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Conserved domains on  [gi|695817689|ref|WP_032731516|]
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MULTISPECIES: 4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase [Klebsiella]

Protein Classification

4-hydroxy-4-methyl-2-oxoglutarate aldolase/4-carboxy-4-hydroxy-2-oxoadipate aldolase( domain architecture ID 10013164)

4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy-4-hydroxy-2-oxoadipate (CHA) aldolase catalyzes the conversion of HMG to pyruvate, and the conversion of CHA to pyruvate and oxaloacetate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09262 PRK09262
hypothetical protein; Provisional
6-230 2.21e-134

hypothetical protein; Provisional


:

Pssm-ID: 181735  Cd Length: 225  Bit Score: 376.96  E-value: 2.21e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689   6 KKGLVIRHLPRHDEAVLRRCEAAGVATLHEAWERQGLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDI 85
Cdd:PRK09262   1 MLGVVVRNIERADAAVVDRLAEFGVATVHEAQGRVGLLKPYMRPIYQGARIAGTAVTVLVQPGDNWMMHVAVEQCQPGDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  86 LVVAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQP 165
Cdd:PRK09262  81 LVVAPTSPCTDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTVKATLGSVNVPVVCAGALVNP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695817689 166 GDVVVADDDGVVVLPHAQVRDVLDKAEARMSNELAKRERMRHGELGLDIYAMRPRLAEKGLRYYD 230
Cdd:PRK09262 161 GDVVVADDDGVVVVPRAQAAAVADAAEAREANEESKRERLAAGELGLDIYKMRERLAKKGLRYVD 225
 
Name Accession Description Interval E-value
PRK09262 PRK09262
hypothetical protein; Provisional
6-230 2.21e-134

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 376.96  E-value: 2.21e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689   6 KKGLVIRHLPRHDEAVLRRCEAAGVATLHEAWERQGLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDI 85
Cdd:PRK09262   1 MLGVVVRNIERADAAVVDRLAEFGVATVHEAQGRVGLLKPYMRPIYQGARIAGTAVTVLVQPGDNWMMHVAVEQCQPGDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  86 LVVAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQP 165
Cdd:PRK09262  81 LVVAPTSPCTDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTVKATLGSVNVPVVCAGALVNP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695817689 166 GDVVVADDDGVVVLPHAQVRDVLDKAEARMSNELAKRERMRHGELGLDIYAMRPRLAEKGLRYYD 230
Cdd:PRK09262 161 GDVVVADDDGVVVVPRAQAAAVADAAEAREANEESKRERLAAGELGLDIYKMRERLAKKGLRYVD 225
ligK_PcmE TIGR02798
4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein ...
8-228 5.76e-89

4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein family 4-carboxy-4-hydroxy-2-oxoadipate aldolase, also called 4-oxalocitramalate aldolase. This enzyme of the protocatechuate 4,5-cleavage pathway converts its substrate to pyruvate plus oxaloacetate. Protocatechuate is an intermediate in many pathways for degrading aromatic compounds, including lignin, fluorene, etc. Hara, et al. showed the LigK gene was not only a 4-carboxy-4-hydroxy-2-oxoadipate aldolase but also the enzyme of the following step, oxaloacetate decarboxylase.


Pssm-ID: 131845  Cd Length: 222  Bit Score: 262.09  E-value: 5.76e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689    8 GLVIRHLPRHDEAVLRRCEAAGVATLHEAWERQGLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILV 87
Cdd:TIGR02798   1 GIVVRNIERADLAAVDGLAAFGVATVHEAMGRVGLLAPYMRPIYTGARVCGTAVTVLLQPGDNWMMHVAAEQIQEGDVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689   88 VAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQPGD 167
Cdd:TIGR02798  81 AACTAECEDGYFGDLLATSFQARGCRGLIIDAGVRDVRDLTEMNFPVWSKAIHAKGTVKATLGSVNIPVVCANALVNPGD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695817689  168 VVVADDDGVVVLPHAQVRDVLDKAEARMSNELAKRERMRHGELGLDIYAMRPRLAEKGLRY 228
Cdd:TIGR02798 161 VVVADDDGVVVVPRANAGAVLDAAQAREANEEAKRVKLASGVLGLDMYKMREPLEKAGLKY 221
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
15-215 3.36e-58

RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 183.06  E-value: 3.36e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  15 PRHDEAVLRRCEAAGVATLHEAWER--QGLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILVVAPTS 92
Cdd:COG0684    1 PRLDAELLERLAAVSTATVSDALDRllRGALDPGIRPLHPGARLVGPAVTVRYRPGDNLMLHEAIDLAPPGDVLVIDAGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  93 PCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKES-LGSVNVPVICAGQLVQPgdvvva 171
Cdd:COG0684   81 DTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVgPGEINVPVSIGGVTVRPgdlvva 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 695817689 172 dddgvvvLPHAQVRDVLDKAEARMSNELAKRERMRHGELGLDIY 215
Cdd:COG0684  161 dddgvvvIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY 204
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
31-170 1.14e-36

Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.


Pssm-ID: 427475 [Multi-domain]  Cd Length: 148  Bit Score: 126.08  E-value: 1.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689   31 ATLHEAWE----RQGLMgPAIRPIQQGVsRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILVVAPTSPCgDGFFGDLLATS 106
Cdd:pfam03737   1 ADLSDALGsyggRLGAM-PGIRPLNPGP-FVGPAVTVKCFPEDNLLVHEALDEAGPGDVLVVDGGGGS-RAALGDLLATL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695817689  107 LQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQPGDVVV 170
Cdd:pfam03737  78 AKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIV 141
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
31-170 1.51e-35

ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.


Pssm-ID: 319245 [Multi-domain]  Cd Length: 150  Bit Score: 123.34  E-value: 1.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  31 ATLHEAWERQ-GLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILVVAPTSPCGDGFFGDLLATSLQS 109
Cdd:cd16841    1 ADLSDALDRLgGVLPGIIRPLGGGARFVGPAVTVKCFPDDNLLVREALDEAGPGDVLVVDGGGSLRCALWGDLLATLAKA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695817689 110 RGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQPGDVVV 170
Cdd:cd16841   81 RGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIV 141
 
Name Accession Description Interval E-value
PRK09262 PRK09262
hypothetical protein; Provisional
6-230 2.21e-134

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 376.96  E-value: 2.21e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689   6 KKGLVIRHLPRHDEAVLRRCEAAGVATLHEAWERQGLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDI 85
Cdd:PRK09262   1 MLGVVVRNIERADAAVVDRLAEFGVATVHEAQGRVGLLKPYMRPIYQGARIAGTAVTVLVQPGDNWMMHVAVEQCQPGDV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  86 LVVAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQP 165
Cdd:PRK09262  81 LVVAPTSPCTDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRAISAQGTVKATLGSVNVPVVCAGALVNP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695817689 166 GDVVVADDDGVVVLPHAQVRDVLDKAEARMSNELAKRERMRHGELGLDIYAMRPRLAEKGLRYYD 230
Cdd:PRK09262 161 GDVVVADDDGVVVVPRAQAAAVADAAEAREANEESKRERLAAGELGLDIYKMRERLAKKGLRYVD 225
ligK_PcmE TIGR02798
4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein ...
8-228 5.76e-89

4-carboxy-4-hydroxy-2-oxoadipate aldolase/oxaloacetate decarboxylase; Members of this protein family 4-carboxy-4-hydroxy-2-oxoadipate aldolase, also called 4-oxalocitramalate aldolase. This enzyme of the protocatechuate 4,5-cleavage pathway converts its substrate to pyruvate plus oxaloacetate. Protocatechuate is an intermediate in many pathways for degrading aromatic compounds, including lignin, fluorene, etc. Hara, et al. showed the LigK gene was not only a 4-carboxy-4-hydroxy-2-oxoadipate aldolase but also the enzyme of the following step, oxaloacetate decarboxylase.


Pssm-ID: 131845  Cd Length: 222  Bit Score: 262.09  E-value: 5.76e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689    8 GLVIRHLPRHDEAVLRRCEAAGVATLHEAWERQGLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILV 87
Cdd:TIGR02798   1 GIVVRNIERADLAAVDGLAAFGVATVHEAMGRVGLLAPYMRPIYTGARVCGTAVTVLLQPGDNWMMHVAAEQIQEGDVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689   88 VAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQPGD 167
Cdd:TIGR02798  81 AACTAECEDGYFGDLLATSFQARGCRGLIIDAGVRDVRDLTEMNFPVWSKAIHAKGTVKATLGSVNIPVVCANALVNPGD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695817689  168 VVVADDDGVVVLPHAQVRDVLDKAEARMSNELAKRERMRHGELGLDIYAMRPRLAEKGLRY 228
Cdd:TIGR02798 161 VVVADDDGVVVVPRANAGAVLDAAQAREANEEAKRVKLASGVLGLDMYKMREPLEKAGLKY 221
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
15-215 3.36e-58

RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 183.06  E-value: 3.36e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  15 PRHDEAVLRRCEAAGVATLHEAWER--QGLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILVVAPTS 92
Cdd:COG0684    1 PRLDAELLERLAAVSTATVSDALDRllRGALDPGIRPLHPGARLVGPAVTVRYRPGDNLMLHEAIDLAPPGDVLVIDAGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  93 PCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKES-LGSVNVPVICAGQLVQPgdvvva 171
Cdd:COG0684   81 DTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVgPGEINVPVSIGGVTVRPgdlvva 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 695817689 172 dddgvvvLPHAQVRDVLDKAEARMSNELAKRERMRHGELGLDIY 215
Cdd:COG0684  161 dddgvvvIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY 204
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
31-170 1.14e-36

Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.


Pssm-ID: 427475 [Multi-domain]  Cd Length: 148  Bit Score: 126.08  E-value: 1.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689   31 ATLHEAWE----RQGLMgPAIRPIQQGVsRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILVVAPTSPCgDGFFGDLLATS 106
Cdd:pfam03737   1 ADLSDALGsyggRLGAM-PGIRPLNPGP-FVGPAVTVKCFPEDNLLVHEALDEAGPGDVLVVDGGGGS-RAALGDLLATL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695817689  107 LQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQPGDVVV 170
Cdd:pfam03737  78 AKANGWAGIVIDGAVRDVDELRELDFPVFARGTTPRGSVKRGPGEVNVPVTIGGVTVRPGDIIV 141
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
31-170 1.51e-35

ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.


Pssm-ID: 319245 [Multi-domain]  Cd Length: 150  Bit Score: 123.34  E-value: 1.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  31 ATLHEAWERQ-GLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILVVAPTSPCGDGFFGDLLATSLQS 109
Cdd:cd16841    1 ADLSDALDRLgGVLPGIIRPLGGGARFVGPAVTVKCFPDDNLLVREALDEAGPGDVLVVDGGGSLRCALWGDLLATLAKA 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695817689 110 RGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQPGDVVV 170
Cdd:cd16841   81 RGWAGIVIDGAVRDVDEIRELDFPVFARGTTPRGSKKVGPGEVNVPVTIGGVTVNPGDIIV 141
PRK06201 PRK06201
hypothetical protein; Validated
15-208 3.39e-34

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 121.98  E-value: 3.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  15 PRHDEAVLRRCEAAGVATLHEAWERQGLMGPAIRPIQQGVSRAGNAVTVLVTPGDNWMFHVAVEQCRAGDILVVAPTSPC 94
Cdd:PRK06201  12 PRVDAALVEAFRELPVANISDSMNRMTAGGAGLRPMHRGGRLAGTALTVRTRPGDNLMIHRALDLARPGDVIVVDGGGDL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  95 GDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQPGDVVVADDD 174
Cdd:PRK06201  92 TNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFARGVTHRGPYKDGPGEINVPVAIGGMVIEPGDLIVGDDD 171
                        170       180       190
                 ....*....|....*....|....*....|....
gi 695817689 175 GVVVLPHAQVRDVLDKAEARMSNELAKRERMRHG 208
Cdd:PRK06201 172 GLVAVPPADAEALLEAARAKHAAEAKQLEAIRAG 205
PRK08245 PRK08245
hypothetical protein; Validated
74-208 2.42e-13

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 67.23  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  74 HVAVEQCRAGDILVVAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVK--ESLGs 151
Cdd:PRK08245  79 RAAIETCPPGCVLVVDARGDARAGSFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGLPVWCAGPSAPTNLTglTAVD- 157
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 695817689 152 VNVPVICAGQLVQPGDVVVADDDGVVVLPHAQVRDVLDKAEARMSNELAKRERMRHG 208
Cdd:PRK08245 158 INVPIGCGGVAVFPGDIIVADDDGVVVIPAALADEVAAEAVEQERWEDFIREEVAAG 214
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
35-208 2.28e-12

