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Conserved domains on  [gi|446878987|ref|WP_000956243|]
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MULTISPECIES: pyrroline-5-carboxylate reductase [Bacillus]

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]; ...
 3-265 3.02e-94

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: 278.10  E-value: 3.02e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   3 TKHRILFIGAGRMAEAIFSGLLKTSKEyIEEIIVSNRSnIEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQL 82
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKSGVP-PEDIIVSDRS-PERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  83 LQELSPLLTE-QFVVTVAAGIGPSYLEKRLPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQF 161
Cdd:COG0345   79 LEELAPLLDPdKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVW 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 162 CTEEEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQN-EDPAMLREQVTTPGGSTAEG 240
Cdd:COG0345  159 VDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESgEHPAELRDRVTSPGGTTIAG 238

                        250       260
                 ....*....|....*....|....*
gi 446878987 241 LKVLYENNFSEVIQQAVEATNKKAR 265
Cdd:COG0345  239 LKVLEEGGLRAAVIEAVEAAAERSK 263
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 3-265 3.02e-94

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: 278.10  E-value: 3.02e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   3 TKHRILFIGAGRMAEAIFSGLLKTSKEyIEEIIVSNRSnIEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQL 82
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKSGVP-PEDIIVSDRS-PERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  83 LQELSPLLTE-QFVVTVAAGIGPSYLEKRLPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQF 161
Cdd:COG0345   79 LEELAPLLDPdKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVW 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 162 CTEEEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQN-EDPAMLREQVTTPGGSTAEG 240
Cdd:COG0345  159 VDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESgEHPAELRDRVTSPGGTTIAG 238

                        250       260
                 ....*....|....*....|....*
gi 446878987 241 LKVLYENNFSEVIQQAVEATNKKAR 265
Cdd:COG0345  239 LKVLEEGGLRAAVIEAVEAAAERSK 263
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 6-265 2.24e-75

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 230.03  E-value: 2.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   6 RILFIGAGRMAEAIFSGLLKtSKEYIEEIIVSNRsNIEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQLLQE 85
Cdd:PRK11880   4 KIGFIGGGNMASAIIGGLLA-SGVPAKDIIVSDP-SPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  86 LSPLLtEQFVVTVAAGIGPSYLEKRLPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTS-QFCTE 164
Cdd:PRK11880  82 LKGQL-DKLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVvWVDDE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 165 EEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQN-EDPAMLREQVTTPGGSTAEGLKV 243
Cdd:PRK11880 161 KQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESgEHPAELRDNVTSPGGTTIAALRV 240

                        250       260
                 ....*....|....*....|..
gi 446878987 244 LYENNFSEVIQQAVEATNKKAR 265
Cdd:PRK11880 241 LEEKGLRAAVIEAVQAAAKRSK 262
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 32-265 1.14e-57

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: 184.38  E-value: 1.14e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   32 EEIIVSNRSNiEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQLLQELSPLLTE-QFVVTVAAGIGPSYLEKR 110
Cdd:TIGR00112  10 YDIYVINRSP-EKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKdKLLISIAAGVTLEKLSQL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  111 LPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQFCTEEEVHQLTAITGSAPAFLYHFAEGLIE 190
Cdd:TIGR00112  89 LGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALAD 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446878987  191 ATKNYGIDEKTANHLVIQMIAGSAAMLQQ-NEDPAMLREQVTTPGGSTAEGLKVLYENNFSEVIQQAVEATNKKAR 265
Cdd:TIGR00112 169 AGVKQGLPRELALELAAQTVKGAAKLLEEsGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSR 244
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 164-265 3.64e-36

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: 124.43  E-value: 3.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  164 EEEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQN-EDPAMLREQVTTPGGSTAEGLK 242
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSgEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|...
gi 446878987  243 VLYENNFSEVIQQAVEATNKKAR 265
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAK 103
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 3-265 3.02e-94

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: 278.10  E-value: 3.02e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   3 TKHRILFIGAGRMAEAIFSGLLKTSKEyIEEIIVSNRSnIEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQL 82
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKSGVP-PEDIIVSDRS-PERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  83 LQELSPLLTE-QFVVTVAAGIGPSYLEKRLPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQF 161
Cdd:COG0345   79 LEELAPLLDPdKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVW 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 162 CTEEEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQN-EDPAMLREQVTTPGGSTAEG 240
Cdd:COG0345  159 VDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESgEHPAELRDRVTSPGGTTIAG 238

                        250       260
                 ....*....|....*....|....*
gi 446878987 241 LKVLYENNFSEVIQQAVEATNKKAR 265
Cdd:COG0345  239 LKVLEEGGLRAAVIEAVEAAAERSK 263
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 6-265 2.24e-75

