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Conserved domains on  [gi|535035218|gb|EQR82347|]
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ATPase [Escherichia coli HVH 137 (4-2124971)]

Protein Classification

BadF/BadG/BcrA/BcrD ATPase family protein( domain architecture ID 10015550)

BadF/BadG/BcrA/BcrD ATPase family protein similar to Escherichia coli protein YjiL

CATH:  3.30.420.40
Gene Ontology:  GO:0005524|GO:0051539
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 3-247 1.12e-131

CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.


:

Pssm-ID: 129344  Cd Length: 248  Bit Score: 371.82  E-value: 1.12e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218    3 YSIGIDSGSTATKGILLADG-VITRRFLVPTPFRPAT--AITEAWETLREGLETTPFLTLTGYGRQLVDFADKQVTEISC 79
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGkVIGYKWLDTTPVIEETarAILEALKEAGIGLEPIDKIVATGYGRHKVGFADKIVTEISC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   80 HGLGARFLEPATRAVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITEN-VIPHAITS 158
Cdd:TIGR00241  81 HGKGANYLAPEARGVIDIGGQDSKVIKIDD-GKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKaDRKAKISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQF 238
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQI 239


                  ....*....
gi 535035218  239 AGAIGAAVI 247
Cdd:TIGR00241 240 VGAVGAALL 248
 
Name Accession Description Interval E-value
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 3-247 1.12e-131

CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.


Pssm-ID: 129344  Cd Length: 248  Bit Score: 371.82  E-value: 1.12e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218    3 YSIGIDSGSTATKGILLADG-VITRRFLVPTPFRPAT--AITEAWETLREGLETTPFLTLTGYGRQLVDFADKQVTEISC 79
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGkVIGYKWLDTTPVIEETarAILEALKEAGIGLEPIDKIVATGYGRHKVGFADKIVTEISC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   80 HGLGARFLEPATRAVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITEN-VIPHAITS 158
Cdd:TIGR00241  81 HGKGANYLAPEARGVIDIGGQDSKVIKIDD-GKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKaDRKAKISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQF 238
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQI 239


                  ....*....
gi 535035218  239 AGAIGAAVI 247
Cdd:TIGR00241 240 VGAVGAALL 248
ASKHA_NBD_YjiL-like cd24109
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ...
 4-247 1.86e-118

nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YjiL, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.


Pssm-ID: 466959 [Multi-domain]  Cd Length: 243  Bit Score: 338.01  E-value: 1.86e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   4 SIGIDSGSTATKGILLADGVITRRFLVPTPFRPATAITEAWETLREGLETTP-FLTLTGYGRQLVDFADKQVTEISCHGL 82
Cdd:cd24109    1 YIGIDIGSRATKIALFEDDKILEKFVIPTGWFYKEYGRRIIKELLEDINYEDdKIVATGYGRNNLDFADKTITEITAHAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  83 GARFLEPATRAVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITENVIPHAITSMCTV 162
Cdd:cd24109   81 GARYLTGKDFTVIDIGGQDTKVIKVEN-GKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAEDPEPLSISSTCAV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 163 FAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEaPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQFAGAI 242
Cdd:cd24109  160 FAESEVISLIAEGVSRERIAAGVNYSIAKRVAPLLNRLKSP-PIVLTGGVARNKAIIELLEKRLGAEVIVPELPQFAGAI 238


                 ....*
gi 535035218 243 GAAVI 247
Cdd:cd24109  239 GAALI 243
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 1-254 1.99e-107

Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];


Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 310.88  E-value: 1.99e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   1 MTYSIGIDSGSTATKGILL-ADGVITRRFLVPTPFRPATAITEAWETLREGLETTP----FLTLTGYGRQLVD--FADKQ 73
Cdd:COG1924    2 GMIYLGIDIGSTTTKAVLLdEDGEILASAYLPTGGDPLEAAKEALKELLEEAGLKRediaGVVATGYGRVLIGaaFADKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  74 VTEISCHGLGARFLEPATRAVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSI---TEN 150
Cdd:COG1924   82 VTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLED-GVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELalkAKN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 151 viPHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPV 230
Cdd:COG1924  161 --PVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEV 238

                        250       260
                 ....*....|....*....|....
gi 535035218 231 QTHPDAQFAGAIGAAVIGQRQRKR 254
Cdd:COG1924  239 IVPPIPQLMGALGAALLAREKVKK 262
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 5-248 3.10e-76

BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.