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 65.81  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  35 EAWERQGLMgPAIRPIQQGVSRAGNAVTVLVTPGDnWMFHV-AVEQCRAGDILV-------VAPtspcgdgfFGDLLATS 106
Cdd:PRK07028 243 DAMHRKGAM-KGIKPLVRGTKMVGKAVTVQTFAGD-WAKPVeAIDVAKPGDVIViynsskdIAP--------WGELATLS 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689 107 LQSRGVVGLVGDIGIRDSQTLREMGFAVWSRQVYAQGTVKESLGSVNVPVICAGQLVQPGDVVVADDDGVVVLPHAQVRD 186
Cdd:PRK07028 313 CLNKGIAGVVIDGAVRDVDEIRKLGFPVFARAIVPNAGEPKGFGEINAEIVCGGQTVRPGDWIIGDENGVVVVPKERAYE 392
                        170       180
                 ....*....|....*....|..
gi 695817689 187 VLDKAEARMSNELAKRERMRHG 208
Cdd:PRK07028 393 IARRALEVKKTEDRIREEIRRG 414
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
18-208 5.72e-12

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 64.39  E-value: 5.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  18 DEAVLRRCEAAGVATLHEAWERQGLMGPAI---RPIQQGVSRAGNAVTVLVTPGDNWMFHV----------AVEQCRAGD 84
Cdd:PRK12764 268 SPELKAKLASVATATLSAQLRKRGLNNVSIdglTPTRPGRRMVGRARTLRYVPNREDLFKEhgggfnaqkrAFDSVNPGE 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  85 ILVVAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFavwsrQVYAQGTVKESLGSVNVP------VIC 158
Cdd:PRK12764 348 VLVIEARGEKGTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGL-----PVFFAGPHPAVLGRRHVPwdvditVAC 422
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 695817689 159 AGQLVQPGDVVVADDDGVVVLPHAQVRDVLDKAEARMSNELAKRERMRHG 208
Cdd:PRK12764 423 GGATVQPGDVIVGDDDGVVVIPPALAEEVADDAIAQEHEEAFIAERVAEG 472
NOT-MenG TIGR01935
RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase ...
57-170 1.37e-04

RraA famliy; The E. coli member of this family has been characterized as a regulator of RNase E and its crystal structure has been analyzed. This model was initially classified as a "hypothetical equivalog" expressing the tentative hypothesis that all members might have the same function as the E. coli enzyme. Considering the second clade of enterobacterial sequences within this family, that appears to be less tenable. The function of these sequences outside of the narrow RraA equivalog model (TIGR02998) remains obscure. All of these were initially annotated as MenG, AKA S-adenosylmethionine: 2-demethylmenaquinone methyltransferase (EC 2.1.-.-). See the references characterizing this as a case of transitive annotation error in the case of the E. coli protein. [Unknown function, General]


Pssm-ID: 130990  Cd Length: 150  Bit Score: 40.78  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689   57 AGNAVTVLVTPgDNWMFHVAVEQCRAGDILVVAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVWS 136
Cdd:TIGR01935  29 AGPIVTVKCFE-DNSLVREVLEQPGAGRVLVVDGGGSLRCALLGDNLAVLAEENGWEGVIVNGCVRDVAELAGMDLGVKA 107
                          90       100       110
                  ....*....|....*....|....*....|....
gi 695817689  137 RQVYAQGTVKESLGSVNVPVICAGQLVQPGDVVV 170
Cdd:TIGR01935 108 LAAHPRKTEKRGAGEVDVPVTFAGVTFVPGDYLY 141
PRK12487 PRK12487
putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
83-168 1.44e-03

putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;


Pssm-ID: 183553  Cd Length: 163  Bit Score: 38.02  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695817689  83 GDILVVAPTSPCGDGFFGDLLATSLQSRGVVGLVGDIGIRDSQTLREMGFAVwsrqvYAQG-----TVKESLGSVNVPVI 157
Cdd:PRK12487  58 GKVLVVDGGGSCRRALLGDQIAQSALDNGWEGIVINGCVRDVGALSTMDLGV-----KALGaspikTEKRGQGEVNVTLT 132
                         90
                 ....*....|.
gi 695817689 158 CAGQLVQPGDV 168
Cdd:PRK12487 133 MGNVIIEPGDM 143
 
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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