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 230.03  E-value: 2.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   6 RILFIGAGRMAEAIFSGLLKtSKEYIEEIIVSNRsNIEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQLLQE 85
Cdd:PRK11880   4 KIGFIGGGNMASAIIGGLLA-SGVPAKDIIVSDP-SPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  86 LSPLLtEQFVVTVAAGIGPSYLEKRLPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTS-QFCTE 164
Cdd:PRK11880  82 LKGQL-DKLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVvWVDDE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 165 EEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQN-EDPAMLREQVTTPGGSTAEGLKV 243
Cdd:PRK11880 161 KQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESgEHPAELRDNVTSPGGTTIAALRV 240

                        250       260
                 ....*....|....*....|..
gi 446878987 244 LYENNFSEVIQQAVEATNKKAR 265
Cdd:PRK11880 241 LEEKGLRAAVIEAVQAAAKRSK 262
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 7-264 4.67e-58

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 186.51  E-value: 4.67e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   7 ILFIGAGRMAEAIFSGLLKTSKEYIEEIIVSNRSNIEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQLLQEL 86
Cdd:PRK07679   6 ISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALIPF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  87 SPLLTE-QFVVTVAAGIGPSYLEKRLPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQFCTEE 165
Cdd:PRK07679  86 KEYIHNnQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVSVVEEE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 166 EVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQNED-PAMLREQVTTPGGSTAEGLKVL 244
Cdd:PRK07679 166 DMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKhPSILRKEITSPGGTTEAGIEVL 245

                        250       260
                 ....*....|....*....|
gi 446878987 245 YENNFSEVIQQAVEATNKKA 264
Cdd:PRK07679 246 QEHRFQQALISCITQATQRS 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 32-265 1.14e-57

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: 184.38  E-value: 1.14e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   32 EEIIVSNRSNiEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQLLQELSPLLTE-QFVVTVAAGIGPSYLEKR 110
Cdd:TIGR00112  10 YDIYVINRSP-EKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKdKLLISIAAGVTLEKLSQL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  111 LPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQFCTEEEVHQLTAITGSAPAFLYHFAEGLIE 190
Cdd:TIGR00112  89 LGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFLFIEALAD 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446878987  191 ATKNYGIDEKTANHLVIQMIAGSAAMLQQ-NEDPAMLREQVTTPGGSTAEGLKVLYENNFSEVIQQAVEATNKKAR 265
Cdd:TIGR00112 169 AGVKQGLPRELALELAAQTVKGAAKLLEEsGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAVRRSR 244
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 6-265 5.82e-43

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 147.03  E-value: 5.82e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   6 RILFIGAGRMAEAIFSGLLKTSKEYIEEIIVSNRSNIEKLEQLQgRYNVSITTDWKQHITSVDTIVLAMPPAAHEQLLQE 85
Cdd:PLN02688   2 RVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRDVFQ-SLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  86 LSPLLTE-QFVVTVAAGIGPSYLEKRLPQGtPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQFCTE 164
Cdd:PLN02688  81 LRPLLSKdKLLVSVAAGITLADLQEWAGGR-RVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 165 EEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAM-LQQNEDPAMLREQVTTPGGSTAEGLKV 243
Cdd:PLN02688 160 KLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMvLETGKHPGQLKDMVTSPGGTTIAGVHE 239

                        250       260
                 ....*....|....*....|..
gi 446878987 244 LYENNFSEVIQQAVEATNKKAR 265
Cdd:PLN02688 240 LEKGGFRAALMNAVVAAAKRSR 261
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 164-265 3.64e-36

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: 124.43  E-value: 3.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  164 EEEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQN-EDPAMLREQVTTPGGSTAEGLK 242
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSgEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|...
gi 446878987  243 VLYENNFSEVIQQAVEATNKKAR 265
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAK 103
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 6-265 3.69e-31

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 116.20  E-value: 3.69e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   6 RILFIGAGRMAEAIFSGLlktskeyieeiivsNRSNIEKLEQL--QGRYNVSITTDWKQHITSV----DTIVLAMPPAAH 79
Cdd:PTZ00431   5 RVGFIGLGKMGSALAYGI--------------ENSNIIGKENIyyHTPSKKNTPFVYLQSNEELaktcDIIVLAVKPDLA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  80 EQLLQELSPLLTEQFVVTVAAGIGPSYLEKRLPQGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTS 159
Cdd:PTZ00431  71 GKVLLEIKPYLGSKLLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGII 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 160 QFCTEEEVHQLTAITGSAPAFLYHFAEGLIEATKNYGIDEKTANHLVIQMIAGSAAMLQQNEDPA-MLREQVTTPGGSTA 238
Cdd:PTZ00431 151 QEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVqQLKDDVCSPGGITI 230

                        250       260
                 ....*....|....*....|....*..
gi 446878987 239 EGLKVLYENNFSEVIQQAVEATNKKAR 265
Cdd:PTZ00431 231 VGLYTLEKHAFKYTVMDAVESACQKSK 257
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 6-263 8.25e-25

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 99.84  E-value: 8.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   6 RILFIGAGRMAEAIFSGLLKTSKEYIEEIIVSNRSNIEKLEQLQGRY-NVSITTDWKQHITSVDTIVLAMPPAAHEQLLQ 84
Cdd:PRK06928   3 KIGFIGYGSMADMIATKLLETEVATPEEIILYSSSKNEHFNQLYDKYpTVELADNEAEIFTKCDHSFICVPPLAVLPLLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  85 ELSPLLT-EQFVVTVAAGIGPSYLEKRLPqGTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQFCT 163
Cdd:PRK06928  83 DCAPVLTpDRHVVSIAAGVSLDDLLEITP-GLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 164 EEEVHQLTAITGSAPAFLYHFAEGLIEAT-KNYGIDEKTANHLVIQMIAGSAAML-QQNEDPAMLREQVTTPGGSTAEGL 241
Cdd:PRK06928 162 EENMDIASNLTSSSPGFIAAIFEEFAEAAvRNSSLSDEEAFQFLNFALAGTGKLLvEEDYTFSGTIERVATKGGITAEGA 241

                        250       260
                 ....*....|....*....|..
gi 446878987 242 KVLyENNFSEVIQQAVEATNKK 263
Cdd:PRK06928 242 EVI-QAQLPQFFDELLDRTQKK 262
PRK07680 PRK07680
late competence protein ComER; Validated
 6-255 3.46e-23

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 95.42  E-value: 3.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   6 RILFIGAGRMAEAIFSGLLKTSKEYIEEIIVSNRSnIEKLEQLQGRY-NVSITTDWKQHITSVDTIVLAMPPAAHEQLLQ 84
Cdd:PRK07680   2 NIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRT-PAKAYHIKERYpGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  85 ELSPLLT-EQFVVTVAAGIGPSYLEKRLPqgTPVAWIMPNTAAEIGKSISLYTTGHSVGETHQETLQLLLKGIGTSQFCT 163
Cdd:PRK07680  81 KLAPHLTdEHCLVSITSPISVEQLETLVP--CQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 164 EEEVHQLTAITGSAPAFLYHFAEGLIE-ATKNYGIDEKTANHLVIQMIAGSAAMLQQNE-DPAMLREQVTTPGGSTAEGL 241
Cdd:PRK07680 159 EDITRVSSDIVSCGPAFFSYLLQRFIDaAVEETNISKEEATTLASEMLIGMGKLLEKGLyTLPTLQEKVCVKGGITGEGI 238

                        250
                 ....*....|....*..
gi 446878987 242 KVLYEN---NFSEVIQQ 255
Cdd:PRK07680 239 KVLEEEvgdMFHRLFQR 255
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
9-101 6.02e-18

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 76.50  E-value: 6.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987    9 FIGAGRMAEAIFSGLLKTSKEyieEIIVSNRSNIEKLEQLQGRYNVSITT-DWKQHITSVDTIVLAMPPAAHEQLLQELS 87
Cdd:pfam03807   2 FIGAGNMGEALARGLVAAGPH---EVVVANSRNPEKAEELAEEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSELS 78

                          90
                  ....*....|....
gi 446878987   88 PLLTEQFVVTVAAG 101
Cdd:pfam03807  79 DLLKGKIVISIAAG 92
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 6-267 2.77e-14

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 70.43  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   6 RILFIGAGRMAEAIFSGLLkTSKEYIEEIIVSNRsNIEKLEQLQGRYN-VSITTDWKQHITSVDTIVLAMPPAAHEQLLQ 84
Cdd:PRK06476   2 KIGFIGTGAITEAMVTGLL-TSPADVSEIIVSPR-NAQIAARLAERFPkVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  85 ELSpLLTEQFVVTVAAGIGPSYLEKrlpqgtpvaWImpNTAAEIGKSISLYTTGHSVGET----HQETLQLLLKGIGTSQ 160
Cdd:PRK06476  80 ALR-FRPGQTVISVIAATDRAALLE---------WI--GHDVKLVRAIPLPFVAERKGVTaiypPDPFVAALFDALGTAV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987 161 FCTEEEVHQLTAITGSAPAFLYhfaeGLIEATKNY----GIDEKTANHLVIQMIAG--SAAMLQQNEDPAMLREQVTTPG 234
Cdd:PRK06476 148 ECDSEEEYDLLAAASALMATYF----GILETATGWleeqGLKRQKARAYLAPLFASlaQDAVRSTKTDFSALSREFSTKG 223

