|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-269 |
6.87e-131 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 371.02 E-value: 6.87e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 1 MEKKIGFIGCGNMGKAILGGLIASGqVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVL 80
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 81 SEITSSLNKdsLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVI 160
Cdd:PRK11880 80 SELKGQLDK--LVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 161 A-EPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEA 239
Cdd:PRK11880 158 DdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAA 237
|
250 260 270
....*....|....*....|....*....|
gi 24111764 240 VRVLEEKGFRAAVIEAMTKCMEKSEKLSKS 269
Cdd:PRK11880 238 LRVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-268 |
1.28e-130 |
|
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: 370.55 E-value: 1.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 1 MEKKIGFIGCGNMGKAILGGLIASGqVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVL 80
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 81 SEITSSLNKDSLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVI 160
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 161 AEPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAV 240
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239
|
250 260
....*....|....*....|....*...
gi 24111764 241 RVLEEKGFRAAVIEAMTKCMEKSEKLSK 268
Cdd:COG0345 240 KVLEEGGLRAAVIEAVEAAAERSKELGK 267
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
21-265 |
3.58e-113 |
|
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: 325.37 E-value: 3.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 21 LIASGQVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVLSEITSSLNKDSLVVSIAAGV 100
Cdd:TIGR00112 1 LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 101 TLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVIAEPMIHPVVGVSGSSPAYVF 180
Cdd:TIGR00112 81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 181 MFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAVRVLEEKGFRAAVIEAMTKCM 260
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240
|
....*
gi 24111764 261 EKSEK 265
Cdd:TIGR00112 241 RRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
162-265 |
2.02e-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: 158.33 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 162 EPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAVR 241
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 24111764 242 VLEEKGFRAAVIEAMTKCMEKSEK 265
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-269 |
6.87e-131 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 371.02 E-value: 6.87e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 1 MEKKIGFIGCGNMGKAILGGLIASGqVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVL 80
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 81 SEITSSLNKdsLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVI 160
Cdd:PRK11880 80 SELKGQLDK--LVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 161 A-EPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEA 239
Cdd:PRK11880 158 DdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAA 237
|
250 260 270
....*....|....*....|....*....|
gi 24111764 240 VRVLEEKGFRAAVIEAMTKCMEKSEKLSKS 269
Cdd:PRK11880 238 LRVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-268 |
1.28e-130 |
|
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: 370.55 E-value: 1.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 1 MEKKIGFIGCGNMGKAILGGLIASGqVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVL 80
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 81 SEITSSLNKDSLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVI 160
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 161 AEPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAV 240
Cdd:COG0345 160 DEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGL 239
|
250 260
....*....|....*....|....*...
gi 24111764 241 RVLEEKGFRAAVIEAMTKCMEKSEKLSK 268
Cdd:COG0345 240 KVLEEGGLRAAVIEAVEAAAERSKELGK 267
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
21-265 |
3.58e-113 |
|
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: 325.37 E-value: 3.58e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 21 LIASGQVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVLSEITSSLNKDSLVVSIAAGV 100
Cdd:TIGR00112 1 LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 101 TLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVIAEPMIHPVVGVSGSSPAYVF 180
Cdd:TIGR00112 81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 181 MFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAVRVLEEKGFRAAVIEAMTKCM 260
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240
|
....*
gi 24111764 261 EKSEK 265
Cdd:TIGR00112 241 RRSRE 245
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
3-269 |
1.53e-99 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 291.86 E-value: 1.53e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 3 KKIGFIGCGNMGKAILGGLIASGQVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVLSE 82
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 83 ITSSLNKDSLVVSIAAGVTLDQLARALGHDRkIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVIAE 162
Cdd:PLN02688 81 LRPLLSKDKLLVSVAAGITLADLQEWAGGRR-VVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 163 PMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAVRV 242
Cdd:PLN02688 160 KLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVHE 239
|
250 260
....*....|....*....|....*..
gi 24111764 243 LEEKGFRAAVIEAMTKCMEKSEKLSKS 269
Cdd:PLN02688 240 LEKGGFRAALMNAVVAAAKRSRELSKS 266
|
|
| PRK07679 |
PRK07679 |
pyrroline-5-carboxylate reductase; Reviewed |
2-269 |
5.42e-53 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 181079 [Multi-domain] Cd Length: 279 Bit Score: 173.42 E-value: 5.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 2 EKKIGFIGCGNMGKAILGGLIASGQVLPGQIWVYTPSPDK-VAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVL 80
Cdd:PRK07679 3 IQNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETrLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 81 SEITSSLNKDSLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVI 160
Cdd:PRK07679 83 IPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVSVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 161 AEPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAV 240
Cdd:PRK07679 163 EEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEAGI 242
|
250 260
....*....|....*....|....*....