Pssm-ID: 396441 [Multi-domain]  Cd Length: 271  Bit Score: 232.24  E-value: 3.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218    5 IGIDSGSTATKGILLADG--VITRRFLVPTPFRPA----------TAITEAWETLREGLET--TPFLTLTGYGRQLVD-- 68
Cdd:pfam01869   1 LGIDGGSTKTKAVLMDDDgeVLGRAIAGSANFESVgveaaernlkDAITEALEEAGLKLDDieYMFLGLTGYGRAGVDgh 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   69 FADKQVT-EISCHGLGARFLEPATR---AVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQL 144
Cdd:pfam01869  81 FGKDIVReEITVHADGAVALAPGTRgedGVIDIGGTGSKVIGLDG-GKVVRFGGNGQCAGGEGSFLEIAARALGAVVREL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  145 DSITENVI--PHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAP-ILFTGGVSHCQRFTHM 221
Cdd:pfam01869 160 DGLAPKTTlnKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFVPDeVVLTGGVAKNAGLVKA 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 535035218  222 L-----ESHLGMPVQTHPDAQFAGAIGAAVIG 248
Cdd:pfam01869 240 LrdylkENILGVKVNVHPDPQYAGAIGAALLA 271
 
Name Accession Description Interval E-value
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 3-247 1.12e-131

CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.


Pssm-ID: 129344  Cd Length: 248  Bit Score: 371.82  E-value: 1.12e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218    3 YSIGIDSGSTATKGILLADG-VITRRFLVPTPFRPAT--AITEAWETLREGLETTPFLTLTGYGRQLVDFADKQVTEISC 79
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGkVIGYKWLDTTPVIEETarAILEALKEAGIGLEPIDKIVATGYGRHKVGFADKIVTEISC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   80 HGLGARFLEPATRAVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITEN-VIPHAITS 158
Cdd:TIGR00241  81 HGKGANYLAPEARGVIDIGGQDSKVIKIDD-GKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKaDRKAKISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQF 238
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQI 239


                  ....*....
gi 535035218  239 AGAIGAAVI 247
Cdd:TIGR00241 240 VGAVGAALL 248
ASKHA_NBD_YjiL-like cd24109
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ...
 4-247 1.86e-118

nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YjiL, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.


Pssm-ID: 466959 [Multi-domain]  Cd Length: 243  Bit Score: 338.01  E-value: 1.86e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   4 SIGIDSGSTATKGILLADGVITRRFLVPTPFRPATAITEAWETLREGLETTP-FLTLTGYGRQLVDFADKQVTEISCHGL 82
Cdd:cd24109    1 YIGIDIGSRATKIALFEDDKILEKFVIPTGWFYKEYGRRIIKELLEDINYEDdKIVATGYGRNNLDFADKTITEITAHAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  83 GARFLEPATRAVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITENVIPHAITSMCTV 162
Cdd:cd24109   81 GARYLTGKDFTVIDIGGQDTKVIKVEN-GKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAEDPEPLSISSTCAV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 163 FAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEaPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQFAGAI 242
Cdd:cd24109  160 FAESEVISLIAEGVSRERIAAGVNYSIAKRVAPLLNRLKSP-PIVLTGGVARNKAIIELLEKRLGAEVIVPELPQFAGAI 238


                 ....*
gi 535035218 243 GAAVI 247
Cdd:cd24109  239 GAALI 243
ASKHA_NBD_BcrAD_BadFG_HgdC_HadI cd24036
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ...
 4-247 1.14e-112

nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.


