|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-268 |
6.38e-99 |
|
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: 292.35 E-value: 6.38e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVlSAHKIIASSPemDLPTVSALR-RMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDR--SPERLEALAeRYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 80 DEIGADVQDRHIVVSCAAGVTISSVEKKLmvfQPAPKVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFC 159
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEAL---GGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 160 TEVEEDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATI 239
Cdd:COG0345 157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236
|
250 260
....*....|....*....|....*....
gi 1211453920 240 HALHFLESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345 237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
1-268 |
3.40e-95 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 282.62 E-value: 3.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVLSAHKIIASSPEmDLPTVSALRRMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTADDS-NPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 81 EIGADVQDRHIVVSCAAGVTISSVEKKLmvfqPAPKVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFCT 160
Cdd:PLN02688 80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 161 EVEEDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATIH 240
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235
|
250 260
....*....|....*....|....*...
gi 1211453920 241 ALHFLESGGFRSLLINAVEASCIRTREL 268
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
21-267 |
8.64e-79 |
|
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: 240.24 E-value: 8.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 21 AAGVLSAHKIIASSPeMDLPTVSALRRMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFILDEIGADVQDRHIVVSCAAGVT 100
Cdd:TIGR00112 3 KAGALAPYDIYVINR-SPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 101 ISSVEKKLMVFQPapkVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFCTEVEEDLIDAITGLSGSGPAY 180
Cdd:TIGR00112 82 LEKLSQLLGGTRR---VVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 181 AFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEA 260
Cdd:TIGR00112 159 VFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEA 238
|
....*..
gi 1211453920 261 SCIRTRE 267
Cdd:TIGR00112 239 AVRRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
164-267 |
3.67e-48 |
|
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: 156.79 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 164 EDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATIHALH 243
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1211453920 244 FLESGGFRSLLINAVEASCIRTRE 267
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-268 |
6.38e-99 |
|
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: 292.35 E-value: 6.38e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVlSAHKIIASSPemDLPTVSALR-RMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFIL 79
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSGV-PPEDIIVSDR--SPERLEALAeRYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 80 DEIGADVQDRHIVVSCAAGVTISSVEKKLmvfQPAPKVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFC 159
Cdd:COG0345 80 EELAPLLDPDKLVISIAAGVTLATLEEAL---GGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 160 TEVEEDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATI 239
Cdd:COG0345 157 VWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTI 236
|
250 260
....*....|....*....|....*....
gi 1211453920 240 HALHFLESGGFRSLLINAVEASCIRTREL 268
Cdd:COG0345 237 AGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
1-268 |
3.40e-95 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 282.62 E-value: 3.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVLSAHKIIASSPEmDLPTVSALRRMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFILD 80
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTADDS-NPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 81 EIGADVQDRHIVVSCAAGVTISSVEKKLmvfqPAPKVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFCT 160
Cdd:PLN02688 80 ELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 161 EVEEDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATIH 240
Cdd:PLN02688 156 VVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIA 235
|
250 260
....*....|....*....|....*...
gi 1211453920 241 ALHFLESGGFRSLLINAVEASCIRTREL 268
Cdd:PLN02688 236 GVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-268 |
1.03e-83 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 253.53 E-value: 1.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVlSAHKIIASSPemDLPTVSALR-RMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFIL 79
Cdd:PRK11880 3 KKIGFIGGGNMASAIIGGLLASGV-PAKDIIVSDP--SPEKRAALAeEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 80 DEIGADVQDrhIVVSCAAGVTISSVEKKLmvfQPAPKVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFC 159
Cdd:PRK11880 80 SELKGQLDK--LVVSIAAGVTLARLERLL---GADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 160 TEVE-EDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGAT 238
Cdd:PRK11880 155 VWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTT 234
|
250 260 270
....*....|....*....|....*....|
gi 1211453920 239 IHALHFLESGGFRSLLINAVEASCIRTREL 268
Cdd:PRK11880 235 IAALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
21-267 |
8.64e-79 |
|
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: 240.24 E-value: 8.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 21 AAGVLSAHKIIASSPeMDLPTVSALRRMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFILDEIGADVQDRHIVVSCAAGVT 100
Cdd:TIGR00112 3 KAGALAPYDIYVINR-SPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 101 ISSVEKKLMVFQPapkVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFCTEVEEDLIDAITGLSGSGPAY 180
Cdd:TIGR00112 82 LEKLSQLLGGTRR---VVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 181 AFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEA 260
Cdd:TIGR00112 159 VFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEA 238
|
....*..