gi 24111764 241 RVLEEKGFRAAVIEAMTKCMEKSEKLSKS 269
Cdd:PRK07679 243 EVLQEHRFQQALISCITQATQRSHNLGKT 271
|
|
| PTZ00431 |
PTZ00431 |
pyrroline carboxylate reductase; Provisional |
1-266 |
6.24e-52 |
|
pyrroline carboxylate reductase; Provisional
Pssm-ID: 173621 [Multi-domain] Cd Length: 260 Bit Score: 170.13 E-value: 6.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 1 MEK-KIGFIGCGNMGKAILGGLIASGQVLPGQIWVYTPSPDKVAalhdqfgINAAESAQEVAQIADIIFAAVKPGIMIKV 79
Cdd:PTZ00431 1 MENiRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPSKKNTP-------FVYLQSNEELAKTCDIIVLAVKPDLAGKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 80 LSEITSSLNKdSLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEV 159
Cdd:PTZ00431 74 LLEIKPYLGS-KLLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 160 IAEPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEA 239
Cdd:PTZ00431 153 IKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIVG 232
|
250 260
....*....|....*....|....*..
gi 24111764 240 VRVLEEKGFRAAVIEAMTKCMEKSEKL 266
Cdd:PTZ00431 233 LYTLEKHAFKYTVMDAVESACQKSKSM 259
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
162-265 |
2.02e-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: 158.33 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 162 EPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAVR 241
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 24111764 242 VLEEKGFRAAVIEAMTKCMEKSEK 265
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
4-245 |
1.47e-36 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 130.86 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 4 KIGFIGCGNMGKAILGGLIASGQVLPGQIWVYTPSPDKVAALHDQF-GINAAESAQEVAQIADIIFAAVKPGIMIKVLSE 82
Cdd:PRK07680 2 NIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYpGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 83 ITSSLNKDSLVVSIAAGVTLDQLARALghDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVIAE 162
Cdd:PRK07680 82 LAPHLTDEHCLVSITSPISVEQLETLV--PCQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 163 PMIHPVVGVSGSSPAYVFMFIEAMADAAV-LGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAVR 241
Cdd:PRK07680 160 DITRVSSDIVSCGPAFFSYLLQRFIDAAVeETNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITGEGIK 239
|
....
gi 24111764 242 VLEE 245
Cdd:PRK07680 240 VLEE 243
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
1-245 |
7.99e-28 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 107.93 E-value: 7.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 1 MEKkIGFIGCGNMGKAILGGLIASGQVLPGQIWVYTPSP-DKVAALHDQF-GINAAESAQEVAQIADIIFAAVKPGIMIK 78
Cdd:PRK06928 1 MEK-IGFIGYGSMADMIATKLLETEVATPEEIILYSSSKnEHFNQLYDKYpTVELADNEAEIFTKCDHSFICVPPLAVLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 79 VLSEITSSLNKDSLVVSIAAGVTLDQLARAlGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAE 158
Cdd:PRK06928 80 LLKDCAPVLTPDRHVVSIAAGVSLDDLLEI-TPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 159 VIAEPMIHPVVGVSGSSPAYVFMFIEAMADAAVL-GGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTI 237
Cdd:PRK06928 159 TIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRnSSLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGITA 238
|
....*...
gi 24111764 238 EAVRVLEE 245
Cdd:PRK06928 239 EGAEVIQA 246
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
6-99 |
1.68e-21 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 85.75 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 6 GFIGCGNMGKAILGGLIASGqvlPGQIWV-YTPSPDKVAALHDQFGINA-AESAQEVAQIADIIFAAVKPGIMIKVLSEI 83
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAG---PHEVVVaNSRNPEKAEELAEEYGVGAtAVDNEEAAEEADVVFLAVKPEDAPDVLSEL 77
|
90
....*....|....*.
gi 24111764 84 TSSLnKDSLVVSIAAG 99
Cdd:pfam03807 78 SDLL-KGKIVISIAAG 92
|
|
| PRK06476 |
PRK06476 |
pyrroline-5-carboxylate reductase; Reviewed |
4-262 |
4.10e-20 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235812 [Multi-domain] Cd Length: 258 Bit Score: 86.61 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 4 KIGFIGCGNMGKAILGGLIASGqVLPGQIWVYTPSPDKVAALHDQFG-INAAESAQEVAQIADIIFAAVKPGIMIKVLSE 82
Cdd:PRK06476 2 KIGFIGTGAITEAMVTGLLTSP-ADVSEIIVSPRNAQIAARLAERFPkVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 83 ItsSLNKDSLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPnalvtpeDTADVLNIFRCFGEAEVIAE 162
Cdd:PRK06476 81 L--RFRPGQTVISVIAATDRAALLEWIGHDVKLVRAIPLPFVAERKGVTAIYP-------PDPFVAALFDALGTAVECDS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 163 PMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMG-SAKMVLETGEHPGALKDMVCSPGGTTIEAVR 241
Cdd:PRK06476 152 EEEYDLLAAASALMATYFGILETATGWLEEQGLKRQKARAYLAPLFASlAQDAVRSTKTDFSALSREFSTKGGLNEQVLN 231
|
250 260
....*....|....*....|.
