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Conserved domains on  [gi|501740221|ref|WP_012631205|]
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pyrroline-5-carboxylate reductase [Methylobacterium nodulans]

Protein Classification

pyrroline-5-carboxylate reductase family protein( domain architecture ID 11417420)

pyrroline-5-carboxylate reductase family protein similar to pyrroline-5-carboxylate reductase that catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline

CATH:  1.10.3730.10|3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0004735|GO:0055129

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 12-243 1.80e-29

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


:

Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 112.85  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  12 PTVGLIGLGRIGMVLLAAL-RRFAPETRVIAAGRDPARVAAATAAWpGVEVMDSERLAV-HANVVVPCLPPEAYRDGVSA 89
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLlKSGVPPEDIIVSDRSPERLEALAERY-GVRVTTDNAEAAaQADVVVLAVKPQDLAEVLEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  90 VAPHMRADAVLMSVTNAVPLPDLGCRC--ARPIVKVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLADP 167
Cdd:COG0345   82 LAPLLDPDKLVISIAAGVTLATLEEALggGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 168 ADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:COG0345  162 ELMDAVTALSGSGPAYVFLFIEAM--ADAGVALGLPRETARELAAQTVLGAAKLLLEsGEHPAELRDRVTSPGGTTI 236
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 12-243 1.80e-29

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 112.85  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  12 PTVGLIGLGRIGMVLLAAL-RRFAPETRVIAAGRDPARVAAATAAWpGVEVMDSERLAV-HANVVVPCLPPEAYRDGVSA 89
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLlKSGVPPEDIIVSDRSPERLEALAERY-GVRVTTDNAEAAaQADVVVLAVKPQDLAEVLEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  90 VAPHMRADAVLMSVTNAVPLPDLGCRC--ARPIVKVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLADP 167
Cdd:COG0345   82 LAPLLDPDKLVISIAAGVTLATLEEALggGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 168 ADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:COG0345  162 ELMDAVTALSGSGPAYVFLFIEAM--ADAGVALGLPRETARELAAQTVLGAAKLLLEsGEHPAELRDRVTSPGGTTI 236
PRK07680 PRK07680
late competence protein ComER; Validated
 14-242 1.83e-17

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 80.40  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  14 VGLIGLGRIGMVLLAAL--RRFAPETRVIAAGRDPARVAAATAAWPGVEVMDS-ERLAVHANVVVPCLPPEAYRDGVSAV 90
Cdd:PRK07680   3 IGFIGTGNMGTILIEAFleSGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTiEEVISQSDLIFICVKPLDIYPLLQKL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  91 APHMRADAVLMSVTNAVPLPDL----GCRCARpivkVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLAD 166
Cdd:PRK07680  83 APHLTDEHCLVSITSPISVEQLetlvPCQVAR----IIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 167 PADGRIASNLAGSAPAILAAFCSAFLEAnAARARAFGPTELRAMMTESVAALAAILDEGL-SFEDVVARTATPGGTT 242
Cdd:PRK07680 159 EDITRVSSDIVSCGPAFFSYLLQRFIDA-AVEETNISKEEATTLASEMLIGMGKLLEKGLyTLPTLQEKVCVKGGIT 234
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 58-243 6.53e-08

pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 272911 [Multi-domain]  Cd Length: 245  Bit Score: 52.65  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221   58 GVEVM-DSERLAVHANVVVPCLPPEAYRDGVSAVAPHMRADAVLMSVTNAVPLPDLGCR--CARPIVKVILSPAHAAGRG 134
Cdd:TIGR00112  30 GIVASsDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLlgGTRRVVRVMPNTPAKVGAG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  135 VCLVTPSPGAGPEQVERICALLQRFCRPVLADPADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTES 214
Cdd:TIGR00112 110 VTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEAL--ADAGVKQGLPRELALELAAQT 187

                         170       180       190
                  ....*....|....*....|....*....|
gi 501740221  215 VAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:TIGR00112 188 VKGAAKLLEEsGEHPALLKDQVTSPGGTTI 217
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 172-243 3.56e-05

Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 464294 [Multi-domain]  Cd Length: 104  Bit Score: 42.00  E-value: 3.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501740221  172 IASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAA-ILDEGLSFEDVVARTATPGGTTE 243
Cdd:pfam14748   6 AVTALSGSGPAYVFLFIEAL--ADAGVAMGLPREEARELAAQTVLGAAKlLLTSGEHPAELRDKVTSPGGTTI 76
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 12-243 1.80e-29

