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Conserved domains on  [gi|2127509678|ref|WP_227686587|]
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MULTISPECIES: succinate dehydrogenase, hydrophobic membrane anchor protein [Psychrobacter]

Protein Classification

succinate dehydrogenase, hydrophobic membrane anchor protein( domain architecture ID 10131267)

succinate dehydrogenase, hydrophobic membrane anchor protein (SdhD), together with subunit SdhC, acts to anchor the catalytic components of succinate dehydrogenase to the cytoplasmic membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SQR_TypeC_SdhD cd03494
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) ...
 14-119 2.55e-30

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. E. coli SQR, a member of this subfamily, reduces the high potential quinine, 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. Members of this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. SdhD and SdhC are the two transmembrane proteins of bacterial SQRs. They contain heme and quinone binding sites. 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: 239574  Cd Length: 99  Bit Score: 104.61  E-value: 2.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678  14 DWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYITTgklgssaA 93
Cdd:cd03494     1 DWLVQRVTAVIMALYTIFLVGFLLASPPLTYEAWSGLFSSLWMKIFTLLALLALLLHAWIGLWDILTDYVKP-------A 73

                          90       100
                  ....*....|....*....|....*.
gi 2127509678  94 GLRLVLQSLMIIAILVFLFWGIMIFW 119
Cdd:cd03494    74 GLRLLLQVLIILVLFGYLIWGIQILW 99
 
Name Accession Description Interval E-value
SQR_TypeC_SdhD cd03494
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) ...
 14-119 2.55e-30

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. E. coli SQR, a member of this subfamily, reduces the high potential quinine, 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. Members of this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. SdhD and SdhC are the two transmembrane proteins of bacterial SQRs. They contain heme and quinone binding sites. 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: 239574  Cd Length: 99  Bit Score: 104.61  E-value: 2.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678  14 DWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYITTgklgssaA 93
Cdd:cd03494     1 DWLVQRVTAVIMALYTIFLVGFLLASPPLTYEAWSGLFSSLWMKIFTLLALLALLLHAWIGLWDILTDYVKP-------A 73

                          90       100
                  ....*....|....*....|....*.
gi 2127509678  94 GLRLVLQSLMIIAILVFLFWGIMIFW 119
Cdd:cd03494    74 GLRLLLQVLIILVLFGYLIWGIQILW 99
succ_dehyd_anc TIGR02968
succinate dehydrogenase, hydrophobic membrane anchor protein; In E. coli and many other ...
 9-119 3.14e-26

succinate dehydrogenase, hydrophobic membrane anchor protein; 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 SdhD, the hydrophobic membrane anchor protein. SdhC is apocytochrome b558, which also plays a role in anchoring the complex. [Energy metabolism, TCA cycle]


Pssm-ID: 274369  Cd Length: 105  Bit Score: 94.17  E-value: 3.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678   9 GSGSRDWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYIttgkl 88
Cdd:TIGR02968   2 RSGLRDWLLQRVTAVVLALYTIFLIGFLLALPGLTYEAWRALFAHPWMKIFTLLALLALLYHAWIGMRVVLEDYV----- 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2127509678  89 gsSAAGLRLVLQSLMIIAILVFLFWGIMIFW 119
Cdd:TIGR02968  77 --KPEGLRLVLQVLIILFLVAYLIWGAFILW 105
SdhD COG2142
Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];
5-123 9.24e-22

Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];


Pssm-ID: 441745  Cd Length: 124  Bit Score: 83.34  E-value: 9.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678   5 TGLTGSGSRDWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYIT 84
Cdd:COG2142    13 LGSAKSGTHHWLLQRVTAVALVVLVLWFLFFLLSLPGADYAEVAAWFASPFWAILTLLFLLSALYHAWLGLRVVIEDYVH 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2127509678  85 TgklgssaAGLRLVLQSLMIIAILVFLFWGIMIFWGSGF 123
Cdd:COG2142    93 G-------TGLRLALLLLLTLALVALAAAGVFALLRIAL 124
sdhD PRK09488
succinate dehydrogenase membrane anchor subunit;
3-120 2.15e-18

succinate dehydrogenase membrane anchor subunit;


Pssm-ID: 181901  Cd Length: 115  Bit Score: 74.39  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678   3 SATGLTGSGSRDWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDY 82
Cdd:PRK09488    4 NASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWRGFFASAFTKVFTLLALFSILIHAWIGMWQVLTDY 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2127509678  83 IttgklgsSAAGLRLVLQSLMIIAILVFLFWGIMIFWG 120
Cdd:PRK09488   84 V-------KPLALRLMLQLVIVVALVVYVIYGFVVVWG 114
 
Name Accession Description Interval E-value
SQR_TypeC_SdhD cd03494
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) ...
 14-119 2.55e-30

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. E. coli SQR, a member of this subfamily, reduces the high potential quinine, 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. Members of this subfamily are classified as Type C SQRs because they contain two transmembrane subunits and one heme group. SdhD and SdhC are the two transmembrane proteins of bacterial SQRs. They contain heme and quinone binding sites. 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: 239574  Cd Length: 99  Bit Score: 104.61  E-value: 2.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678  14 DWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYITTgklgssaA 93
Cdd:cd03494     1 DWLVQRVTAVIMALYTIFLVGFLLASPPLTYEAWSGLFSSLWMKIFTLLALLALLLHAWIGLWDILTDYVKP-------A 73

