|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-267 |
2.76e-128 |
|
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: 364.77 E-value: 2.76e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 1 MNKQIGFIGCGNMGIAMIGGMIKkNIVSPDQIICSDLNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVI 80
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLK-SGVPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 81 NQIKDQIKNDVIVVTIAAGKSIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVV 160
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 161 NEKLMDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAV 240
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239
|
250 260
....*....|....*....|....*..
gi 1000870713 241 ATLEEKGLRTAIISAMKRCTKKSMEMS 267
Cdd:COG0345 240 KVLEEGGLRAAVIEAVEAAAERSKELG 266
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-269 |
1.54e-123 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 352.53 E-value: 1.54e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 1 MNKQIGFIGCGNMGIAMIGGMIKKNiVSPDQIICSDLNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVI 80
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 81 NQIKDQIknDVIVVTIAAGKSIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVV 160
Cdd:PRK11880 80 SELKGQL--DKLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 161 -NEKLMDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEA 239
Cdd:PRK11880 158 dDEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAA 237
|
250 260 270
....*....|....*....|....*....|
gi 1000870713 240 VATLEEKGLRTAIISAMKRCTKKSMEMSSL 269
Cdd:PRK11880 238 LRVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
21-265 |
1.94e-91 |
|
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: 270.67 E-value: 1.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 21 MIKKNIVSPDQIICSDLNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVINQIKDQIKNDVIVVTIAAGK 100
Cdd:TIGR00112 1 LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 101 SIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVVNEKLMDVVTSISGSSPAYVY 180
Cdd:TIGR00112 81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 181 MFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAVATLEEKGLRTAIISAMKRCT 260
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240
|
....*
gi 1000870713 261 KKSME 265
Cdd:TIGR00112 241 RRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
162-265 |
1.24e-57 |
|
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: 179.51 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 162 EKLMDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAVA 241
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1000870713 242 TLEEKGLRTAIISAMKRCTKKSME 265
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-267 |
2.76e-128 |
|
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: 364.77 E-value: 2.76e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 1 MNKQIGFIGCGNMGIAMIGGMIKkNIVSPDQIICSDLNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVI 80
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLK-SGVPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 81 NQIKDQIKNDVIVVTIAAGKSIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVV 160
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 161 NEKLMDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAV 240
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239
|
250 260
....*....|....*....|....*..
gi 1000870713 241 ATLEEKGLRTAIISAMKRCTKKSMEMS 267
Cdd:COG0345 240 KVLEEGGLRAAVIEAVEAAAERSKELG 266
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-269 |
1.54e-123 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 352.53 E-value: 1.54e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 1 MNKQIGFIGCGNMGIAMIGGMIKKNiVSPDQIICSDLNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVI 80
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 81 NQIKDQIknDVIVVTIAAGKSIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVV 160
Cdd:PRK11880 80 SELKGQL--DKLVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 161 -NEKLMDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEA 239
Cdd:PRK11880 158 dDEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAA 237
|
250 260 270
....*....|....*....|....*....|
gi 1000870713 240 VATLEEKGLRTAIISAMKRCTKKSMEMSSL 269
Cdd:PRK11880 238 LRVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
5-267 |
3.25e-100 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 293.40 E-value: 3.25e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 5 IGFIGCGNMGIAMIGGMIKKNIVSPDQIICSDLNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVINQIK 84
Cdd:PLN02688 3 VGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 85 DQIKNDVIVVTIAAGKSIKSTEnEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVVNEKL 164
Cdd:PLN02688 83 PLLSKDKLLVSVAAGITLADLQ-EWAGGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 165 MDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAVATLE 244
Cdd:PLN02688 162 LDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHELE 241
|
250 260
....*....|....*....|...
