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2B76

E. coli Quinol fumarate reductase FrdA E49Q 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_componentobsolete plasma 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_componentobsolete plasma 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_componentobsolete plasma 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_componentobsolete plasma membrane fumarate reductase complex
M0000104molecular_functionsuccinate dehydrogenase activity
M0000166molecular_functionnucleotide binding
M0005515molecular_functionprotein binding
M0005829cellular_componentcytosol
M0005886cellular_componentplasma membrane
M0006113biological_processfermentation
M0006974biological_processDNA damage response
M0008177molecular_functionsuccinate dehydrogenase (quinone) activity
M0009055molecular_functionelectron transfer activity
M0009061biological_processanaerobic respiration
M0016020cellular_componentmembrane
M0016491molecular_functionoxidoreductase activity
M0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
M0019645biological_processanaerobic electron transport chain
M0022900biological_processelectron transport chain
M0044780biological_processbacterial-type flagellum assembly
M0045284cellular_componentobsolete plasma membrane fumarate reductase complex
M0050660molecular_functionflavin adenine dinucleotide binding
M0071949molecular_functionFAD binding
N0005515molecular_functionprotein binding
N0005829cellular_componentcytosol
N0005886cellular_componentplasma membrane
N0006099biological_processtricarboxylic acid cycle
N0006113biological_processfermentation
N0008177molecular_functionsuccinate dehydrogenase (quinone) activity
N0009055molecular_functionelectron transfer activity
N0009061biological_processanaerobic respiration
N0016020cellular_componentmembrane
N0016491molecular_functionoxidoreductase activity
N0019645biological_processanaerobic electron transport chain
N0044780biological_processbacterial-type flagellum assembly
N0045284cellular_componentobsolete plasma membrane fumarate reductase complex
N0046872molecular_functionmetal ion binding
N0051536molecular_functioniron-sulfur cluster binding
N0051537molecular_function2 iron, 2 sulfur cluster binding
N0051538molecular_function3 iron, 4 sulfur cluster binding
N0051539molecular_function4 iron, 4 sulfur cluster binding
O0000104molecular_functionsuccinate dehydrogenase activity
O0005886cellular_componentplasma membrane
O0006113biological_processfermentation
O0009061biological_processanaerobic respiration
O0016020cellular_componentmembrane
O0019645biological_processanaerobic electron transport chain
O0044780biological_processbacterial-type flagellum assembly
O0045284cellular_componentobsolete plasma membrane fumarate reductase complex
P0000104molecular_functionsuccinate dehydrogenase activity
P0005886cellular_componentplasma membrane
P0006106biological_processfumarate metabolic process
P0006113biological_processfermentation
P0009061biological_processanaerobic respiration
P0016020cellular_componentmembrane
P0019645biological_processanaerobic electron transport chain
P0044780biological_processbacterial-type flagellum assembly
P0045284cellular_componentobsolete plasma membrane fumarate reductase complex
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FLC A 702
ChainResidue
AGLN230
AFAD703
AHIS232
ATHR244
AGLU245
AARG287
AHIS355
AARG390
AGLY392
ASER393

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FLC M 802
ChainResidue
MPHE116
MGLN230
MHIS232
MLEU242
MGLU245
MARG287
MHIS355
MARG390
MASN394

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES B 244
ChainResidue
BSER56
BCYS57
BARG58
BCYS62
BGLY63
BCYS65
BCYS77

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F3S B 245
ChainResidue
BCYS158
BGLN160
BCYS204
BTHR205
BPHE206
BVAL207
BGLY208
BTYR209
BCYS210
BALA221

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 B 246
ChainResidue
BCYS148
BILE149
BCYS151
BGLY152
BCYS154
BCYS214

site_idAC6
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD A 703
ChainResidue
AGLY11
AALA12
AGLY14
AALA15
ASER36
ALYS37
ASER43
AHIS44
ATHR45
AALA47
AALA48
AGLN49
AGLY50
AGLY51
AHIS155
AVAL157
ATHR192
AGLY193
ATHR203
AASN204
AASP211
AMET215
ALEU242
ATYR356
AGLY378
AGLU379
ASER393
ASER395
ALEU396
ALEU399
AFLC702

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MQ7 D 700
ChainResidue
CGLY45
CTRP56
CILE123
CALA127
DVAL35
DLEU49
DPHE57
DLEU67

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES N 244
ChainResidue
NLEU37
NCYS57
NILE61
NCYS62
NGLY63
NSER64
NCYS65
NCYS77

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE F3S N 245
ChainResidue
NGLN225
NCYS158
NCYS204
NTHR205
NPHE206
NVAL207
NGLY208
NTYR209
NCYS210
NALA221
NILE224

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 N 246
ChainResidue
NCYS148
NILE149
NCYS151
NGLY152
NCYS154
NCYS214
NPRO215
NVAL218

site_idBC2
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD M 803
ChainResidue
MVAL10
MGLY11
MALA12
MGLY13
MGLY14
MALA15
MSER36
MLYS37
MSER43
MHIS44
MTHR45
MALA47
MALA48
MGLN49
MGLY50
MGLY51
MVAL157
MALA191
MTHR192
MTHR203
MASN204
MILE207
MVAL208
MASP211
MGLY212
MLEU242
MHIS355
MTYR356
MGLY378
MGLU379
MLEU396
MLEU399

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MQ7 P 800
ChainResidue
OILE123
OVAL126
PVAL35
PLEU49
PPHE57
PILE62
PPHE66
PLEU67

Functional Information from PROSITE/UniProt
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

site_idPS00504
Number of Residues10
DetailsFRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG
ChainResidueDetails
AARG42-GLY51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:1856194
ChainResidueDetails
AHIS232
AARG248
MHIS232
MARG248
OASN65-LEU89
OGLY104-ALA127

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0007744|PDB:1KF6, ECO:0007744|PDB:1KFY, ECO:0007744|PDB:1L0V
ChainResidueDetails
AGLY11
MSER43
MHIS155
MASP211
MGLU379
MARG390
NLYS78
NILE149
NGLY152
NTYR155
NPRO159
AILE35
NTHR205
NSER211
NPRO215
ASER43
AHIS155
AASP211
AGLU379
AARG390
MGLY11
MILE35

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1KF6
ChainResidueDetails
AALA191
MALA191

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:2B76, ECO:0007744|PDB:3CIR
ChainResidueDetails
AHIS355
MHIS355

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Tele-8alpha-FAD histidine => ECO:0000269|PubMed:10373108, ECO:0007744|PDB:1L0V
ChainResidueDetails
AHIS44
MHIS44

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1L0V
ChainResidueDetails
CTRP86
OTRP86

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
AARG287
AHIS355
AARG390
AHIS232

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d4c
ChainResidueDetails
MARG287
MHIS355
MARG390
MHIS232

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PDB entries from 2024-07-24

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