|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-269 |
7.72e-130 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 368.32 E-value: 7.72e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 1 MDKKIGFIGCGNMGKAILGGLIASGqVQPGQIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVL 80
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 81 GDIASSLNKesLVVSIAAGVTLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQI 160
Cdd:PRK11880 80 SELKGQLDK--LVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 161 A-EPMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEA 239
Cdd:PRK11880 158 DdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAA 237
|
250 260 270
....*....|....*....|....*....|
gi 1728596118 240 VRVLEEKGFRSAVIEAITQCMEKSEKLSRS 269
Cdd:PRK11880 238 LRVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-268 |
1.59e-129 |
|
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: 367.85 E-value: 1.59e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 1 MDKKIGFIGCGNMGKAILGGLIASGqVQPGQIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVL 80
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 81 GDIASSLNKESLVVSIAAGVTLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQI 160
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 161 AEPMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAV 240
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239
|
250 260
....*....|....*....|....*...
gi 1728596118 241 RVLEEKGFRSAVIEAITQCMEKSEKLSR 268
Cdd:COG0345 240 KVLEEGGLRAAVIEAVEAAAERSKELGK 267
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
21-265 |
1.48e-111 |
|
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: 321.52 E-value: 1.48e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 21 LIASGQVQPGQIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVLGDIASSLNKESLVVSIAAGV 100
Cdd:TIGR00112 1 LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 101 TLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQIAEPMIHPVVGVSGSAPAYVF 180
Cdd:TIGR00112 81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 181 MFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAVRVLEEKGFRSAVIEAITQCM 260
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240
|
....*
gi 1728596118 261 EKSEK 265
Cdd:TIGR00112 241 RRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
162-265 |
1.54e-49 |
|
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: 158.71 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 162 EPMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAVR 241
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1728596118 242 VLEEKGFRSAVIEAITQCMEKSEK 265
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-269 |
7.72e-130 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 368.32 E-value: 7.72e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 1 MDKKIGFIGCGNMGKAILGGLIASGqVQPGQIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVL 80
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 81 GDIASSLNKesLVVSIAAGVTLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQI 160
Cdd:PRK11880 80 SELKGQLDK--LVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 161 A-EPMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEA 239
Cdd:PRK11880 158 DdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAA 237
|
250 260 270
....*....|....*....|....*....|
gi 1728596118 240 VRVLEEKGFRSAVIEAITQCMEKSEKLSRS 269
Cdd:PRK11880 238 LRVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-268 |
1.59e-129 |
|
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: 367.85 E-value: 1.59e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 1 MDKKIGFIGCGNMGKAILGGLIASGqVQPGQIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVL 80
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 81 GDIASSLNKESLVVSIAAGVTLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQI 160
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 161 AEPMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAV 240
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239
|
250 260
....*....|....*....|....*...
gi 1728596118 241 RVLEEKGFRSAVIEAITQCMEKSEKLSR 268
Cdd:COG0345 240 KVLEEGGLRAAVIEAVEAAAERSKELGK 267
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
21-265 |
1.48e-111 |
|
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: 321.52 E-value: 1.48e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 21 LIASGQVQPGQIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVLGDIASSLNKESLVVSIAAGV 100
Cdd:TIGR00112 1 LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 101 TLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQIAEPMIHPVVGVSGSAPAYVF 180
Cdd:TIGR00112 81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 181 MFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAVRVLEEKGFRSAVIEAITQCM 260
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240
|
....*
gi 1728596118 261 EKSEK 265
Cdd:TIGR00112 241 RRSRE 245
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
3-269 |
1.55e-95 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 281.46 E-value: 1.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 3 KKIGFIGCGNMGKAILGGLIASGQVQPGQIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVLGD 82
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 83 IASSLNKESLVVSIAAGVTLEQLARALGHDRkIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQIAE 162
Cdd:PLN02688 81 LRPLLSKDKLLVSVAAGITLADLQEWAGGRR-VVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 163 PMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAVRV 242
Cdd:PLN02688 160 KLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHE 239
|
250 260
....*....|....*....|....*..
gi 1728596118 243 LEEKGFRSAVIEAITQCMEKSEKLSRS 269
Cdd:PLN02688 240 LEKGGFRAALMNAVVAAAKRSRELSKS 266
|
|
| PRK07679 |
PRK07679 |
pyrroline-5-carboxylate reductase; Reviewed |
2-266 |
1.88e-54 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 181079 [Multi-domain] Cd Length: 279 Bit Score: 177.27 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 2 DKKIGFIGCGNMGKAILGGLIASGQVQPGQIWVYTPSPDK-VAALRDQYGINAASSAQEVAQIADIVFGAVKPGIMTKVL 80
Cdd:PRK07679 3 IQNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETrLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 81 GDIASSLNKESLVVSIAAGVTLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQI 160
Cdd:PRK07679 83 IPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVSVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 161 AEPMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAV 240
Cdd:PRK07679 163 EEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEAGI 242
|
250 260
....*....|....*....|....*.
