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Conserved domains on  [gi|446084550|ref|WP_000162405|]
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MULTISPECIES: L(+)-tartrate dehydratase subunit beta [Enterobacteriaceae]

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
 1-205 5.05e-154

L(+)-tartrate dehydratase subunit beta; Validated


:

Pssm-ID: 236192  Cd Length: 204  Bit Score: 424.47  E-value: 5.05e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   1 MTKKILTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRLIEGGRELPVDVRGGAILHAGPIVRPIKgEDDKFEMVSVG 80
Cdd:PRK08228   1 MMKKILTTPIKDEDLQDIKVGDVIYLTGTLVTCRDVAHRRLIELGRELPVDLNGGAIFHAGPIVRPKK-NDDKFEMVSVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  81 PTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMPETLWVCR 160
Cdd:PRK08228  80 PTTSMRMEKFEKEFIEQTGVKLIVGKGGMGPGTEEGCQEFKALHCVFPAGCAVLAATQVEEIEDAQWRDLGMPETLWVCR 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446084550 161 VKEFGPLIVSIDTHGNNLFEQNKIIFNQRKEIVADEICQNVSFIK 205
Cdd:PRK08228 160 VKEFGPLIVSIDTHGNNLFEENKKLFNERKEPIVEEICEHVHFIK 204
 
Name Accession Description Interval E-value
PRK08228 PRK08228
L(+)-tartrate dehydratase subunit beta; Validated
 1-205 5.05e-154

L(+)-tartrate dehydratase subunit beta; Validated


Pssm-ID: 236192  Cd Length: 204  Bit Score: 424.47  E-value: 5.05e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   1 MTKKILTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRLIEGGRELPVDVRGGAILHAGPIVRPIKgEDDKFEMVSVG 80
Cdd:PRK08228   1 MMKKILTTPIKDEDLQDIKVGDVIYLTGTLVTCRDVAHRRLIELGRELPVDLNGGAIFHAGPIVRPKK-NDDKFEMVSVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  81 PTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMPETLWVCR 160
Cdd:PRK08228  80 PTTSMRMEKFEKEFIEQTGVKLIVGKGGMGPGTEEGCQEFKALHCVFPAGCAVLAATQVEEIEDAQWRDLGMPETLWVCR 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446084550 161 VKEFGPLIVSIDTHGNNLFEQNKIIFNQRKEIVADEICQNVSFIK 205
Cdd:PRK08228 160 VKEFGPLIVSIDTHGNNLFEENKKLFNERKEPIVEEICEHVHFIK 204
ttdB_fumA_fumB TIGR00723
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S ...
 13-181 7.30e-80

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: 235.41  E-value: 7.30e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   13 EDLADIKAGDIIYLNGHIVTCRDVAHRRLIE---GGRELPVDVRGGAILHAGPIVRPikgeDDKFEMVSVGPTTSMRMEK 89
Cdd:TIGR00723   1 EQILKLKVGDVVYLTGTIFTARDEAHARLLElidEGKELPFDLNGSVIYHAGPIVTK----NGEWEVVSVGPTTSARMNP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   90 FEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMPETLWVCRVKEFGPLIV 169
Cdd:TIGR00723  77 FEPELLEKLGVMAIIGKGGMSKEVVEACRKYKAVYLAFPGGCAALLAQSVKKVEGVAWEDLGMPEAIWELEVEDFGPLIV 156

                         170
                  ....*....|..
gi 446084550  170 SIDTHGNNLFEQ 181
Cdd:TIGR00723 157 AIDSHGNSIFQE 168
FumA COG1838
Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy ...
 1-181 1.87e-70

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: 212.28  E-value: 1.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   1 MTKKILTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRLIE---GGRELPVDVRGGAILHAGPIVRPikgedDKFEMV 77
Cdd:COG1838    1 MATIRLNTPLTEEDVRKLKAGDRVLLSGTIYTARDAAHKRLVElldRGEPLPVDLKGQVIYYVGPAPAK-----PGYVIG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  78 SVGPTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMpETLW 157
Cdd:COG1838   76 SAGPTTSTRMDKYTPELLEELGLKGMIGKGGRSPEVIEAMKKHGAVYLAAVGGAAALLAKAIKKVEVVAYEDLGP-EAIW 154