Pssm-ID: 466886 [Multi-domain]  Cd Length: 250  Bit Score: 323.72  E-value: 1.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   4 SIGIDSGSTATKGILLAD-GVITRRFLVPTPFRP----ATAITEAWETLREGLETTPFLTLTGYGRQLVDFADKQVTEIS 78
Cdd:cd24036    1 FAGIDVGSTTTKAVILDDkGKILGKAVIRTGTDPektaERALEEALEEAGLSREDIEYIVATGYGRNSVPFADKTITEIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  79 CHGLGARFLEPATRAVIDIGGQDSKVIQLDDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITENVIPHA-IT 157
Cdd:cd24036   81 CHARGAHFLFPEARTVIDIGGQDSKVIRLDEDGKVLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELALKSTNPVeIS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 158 SMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQ 237
Cdd:cd24036  161 STCTVFAESEVISLIAEGVPKEDIIAGIHNSIAKRVAALAKRVGVEDPVVLTGGVAKNPGVVKALEEKLGVEVIVPPNPQ 240

                        250
                 ....*....|
gi 535035218 238 FAGAIGAAVI 247
Cdd:cd24036  241 LVGALGAALL 250
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 1-254 1.99e-107

Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];


Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 310.88  E-value: 1.99e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   1 MTYSIGIDSGSTATKGILL-ADGVITRRFLVPTPFRPATAITEAWETLREGLETTP----FLTLTGYGRQLVD--FADKQ 73
Cdd:COG1924    2 GMIYLGIDIGSTTTKAVLLdEDGEILASAYLPTGGDPLEAAKEALKELLEEAGLKRediaGVVATGYGRVLIGaaFADKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  74 VTEISCHGLGARFLEPATRAVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSI---TEN 150
Cdd:COG1924   82 VTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLED-GVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELalkAKN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 151 viPHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPV 230
Cdd:COG1924  161 --PVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEV 238

                        250       260
                 ....*....|....*....|....
gi 535035218 231 QTHPDAQFAGAIGAAVIGQRQRKR 254
Cdd:COG1924  239 IVPPIPQLMGALGAALLAREKVKK 262
ASKHA_NBD_HgdC_HadI-like cd24103
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ...
 4-246 7.48e-82

nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily includes a group of proteins such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). HgdC (EC 3.6.1.-), also called (R)-2-hydroxyglutaryl-CoA dehydratase activase, (R)-2-hydroxyglutaryl-CoA dehydratase (component A), ATP-coupled electron transfer protein HgdC, or activator of (R)-2-hydroxyglutaryl-CoA dehydratase, is involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity. Its role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transfer. The dehydratase requires only catalytic amounts of ATP and substoichiometric amounts of HgdC (CompA) to be functional. HadI is involved in the reductive branch of L-leucine fermentation. It is required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. FldI (EC 3.6.1.-), also called initiator of phenyllactate dehydratase, is involved in the fermentation of L-phenylalanine via a Stickland reaction. It is required for the activation of the (R)-phenyllactate dehydratase complex FldABC. Only in the oxidized state, FldI exhibits significant ATPase activity, which appears to be essential for unidirectional electron transfer. LcdC, also called lactoyl-CoA dehydratase component E I, is required for the activation of lactoyl-CoA dehydratase. HadI, FldI and LcdC are extremely sensitive towards oxygen.