gi 24111764 242 VLEEKGFRAAVIEAMTKCMEK 262
Cdd:PRK06476 232 DFSRQGGYAALTDALDRVLRR 252
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
3-228 |
1.97e-09 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 57.05 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 3 KKIGFIGCGNMGKAILGGLIASGQvlpgQIWVYTPSPDKVAALHDQfGINAAESAQEVAQIADIIFAAVK-PGIMIKVL- 80
Cdd:COG2084 2 MKVGFIGLGAMGAPMARNLLKAGH----EVTVWNRTPAKAEALVAA-GARVAASPAEAAAAADVVITMLPdDAAVEEVLl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 81 --SEITSSLNKDSLVV---SIAAGVTLDQLARALGHDRKIIRAmP--NTPALVNAGMTSVtpnaLV--TPEDTADVLNIF 151
Cdd:COG2084 77 geDGLLAALRPGAVVVdmsTISPETARELAAAAAARGVRYLDA-PvsGGPAGAEAGTLTI----MVggDEAAFERARPVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 152 RCFGEAeviaepMIHpvVGVSGSSPAY-------VFMFIEAMADAAVLG---GMPRAQAYKFAAQAVMGS------AKMV 215
Cdd:COG2084 152 EAMGKR------IVH--VGDAGAGQAAklannllLAGTMAALAEALALAekaGLDPETLLEVLSGGAAGSwvlenrGPRM 223
|
250
....*....|....*...
gi 24111764 216 LETGEHPG-----ALKDM 228
Cdd:COG2084 224 LAGDFDPGfaldlMLKDL 241
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-72 |
6.98e-08 |
|
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: 50.93 E-value: 6.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24111764 4 KIGFIGCGNMGKAILGGLIASGQvlpgQIWVYTPSPDKVAALHDQfGINAAESAQEVAQIADIIFAAVK 72
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGY----TVTVYNRTPEKVEELVAA-GAIAAASPAEFVAGLDVVITMVP 64
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
1-68 |
2.80e-06 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 47.74 E-value: 2.80e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24111764 1 MEKKIGFIGCGNMGKAILGGLIASGQVLPgqiwVYTPSPDKVAALhDQFGINAAESAQEVAQIADIIF 68
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLV----VYDRNPEAVAEV-IAAGAETASTAKAVAEQCDVII 63
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-108 |
5.58e-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: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 1 MEKKIGFIGCGNMGKAILGGLIASGQVLPGqiwVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVL 80
Cdd:COG5495 2 ARMKIGIIGAGRVGTALAAALRAAGHEVVG---VYSRSPASAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEVA 78
|
90 100 110
....*....|....*....|....*....|
gi 24111764 81 SEI--TSSLNKDSLVVSIAAGVTLDQLARA 108
Cdd:COG5495 79 AGLaaAGALRPGQLVVHTSGALGSDVLAPA 108
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-66 |
1.19e-04 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 42.60 E-value: 1.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24111764 1 MEK-KIGFIGCGNMGKAILGGLIASGQV-LPGqiwVYTPSPDKVAALHDQFGINAAESAQEVAQIADI 66
Cdd:COG0673 1 MDKlRVGIIGAGGIGRAHAPALAALPGVeLVA---VADRDPERAEAFAEEYGVRVYTDYEELLADPDI 65
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
4-97 |
1.13e-03 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 39.84 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111764 4 KIGFIGCGNMGKAILGGLIASGQvlpgQIWVYTPSPDKVAALHDQfGINAAESAQEVAQIADIIFAAVKPGIMIKVLSE- 82
Cdd:PRK15461 3 AIAFIGLGQMGSPMASNLLKQGH----QLQVFDVNPQAVDALVDK-GATPAASPAQAAAGAEFVITMLPNGDLVRSVLFg 77
|
90
....*....|....*...
gi 24111764 83 ---ITSSLNKDSLVVSIA 97
Cdd:PRK15461 78 engVCEGLSRDALVIDMS 95
|
|
| |
