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Conserved domains on  [gi|535035219|gb|EQR82348|]
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2-hydroxyglutaryl-CoA dehydratase [Escherichia coli HVH 137 (4-2124971)]

Protein Classification

2-hydroxyacyl-CoA dehydratase subunit D( domain architecture ID 11448412)

2-hydroxyacyl-CoA dehydratase similar to Escherichia coli YjiM, a putative 2-hydroxyglutaryl-CoA dehydratase encoded in the yjiL-mdtM gene cluster which encodes a bacterial transporter system implicated in the uptake of proline-rich antimicrobial peptides in cells lacking the ABC transporter SbmA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
double_cubane NF040772
double-cubane-cluster-containing anaerobic reductase; This subfamily of double-cubane proteins ...
14-383 0e+00

double-cubane-cluster-containing anaerobic reductase; This subfamily of double-cubane proteins occurs strictly in anaerobes (facultative or obligate), such as Escherichia coli and Clostridium difficile. The enzyme always co-occurs with an accessory protein, an ATP-dependent activase. The cofactor contains a pair of 4Fe-4S cubane clusters, bridged by a sulfur atom, for an overall 8Fe-9S cofactor structure. However, we observe that that this family essentially always co-occurs in bacteria with SelD, the selenium donor protein required for biosynthesis of selenoproteins, selenouridine-modified tRNAs, selenium-dependent molybdenum hydroxylases, and selenoneine.


:

Pssm-ID: 468731  Cd Length: 372  Bit Score: 655.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  14 FSEARQTGFLTVMDLKERGIPLVGTYCTFMPQEIPMAAGAVVVSLCSTSDETIEEAEKDLPRNLCPLIKSSYGFGKTDKC 93
Cdd:NF040772   1 FDEARKEGFLAEKEEKEEGKKVVGTFCTYVPEELILAAGAIPVGLCGGSQEPIPAAEKVLPRNLCPLIKSSYGFALTDTC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  94 PYFYFSDLVVGETTCDGKKKMYEYMAEFKPVHVMQLPNSVKDDASRALWKAEMLRLQKTVEERFGHEISEDALRDAIALK 173
Cdd:NF040772  81 PYFYFSDLVVGETTCDGKKKMYELLAELKPVHVMELPQMKDEEAALALWREEVRRLKERLEELFGVKITDEKLREAIKLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 174 NRERRALANFYHLGQLNPPALSGSDILKVVYGATFRFDKEALINELDAMTARVRQQWEEGQRLDP--RPRILITGCPIGG 251
Cdd:NF040772 161 NRERKALKRLYELRKLDPPPISGLEDLLLLFQIAFYFDPERFTELLEELCDELEERYEAGGGVAPkgAPRILITGCPMGG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 252 AAEKVVRAIEENGGWVVGYENCTGAKATEQCVAET-GDVYDALADKYLAIGCSCVSPNDQRLQMLSQMVEEYQVDGVVDV 330
Cdd:NF040772 241 PNEKVIRLIEESGGVVVAEENCTGTRYFEDLVDEDlEDPLDALAERYLKIPCSCMTPNTGRLELLLRLIDEYKVDGVVDV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 535035219 331 ILQACHTYAVESLAIKRHVrQQHNIPYIAIETDYSTSDVGQLSTRVAAFIEML 383
Cdd:NF040772 321 TLQACHTYNVESYKVKKFL-KEKGIPYLHIETDYSESDVGQLKTRIEAFLEML 372
 
Name Accession Description Interval E-value
double_cubane NF040772
double-cubane-cluster-containing anaerobic reductase; This subfamily of double-cubane proteins ...
14-383 0e+00

double-cubane-cluster-containing anaerobic reductase; This subfamily of double-cubane proteins occurs strictly in anaerobes (facultative or obligate), such as Escherichia coli and Clostridium difficile. The enzyme always co-occurs with an accessory protein, an ATP-dependent activase. The cofactor contains a pair of 4Fe-4S cubane clusters, bridged by a sulfur atom, for an overall 8Fe-9S cofactor structure. However, we observe that that this family essentially always co-occurs in bacteria with SelD, the selenium donor protein required for biosynthesis of selenoproteins, selenouridine-modified tRNAs, selenium-dependent molybdenum hydroxylases, and selenoneine.


