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Conserved domains on  [gi|16130958|ref|NP_417534|]
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L(+)-tartrate dehydratase subunit beta [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

L(+)-tartrate dehydratase subunit beta( domain architecture ID 10013023)

L(+)-tartrate dehydratase (L-TTD) catalyzes the conversion from (R,R)-tartrate to oxaloacetate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08228 PRK08228
L(+)-tartrate dehydratase subunit beta; Validated
 1-201 1.25e-145

L(+)-tartrate dehydratase subunit beta; Validated


:

Pssm-ID: 236192  Cd Length: 204  Bit Score: 402.90  E-value: 1.25e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    1 MKKILTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIELKRPIPYDLNGKAIFHAGPIVRKNG--DKWEMVSVGPT 78
Cdd:PRK08228   2 MKKILTTPIKDEDLQDIKVGDVIYLTGTLVTCRDVAHRRLIELGRELPVDLNGGAIFHAGPIVRPKKndDKFEMVSVGPT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   79 TSMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMPESLWVCRVK 158
Cdd:PRK08228  82 TSMRMEKFEKEFIEQTGVKLIVGKGGMGPGTEEGCQEFKALHCVFPAGCAVLAATQVEEIEDAQWRDLGMPETLWVCRVK 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 16130958  159 EFGPLIVSIDTHGNNLIAENKKLFAERRDPIVEEICEHVHYIK 201
Cdd:PRK08228 162 EFGPLIVSIDTHGNNLFEENKKLFNERKEPIVEEICEHVHFIK 204
 
Name Accession Description Interval E-value
PRK08228 PRK08228
L(+)-tartrate dehydratase subunit beta; Validated
 1-201 1.25e-145

L(+)-tartrate dehydratase subunit beta; Validated


Pssm-ID: 236192  Cd Length: 204  Bit Score: 402.90  E-value: 1.25e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    1 MKKILTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIELKRPIPYDLNGKAIFHAGPIVRKNG--DKWEMVSVGPT 78
Cdd:PRK08228   2 MKKILTTPIKDEDLQDIKVGDVIYLTGTLVTCRDVAHRRLIELGRELPVDLNGGAIFHAGPIVRPKKndDKFEMVSVGPT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   79 TSMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMPESLWVCRVK 158
Cdd:PRK08228  82 TSMRMEKFEKEFIEQTGVKLIVGKGGMGPGTEEGCQEFKALHCVFPAGCAVLAATQVEEIEDAQWRDLGMPETLWVCRVK 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 16130958  159 EFGPLIVSIDTHGNNLIAENKKLFAERRDPIVEEICEHVHYIK 201
Cdd:PRK08228 162 EFGPLIVSIDTHGNNLFEENKKLFNERKEPIVEEICEHVHFIK 204
ttdB_fumA_fumB TIGR00723
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S ...
 12-177 4.00e-98

hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase beta chain and the C-terminal region of the class I fumarase (where the N-terminal region is homologous to the tartrate dehydratase alpha chain). The activity of archaeal proteins in this subfamily has not been established.


Pssm-ID: 129806  Cd Length: 168  Bit Score: 281.63  E-value: 4.00e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    12 EDLQDIRVGDVIYLTGTLVTCRDVCHRRLIEL---KRPIPYDLNGKAIFHAGPIVRKNGDkWEMVSVGPTTSMRMESFER 88
Cdd:TIGR00723   1 EQILKLKVGDVVYLTGTIFTARDEAHARLLELideGKELPFDLNGSVIYHAGPIVTKNGE-WEVVSVGPTTSARMNPFEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    89 EFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMPESLWVCRVKEFGPLIVSID 168
Cdd:TIGR00723  80 ELLEKLGVMAIIGKGGMSKEVVEACRKYKAVYLAFPGGCAALLAQSVKKVEGVAWEDLGMPEAIWELEVEDFGPLIVAID 159


                  ....*....
gi 16130958   169 THGNNLIAE 177
Cdd:TIGR00723 160 SHGNSIFQE 168
FumA COG1838
Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy ...
 3-189 1.54e-71

Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy production and conversion]; Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 441443  Cd Length: 190  Bit Score: 214.97  E-value: 1.54e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   3 KILTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIEL---KRPIPYDLNGKAIFHAGPIVRKNGdkWEMVSVGPTT 79
Cdd:COG1838   4 IRLNTPLTEEDVRKLKAGDRVLLSGTIYTARDAAHKRLVELldrGEPLPVDLKGQVIYYVGPAPAKPG--YVIGSAGPTT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958  80 SMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMpESLWVCRVKE 159
Cdd:COG1838  82 STRMDKYTPELLEELGLKGMIGKGGRSPEVIEAMKKHGAVYLAAVGGAAALLAKAIKKVEVVAYEDLGP-EAIWKLEVED 160