Pssm-ID: 466953  Cd Length: 255  Bit Score: 245.78  E-value: 7.48e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   4 SIGIDSGSTATKGILLADG-VITRRFLVPT---PFRPATAITEAWETLREGLETTPFLTLTGYGRQLVDFADKQVTEISC 79
Cdd:cd24103    1 TMGIDIGSTASKCVILKDGkEIVAQSVISVgtgTSGPARALEEVLEKAGLAKEDIAYTVATGYGRNSFEGADKQISELSC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  80 HGLGARFLEPATRAVIDIGGQDSKVIQLDDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITENVI-PHAITS 158
Cdd:cd24103   81 HARGVNFLLPEVRTIIDIGGQDVKVLKLDDNGRLLNFVMNDKCAAGTGRFLDVMARVLEVKVSELGELDAQSTnPVSISS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQF 238
Cdd:cd24103  161 TCTVFAESEVISQLSEGAKIPDIIAGIHTSVASRVAGLAKRVGIEKDVVMTGGVAQNSGVVRAMEEELGTEIIVSPNPQL 240


                 ....*...
gi 535035218 239 AGAIGAAV 246
Cdd:cd24103  241 TGALGAAL 248
ASKHA_NBD_benz_CoA_BzdP cd24107
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ...
 5-247 1.87e-77

nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar proteins; bzd-type benzoyl-CoA reductase BzdP is encoded by the gene bzdP from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdP may function the same as the D subunit of benzoyl-CoA reductase BcrD from Thauera aromatica and benzoyl-CoA reductase BadG from Rhodopseudomonas palustris.


Pssm-ID: 466957 [Multi-domain]  Cd Length: 250  Bit Score: 234.36  E-value: 1.87e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   5 IGIDSGSTATKGILLADGVITRRFLVPTPFRPATAITEAWETLREGLETTPF----LTLTGYGRQLVDFADKQVTEISCH 80
Cdd:cd24107    2 AGIDVGSKFTKAVILEDGEILAKAIVPTGFDVAKAAERALDEALAAAGISRDdvkkIVATGAGRKLVSFADDTVTEVVCA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  81 GLGARFLEPATRAVIDIGGQDSKVIQLDDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITENV-IPHAITSM 159
Cdd:cd24107   82 AKGAYFLFPSARTVIDVGAEEGRAIKLDENGKVVDFAQNDKCAAGAGAFLEAMSRALEVPLEELGELSLKStKKIPMNAQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 160 CTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQFA 239
Cdd:cd24107  162 CAVFAESEVVSLIHAGTPKEDIAAAVHDAIASRIASMVRRVGIEDDVALIGGVAKNPGFVESLKELLGKEVLVPEDPEYV 241


                 ....*...
gi 535035218 240 GAIGAAVI 247
Cdd:cd24107  242 GALGAALI 249
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 5-248 3.10e-76

BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.


Pssm-ID: 396441 [Multi-domain]  Cd Length: 271  Bit Score: 232.24  E-value: 3.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218    5 IGIDSGSTATKGILLADG--VITRRFLVPTPFRPA----------TAITEAWETLREGLET--TPFLTLTGYGRQLVD-- 68
Cdd:pfam01869   1 LGIDGGSTKTKAVLMDDDgeVLGRAIAGSANFESVgveaaernlkDAITEALEEAGLKLDDieYMFLGLTGYGRAGVDgh 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   69 FADKQVT-EISCHGLGARFLEPATR---AVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQL 144
Cdd:pfam01869  81 FGKDIVReEITVHADGAVALAPGTRgedGVIDIGGTGSKVIGLDG-GKVVRFGGNGQCAGGEGSFLEIAARALGAVVREL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  145 DSITENVI--PHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAP-ILFTGGVSHCQRFTHM 221
Cdd:pfam01869 160 DGLAPKTTlnKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFVPDeVVLTGGVAKNAGLVKA 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 535035218  222 L-----ESHLGMPVQTHPDAQFAGAIGAAVIG 248
Cdd:pfam01869 240 LrdylkENILGVKVNVHPDPQYAGAIGAALLA 271
ASKHA_NBD_benz_CoA_BcrA_BadF cd24104
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ...
 5-250 2.11e-73

nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar proteins; Benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit A of benzoyl-CoA reductase.


