E-value: 2.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  13 RSKIAGRMDFFQMVSGALLILFLWAHMMLVSSVILSPSLMNGIAWFFEATYMAQIGGPA--------VFVLMVVHFILAA 84
Cdd:PRK13553   17 KSRIPAKLDFLQSATGLFLGLFMWAHMFFVSTILISDDAMYKVAKFFEGSFFFKAGEPAlvsfvaagVILIFVVHAFLAM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  85 RKMPFKQDEWKTFRVHACMLHHKDTTMWVVQVISAIFILVLGAVHMFVVLTDLP-ITAAKSAARLQSGWLYLYLVLLPLA 163
Cdd:PRK13553   97 RKFPINYRQYQIFRTHKHLMKHGDTSLWFIQAFTGFAMFFLASVHLYVMLTNPDkIGPYGSSDRVVSQNMWLLYIVLLFA 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1397983263 164 -ELHVGVGFYRIGVKYG-FVGRN---KRKWFQKTENLMMIGFITIGLLTLVRFM 212
Cdd:PRK13553  177 vELHGSIGLYRLAVKWGwFEGKNpkeSRKKLKKVKWALSVFFLVLGLLTLAAYI 230
PRK13554 PRK13554
fumarate reductase cytochrome b-556 subunit; Provisional
 17-214 1.04e-18

fumarate reductase cytochrome b-556 subunit; Provisional


Pssm-ID: 237424  Cd Length: 241  Bit Score: 81.33  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  17 AGRMDFFQMVSGALLILFLWAHMMLVSSVILSPSLMNGIAWFFEATYMAQIGGP--------AVFVLMVV--HFILAARK 86
Cdd:PRK13554   21 SAKADKLQSATGIMLGCFLLLHMHFESSILLGKEAFYHVVQFLEGGMFSSTGHGfpivtkvfSVFMLLVVivHAAVALRR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  87 MPFKQDEWKTFRVHACMLHHKDTTMWVVQVISAIFILVLGAVHMFVVLTDLPITAAKSAARL--QSGWLYLYLVLLPLAe 164
Cdd:PRK13554  101 FPAQLGQWRALRSHMGSIKHKDTHAWFWQLITGFILFFLVPVHLFTMILNPEIGPHLSAERVyhDNAWLLYALLLPAVV- 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1397983263 165 LHVGVGFYRIGVKYGFVgrNKRKWFQKTENLMMIGFITIGLLTLVRFMLL 214
Cdd:PRK13554  180 IHAMIGLYRVAVKWGLT--TNRSGLRKVAKVLIIYLLCLGTLSLVSYIFI 227
SQR_QFR_TypeB_TM cd03526
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) Type B subfamily, ...
 20-180 4.23e-07

Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) Type B subfamily, transmembrane subunit; 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. 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. Type B proteins contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunits. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit 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.


Pssm-ID: 239602  Cd Length: 199  Bit Score: 48.76  E-value: 4.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263  20 MDFFQMVSGALLILFLWAHMMLVSSVILSPSLMNGIAWFFEATYMAQIGGPAVFVLMVVHFILAARKMPFKQDEWKTFRV 99
Cdd:cd03526     1 LDWLQSATGLFLGLFMIGHLFFNSTILLGDNVMNWVAKKFELLPIVVSFLAAFIFAVFIAHAFLGVRKFPIYRQALTFKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397983263 100 HACMLhHKDTTMWVVQVISAIFILVLGAVHMFVVLT----DLPITAAKSAARLQSGWLYLYLVLLPLA-ELHVGVGFYRI 174
Cdd:cd03526    81 HKDLM-HGDTTLWWIQAMTGFAMLFFGSVHLYIMMTqaqpDRTIGFVMSSNRMSSEWMWPLYIVLLFAvELHGSVGLYSF 159


                  ....*.
gi 1397983263 175 GVKYGF 180
Cdd:cd03526   160 AVTWGW 165
 
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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