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 112.85  E-value: 1.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  12 PTVGLIGLGRIGMVLLAAL-RRFAPETRVIAAGRDPARVAAATAAWpGVEVMDSERLAV-HANVVVPCLPPEAYRDGVSA 89
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLlKSGVPPEDIIVSDRSPERLEALAERY-GVRVTTDNAEAAaQADVVVLAVKPQDLAEVLEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  90 VAPHMRADAVLMSVTNAVPLPDLGCRC--ARPIVKVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLADP 167
Cdd:COG0345   82 LAPLLDPDKLVISIAAGVTLATLEEALggGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVDE 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 168 ADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:COG0345  162 ELMDAVTALSGSGPAYVFLFIEAM--ADAGVALGLPRETARELAAQTVLGAAKLLLEsGEHPAELRDRVTSPGGTTI 236
PRK07680 PRK07680
late competence protein ComER; Validated
 14-242 1.83e-17

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 80.40  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  14 VGLIGLGRIGMVLLAAL--RRFAPETRVIAAGRDPARVAAATAAWPGVEVMDS-ERLAVHANVVVPCLPPEAYRDGVSAV 90
Cdd:PRK07680   3 IGFIGTGNMGTILIEAFleSGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTiEEVISQSDLIFICVKPLDIYPLLQKL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  91 APHMRADAVLMSVTNAVPLPDL----GCRCARpivkVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLAD 166
Cdd:PRK07680  83 APHLTDEHCLVSITSPISVEQLetlvPCQVAR----IIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501740221 167 PADGRIASNLAGSAPAILAAFCSAFLEAnAARARAFGPTELRAMMTESVAALAAILDEGL-SFEDVVARTATPGGTT 242
Cdd:PRK07680 159 EDITRVSSDIVSCGPAFFSYLLQRFIDA-AVEETNISKEEATTLASEMLIGMGKLLEKGLyTLPTLQEKVCVKGGIT 234
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 13-280 6.86e-17

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 79.04  E-value: 6.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  13 TVGLIGLGRIGMVLLAAL---RRFAPETRVIAAGRDPARVAAATAAWPGVEVMDSE-RLAVHANVVVPCLPPEAYRDGVS 88
Cdd:PRK06928   3 KIGFIGYGSMADMIATKLletEVATPEEIILYSSSKNEHFNQLYDKYPTVELADNEaEIFTKCDHSFICVPPLAVLPLLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  89 AVAPHMRADAVLMSVTNAVPLPDL-GCRCARPIVKVILSPAHAAGRGVCLVTPSPGAGPEQVERICALLQRFCRPVLADP 167
Cdd:PRK06928  83 DCAPVLTPDRHVVSIAAGVSLDDLlEITPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIRE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 168 ADGRIASNLAGSAPAILAAFCSAFLEAnAARARAFGPTELRAMMTESVAALAAIL-DEGLSFEDVVARTATPGGTTEAAI 246
Cdd:PRK06928 163 ENMDIASNLTSSSPGFIAAIFEEFAEA-AVRNSSLSDEEAFQFLNFALAGTGKLLvEEDYTFSGTIERVATKGGITAEGA 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 501740221 247 AALNAEAPALCGRLVDATFQREAQLL-AIPPRTRD 280
Cdd:PRK06928 242 EVIQAQLPQFFDELLDRTQKKYASSKkEIQAQKRD 276
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 13-243 1.89e-09

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 57.08  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  13 TVGLIGLGRIGMVLLAAL-RRFAPETRVIAAGRDPARVAAATAAWpGVEVM-DSERLAVHANVVVPCLPPEAYRDGVSAV 90
Cdd:PRK11880   4 KIGFIGGGNMASAIIGGLlASGVPAKDIIVSDPSPEKRAALAEEY-GVRAAtDNQEAAQEADVVVLAVKPQVMEEVLSEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  91 APHmrADAVLMSVTNAVPLPDLGCRC--ARPIVKVIlsPAHAA--GRGVCLVTPSPGAGPEQVERICALLQRFCRPV-LA 165
Cdd:PRK11880  83 KGQ--LDKLVVSIAAGVTLARLERLLgaDLPVVRAM--PNTPAlvGAGMTALTANALVSAEDRELVENLLSAFGKVVwVD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221 166 DPADGRIASNLAGSAPAilaaFCSAFLEANAARARAFG-PTEL-RAMMTESVAALAAILDE-GLSFEDVVARTATPGGTT 242
Cdd:PRK11880 159 DEKQMDAVTAVSGSGPA----YVFLFIEALADAGVKLGlPREQaRKLAAQTVLGAAKLLLEsGEHPAELRDNVTSPGGTT 234


                 .
gi 501740221 243 E 243
Cdd:PRK11880 235 I 235
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 13-169 7.08e-09