                        170       180
                 ....*....|....*....|....
gi 446084550 158 VCRVKEFgPLIVSIDTHGNNLFEQ 181
Cdd:COG1838  155 KLEVEDF-PLIVAIDSKGNSLYEQ 177
Fumerase_C pfam05683
Fumarase C-terminus; This family consists of the C terminal region of several bacterial ...
 2-181 3.37e-41

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: 138.37  E-value: 3.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550    2 TKKI-LTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRL---IEGGRELP--VDVRGGAILHAGPiVRPIKGEDDKfe 75
Cdd:pfam05683  26 AVRVdLNRPETREELSKWPVGTRLLLSGTLLTGRDAAHKRIkemLDKGEPLPeyVDLNGRPIYYAGP-VDTPGGEVVG-- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   76 mvSVGPTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMpET 155
Cdd:pfam05683 103 --SAGPTTATRMDKYVDDFLEKGGSMGMIGKGNRGPAVTEACKKHGGFYLGAIGGAAYLAAKAIKKVEVVAFEELGM-EA 179

                         170       180
                  ....*....|....*....|....*.
gi 446084550  156 LWVCRVKEFgPLIVSIDTHGNNLFEQ 181
Cdd:pfam05683 180 IWEFEVEDF-PAFVAVDDKGNSFHKT 204
 
Name Accession Description Interval E-value
PRK08228 PRK08228
L(+)-tartrate dehydratase subunit beta; Validated
 1-205 5.05e-154

L(+)-tartrate dehydratase subunit beta; Validated


Pssm-ID: 236192  Cd Length: 204  Bit Score: 424.47  E-value: 5.05e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   1 MTKKILTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRLIEGGRELPVDVRGGAILHAGPIVRPIKgEDDKFEMVSVG 80
Cdd:PRK08228   1 MMKKILTTPIKDEDLQDIKVGDVIYLTGTLVTCRDVAHRRLIELGRELPVDLNGGAIFHAGPIVRPKK-NDDKFEMVSVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  81 PTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMPETLWVCR 160
Cdd:PRK08228  80 PTTSMRMEKFEKEFIEQTGVKLIVGKGGMGPGTEEGCQEFKALHCVFPAGCAVLAATQVEEIEDAQWRDLGMPETLWVCR 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446084550 161 VKEFGPLIVSIDTHGNNLFEQNKIIFNQRKEIVADEICQNVSFIK 205
Cdd:PRK08228 160 VKEFGPLIVSIDTHGNNLFEENKKLFNERKEPIVEEICEHVHFIK 204
ttdB_fumA_fumB TIGR00723
hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region; A number of Fe-S ...
 13-181 7.30e-80

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: 235.41  E-value: 7.30e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   13 EDLADIKAGDIIYLNGHIVTCRDVAHRRLIE---GGRELPVDVRGGAILHAGPIVRPikgeDDKFEMVSVGPTTSMRMEK 89
Cdd:TIGR00723   1 EQILKLKVGDVVYLTGTIFTARDEAHARLLElidEGKELPFDLNGSVIYHAGPIVTK----NGEWEVVSVGPTTSARMNP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   90 FEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMPETLWVCRVKEFGPLIV 169
Cdd:TIGR00723  77 FEPELLEKLGVMAIIGKGGMSKEVVEACRKYKAVYLAFPGGCAALLAQSVKKVEGVAWEDLGMPEAIWELEVEDFGPLIV 156

                         170
                  ....*....|..
gi 446084550  170 SIDTHGNNLFEQ 181
Cdd:TIGR00723 157 AIDSHGNSIFQE 168
FumA COG1838
Tartrate dehydratase beta subunit/Fumarate hydratase class I, C-terminal domain [Energy ...
 1-181 1.87e-70

