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E. coli Quinol fumarate reductase FrdA E245Q mutation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000104molecular_functionsuccinate dehydrogenase activity
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006113biological_processfermentation
A0006974biological_processDNA damage response
A0008177molecular_functionsuccinate dehydrogenase (quinone) activity
A0009055molecular_functionelectron transfer activity
A0009061biological_processanaerobic respiration
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0019645biological_processanaerobic electron transport chain
A0022900biological_processelectron transport chain
A0044780biological_processbacterial-type flagellum assembly
A0045284cellular_componentplasma membrane fumarate reductase complex
A0050660molecular_functionflavin adenine dinucleotide binding
A0071949molecular_functionFAD binding
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006099biological_processtricarboxylic acid cycle
B0006113biological_processfermentation
B0008177molecular_functionsuccinate dehydrogenase (quinone) activity
B0009055molecular_functionelectron transfer activity
B0009061biological_processanaerobic respiration
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0019645biological_processanaerobic electron transport chain
B0044780biological_processbacterial-type flagellum assembly
B0045284cellular_componentplasma membrane fumarate reductase complex
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
B0051538molecular_function3 iron, 4 sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0000104molecular_functionsuccinate dehydrogenase activity
C0005886cellular_componentplasma membrane
C0006113biological_processfermentation
C0009061biological_processanaerobic respiration
C0016020cellular_componentmembrane
C0019645biological_processanaerobic electron transport chain
C0044780biological_processbacterial-type flagellum assembly
C0045284cellular_componentplasma membrane fumarate reductase complex
D0000104molecular_functionsuccinate dehydrogenase activity
D0005886cellular_componentplasma membrane
D0006106biological_processfumarate metabolic process
D0006113biological_processfermentation
D0009061biological_processanaerobic respiration
D0016020cellular_componentmembrane
D0019645biological_processanaerobic electron transport chain
D0044780biological_processbacterial-type flagellum assembly
D0045284cellular_componentplasma membrane fumarate reductase complex
E0000104molecular_functionsuccinate dehydrogenase activity
E0000166molecular_functionnucleotide binding
E0005515molecular_functionprotein binding
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006113biological_processfermentation
E0006974biological_processDNA damage response
E0008177molecular_functionsuccinate dehydrogenase (quinone) activity
E0009055molecular_functionelectron transfer activity
E0009061biological_processanaerobic respiration
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
E0019645biological_processanaerobic electron transport chain
E0022900biological_processelectron transport chain
E0044780biological_processbacterial-type flagellum assembly
E0045284cellular_componentplasma membrane fumarate reductase complex
E0050660molecular_functionflavin adenine dinucleotide binding
E0071949molecular_functionFAD binding
F0005515molecular_functionprotein binding
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0006099biological_processtricarboxylic acid cycle
F0006113biological_processfermentation
F0008177molecular_functionsuccinate dehydrogenase (quinone) activity
F0009055molecular_functionelectron transfer activity
F0009061biological_processanaerobic respiration
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
F0019645biological_processanaerobic electron transport chain
F0044780biological_processbacterial-type flagellum assembly
F0045284cellular_componentplasma membrane fumarate reductase complex
F0046872molecular_functionmetal ion binding
F0051536molecular_functioniron-sulfur cluster binding
F0051537molecular_function2 iron, 2 sulfur cluster binding
F0051538molecular_function3 iron, 4 sulfur cluster binding
F0051539molecular_function4 iron, 4 sulfur cluster binding
G0000104molecular_functionsuccinate dehydrogenase activity
G0005886cellular_componentplasma membrane
G0006113biological_processfermentation
G0009061biological_processanaerobic respiration
G0016020cellular_componentmembrane
G0019645biological_processanaerobic electron transport chain
G0044780biological_processbacterial-type flagellum assembly
G0045284cellular_componentplasma membrane fumarate reductase complex
H0000104molecular_functionsuccinate dehydrogenase activity
H0005886cellular_componentplasma membrane
H0006106biological_processfumarate metabolic process
H0006113biological_processfermentation
H0009061biological_processanaerobic respiration
H0016020cellular_componentmembrane
H0019645biological_processanaerobic electron transport chain
H0044780biological_processbacterial-type flagellum assembly
H0045284cellular_componentplasma membrane fumarate reductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues31
Detailsbinding site for residue FAD A 601
ChainResidue
AGLY11
AHIS44
ATHR45
AALA47
AALA48
AGLY50
AGLY51
AHIS155
AVAL157
AALA191
ATHR192
AALA12
AGLY193
ATHR203
AASP211
ALEU242
AHIS355
ATYR356
AGLU379
ASER393
AASN394
ASER395
AGLY13
ALEU396
ALEU399
AGLY14
AALA15
ASER36
ALYS37
AVAL38
ASER43