gi 1000870713 245 EKGLRTAIISAMKRCTKKSMEMS 267
Cdd:PLN02688 242 KGGFRAALMNAVVAAAKRSRELS 264
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
21-265 |
1.94e-91 |
|
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: 270.67 E-value: 1.94e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 21 MIKKNIVSPDQIICSDLNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVINQIKDQIKNDVIVVTIAAGK 100
Cdd:TIGR00112 1 LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 101 SIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVVNEKLMDVVTSISGSSPAYVY 180
Cdd:TIGR00112 81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 181 MFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAVATLEEKGLRTAIISAMKRCT 260
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240
|
....*
gi 1000870713 261 KKSME 265
Cdd:TIGR00112 241 RRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
162-265 |
1.24e-57 |
|
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: 179.51 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 162 EKLMDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAVA 241
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1000870713 242 TLEEKGLRTAIISAMKRCTKKSME 265
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| PTZ00431 |
PTZ00431 |
pyrroline carboxylate reductase; Provisional |
2-266 |
6.13e-57 |
|
pyrroline carboxylate reductase; Provisional
Pssm-ID: 173621 [Multi-domain] Cd Length: 260 Bit Score: 183.23 E-value: 6.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 2 NKQIGFIGCGNMGIAMIGGMIKKNIVSPDqiicsdlNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVIN 81
Cdd:PTZ00431 3 NIRVGFIGLGKMGSALAYGIENSNIIGKE-------NIYYHTPSKKNTPFVYLQSNEELAKTCDIIVLAVKPDLAGKVLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 82 QIKDQIKNDVIVvTIAAGKSIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVVN 161
Cdd:PTZ00431 76 EIKPYLGSKLLI-SICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQEIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 162 EKLMDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAVA 241
Cdd:PTZ00431 155 EKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIVGLY 234
|
250 260
....*....|....*....|....*
gi 1000870713 242 TLEEKGLRTAIISAMKRCTKKSMEM 266
Cdd:PTZ00431 235 TLEKHAFKYTVMDAVESACQKSKSM 259
|
|
| PRK07679 |
PRK07679 |
pyrroline-5-carboxylate reductase; Reviewed |
3-266 |
5.59e-56 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 181079 [Multi-domain] Cd Length: 279 Bit Score: 181.12 E-value: 5.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 3 KQIGFIGCGNMGIAMIGGMIKKNIVSPDQIICSD-LNVINLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVIN 81
Cdd:PRK07679 4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNrSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 82 QIKDQIKNDVIVVTIAAGKSIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEVVN 161
Cdd:PRK07679 84 PFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVSVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 162 EKLMDVVTSISGSSPAYVYMFIEAMADAAVLDGMPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTIEAVA 241
Cdd:PRK07679 164 EEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEAGIE 243
|
250 260
....*....|....*....|....*
gi 1000870713 242 TLEEKGLRTAIISAMKRCTKKSMEM 266
Cdd:PRK07679 244 VLQEHRFQQALISCITQATQRSHNL 268
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
1-245 |
6.78e-27 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 105.44 E-value: 6.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 1 MNkqIGFIGCGNMGIAMIGGMIKKNIVSPDQIICSDLNVINLKNASNEY-GIIITTNNNEVANSADILILSIKPDLYTSV 79
Cdd:PRK07680 1 MN--IGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYpGIHVAKTIEEVISQSDLIFICVKPLDIYPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 80 INQIKDQIKNDVIVVTIAAGKSIKSTENEFgrKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTEV 159
Cdd:PRK07680 79 LQKLAPHLTDEHCLVSITSPISVEQLETLV--PCQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 160 VNEKLMDVVTSISGSSPAYVYMFIEAMADAAVLD-GMPRKQAYKFAAQAVLGSAKMvLETGIH-PGELKDMVCSPGGTTI 237
Cdd:PRK07680 157 IEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKL-LEKGLYtLPTLQEKVCVKGGITG 235
|
....*...
gi 1000870713 238 EAVATLEE 245
Cdd:PRK07680 236 EGIKVLEE 243
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
1-245 |
3.29e-24 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 98.30 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 1 MNKqIGFIGCGNMGIAMIGGMIKKNIVSPDQIIC-SDLNVINLKNASNEY-GIIITTNNNEVANSADILILSIKPDLYTS 78
Cdd:PRK06928 1 MEK-IGFIGYGSMADMIATKLLETEVATPEEIILySSSKNEHFNQLYDKYpTVELADNEAEIFTKCDHSFICVPPLAVLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 79 VINQIKDQIKNDVIVVTIAAGKSIkSTENEFGRKLKVVRVMPNTPVLVGEGMSALSFNEMVTEKDIKEVLTIFNIFGQTE 158
Cdd:PRK06928 80 LLKDCAPVLTPDRHVVSIAAGVSL-DDLLEITPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 159 VVNEKLMDVVTSISGSSPAYVYMFIEAMADAAVLDG-MPRKQAYKFAAQAVLGSAKMVLETGIHPGELKDMVCSPGGTTI 237
Cdd:PRK06928 159 TIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGITA 238
|
....*...