Pssm-ID: 468731  Cd Length: 372  Bit Score: 655.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  14 FSEARQTGFLTVMDLKERGIPLVGTYCTFMPQEIPMAAGAVVVSLCSTSDETIEEAEKDLPRNLCPLIKSSYGFGKTDKC 93
Cdd:NF040772   1 FDEARKEGFLAEKEEKEEGKKVVGTFCTYVPEELILAAGAIPVGLCGGSQEPIPAAEKVLPRNLCPLIKSSYGFALTDTC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  94 PYFYFSDLVVGETTCDGKKKMYEYMAEFKPVHVMQLPNSVKDDASRALWKAEMLRLQKTVEERFGHEISEDALRDAIALK 173
Cdd:NF040772  81 PYFYFSDLVVGETTCDGKKKMYELLAELKPVHVMELPQMKDEEAALALWREEVRRLKERLEELFGVKITDEKLREAIKLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 174 NRERRALANFYHLGQLNPPALSGSDILKVVYGATFRFDKEALINELDAMTARVRQQWEEGQRLDP--RPRILITGCPIGG 251
Cdd:NF040772 161 NRERKALKRLYELRKLDPPPISGLEDLLLLFQIAFYFDPERFTELLEELCDELEERYEAGGGVAPkgAPRILITGCPMGG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 252 AAEKVVRAIEENGGWVVGYENCTGAKATEQCVAET-GDVYDALADKYLAIGCSCVSPNDQRLQMLSQMVEEYQVDGVVDV 330
Cdd:NF040772 241 PNEKVIRLIEESGGVVVAEENCTGTRYFEDLVDEDlEDPLDALAERYLKIPCSCMTPNTGRLELLLRLIDEYKVDGVVDV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 535035219 331 ILQACHTYAVESLAIKRHVrQQHNIPYIAIETDYSTSDVGQLSTRVAAFIEML 383
Cdd:NF040772 321 TLQACHTYNVESYKVKKFL-KEKGIPYLHIETDYSESDVGQLKTRIEAFLEML 372
HgdB COG1775
Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB [Amino acid ...
1-383 3.07e-164

Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441381  Cd Length: 384  Bit Score: 465.15  E-value: 3.07e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219   1 MSLVTDLPAIFDQFSEARQTGFLTVMDLKERGIPLVGTYCTFMPQEIPMAAGAVVVSLCSTSDETIEEAEKDLPRNLCPL 80
Cdd:COG1775    1 MSDEKKIMKYFKVLKELAAKYYEELKEAKEEGKKVVGWFCSYVPEELIHAAGAVPVGLEGGSDEPIEAAEKGLPRNLCSY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  81 IKSSYGFGKTDKCPYfyfSDLVVGETTCDGKKKMYEYMAEFKPVHVMQLPNSVKDDASRALWKAEMLRLQKTVEERFGHE 160
Cdd:COG1775   81 IKSSLGFALTGKLPF---PDLVVGETTCDGKKKMYELLARDVPVYVMDLPQNKDDEEAVDYWKEELKELIEFLEELTGRK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 161 ISEDALRDAIALKNRERRALANFYHLGQLNPPALSGSDILKVVYGATFrFDKEALINELDAMTARVRQQWEEGQRLDP-- 238
Cdd:COG1775  158 IDEEKLREAIKLYNEARKLLRELYELRKAKPPPISGFDLLLVMAAAFF-MDKEEATELLEELLDELEERIAEGIGAVPee 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 239 RPRILITGCPIGGAAEKVVRAIEENGGWVVGYENCTGAKATEQCVAETGDVYDALADKYL-AIGCSCVSPNDQRLQMLSQ 317
Cdd:COG1775  237 KPRILWTGIPPWPPNRKLLKLIEEAGAVVVADDYCTGSRYFETDVDEPEDPLEALARRYLsNIPCSCNTPNERRLELLLK 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535035219 318 MVEEYQVDGVVDVILQACHTYAVESLAIKRHVrQQHNIPYIAIETDYSTSDVGQLSTRVAAFIEML 383
Cdd:COG1775  317 LAKEYKADGVIYHSLKFCKPYSVEYPLLKKAL-EEAGIPVLSLETDYSDSDEGQLRTRIEAFLEML 381
HGD-D pfam06050
2-hydroxyglutaryl-CoA dehydratase, D-component; Degradation of glutamate via the ...
41-382 1.34e-146

2-hydroxyglutaryl-CoA dehydratase, D-component; Degradation of glutamate via the hydroxyglutarate pathway involves the syn-elimination of water from 2-hydroxyglutaryl-CoA. This anaerobic process is catalyzed by 2-hydroxyglutaryl-CoA dehydratase, an enzyme with two components (A and D) that reversibly associate during reaction cycles. This component contains one non-reducible [4Fe-4S]2+ cluster and a reduced riboflavin 5'-monophosphate.