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: 212.28  E-value: 1.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   1 MTKKILTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRLIE---GGRELPVDVRGGAILHAGPIVRPikgedDKFEMV 77
Cdd:COG1838    1 MATIRLNTPLTEEDVRKLKAGDRVLLSGTIYTARDAAHKRLVElldRGEPLPVDLKGQVIYYVGPAPAK-----PGYVIG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  78 SVGPTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMpETLW 157
Cdd:COG1838   76 SAGPTTSTRMDKYTPELLEELGLKGMIGKGGRSPEVIEAMKKHGAVYLAAVGGAAALLAKAIKKVEVVAYEDLGP-EAIW 154

                        170       180
                 ....*....|....*....|....
gi 446084550 158 VCRVKEFgPLIVSIDTHGNNLFEQ 181
Cdd:COG1838  155 KLEVEDF-PLIVAIDSKGNSLYEQ 177
PRK06043 PRK06043
fumarate hydratase; Provisional
 6-179 2.56e-55

fumarate hydratase; Provisional


Pssm-ID: 180366  Cd Length: 192  Bit Score: 174.18  E-value: 2.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   6 LTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRLIE---GGRELPVDVRGGAILHAGPIvrpIKGEDDKFEMVSVGPT 82
Cdd:PRK06043   5 LKTPLKKEDIEKLNVGDIVYISGEILTARDEAHARILEmkeKGKELPFSLEGAVIYHCGPL---MKKTDEGWKVVSAGPT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  83 TSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEgcAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMPETLWVCRVK 162
Cdd:PRK06043  82 TSARMSKMTPKLLEKVEVRAIIGKGGMKNVADA--LKGKCVYLAYTGGCAALAAESIKRVKAVHWLDLGMPEAVWVLEVE 159

                        170
                 ....*....|....*..
gi 446084550 163 EFGPLIVSIDTHGNNLF 179
Cdd:PRK06043 160 EFGPLIVGIDAKGNDLY 176
PRK08395 PRK08395
fumarate hydratase; Provisional
 6-179 1.38e-46

fumarate hydratase; Provisional


Pssm-ID: 169425  Cd Length: 162  Bit Score: 150.73  E-value: 1.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   6 LTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRLIEGGreLPVDVRGGAILHAGPIVRpikgeddKFEMVSVGPTTSM 85
Cdd:PRK08395   3 LKTPLSWEDVLKLKAGDVVYLSGIIYTARDLAHRRFLSEG--FPFNPEGAVIYHCGPLVK-------NKKIVSAGPTTSA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  86 RMEKFeKEFIAQTGVKLIVGKGGMGKGTEEGcaehKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMPETLWVCRVKEFg 165
Cdd:PRK08395  74 RMNKY-LDFLFSLGVRGIIGKGGMNAEPFKG----RAVYFAFPGGAGSLAAKSIKRVRDVYWEDLGMPDAVWELEVEDF- 147

                        170
                 ....*....|....
gi 446084550 166 PLIVSIDTHGNNLF 179
Cdd:PRK08395 148 PLLVAIDSKGRSLY 161
Fumerase_C pfam05683
Fumarase C-terminus; This family consists of the C terminal region of several bacterial ...
 2-181 3.37e-41

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: 138.37  E-value: 3.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550    2 TKKI-LTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRL---IEGGRELP--VDVRGGAILHAGPiVRPIKGEDDKfe 75
Cdd:pfam05683  26 AVRVdLNRPETREELSKWPVGTRLLLSGTLLTGRDAAHKRIkemLDKGEPLPeyVDLNGRPIYYAGP-VDTPGGEVVG-- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   76 mvSVGPTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGMpET 155
Cdd:pfam05683 103 --SAGPTTATRMDKYVDDFLEKGGSMGMIGKGNRGPAVTEACKKHGGFYLGAIGGAAYLAAKAIKKVEVVAFEELGM-EA 179

                         170       180
                  ....*....|....*....|....*.
gi 446084550  156 LWVCRVKEFgPLIVSIDTHGNNLFEQ 181
Cdd:pfam05683 180 IWEFEVEDF-PAFVAVDDKGNSFHKT 204
PRK06842 PRK06842
Fe-S-containing hydro-lyase;
1-180 2.82e-34

Fe-S-containing hydro-lyase;