gi 1000870713 238 EAVATLEE 245
Cdd:PRK06928 239 EGAEVIQA 246
|
|
| PRK06476 |
PRK06476 |
pyrroline-5-carboxylate reductase; Reviewed |
5-258 |
2.53e-13 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235812 [Multi-domain] Cd Length: 258 Bit Score: 68.12 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 5 IGFIGCGNMGIAMIGGMIKKNIvSPDQIICSDLNVINLKNASNEYG-IIITTNNNEVANSADILILSIKPDLYTSVINQI 83
Cdd:PRK06476 3 IGFIGTGAITEAMVTGLLTSPA-DVSEIIVSPRNAQIAARLAERFPkVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLRAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 84 KdqIKNDVIVVTIAAGKSIKSTENEFGRKLKVVRVMPNTPVLVGEGMSALSfnemvteKDIKEVLTIFNIFGQT-EVVNE 162
Cdd:PRK06476 82 R--FRPGQTVISVIAATDRAALLEWIGHDVKLVRAIPLPFVAERKGVTAIY-------PPDPFVAALFDALGTAvECDSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 163 KLMDVVTSISGSSPAYvYMFIEAMADAAVLDGMPRKQAYKFAAQAVLG-SAKMVLETGIHPGELKDMVCSPGGTTIEAVA 241
Cdd:PRK06476 153 EEYDLLAAASALMATY-FGILETATGWLEEQGLKRQKARAYLAPLFASlAQDAVRSTKTDFSALSREFSTKGGLNEQVLN 231
|
250
....*....|....*..
gi 1000870713 242 TLEEKGLRTAIISAMKR 258
Cdd:PRK06476 232 DFSRQGGYAALTDALDR 248
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
6-99 |
1.55e-11 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 59.17 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 6 GFIGCGNMGIAMIGGMIKKNivsPDQIICSdlNVINLKNAS---NEYGI-IITTNNNEVANSADILILSIKPDLYTSVIN 81
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAG---PHEVVVA--NSRNPEKAEelaEEYGVgATAVDNEEAAEEADVVFLAVKPEDAPDVLS 75
|
90
....*....|....*...
gi 1000870713 82 QIKDQIKnDVIVVTIAAG 99
Cdd:pfam03807 76 ELSDLLK-GKIVISIAAG 92
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
3-104 |
2.47e-04 |
|
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: 41.65 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 3 KQIGFIGCGNMG--IAMigGMIKKNIVspDQIICSDLNVINLKNAsNEYGII--ITTNNNEVANSADILILSIKPDLYTS 78
Cdd:COG0287 2 MRIAIIGLGLIGgsLAL--ALKRAGLA--HEVVGVDRSPETLERA-LELGVIdrAATDLEEAVADADLVVLAVPVGATIE 76
|
90 100
....*....|....*....|....*.
gi 1000870713 79 VINQIKDQIKNDVIVVTIAagkSIKS 104
Cdd:COG0287 77 VLAELAPHLKPGAIVTDVG---SVKG 99
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-94 |
2.62e-04 |
|
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];
Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 41.72 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000870713 1 MNKQIGFIGCGNMGIAMIGGMIKKNIvSPDQIICSDLNviNLKNASNEYGIIITTNNNEVANSADILILSIKPDLYTSVI 80
Cdd:COG5495 2 ARMKIGIIGAGRVGTALAAALRAAGH-EVVGVYSRSPA--SAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEVA 78
|
90
....*....|....*.
gi 1000870713 81 NQIKDQ--IKNDVIVV 94
Cdd:COG5495 79 AGLAAAgaLRPGQLVV 94
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-72 |
3.12e-03 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 37.45 E-value: 3.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1000870713 4 QIGFIGCGNMGIAMIGGMIKKNIvspdqiicsDLNVINLKNASNE----YGIIITTNNNEVANSADILILSIK 72
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGY---------TVTVYNRTPEKVEelvaAGAIAAASPAEFVAGLDVVITMVP 64
|
|
| |