Pssm-ID: 461814  Cd Length: 339  Bit Score: 418.62  E-value: 1.34e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219   41 TFMPQEIPMAAGAVVVSLCSTSDETIEEAEKDLPRNLCPLIKSSYGFGKTDKcPYFYFSDLVVGETTCDGKKKMYEYMAE 120
Cdd:pfam06050   1 SYVPEELIYAAGAVPVGLCGGSQESIELAEKYLPRNLCSLIKSSLGFALTGK-PYFDPLDLVVGETTCDGKKKMYENLAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  121 FKPVHVMQLPNsVKDDASRALWKAEMLRLQKTVEERFGHEISEDALRDAIALKNRERRALANFYHLGQLNPPALSGSDIL 200
Cdd:pfam06050  80 LVPVFVLDLPQ-NKDEAALDYWRDELRRLIEFLEELTGVKITDEKLREAIKLYNETRRLLRELYELRKADPSPISGFDLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  201 kVVYGATFRFDKEALINELDAMTARVRQQWEEGQRLDPRPRILITGCPIGGAAEKVVRAIEENGGWVVGYENCTGAKATE 280
Cdd:pfam06050 159 -LLLQASFFLGKEEATELLEELLDELEERPADGEGPEERPRILLTGIPPWPPNEKLLKLIEESGAVVVADELCTGSRYFR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  281 QCV-AETGDVYDALADKYLAIGCSCVSPNDQRLQMLSQMVEEYQVDGVVDVILQACHTYAVESLAIKRHVrQQHNIPYIA 359
Cdd:pfam06050 238 DDVdEEDPDPLEALAERYLKIPCPCMTPNERRLELLLDLAKEYKADGVIYHTLKFCKPYSFESPLIRKAL-EEAGIPVLS 316
                         330       340
                  ....*....|....*....|...
gi 535035219  360 IETDYSTSDVGQLSTRVAAFIEM 382
Cdd:pfam06050 317 IETDYSDSDEGQLKTRVEAFLEM 339
 
Name Accession Description Interval E-value
double_cubane NF040772
double-cubane-cluster-containing anaerobic reductase; This subfamily of double-cubane proteins ...
14-383 0e+00

double-cubane-cluster-containing anaerobic reductase; This subfamily of double-cubane proteins occurs strictly in anaerobes (facultative or obligate), such as Escherichia coli and Clostridium difficile. The enzyme always co-occurs with an accessory protein, an ATP-dependent activase. The cofactor contains a pair of 4Fe-4S cubane clusters, bridged by a sulfur atom, for an overall 8Fe-9S cofactor structure. However, we observe that that this family essentially always co-occurs in bacteria with SelD, the selenium donor protein required for biosynthesis of selenoproteins, selenouridine-modified tRNAs, selenium-dependent molybdenum hydroxylases, and selenoneine.


Pssm-ID: 468731  Cd Length: 372  Bit Score: 655.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  14 FSEARQTGFLTVMDLKERGIPLVGTYCTFMPQEIPMAAGAVVVSLCSTSDETIEEAEKDLPRNLCPLIKSSYGFGKTDKC 93
Cdd:NF040772   1 FDEARKEGFLAEKEEKEEGKKVVGTFCTYVPEELILAAGAIPVGLCGGSQEPIPAAEKVLPRNLCPLIKSSYGFALTDTC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  94 PYFYFSDLVVGETTCDGKKKMYEYMAEFKPVHVMQLPNSVKDDASRALWKAEMLRLQKTVEERFGHEISEDALRDAIALK 173
Cdd:NF040772  81 PYFYFSDLVVGETTCDGKKKMYELLAELKPVHVMELPQMKDEEAALALWREEVRRLKERLEELFGVKITDEKLREAIKLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 174 NRERRALANFYHLGQLNPPALSGSDILKVVYGATFRFDKEALINELDAMTARVRQQWEEGQRLDP--RPRILITGCPIGG 251
Cdd:NF040772 161 NRERKALKRLYELRKLDPPPISGLEDLLLLFQIAFYFDPERFTELLEELCDELEERYEAGGGVAPkgAPRILITGCPMGG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 252 AAEKVVRAIEENGGWVVGYENCTGAKATEQCVAET-GDVYDALADKYLAIGCSCVSPNDQRLQMLSQMVEEYQVDGVVDV 330
Cdd:NF040772 241 PNEKVIRLIEESGGVVVAEENCTGTRYFEDLVDEDlEDPLDALAERYLKIPCSCMTPNTGRLELLLRLIDEYKVDGVVDV 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 535035219 331 ILQACHTYAVESLAIKRHVrQQHNIPYIAIETDYSTSDVGQLSTRVAAFIEML 383
Cdd:NF040772 321 TLQACHTYNVESYKVKKFL-KEKGIPYLHIETDYSESDVGQLKTRIEAFLEML 372
HgdB COG1775
Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB [Amino acid ...
1-383 3.07e-164

Benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit, BcrC/BadD/HgdB [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441381  Cd Length: 384  Bit Score: 465.15  E-value: 3.07e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219   1 MSLVTDLPAIFDQFSEARQTGFLTVMDLKERGIPLVGTYCTFMPQEIPMAAGAVVVSLCSTSDETIEEAEKDLPRNLCPL 80
Cdd:COG1775    1 MSDEKKIMKYFKVLKELAAKYYEELKEAKEEGKKVVGWFCSYVPEELIHAAGAVPVGLEGGSDEPIEAAEKGLPRNLCSY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  81 IKSSYGFGKTDKCPYfyfSDLVVGETTCDGKKKMYEYMAEFKPVHVMQLPNSVKDDASRALWKAEMLRLQKTVEERFGHE 160
Cdd:COG1775   81 IKSSLGFALTGKLPF---PDLVVGETTCDGKKKMYELLARDVPVYVMDLPQNKDDEEAVDYWKEELKELIEFLEELTGRK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 161 ISEDALRDAIALKNRERRALANFYHLGQLNPPALSGSDILKVVYGATFrFDKEALINELDAMTARVRQQWEEGQRLDP-- 238
Cdd:COG1775  158 IDEEKLREAIKLYNEARKLLRELYELRKAKPPPISGFDLLLVMAAAFF-MDKEEATELLEELLDELEERIAEGIGAVPee 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219 239 RPRILITGCPIGGAAEKVVRAIEENGGWVVGYENCTGAKATEQCVAETGDVYDALADKYL-AIGCSCVSPNDQRLQMLSQ 317
Cdd:COG1775  237 KPRILWTGIPPWPPNRKLLKLIEEAGAVVVADDYCTGSRYFETDVDEPEDPLEALARRYLsNIPCSCNTPNERRLELLLK 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535035219 318 MVEEYQVDGVVDVILQACHTYAVESLAIKRHVrQQHNIPYIAIETDYSTSDVGQLSTRVAAFIEML 383
Cdd:COG1775  317 LAKEYKADGVIYHSLKFCKPYSVEYPLLKKAL-EEAGIPVLSLETDYSDSDEGQLRTRIEAFLEML 381
HGD-D pfam06050
2-hydroxyglutaryl-CoA dehydratase, D-component; Degradation of glutamate via the ...
41-382 1.34e-146

2-hydroxyglutaryl-CoA dehydratase, D-component; Degradation of glutamate via the hydroxyglutarate pathway involves the syn-elimination of water from 2-hydroxyglutaryl-CoA. This anaerobic process is catalyzed by 2-hydroxyglutaryl-CoA dehydratase, an enzyme with two components (A and D) that reversibly associate during reaction cycles. This component contains one non-reducible [4Fe-4S]2+ cluster and a reduced riboflavin 5'-monophosphate.


Pssm-ID: 461814  Cd Length: 339  Bit Score: 418.62  E-value: 1.34e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219   41 TFMPQEIPMAAGAVVVSLCSTSDETIEEAEKDLPRNLCPLIKSSYGFGKTDKcPYFYFSDLVVGETTCDGKKKMYEYMAE 120
Cdd:pfam06050   1 SYVPEELIYAAGAVPVGLCGGSQESIELAEKYLPRNLCSLIKSSLGFALTGK-PYFDPLDLVVGETTCDGKKKMYENLAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  121 FKPVHVMQLPNsVKDDASRALWKAEMLRLQKTVEERFGHEISEDALRDAIALKNRERRALANFYHLGQLNPPALSGSDIL 200
Cdd:pfam06050  80 LVPVFVLDLPQ-NKDEAALDYWRDELRRLIEFLEELTGVKITDEKLREAIKLYNETRRLLRELYELRKADPSPISGFDLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  201 kVVYGATFRFDKEALINELDAMTARVRQQWEEGQRLDPRPRILITGCPIGGAAEKVVRAIEENGGWVVGYENCTGAKATE 280
Cdd:pfam06050 159 -LLLQASFFLGKEEATELLEELLDELEERPADGEGPEERPRILLTGIPPWPPNEKLLKLIEESGAVVVADELCTGSRYFR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535035219  281 QCV-AETGDVYDALADKYLAIGCSCVSPNDQRLQMLSQMVEEYQVDGVVDVILQACHTYAVESLAIKRHVrQQHNIPYIA 359
Cdd:pfam06050 238 DDVdEEDPDPLEALAERYLKIPCPCMTPNERRLELLLDLAKEYKADGVIYHTLKFCKPYSFESPLIRKAL-EEAGIPVLS 316
                         330       340
                  ....*....|....*....|...
gi 535035219  360 IETDYSTSDVGQLSTRVAAFIEM 382
Cdd:pfam06050 317 IETDYSDSDEGQLKTRVEAFLEM 339
 
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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