                          90       100
                  ....*....|....*....|....*.
gi 2127509678  94 GLRLVLQSLMIIAILVFLFWGIMIFW 119
Cdd:cd03494    74 GLRLLLQVLIILVLFGYLIWGIQILW 99
succ_dehyd_anc TIGR02968
succinate dehydrogenase, hydrophobic membrane anchor protein; In E. coli and many other ...
 9-119 3.14e-26

succinate dehydrogenase, hydrophobic membrane anchor protein; 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 SdhD, the hydrophobic membrane anchor protein. SdhC is apocytochrome b558, which also plays a role in anchoring the complex. [Energy metabolism, TCA cycle]


Pssm-ID: 274369  Cd Length: 105  Bit Score: 94.17  E-value: 3.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678   9 GSGSRDWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYIttgkl 88
Cdd:TIGR02968   2 RSGLRDWLLQRVTAVVLALYTIFLIGFLLALPGLTYEAWRALFAHPWMKIFTLLALLALLYHAWIGMRVVLEDYV----- 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2127509678  89 gsSAAGLRLVLQSLMIIAILVFLFWGIMIFW 119
Cdd:TIGR02968  77 --KPEGLRLVLQVLIILFLVAYLIWGAFILW 105
SdhD COG2142
Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];
5-123 9.24e-22

Succinate dehydrogenase, hydrophobic anchor subunit [Energy production and conversion];


Pssm-ID: 441745  Cd Length: 124  Bit Score: 83.34  E-value: 9.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678   5 TGLTGSGSRDWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYIT 84
Cdd:COG2142    13 LGSAKSGTHHWLLQRVTAVALVVLVLWFLFFLLSLPGADYAEVAAWFASPFWAILTLLFLLSALYHAWLGLRVVIEDYVH 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2127509678  85 TgklgssaAGLRLVLQSLMIIAILVFLFWGIMIFWGSGF 123
Cdd:COG2142    93 G-------TGLRLALLLLLTLALVALAAAGVFALLRIAL 124
sdhD PRK09488
succinate dehydrogenase membrane anchor subunit;
3-120 2.15e-18

succinate dehydrogenase membrane anchor subunit;


Pssm-ID: 181901  Cd Length: 115  Bit Score: 74.39  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678   3 SATGLTGSGSRDWIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDY 82
Cdd:PRK09488    4 NASALGRNGVHDFILVRATAIVLTLYIIYMVGFFATSGELTYEVWRGFFASAFTKVFTLLALFSILIHAWIGMWQVLTDY 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2127509678  83 IttgklgsSAAGLRLVLQSLMIIAILVFLFWGIMIFWG 120
Cdd:PRK09488   84 V-------KPLALRLMLQLVIVVALVVYVIYGFVVVWG 114
SQR_QFR_TM cd03493
Succinate:quinone oxidoreductase (SQR) and Quinol:fumarate reductase (QFR) family, ...
 16-111 2.72e-04

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: 37.65  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678  16 IIQRISAVVLAVYSVVLLGFFLT--HGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYITTGKLGSSAA 93
Cdd:cd03493     1 ILHRITGVALLLFLPLHLLGLLAllGGPYAFAEVVAFLSSPLGKLLYLLLLLALLYHALNGIRHLIWDYGKGLELKLRKA 80

                          90
                  ....*....|....*...
gi 2127509678  94 GLRLVLQSLMIIAILVFL 111
Cdd:cd03493    81 LGYAVLALSVLLTVLLLF 98
SQR_TypeC_SdhD_like cd03495
Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) ...
 15-118 3.99e-04

Succinate:quinone oxidoreductase (SQR) Type C subfamily, Succinate dehydrogenase D (SdhD) subunit-like; composed of predominantly uncharacterized bacterial proteins with similarity to the E. coli SdhD subunit. One characterized protein is the respiratory Complex II SdhD subunit of the only eukaryotic member, Reclinomonas americana. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. It 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. E. coli SQR is classified as Type C SQRs because it contains two transmembrane subunits and one heme group. The SdhD and SdhC subunits are membrane anchor subunits containing heme and quinone binding sites. 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: 239575  Cd Length: 100  Bit Score: 37.19  E-value: 3.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127509678  15 WIIQRISAVVLAVYSVVLLGFFLTHGDVTYLEWSSFMTSLPMRLFSLVAVLALAGHAWVGMWTVFTDYITTGKLGSSAag 94
Cdd:cd03495     3 WWAQRVTAVALVPLVLWFVFSVALLLGASYAEVVAWLAHPFNAILLILTLVSAFYHARLGMQVVIEDYVHSEGLRLAL-- 80

                          90       100
                  ....*....|....*....|....
gi 2127509678  95 lrlvlqsLMIIAILVFLFWGIMIF 118
Cdd:cd03495    81 -------IIAVKLFAIATAAAGIF 97
 
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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