Pssm-ID: 466954  Cd Length: 253  Bit Score: 224.10  E-value: 2.11e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   5 IGIDSGSTATKGILL-ADGVITRRFLVPTPFR----PATAITEAWETLREGLETTPFLTLTGYGRQLVDFADKQVTEISC 79
Cdd:cd24104    2 AGVDVGSTQTKAVIIdEDGEIVGRGLTNTGANvvvaAERAFREAIEEAGIKEEEVEYVVGTGYGRYKVTFGNAQRTEISC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  80 HGLGARFLEPATRAVIDIGGQDSKVIQLDDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSIT-ENVIPHAITS 158
Cdd:cd24104   82 HARGAHHMFPNTRTVLDIGGQDTKAIRVDETGEVVDFVMNDKCAAGTGRFLGYAADALGIPLDELGPLAlKSTKPVRISS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPVQTHPDAQF 238
Cdd:cd24104  162 TCTVFAESEIRSWLALGKKREDILGGVHRAIAARAVSLIRRVGIEPEFTFTGGVARNEAMVKALEELLGVKINVSPDSHF 241

                        250
                 ....*....|..
gi 535035218 239 AGAIGAAVIGQR 250
Cdd:cd24104  242 MGALGAALFALE 253
ASKHA_NBD_benz_CoA_BcrD_BadG cd24105
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ...
 5-251 1.22e-70

nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar proteins; benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit D of benzoyl-CoA reductase.


Pssm-ID: 466955  Cd Length: 256  Bit Score: 217.45  E-value: 1.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   5 IGIDSGSTATKGILLADG--VITRRFLvPTPFRPATAITEAW-ETLRE-GL--ETTPFLTLTGYGRQLVDFADKQVTEIS 78
Cdd:cd24105    2 AGIDVGSGYTKAVIMDDGekILAKRVE-RTRQRDEEVAREAYnEALEEaGLkrDDIAYVATTGEGRYVVFFRDGHFTDLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  79 CHGLGARFLEPATRAVIDIGGQDSKVIQLDDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITENV-IPHAIT 157
Cdd:cd24105   81 THARGAIFLFPGTRTVLDIGAQHTRAIRIDEKGKVLSFRMNDKCAAGSGQFLENIARYLGVALDEIGDLSLQAdNPEPIS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 158 SMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGMPVQT--HPD 235
Cdd:cd24105  161 GVCAVLAETEVINMVSRGIPVPDILRGIHLSLAGRSVQLLKRVGAEPEVTLTGGLARNEGMVEALEELLGAKVNVaeHDD 240

                        250
                 ....*....|....*.
gi 535035218 236 AQFAGAIGAAVIGQRQ 251
Cdd:cd24105  241 SIYAGALGAALLGAFR 256
ASKHA_NBD_benz_CoA_BzdQ cd24106
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ...
 6-248 8.90e-67

nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and similar proteins; bzd-type benzoyl-CoA reductase BzdQ is encoded by the gene bzdQ from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdQ may function the same as the A subunit of benzoyl-CoA reductase BcrA from Thauera aromatica and benzoyl-CoA reductase BadF from Rhodopseudomonas palustris.


Pssm-ID: 466956  Cd Length: 253  Bit Score: 207.46  E-value: 8.90e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   6 GIDSGSTATKGILLADGVITRRFLVPT-PFRPATAiteaWETLREGLETTPfLTL--------TGYGRQLVDFADKQVTE 76
Cdd:cd24106    3 GIDVGSVSSQAVIMVDGELYAYSNMRTgSDSPESA----QKALNAALEKTG-LKLedihyivgTGYGRVNVPFANKAITE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  77 ISCHGLGARFLEPAT-RAVIDIGGQDSKVIQLDDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQ-----LDSITEn 150
Cdd:cd24106   78 IACHARGANYMYGPSvRTVLDMGGQDCKAIRCDEKGKVTNFLMNDKCAAGTGRGMEVFADLLQVPIEEigelsLEVDKE- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 151 viPHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARLSCEAPILFTGGVSHCQRFTHMLESHLGM-P 229
Cdd:cd24106  157 --PPPVSSTCVVFAKSEALGLLREGWPKNDVLAAYCEAMAHRVVTLLERVGVEKDFVITGGIAKNIGVVKRIEKELGIkA 234