Pssm-ID: 180724 [Multi-domain]  Cd Length: 185  Bit Score: 120.28  E-value: 2.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   1 MTKKIlTTPIKDEDLADIKAGDIIYLNGHIVTCRDVAHRRLIE---GGRELPVDVRGGAILHAGPivRPIK-GEddkfEM 76
Cdd:PRK06842   1 MEKKI-TTPLTEEKVKDLKAGDSVLISGYIYTARDAAHKRLIElldKGEELPIDIKDQIIYYVGP--SPAKpGK----VI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  77 VSVGPTTSMRMEKFEKEFIaQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAGCAVVAAVCVEEIEDAQWRDLGmPETL 156
Cdd:PRK06842  74 GSAGPTTSYRMDAYAPRLL-DIGLKGMIGKGARSDEVIESIKKNKAVYFGAIGGAAALIAKSIKKSEVIAYEDLG-AEAI 151

                        170       180
                 ....*....|....*....|....
gi 446084550 157 WVCRVKEFgPLIVSIDTHGNNLFE 180
Cdd:PRK06842 152 RKLEVKDF-PVVVIIDSEGNNLYE 174
PRK15390 PRK15390
fumarate hydratase FumA; Provisional
 26-181 1.67e-19

fumarate hydratase FumA; Provisional


Pssm-ID: 185288 [Multi-domain]  Cd Length: 548  Bit Score: 85.86  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  26 LNGHIVTCRDVAHRRL---IEGGRELPVDVRGGAILHAGPIVRPikgedDKFEMVSVGPTTSMRMEKFEKEFIAQTGVKL 102
Cdd:PRK15390 385 LNGTIIVGRDIAHAKLkerMDNGEGLPQYIKDHPIYYAGPAKTP-----EGYASGSLGPTTAGRMDSYVDQLQAQGGSMI 459

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550 103 IVGKGGMGKGTEEGCAEHKALHCVFPAG-CAVVAAVCVEEIEDAQWRDLGMpETLWVCRVKEFgPLIVSIDTHGNNLFEQ 181
Cdd:PRK15390 460 MLAKGNRSQQVTDACKKHGGFYLGSIGGpAAVLAQGSIKSLECVEYPELGM-EAIWKIEVEDF-PAFILVDDKGNDFFQQ 537
PRK15391 PRK15391
class I fumarate hydratase;
6-181 2.19e-19

class I fumarate hydratase;


Pssm-ID: 185289 [Multi-domain]  Cd Length: 548  Bit Score: 85.47  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   6 LTTPIKdEDLADIKAGDI---IYLNGHIVTCRDVAH---RRLIEGGRELPVDVRGGAILHAGPIVRPikgedDKFEMVSV 79
Cdd:PRK15391 363 LNRPMK-EILAQLSQYPVstrLSLTGTIIVGRDIAHaklKELIDAGKELPQYIKDHPIYYAGPAKTP-----AGYPSGSL 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  80 GPTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAG-CAVVAAVCVEEIEDAQWRDLGMpETLWV 158
Cdd:PRK15391 437 GPTTAGRMDSYVDLLQSHGGSMIMLAKGNRSQQVTDACHKHGGFYLGSIGGpAAVLAQQSIKHLECVAYPELGM-EAIWK 515

                        170       180
                 ....*....|....*....|...
gi 446084550 159 CRVKEFgPLIVSIDTHGNNLFEQ 181
Cdd:PRK15391 516 IEVEDF-PAFILVDDKGNDFFQQ 537
PLN00133 PLN00133
class I-fumerate hydratase; Provisional
 26-181 3.74e-19

class I-fumerate hydratase; Provisional


Pssm-ID: 215068 [Multi-domain]  Cd Length: 576  Bit Score: 84.54  E-value: 3.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  26 LNGHIVTCRDVAHRRL---IEGGRELPVDVRGGAILHAGPIVRPikgedDKFEMVSVGPTTSMRMEKFEKEFIAQTGVKL 102
Cdd:PLN00133 421 LTGTLVVARDIAHAKLlerLEAGEGLPQYAKDHIIYYAGPAKTP-----EGYASGSFGPTTAGRMDSYVDRFMAAGGSFV 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550 103 IVGKGGMGKGTEEGCAEHKALHCVFPAG-CAVVAAVCVEEIEDAQWRDLGMpETLWVCRVKEFgPLIVSIDTHGNNLFEQ 181
Cdd:PLN00133 496 TLAKGNRSAQVTNACKKHGGFYLGSIGGpAAILAQNCIKKVEVLENPELGM-EAVWKIEVEDF-PAFIVVDDKGNDFFKK 573
PRK15392 PRK15392
class I fumarate hydratase;
6-181 1.28e-18

class I fumarate hydratase;