gi 1728596118 241 RVLEEKGFRSAVIEAITQCMEKSEKL 266
Cdd:PRK07679 243 EVLQEHRFQQALISCITQATQRSHNL 268
|
|
| PTZ00431 |
PTZ00431 |
pyrroline carboxylate reductase; Provisional |
4-266 |
5.45e-53 |
|
pyrroline carboxylate reductase; Provisional
Pssm-ID: 173621 [Multi-domain] Cd Length: 260 Bit Score: 172.83 E-value: 5.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 4 KIGFIGCGNMGKAILGGLIASGQVQPGQIWVYTPSPDKVAalrdqygINAASSAQEVAQIADIVFGAVKPGIMTKVLGDI 83
Cdd:PTZ00431 5 RVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTP-------FVYLQSNEELAKTCDIIVLAVKPDLAGKVLLEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 84 ASSLNKEsLVVSIAAGVTLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQIAEP 163
Cdd:PTZ00431 78 KPYLGSK-LLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQEIKEK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 164 MIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAVRVL 243
Cdd:PTZ00431 157 DMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIVGLYTL 236
|
250 260
....*....|....*....|...
gi 1728596118 244 EEKGFRSAVIEAITQCMEKSEKL 266
Cdd:PTZ00431 237 EKHAFKYTVMDAVESACQKSKSM 259
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
162-265 |
1.54e-49 |
|
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: 158.71 E-value: 1.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 162 EPMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAVR 241
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1728596118 242 VLEEKGFRSAVIEAITQCMEKSEK 265
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
4-245 |
1.44e-37 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 133.17 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 4 KIGFIGCGNMGKAILGGLIASGQVQPGQIWVYTPSPDKVAALRDQY-GINAASSAQEVAQIADIVFGAVKPGIMTKVLGD 82
Cdd:PRK07680 2 NIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYpGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 83 IASSLNKESLVVSIAAGVTLEQLARALghDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQIAE 162
Cdd:PRK07680 82 LAPHLTDEHCLVSITSPISVEQLETLV--PCQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 163 PMIHPVVGVSGSAPAYVFMFIEAMADAAV-LGGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAVR 241
Cdd:PRK07680 160 DITRVSSDIVSCGPAFFSYLLQRFIDAAVeETNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITGEGIK 239
|
....
gi 1728596118 242 VLEE 245
Cdd:PRK07680 240 VLEE 243
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
4-245 |
1.84e-29 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 112.17 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 4 KIGFIGCGNMGKAILGGLIASGQVQPGQIWVYTPSP-DKVAALRDQY-GINAASSAQEVAQIADIVFGAVKPGIMTKVLG 81
Cdd:PRK06928 3 KIGFIGYGSMADMIATKLLETEVATPEEIILYSSSKnEHFNQLYDKYpTVELADNEAEIFTKCDHSFICVPPLAVLPLLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 82 DIASSLNKESLVVSIAAGVTLEQLARAlGHDRKIIRAMPNTPSLVNAGMTSVTPNALVSSEDVAEVLTIFRCFGQAEQIA 161
Cdd:PRK06928 83 DCAPVLTPDRHVVSIAAGVSLDDLLEI-TPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 162 EPMIHPVVGVSGSAPAYVFMFIEAMADAAVL-GGMPRAQAYKFAAQAVMGSAKMVLESGEHPGALKDMVCSPGGTTIEAV 240
Cdd:PRK06928 162 EENMDIASNLTSSSPGFIAAIFEEFAEAAVRnSSLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGITAEGA 241
|
....*
gi 1728596118 241 RVLEE 245
Cdd:PRK06928 242 EVIQA 246
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
6-99 |
2.90e-21 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 85.36 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 6 GFIGCGNMGKAILGGLIASGqvqPGQIWV-YTPSPDKVAALRDQYGINA-ASSAQEVAQIADIVFGAVKPGIMTKVLGDI 83
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAG---PHEVVVaNSRNPEKAEELAEEYGVGAtAVDNEEAAEEADVVFLAVKPEDAPDVLSEL 77
|
90
....*....|....*.
gi 1728596118 84 ASSLnKESLVVSIAAG 99
Cdd:pfam03807 78 SDLL-KGKIVISIAAG 92
|
|
| PRK06476 |
PRK06476 |
pyrroline-5-carboxylate reductase; Reviewed |
4-262 |
1.27e-20 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235812 [Multi-domain] Cd Length: 258 Bit Score: 88.15 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 4 KIGFIGCGNMGKAILGGLIASGqVQPGQIWVYTPSPDKVAALRDQYG-INAASSAQEVAQIADIVFGAVKPGIMTKVLGd 82
Cdd:PRK06476 2 KIGFIGTGAITEAMVTGLLTSP-ADVSEIIVSPRNAQIAARLAERFPkVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 83 iASSLNKESLVVSIAAGVTLEQLARALGHDRKIIRAMPNTPSLVNAGMTSVTPnalvsseDVAEVLTIFRCFGQAEQIAE 162
Cdd:PRK06476 80 -ALRFRPGQTVISVIAATDRAALLEWIGHDVKLVRAIPLPFVAERKGVTAIYP-------PDPFVAALFDALGTAVECDS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 163 PMIHPVVGVSGSAPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLESGEHP-GALKDMVCSPGGTTIEAVR 241
Cdd:PRK06476 152 EEEYDLLAAASALMATYFGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLNEQVLN 231
|
250 260
....*....|....*....|.