site_idAC2
Number of Residues9
Detailsbinding site for residue FES B 301
ChainResidue
BSER56
BCYS57
BARG58
BALA60
BILE61
BCYS62
BGLY63
BCYS65
BCYS77

site_idAC3
Number of Residues10
Detailsbinding site for residue F3S B 302
ChainResidue
BCYS158
BCYS204
BTHR205
BPHE206
BVAL207
BGLY208
BTYR209
BCYS210
BALA221
BILE224

site_idAC4
Number of Residues10
Detailsbinding site for residue SF4 B 303
ChainResidue
BCYS148
BILE149
BCYS151
BGLY152
BLEU153
BCYS154
BALA171
BCYS214
BPRO215
BVAL218

site_idAC5
Number of Residues34
Detailsbinding site for residue FAD E 601
ChainResidue
EGLY11
EALA12
EGLY13
EGLY14
EALA15
ESER36
ELYS37
EVAL38
ESER43
EHIS44
ETHR45
EALA47
EALA48
EGLU49
EGLY50
EGLY51
EHIS155
EVAL157
EALA191
ETHR192
EGLY193
ETHR203
EASP211
ELEU242
EHIS355
ETYR356
EGLY378
EGLU379
EARG390
ESER393
EASN394
ESER395
ELEU396
ELEU399

site_idAC6
Number of Residues8
Detailsbinding site for residue FES F 301
ChainResidue
FGLY63
FCYS65
FCYS77
FCYS57
FARG58
FALA60
FILE61
FCYS62

site_idAC7
Number of Residues9
Detailsbinding site for residue F3S F 302
ChainResidue
FCYS158
FCYS204
FTHR205
FPHE206
FVAL207
FGLY208
FTYR209
FCYS210
FALA221

site_idAC8
Number of Residues7
Detailsbinding site for residue SF4 F 303
ChainResidue
FCYS148
FILE149
FCYS151
FGLY152
FLEU153
FCYS154
FCYS214

Functional Information from PROSITE/UniProt
site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAeGG
ChainResidueDetails
AARG42-GLY51

site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRMAICGSC
ChainResidueDetails
BCYS57-CYS65

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiNCGlCYaACP
ChainResidueDetails
BCYS148-PRO159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10373108, ECO:0007744|PDB:1L0V
ChainResidueDetails
GASN65-LEU89
GGLY104-ALA127
BTYR13
BGLN225
FTYR13
FGLN225

site_idSWS_FT_FI2
Number of Residues22
DetailsBINDING: BINDING => ECO:0000269|PubMed:10373108, ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, ECO:0007744|PDB:1L0V
ChainResidueDetails
FCYS77
FCYS148
FCYS151
FCYS154
FCYS158
FCYS204
FCYS210
FCYS214
BCYS204
BCYS210
BCYS214
FCYS57
FCYS62
FCYS65
BCYS57
BCYS62
BCYS65
BCYS77
BCYS148
BCYS151
BCYS154
BCYS158

site_idSWS_FT_FI3
Number of Residues48
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:10373108
ChainResidueDetails
DVAL35-GLN59
HVAL35-GLN59

site_idSWS_FT_FI4
Number of Residues6
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:10373108, ECO:0000269|PubMed:15919996
ChainResidueDetails
DVAL115-ILE118
HVAL115-ILE118

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1L0V
ChainResidueDetails
DTRP14
HTRP14

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1L0V
ChainResidueDetails
CTRP86
GTRP86

219869

PDB entries from 2024-05-15

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