                       170       180       190
                ....*....|....*....|....*....|
gi 16130958 160 FgPLIVSIDTHGNNLIAENKKLFAERRDPI 189
Cdd:COG1838 161 F-PLIVAIDSKGNSLYEQGRAKARARLAAL 189
Fumerase_C pfam05683
Fumarase C-terminus; This family consists of the C terminal region of several bacterial ...
 5-174 8.05e-42

Fumarase C-terminus; This family consists of the C terminal region of several bacterial fumarate hydratase proteins (FumA and FumB). Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth.


Pssm-ID: 461714 [Multi-domain]  Cd Length: 204  Bit Score: 139.92  E-value: 8.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958     5 LTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIELKR---PIPY--DLNGKAIFHAGPiVRKNGDkWEMVSVGPTT 79
Cdd:pfam05683  31 LNRPETREELSKWPVGTRLLLSGTLLTGRDAAHKRIKEMLDkgePLPEyvDLNGRPIYYAGP-VDTPGG-EVVGSAGPTT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    80 SMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMpESLWVCRVKE 159
Cdd:pfam05683 109 ATRMDKYVDDFLEKGGSMGMIGKGNRGPAVTEACKKHGGFYLGAIGGAAYLAAKAIKKVEVVAFEELGM-EAIWEFEVED 187

                         170
                  ....*....|....*
gi 16130958   160 FgPLIVSIDTHGNNL 174
Cdd:pfam05683 188 F-PAFVAVDDKGNSF 201
 
Name Accession Description Interval E-value
PRK08228 PRK08228
L(+)-tartrate dehydratase subunit beta; Validated
 1-201 1.25e-145

L(+)-tartrate dehydratase subunit beta; Validated


Pssm-ID: 236192  Cd Length: 204  Bit Score: 402.90  E-value: 1.25e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    1 MKKILTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIELKRPIPYDLNGKAIFHAGPIVRKNG--DKWEMVSVGPT 78
Cdd:PRK08228   2 MKKILTTPIKDEDLQDIKVGDVIYLTGTLVTCRDVAHRRLIELGRELPVDLNGGAIFHAGPIVRPKKndDKFEMVSVGPT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   79 TSMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMPESLWVCRVK 158
Cdd:PRK08228  82 TSMRMEKFEKEFIEQTGVKLIVGKGGMGPGTEEGCQEFKALHCVFPAGCAVLAATQVEEIEDAQWRDLGMPETLWVCRVK 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 16130958  159 EFGPLIVSIDTHGNNLIAENKKLFAERRDPIVEEICEHVHYIK 201
Cdd:PRK08228 162 EFGPLIVSIDTHGNNLFEENKKLFNERKEPIVEEICEHVHFIK 204
ttdB_fumA_fumB TIGR00723
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S ...
 12-177 4.00e-98

hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S cluster-containing hydro-lyases share a conserved motif, including argininosuccinate lyase, adenylosuccinate lyase, aspartase, class I fumarate hydratase (fumarase), and tartrate dehydratase (see PROSITE:PDOC00147). This model represents a subset of closely related proteins or modules, including the E. coli tartrate dehydratase beta chain and the C-terminal region of the class I fumarase (where the N-terminal region is homologous to the tartrate dehydratase alpha chain). The activity of archaeal proteins in this subfamily has not been established.


Pssm-ID: 129806  Cd Length: 168  Bit Score: 281.63  E-value: 4.00e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    12 EDLQDIRVGDVIYLTGTLVTCRDVCHRRLIEL---KRPIPYDLNGKAIFHAGPIVRKNGDkWEMVSVGPTTSMRMESFER 88
Cdd:TIGR00723   1 EQILKLKVGDVVYLTGTIFTARDEAHARLLELideGKELPFDLNGSVIYHAGPIVTKNGE-WEVVSVGPTTSARMNPFEP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    89 EFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMPESLWVCRVKEFGPLIVSID 168
Cdd:TIGR00723  80 ELLEKLGVMAIIGKGGMSKEVVEACRKYKAVYLAFPGGCAALLAQSVKKVEGVAWEDLGMPEAIWELEVEDFGPLIVAID 159