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 55.52  E-value: 7.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  13 TVGLIGLGRIGMVLLAALRRFAPETRVIAAGRDPARVAAATAAwpGV--EVMDSERLAVH-ANVVVPCLPPEAYRDGVSA 89
Cdd:COG0287    3 RIAIIGLGLIGGSLALALKRAGLAHEVVGVDRSPETLERALEL--GVidRAATDLEEAVAdADLVVLAVPVGATIEVLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  90 VAPHMRADAVLM---SVTNAVplpdlgCRCARPIVKVILS--PAH-AAGR---GV------------CLVTPSPGAGPEQ 148
Cdd:COG0287   81 LAPHLKPGAIVTdvgSVKGAV------VEAAEALLPDGVRfvGGHpMAGTeksGPeaadadlfegapYILTPTEGTDPEA 154

                        170       180
                 ....*....|....*....|..
gi 501740221 149 VERICALLQRF-CRPVLADPAD 169
Cdd:COG0287  155 LERVEELWEALgARVVEMDPEE 176
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 58-243 6.53e-08

pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 272911 [Multi-domain]  Cd Length: 245  Bit Score: 52.65  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221   58 GVEVM-DSERLAVHANVVVPCLPPEAYRDGVSAVAPHMRADAVLMSVTNAVPLPDLGCR--CARPIVKVILSPAHAAGRG 134
Cdd:TIGR00112  30 GIVASsDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLlgGTRRVVRVMPNTPAKVGAG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  135 VCLVTPSPGAGPEQVERICALLQRFCRPVLADPADGRIASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTES 214
Cdd:TIGR00112 110 VTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEAL--ADAGVKQGLPRELALELAAQT 187

                         170       180       190
                  ....*....|....*....|....*....|
gi 501740221  215 VAALAAILDE-GLSFEDVVARTATPGGTTE 243
Cdd:TIGR00112 188 VKGAAKLLEEsGEHPALLKDQVTSPGGTTI 217
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
12-159 3.27e-05

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 44.58  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  12 PTVGLIGLGRIGMVLLAALRRFAPETRVIAAGRDPARVAAATAAWPGVEVMDSERLAVH-ANVVVPCLPPEAYRDGVSAV 90
Cdd:PRK07502   7 DRVALIGIGLIGSSLARAIRRLGLAGEIVGADRSAETRARARELGLGDRVTTSAAEAVKgADLVILCVPVGASGAVAAEI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221  91 APHMRADAVLM---SVTNAV------PLPDlgcrcarpivKVILSPAHA-AG--------------RGV-CLVTPSPGAG 145
Cdd:PRK07502  87 APHLKPGAIVTdvgSVKASViaamapHLPE----------GVHFIPGHPlAGtehsgpdagfaelfENRwCILTPPEGTD 156

                        170
                 ....*....|....
gi 501740221 146 PEQVERICALLQRF 159
Cdd:PRK07502 157 PAAVARLTAFWRAL 170
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 172-243 3.56e-05

Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 464294 [Multi-domain]  Cd Length: 104  Bit Score: 42.00  E-value: 3.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501740221  172 IASNLAGSAPAILAAFCSAFleANAARARAFGPTELRAMMTESVAALAA-ILDEGLSFEDVVARTATPGGTTE 243
Cdd:pfam14748   6 AVTALSGSGPAYVFLFIEAL--ADAGVAMGLPREEARELAAQTVLGAAKlLLTSGEHPAELRDKVTSPGGTTI 76
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
15-105 1.71e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 36.83  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221   15 GLIGLGRIGMVLLAALRRFAPETRVIAAGRDPARVAAATAAW-PGVEVMDSERLAVHANVVVPCLPPEAYRDGVSAvAPH 93
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHEVVVANSRNPEKAEELAEEYgVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSE-LSD 79

                          90
                  ....*....|..
gi 501740221   94 MRADAVLMSVTN 105
Cdd:pfam03807  80 LLKGKIVISIAA 91
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 29-147 1.96e-03

Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face.


Pssm-ID: 460467 [Multi-domain]  Cd Length: 154  Bit Score: 38.14  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501740221   29 ALRRFAPETRVIAAGRDPARVAAATAAWPGVEVMDSERLAVHANVVVPCLPPEAYRDGVSAVAPHMRADAVLMSVTNavp 108
Cdd:pfam02153   4 ALRRHGFFVTVIGYDINPEAAVAALRLGLGDEATDDIEAVREADIVFLAVPVEQTLPVLKELAPHLKEDALITDVGS--- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 501740221  109 lpdlgcrcarpiVKVILS-PAHAAGRGVCLVTPSPGAGPE 147
Cdd:pfam02153  81 ------------VKVKIIrELEQHLPDKSFVPGHPMAGTE 108
 
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.
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