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446878987 235 GSTAEGLKVLYENNFSEVIQQAVEATNKKARGK 267
Cdd:PRK06476 224 GLNEQVLNDFSRQGGYAALTDALDRVLRRINGR 256
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 6-130 8.25e-06

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 46.18  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   6 RILFIGAGRMAEAIFSGLLK---------TSKEYIEEIIvSNRSNIekleqlqgRY--------NVSITTDWKQHITSVD 68
Cdd:COG0240    2 KIAVLGAGSWGTALAKVLARnghevtlwgRDPEVAEEIN-ETRENP--------RYlpgvklpeNLRATSDLEEALAGAD 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446878987  69 TIVLAMPPAAHEQLLQELSPLLTE-QFVVTVAAGIGPS-------YLEKRLPQGTPVAWIM-PNTAAEIGK 130
Cdd:COG0240   73 LVLLAVPSQALREVLEQLAPLLPPgAPVVSATKGIEPGtgllmseVIAEELPGALRIAVLSgPSFAEEVAR 143
MviM COG0673
Predicted dehydrogenase [General function prediction only];
6-82 3.91e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 41.06  E-value: 3.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446878987   6 RILFIGAGRMAEAIFSGLLKTSKeyIEEIIVSNRsNIEKLEQLQGRYNVSITTDWKQHITS--VDTIVLAMPPAAHEQL 82
Cdd:COG0673    5 RVGIIGAGGIGRAHAPALAALPG--VELVAVADR-DPERAEAFAEEYGVRVYTDYEELLADpdIDAVVIATPNHLHAEL 80
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
53-130 2.83e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 38.51  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987  53 NVSITTDWKQHITSVDTIVLAMPPAAHEQLLQELSPLLTE-QFVVTVAAGIGPSY-------LEKRLPQGTPVAWIM-PN 123
Cdd:PRK00094  58 NLRATTDLAEALADADLILVAVPSQALREVLKQLKPLLPPdAPIVWATKGIEPGTgkllsevLEEELPDLAPIAVLSgPS 137


                 ....*..
gi 446878987 124 TAAEIGK 130
Cdd:PRK00094 138 FAKEVAR 144
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 2-71 4.17e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 38.24  E-value: 4.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446878987   2 LTKHRILFIGAGRMAEAIFSGLLktsKEYIEEIIVSNRSnIEKLEQLQGRYNVSITT--DWKQHITSVDTIV 71
Cdd:PRK00045 180 LSGKKVLVIGAGEMGELVAKHLA---EKGVRKITVANRT-LERAEELAEEFGGEAIPldELPEALAEADIVI 247
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 3-96 5.82e-03

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 37.48  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   3 TKHRILFIGAGRMAEAIFSGLLKtsKEYieEII-VSNRSnIEKLEQLQGRYNVSITTDWKQHITSVDTIVLAMPPAAHEQ 81
Cdd:COG5495    2 ARMKIGIIGAGRVGTALAAALRA--AGH--EVVgVYSRS-PASAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAE 76

                         90
                 ....*....|....*...
gi 446878987  82 LLQELSP---LLTEQFVV 96
Cdd:COG5495   77 VAAGLAAagaLRPGQLVV 94
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 2-96 5.96e-03

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 37.43  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446878987   2 LTKHRILFIGAGRMAEAIFSGLLktsKEYIEEIIVSNRsNIEKLEQLQGRYNVSITT--DWKQHITSVDTIVLAMPPAAH 79
Cdd:COG0169  119 LAGKRVLVLGAGGAARAVAAALA---EAGAAEITIVNR-TPERAEALAARLGVRAVPldDLAAALAGADLVINATPLGMA 194

                         90
                 ....*....|....*...
gi 446878987  80 EQLLQELSP-LLTEQFVV 96
Cdd:COG0169  195 GGDALPLPAsLLAPGAVV 212
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 6-73 9.37e-03

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 35.63  E-value: 9.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446878987    6 RILFIGAGRMAEAIFSGLLktSKEyIEEIIVSNRSnIEKLEQLQGRYNVSIT---TDWKQHITSVDTIVLA 73
Cdd:pfam01488  14 KVLLIGAGEMGELVAKHLL--AKG-AKEVTIANRT-IERAQELAEKFGGVEAlplDDLKEYLAEADIVISA 80
 
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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