                  ....*....
gi 16130958   169 THGNNLIAE 177
Cdd:TIGR00723 160 SHGNSIFQE 168
FumA COG1838
Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy ...
 3-189 1.54e-71

Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy production and conversion]; Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 441443  Cd Length: 190  Bit Score: 214.97  E-value: 1.54e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   3 KILTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIEL---KRPIPYDLNGKAIFHAGPIVRKNGdkWEMVSVGPTT 79
Cdd:COG1838   4 IRLNTPLTEEDVRKLKAGDRVLLSGTIYTARDAAHKRLVELldrGEPLPVDLKGQVIYYVGPAPAKPG--YVIGSAGPTT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958  80 SMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMpESLWVCRVKE 159
Cdd:COG1838  82 STRMDKYTPELLEELGLKGMIGKGGRSPEVIEAMKKHGAVYLAAVGGAAALLAKAIKKVEVVAYEDLGP-EAIWKLEVED 160

                       170       180       190
                ....*....|....*....|....*....|
gi 16130958 160 FgPLIVSIDTHGNNLIAENKKLFAERRDPI 189
Cdd:COG1838 161 F-PLIVAIDSKGNSLYEQGRAKARARLAAL 189
PRK06043 PRK06043
fumarate hydratase; Provisional
 1-180 2.87e-62

fumarate hydratase; Provisional


Pssm-ID: 180366  Cd Length: 192  Bit Score: 191.51  E-value: 2.87e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    1 MKKILTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIELKRP---IPYDLNGKAIFHAGPIVRKNGDKWEMVSVGP 77
Cdd:PRK06043   1 MEYHLKTPLKKEDIEKLNVGDIVYISGEILTARDEAHARILEMKEKgkeLPFSLEGAVIYHCGPLMKKTDEGWKVVSAGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   78 TTSMRMESFEREFIEQTGVKLVVGKGGMGPLTEEgcQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMPESLWVCRV 157
Cdd:PRK06043  81 TTSARMSKMTPKLLEKVEVRAIIGKGGMKNVADA--LKGKCVYLAYTGGCAALAAESIKRVKAVHWLDLGMPEAVWVLEV 158

                        170       180
                 ....*....|....*....|...
gi 16130958  158 KEFGPLIVSIDTHGNNLIAENKK 180
Cdd:PRK06043 159 EEFGPLIVGIDAKGNDLYSEVRE 181
PRK08395 PRK08395
fumarate hydratase; Provisional
 5-174 3.81e-48

fumarate hydratase; Provisional


Pssm-ID: 169425  Cd Length: 162  Bit Score: 154.58  E-value: 3.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    5 LTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIElkRPIPYDLNGKAIFHAGPIVRKNgdkwEMVSVGPTTSMRME 84
Cdd:PRK08395   3 LKTPLSWEDVLKLKAGDVVYLSGIIYTARDLAHRRFLS--EGFPFNPEGAVIYHCGPLVKNK----KIVSAGPTTSARMN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   85 SFeREFIEQTGVKLVVGKGGMGPlteegcQKFK--ALHVIFPAGCAVLAATQVEEIEEVHWTELGMPESLWVCRVKEFgP 162
Cdd:PRK08395  77 KY-LDFLFSLGVRGIIGKGGMNA------EPFKgrAVYFAFPGGAGSLAAKSIKRVRDVYWEDLGMPDAVWELEVEDF-P 148

                        170
                 ....*....|..
gi 16130958  163 LIVSIDTHGNNL 174
Cdd:PRK08395 149 LLVAIDSKGRSL 160
Fumerase_C pfam05683
Fumarase C-terminus; This family consists of the C terminal region of several bacterial ...
 5-174 8.05e-42

Fumarase C-terminus; This family consists of the C terminal region of several bacterial fumarate hydratase proteins (FumA and FumB). Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth.