Pssm-ID: 185290 [Multi-domain]  Cd Length: 550  Bit Score: 83.13  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550   6 LTTPIKD--EDLADIKAGDIIYLNGHIVTCRDVAHRRL---IEGGRELPVDVRGGAILHAGPIVRPikgedDKFEMVSVG 80
Cdd:PRK15392 362 LNRPLRDvmQDLARLPVGTRVSLSGPIVVARDIAHAKIkarLDSGEPMPEYLKHHIVYYAGPAKTP-----ENMACGSLG 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  81 PTTSMRMEKFEKEFIAQTGVKLIVGKGGMGKGTEEGCAEHKALHCVFPAG-CAVVAAVCVEEIEDAQWRDLGMpETLWVC 159
Cdd:PRK15392 437 PTTGGRMDGYVDTFQAAGGSLVMLSKGNRSQQVTDACHKHGGFNLGSIGGaAALLAQEYVKSLRCLEYPELGM-EAVWMM 515

                        170       180
                 ....*....|....*....|..
gi 446084550 160 RVKEFgPLIVSIDTHGNNLFEQ 181
Cdd:PRK15392 516 EVENL-PAFILVDDKGNNFFSQ 536
PTZ00226 PTZ00226
fumarate hydratase; Provisional
 26-181 6.91e-17

fumarate hydratase; Provisional


Pssm-ID: 240319 [Multi-domain]  Cd Length: 570  Bit Score: 78.16  E-value: 6.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  26 LNGHIVTCRDVAHRRL---IEGGRELPVDVRGGAILHAGPIVRPikgedDKFEMVSVGPTTSMRMEKFEKEFIAQTGVKL 102
Cdd:PTZ00226 415 LTGTLIVARDIAHAKIvemLENGEPLPEYMKNHPIYYAGPAKTP-----DGYASGSFGPTTAGRMDSYVDLFMENGGSFI 489

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550 103 IVGKGGMGKGTEEGCAEHKALHCVFPAG-CAVVAAVCVEEIEDAQWRDLGMpETLWVCRVKEFGPLIVsIDTHGNNLFEQ 181
Cdd:PTZ00226 490 TLAKGNRSKAVTNACKKYGGFYLGSIGGpAAILAKDNIKKVEVLDFPELGM-EAVWKIEVENFPAFIV-VDDKGNDFYSQ 567
PRK15389 PRK15389
fumarate hydratase; Provisional
 26-181 2.32e-15

fumarate hydratase; Provisional


Pssm-ID: 237955 [Multi-domain]  Cd Length: 536  Bit Score: 73.79  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550  26 LNGHIVTCRDVAHRRL---IEGGRELPVDVRGGAILHAGPIVRPikgedDKFEMVSVGPTTSMRMEKFEKEFIAQTGVKL 102
Cdd:PRK15389 384 LTGTIIVARDIAHAKLkerLDAGEGLPQYLKDHPVYYAGPAKTP-----EGYASGSFGPTTAGRMDSYVDLFQAAGGSMV 458

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446084550 103 IVGKGGMGKGTEEGCAEHKAlhcvF-------PAgcAVVAAVCVEEIEDAQWRDLGMpETLWVCRVKEFGPLIVsIDTHG 175
Cdd:PRK15389 459 MLAKGNRSQQVTDACKKHGG----FylgsiggPA--ARLAQDCIKKVEVLEYPELGM-EAVWKIEVEDFPAFIL-VDDKG 530


                 ....*.
gi 446084550 176 NNLFEQ 181
Cdd:PRK15389 531 NDFFKE 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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