gi 1728596118 242 VLEEKGFRSAVIEAITQCMEK 262
Cdd:PRK06476 232 DFSRQGGYAALTDALDRVLRR 252
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
3-228 |
1.21e-12 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 66.29 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 3 KKIGFIGCGNMGKAILGGLIASGQvqpgQIWVYTPSPDKVAALRDQyGINAASSAQEVAQIADIVFGAVK-PGIMTKVL- 80
Cdd:COG2084 2 MKVGFIGLGAMGAPMARNLLKAGH----EVTVWNRTPAKAEALVAA-GARVAASPAEAAAAADVVITMLPdDAAVEEVLl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 81 --GDIASSLNKESLVV---SIAAGVTLEQLARALGHDRKIIRAmP--NTPSLVNAGMTSVtpnaLVS--SEDVAEVLTIF 151
Cdd:COG2084 77 geDGLLAALRPGAVVVdmsTISPETARELAAAAAARGVRYLDA-PvsGGPAGAEAGTLTI----MVGgdEAAFERARPVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 152 RCFGQAeqiaepMIHpvVGVSGSAPAY-------VFMFIEAMADAAVLG---GMPRAQAYKFAAQAVMGS------AKMV 215
Cdd:COG2084 152 EAMGKR------IVH--VGDAGAGQAAklannllLAGTMAALAEALALAekaGLDPETLLEVLSGGAAGSwvlenrGPRM 223
|
250
....*....|....*...
gi 1728596118 216 LESGEHPG-----ALKDM 228
Cdd:COG2084 224 LAGDFDPGfaldlMLKDL 241
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-68 |
1.42e-07 |
|
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: 49.78 E-value: 1.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728596118 4 KIGFIGCGNMGKAILGGLIASGQvqpgQIWVYTPSPDKVAALRDQyGINAASSAQEVAQIADIVF 68
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGY----TVTVYNRTPEKVEELVAA-GAIAAASPAEFVAGLDVVI 60
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
1-103 |
1.01e-06 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 48.89 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 1 MDKKIGFIGCGNMGKAILGGLIASGQvqpgQIWVYTPSPDKVAALRdQYGINAASSAQEVAQIADIVFGAV--KPGIMTK 78
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGY----SLVVYDRNPEAVAEVI-AAGAETASTAKAVAEQCDVIITMLpnSPHVKEV 75
|
90 100 110
....*....|....*....|....*....|
gi 1728596118 79 VLGD--IASSLNKESLVV---SIAAGVTLE 103
Cdd:PRK11559 76 ALGEngIIEGAKPGTVVIdmsSIAPLASRE 105
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-66 |
4.02e-06 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 47.23 E-value: 4.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728596118 1 MDK-KIGFIGCGNMGKAILGGLIASGQVQPgqIWVYTPSPDKVAALRDQYGINAASSAQEVAQIADI 66
Cdd:COG0673 1 MDKlRVGIIGAGGIGRAHAPALAALPGVEL--VAVADRDPERAEAFAEEYGVRVYTDYEELLADPDI 65
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-72 |
5.85e-06 |
|
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];
Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 46.73 E-value: 5.85e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728596118 1 MDKKIGFIGCGNMGKAILGGLIASGqVQPGQiwVYTPSPDKVAALRDQYGINAASSAQEVAQIADIVFGAVK 72
Cdd:COG5495 2 ARMKIGIIGAGRVGTALAAALRAAG-HEVVG--VYSRSPASAERAAALLGAVPALDLEELAAEADLVLLAVP 70
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
4-97 |
9.73e-04 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 39.84 E-value: 9.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728596118 4 KIGFIGCGNMGKAILGGLIASGQvqpgQIWVYTPSPDKVAALRDQyGINAASSAQEVAQIADIVFGAVKPG--IMTKVLG 81
Cdd:PRK15461 3 AIAFIGLGQMGSPMASNLLKQGH----QLQVFDVNPQAVDALVDK-GATPAASPAQAAAGAEFVITMLPNGdlVRSVLFG 77
|
90
....*....|....*...
gi 1728596118 82 D--IASSLNKESLVVSIA 97
Cdd:PRK15461 78 EngVCEGLSRDALVIDMS 95
|
|
| |