Pssm-ID: 461714 [Multi-domain]  Cd Length: 204  Bit Score: 139.92  E-value: 8.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958     5 LTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIELKR---PIPY--DLNGKAIFHAGPiVRKNGDkWEMVSVGPTT 79
Cdd:pfam05683  31 LNRPETREELSKWPVGTRLLLSGTLLTGRDAAHKRIKEMLDkgePLPEyvDLNGRPIYYAGP-VDTPGG-EVVGSAGPTT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    80 SMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGMpESLWVCRVKE 159
Cdd:pfam05683 109 ATRMDKYVDDFLEKGGSMGMIGKGNRGPAVTEACKKHGGFYLGAIGGAAYLAAKAIKKVEVVAFEELGM-EAIWEFEVED 187

                         170
                  ....*....|....*
gi 16130958   160 FgPLIVSIDTHGNNL 174
Cdd:pfam05683 188 F-PAFVAVDDKGNSF 201
PRK06842 PRK06842
Fe-S-containing hydro-lyase;
1-174 4.17e-34

Fe-S-containing hydro-lyase;


Pssm-ID: 180724 [Multi-domain]  Cd Length: 185  Bit Score: 119.51  E-value: 4.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    1 MKKILTTPIKAEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIEL---KRPIPYDLNGKAIFHAGPIVRKNGDKweMVSVGP 77
Cdd:PRK06842   1 MEKKITTPLTEEKVKDLKAGDSVLISGYIYTARDAAHKRLIELldkGEELPIDIKDQIIYYVGPSPAKPGKV--IGSAGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   78 TTSMRMESFEREFIEQtGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQVEEIEEVHWTELGmPESLWVCRV 157
Cdd:PRK06842  79 TTSYRMDAYAPRLLDI-GLKGMIGKGARSDEVIESIKKNKAVYFGAIGGAAALIAKSIKKSEVIAYEDLG-AEAIRKLEV 156

                        170
                 ....*....|....*..
gi 16130958  158 KEFgPLIVSIDTHGNNL 174
Cdd:PRK06842 157 KDF-PVVVIIDSEGNNL 172
PRK15392 PRK15392
class I fumarate hydratase;
5-177 2.73e-18

class I fumarate hydratase;


Pssm-ID: 185290 [Multi-domain]  Cd Length: 550  Bit Score: 81.98  E-value: 2.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    5 LTTPIKA--EDLQDIRVGDVIYLTGTLVTCRDVCHRRL---IELKRPIPYDLNGKAIFHAGPIvrKNGDKWEMVSVGPTT 79
Cdd:PRK15392 362 LNRPLRDvmQDLARLPVGTRVSLSGPIVVARDIAHAKIkarLDSGEPMPEYLKHHIVYYAGPA--KTPENMACGSLGPTT 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   80 SMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAGCAVLAATQ-VEEIEEVHWTELGMpESLWVCRVK 158
Cdd:PRK15392 440 GGRMDGYVDTFQAAGGSLVMLSKGNRSQQVTDACHKHGGFNLGSIGGAAALLAQEyVKSLRCLEYPELGM-EAVWMMEVE 518

                        170
                 ....*....|....*....
gi 16130958  159 EFgPLIVSIDTHGNNLIAE 177
Cdd:PRK15392 519 NL-PAFILVDDKGNNFFSQ 536
PTZ00226 PTZ00226
fumarate hydratase; Provisional
 1-177 3.92e-18

fumarate hydratase; Provisional


Pssm-ID: 240319 [Multi-domain]  Cd Length: 570  Bit Score: 81.63  E-value: 3.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    1 MKKILttpikaEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIE-LKR--PIPYDLNGKAIFHAGPIVRKNGdkweMVS--V 75
Cdd:PTZ00226 397 MEEIL------KQLSKYPVKTRLSLTGTLIVARDIAHAKIVEmLENgePLPEYMKNHPIYYAGPAKTPDG----YASgsF 466

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   76 GPTTSMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAG-CAVLAATQVEEIEEVHWTELGMpESLWV 154
Cdd:PTZ00226 467 GPTTAGRMDSYVDLFMENGGSFITLAKGNRSKAVTNACKKYGGFYLGSIGGpAAILAKDNIKKVEVLDFPELGM-EAVWK 545

                        170       180
                 ....*....|....*....|...
gi 16130958  155 CRVKEFGPLIVsIDTHGNNLIAE 177
Cdd:PTZ00226 546 IEVENFPAFIV-VDDKGNDFYSQ 567
PLN00133 PLN00133
class I-fumerate hydratase; Provisional
 25-177 1.77e-17

class I-fumerate hydratase; Provisional


Pssm-ID: 215068 [Multi-domain]  Cd Length: 576  Bit Score: 79.92  E-value: 1.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   25 LTGTLVTCRDVCHRRL---IELKRPIPYDLNGKAIFHAGPIvrKNGDKWEMVSVGPTTSMRMESFEREFIEQTGVKLVVG 101
Cdd:PLN00133 421 LTGTLVVARDIAHAKLlerLEAGEGLPQYAKDHIIYYAGPA--KTPEGYASGSFGPTTAGRMDSYVDRFMAAGGSFVTLA 498