                        250
                 ....*....|....*....
gi 535035218 230 VQTHPDAQFAGAIGAAVIG 248
Cdd:cd24106  235 LIPKEDPQIAGALGAALFA 253
ASKHA_NBD_BcrAD_BadFG-like cd24002
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ...
 5-247 1.26e-61

nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ATPase family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL, Methanocaldococcus jannaschii protein MJ0800, and Aquifex aeolicus hypothetical protein O66634, are also includes in this family. The members of the O66634-like group contain two copies of the BcrAD/BadFG-like region suggesting that they may structurally dimerize. The BcrAD/BadFG-like ATPase family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466852 [Multi-domain]  Cd Length: 255  Bit Score: 194.19  E-value: 1.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   5 IGIDSGSTATKGILLADG--VITRRFLV--PTPFRPATAITEAWETLREGLETTPFLTL----TGYGRQLVDF-ADKQVT 75
Cdd:cd24002    2 LGLDIGSTTSKAVLLDEGknIVATEYERsgTGTSGPIEAVKKTLEKFLLEKGVKEEDIActgvTGYGRVELFIdGDKQIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  76 EISCHGLGARFLEPATRAVIDIGGQDSKVIQLDDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITENVIP-H 154
Cdd:cd24002   82 EVSAHARGANHIYPDARTIIDVGGQDAKVIILDENGQMKNFKMNDKCAAGTGAFLDSMANKLNVKVEELADVKMNSKKeV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 155 AITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARL-SCEAPILFTGGVSHCQRFTHMLESHLGMPVQTH 233
Cdd:cd24002  162 SVSSTCAVFAETDINSFQSRGAPKEDIIAGLHKAVALRVMSLVGRLgVPKKDVVLQGGVARNSAVVRALEEIINNEIIVP 241

                        250
                 ....*....|....
gi 535035218 234 PDAQFAGAIGAAVI 247
Cdd:cd24002  242 EIAQVMGALGAALL 255
ASKHA_NBD_O66634-like_rpt1 cd24034
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ...
 4-251 8.07e-59

nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.


Pssm-ID: 466884 [Multi-domain]  Cd Length: 258  Bit Score: 187.03  E-value: 8.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   4 SIGIDSGSTATKGILL-ADGVITRRFLVPTPFRPATAITEAWETLREGLETTPF-LTLTG-YGRQLVDFAD-KQVTEISC 79
Cdd:cd24034    1 YLGIDIGSTTVKAVVLdEKGNIVFSDYERHFGNPREALLELLEEIKERLGDEIArIAVTGsGGRGLAELLGlPFVQEVVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  80 HGLGARFLEPATRAVIDIGGQDSKVIQLDDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSIT-ENVIPHAITS 158
Cdd:cd24034   81 IEAAVKHLHPDARTVIEIGGEDFKLIELDGDGKLKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELAlKAEPPAPIAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARrsaNFIARLSC----EAPILFTGGVSH-CQRFTHMLESHLGM-PVQT 232
Cdd:cd24034  161 RCSVFAKSDMIHLQNKGVPKEDIAAGLCRAVAR---NVIATLAKgreiEGPVILVGGVATnNAVLREAFEELLGDeELIV 237

                        250
                 ....*....|....*....
gi 535035218 233 HPDAQFAGAIGAAVIGQRQ 251
Cdd:cd24034  238 PEHAEYFEALGAALYALEE 256
ASKHA_NBD_O66634-like_rpt2 cd24035
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ...
 5-253 3.97e-53

nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the second copy of the BcrAD/BadFG-like domain.