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130958  102 KGGMGPLTEEGCQKFKALHVIFPAG-CAVLAATQVEEIEEVHWTELGMpESLWVCRVKEFgPLIVSIDTHGNNLIAE 177
Cdd:PLN00133 499 KGNRSAQVTNACKKHGGFYLGSIGGpAAILAQNCIKKVEVLENPELGM-EAVWKIEVEDF-PAFIVVDDKGNDFFKK 573
PRK15390 PRK15390
fumarate hydratase FumA; Provisional
 1-177 5.39e-17

fumarate hydratase FumA; Provisional


Pssm-ID: 185288 [Multi-domain]  Cd Length: 548  Bit Score: 78.16  E-value: 5.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    1 MKKILttpikaEDLQDIRVGDVIYLTGTLVTCRDVCHRRLIEL---KRPIPYDLNGKAIFHAGPIvrKNGDKWEMVSVGP 77
Cdd:PRK15390 367 MKEIL------AQLSQYPVSTRLSLNGTIIVGRDIAHAKLKERmdnGEGLPQYIKDHPIYYAGPA--KTPEGYASGSLGP 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   78 TTSMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAG-CAVLAATQVEEIEEVHWTELGMpESLWVCR 156
Cdd:PRK15390 439 TTAGRMDSYVDQLQAQGGSMIMLAKGNRSQQVTDACKKHGGFYLGSIGGpAAVLAQGSIKSLECVEYPELGM-EAIWKIE 517

                        170       180
                 ....*....|....*....|.
gi 16130958  157 VKEFgPLIVSIDTHGNNLIAE 177
Cdd:PRK15390 518 VEDF-PAFILVDDKGNDFFQQ 537
PRK15391 PRK15391
class I fumarate hydratase;
1-177 2.50e-16

class I fumarate hydratase;


Pssm-ID: 185289 [Multi-domain]  Cd Length: 548  Bit Score: 76.22  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958    1 MKKILTtpikaeDLQDIRVGDVIYLTGTLVTCRDVCHRRLIEL---KRPIPYDLNGKAIFHAGPIvrKNGDKWEMVSVGP 77
Cdd:PRK15391 367 MKEILA------QLSQYPVSTRLSLTGTIIVGRDIAHAKLKELidaGKELPQYIKDHPIYYAGPA--KTPAGYPSGSLGP 438

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   78 TTSMRMESFEREFIEQTGVKLVVGKGGMGPLTEEGCQKFKALHVIFPAG-CAVLAATQVEEIEEVHWTELGMpESLWVCR 156
Cdd:PRK15391 439 TTAGRMDSYVDLLQSHGGSMIMLAKGNRSQQVTDACHKHGGFYLGSIGGpAAVLAQQSIKHLECVAYPELGM-EAIWKIE 517

                        170       180
                 ....*....|....*....|.
gi 16130958  157 VKEFgPLIVSIDTHGNNLIAE 177
Cdd:PRK15391 518 VEDF-PAFILVDDKGNDFFQQ 537
PRK15389 PRK15389
fumarate hydratase; Provisional
 25-177 6.18e-15

fumarate hydratase; Provisional


Pssm-ID: 237955 [Multi-domain]  Cd Length: 536  Bit Score: 72.25  E-value: 6.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958   25 LTGTLVTCRDVCHRRLIE-LKR--PIPYDLNGKAIFHAGPIvrKNGDKWEMVSVGPTTSMRMESFEREFIEQTGVKLVVG 101
Cdd:PRK15389 384 LTGTIIVARDIAHAKLKErLDAgeGLPQYLKDHPVYYAGPA--KTPEGYASGSFGPTTAGRMDSYVDLFQAAGGSMVMLA 461

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130958  102 KGGMGPLTEEGCQKfkalHVIF-------PAgcAVLAATQVEEIEEVHWTELGMpESLWVCRVKEFGPLIVsIDTHGNNL 174
Cdd:PRK15389 462 KGNRSQQVTDACKK----HGGFylgsiggPA--ARLAQDCIKKVEVLEYPELGM-EAVWKIEVEDFPAFIL-VDDKGNDF 533


                 ...
gi 16130958  175 IAE 177
Cdd:PRK15389 534 FKE 536
 
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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