Pssm-ID: 466885  Cd Length: 258  Bit Score: 172.72  E-value: 3.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   5 IGIDSGSTATKGILL-ADGVITRRFLVPTPFRPATAITEAWETLREGLETTPFLT---LTGYGRQLV-DF--ADKQVTEI 77
Cdd:cd24035    2 LGIDVGSTTTKAVLIdEDGEILASVYLRTKGNPIEAVKKGLKELREQLPEKVVIVgvgTTGSGRELLkDAlgADVVKVEI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  78 SCHGLGARFLEPATRAVIDIGGQDSKVIQLdDDGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSIT-ENVIPHAI 156
Cdd:cd24035   82 TAHATAALHFDPDVDTIFEIGGQDSKYISL-KNGVVKDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELAlKAKNPPDL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 157 TSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIARL-SCEAPILFTGGVSHCQRFTHMLESHLGMPVQTHPD 235
Cdd:cd24035  161 GSRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVVGGrNLGKKIVFQGGTFLNKAVLAAFEQVTGKEIIVPPH 240

                        250
                 ....*....|....*...
gi 535035218 236 AQFAGAIGAAVIGQRQRK 253
Cdd:cd24035  241 PGLMGAYGAALLAKEEIK 258
ASKHA_NBD_MJ0800-like cd24108
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ...
 4-247 6.06e-28

nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ0800, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.


Pssm-ID: 466958  Cd Length: 259  Bit Score: 107.15  E-value: 6.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218   4 SIGIDSGSTATKGILLADGVITRRFLVPTpfrpATAITEAWETLREGLETTPF-------LTLTGYGRQLVD---FADKQ 73
Cdd:cd24108    1 TAGIDSGSTTTKAVVMKDNEIIGTGWMPT----TDVIESAEKAFEEALEEAGIklsdieaIGTTGYGRYTIGkhfNADLV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218  74 VTEISCHGLGARFL---EPATRAVIDIGGQDSKVIQLDDdGNLCDFLMNDKCAAGTGRFLEVISRTLGTSVEQLDSITEN 150
Cdd:cd24108   77 QEELTVNSKGAVYLadkQKGEATVIDIGGMDNKAITVND-GIPDNFTMGGICAGASGRFLEMTARRLGVDITELGELALK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035218 151 VIPHAIT--SMCTVFAESEVISLRSAGVAPEAILAGVINAMARRS-ANFIARLSCEAPILFTGGVSHCQRFTHMLESHLG 227
Cdd:cd24108  156 GDWRKIRmnSYCIVFGIQDLVTSLAEGARAEDVAAAACHSVAEQVyEQQLQEIDVREPVIQVGGTSLIEGLVKALGEVLG 235

                        250       260
                 ....*....|....*....|
gi 535035218 228 MPVQTHPDAQFAGAIGAAVI 247
Cdd:cd24108  236 IEVIVPPYSQLIGAVGAALL 255
ASKHA_NBD_BK cd24011
nucleotide-binding domain (NBD) of the butyrate kinase (BK) domain family; Butyrate kinase (EC ...
 167-227 6.80e-03

nucleotide-binding domain (NBD) of the butyrate kinase (BK) domain family; Butyrate kinase (EC 2.7.2.7) catalyzes the formation of butyryl-CoA by phosphorylating butyrate in the presence of ATP to form butyryl phosphate. Butyrate kinases exist in many fermentative species of the bacterial and archaeal families. They belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466861  Cd Length: 345  Bit Score: 37.13  E-value: 6.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535035218 167 EVISLRSAGvAPEAILagVINAMARRSANFIARLSCEAP-----ILFTGGVSHCQRFTHMLESHLG 227
Cdd:cd24011  256 EVEKRIEAG-DEKAKL--VLDAMAYQIAKEIGALAAVLKgkvdaIILTGGLAYSKRLVDRIKERVG 318
 
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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