gi 1211453920 261 SCIRTRE 267
Cdd:TIGR00112 239 AVRRSRE 245
|
|
| PTZ00431 |
PTZ00431 |
pyrroline carboxylate reductase; Provisional |
1-268 |
1.28e-50 |
|
pyrroline carboxylate reductase; Provisional
Pssm-ID: 173621 [Multi-domain] Cd Length: 260 Bit Score: 168.59 E-value: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVLSAHKIIASSP-EMDLPtvsalrrmgVNLTRSNKDTVRHSDVLFLAVKPHIIPFIL 79
Cdd:PTZ00431 4 IRVGFIGLGKMGSALAYGIENSNIIGKENIYYHTPsKKNTP---------FVYLQSNEELAKTCDIIVLAVKPDLAGKVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 80 DEIgADVQDRHIVVSCAAGVTISSVEKklMVFQPApKVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFC 159
Cdd:PTZ00431 75 LEI-KPYLGSKLLISICGGLNLKTLEE--MVGVEA-KIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGII 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 160 TEVEEDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATI 239
Cdd:PTZ00431 151 QEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITI 230
|
250 260
....*....|....*....|....*....
gi 1211453920 240 HALHFLESGGFRSLLINAVEASCIRTREL 268
Cdd:PTZ00431 231 VGLYTLEKHAFKYTVMDAVESACQKSKSM 259
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
164-267 |
3.67e-48 |
|
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: 156.79 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 164 EDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATIHALH 243
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1211453920 244 FLESGGFRSLLINAVEASCIRTRE 267
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| PRK07679 |
PRK07679 |
pyrroline-5-carboxylate reductase; Reviewed |
1-274 |
7.48e-46 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 181079 [Multi-domain] Cd Length: 279 Bit Score: 156.85 E-value: 7.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVLSAHKIIASSPEMDLPTVSALRRMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07679 4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRLQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 81 EIGADVQDRHIVVSCAAGVTISSVEKklmVFQPAPKVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFCT 160
Cdd:PRK07679 84 PFKEYIHNNQLIISLLAGVSTHSIRN---LLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 161 EVEEDLIDAITGLSGSGPAYAFMALDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGATIH 240
Cdd:PRK07679 161 VVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1211453920 241 ALHFLESGGFRSLLINAVEASCIRTRELQSMADQ 274
Cdd:PRK07679 241 GIEVLQEHRFQQALISCITQATQRSHNLGKTLEQ 274
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
1-254 |
7.04e-22 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 92.73 E-value: 7.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVLSAHKIIASSPEMDLPTVSALRRMGVNLTRSNKDTVRHSDVLFLAVKPHIIPFILD 80
Cdd:PRK07680 1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 81 EIGADVQDRHIVVSCAAGVTISSVEKKLmvfqP--APKVIRCMTNTpvvVREGATVYATGTHALVEDGKLLEQLMSSVGF 158
Cdd:PRK07680 81 KLAPHLTDEHCLVSITSPISVEQLETLV----PcqVARIIPSITNR---ALSGASLFTFGSRCSEEDQQKLERLFSNIST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 159 CTEVEEDLIDAITGLSGSGPAYAFMALDALADGGVKM-GVPRRLAVRLGAQALLGAAKmLLDSEDH-PGQLKDNVCSPGG 236
Cdd:PRK07680 154 PLVIEEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGK-LLEKGLYtLPTLQEKVCVKGG 232
|
250 260
....*....|....*....|.
gi 1211453920 237 ATIHALHFLES---GGFRSLL 254
Cdd:PRK07680 233 ITGEGIKVLEEevgDMFHRLF 253
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
4-98 |
3.01e-17 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 75.35 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 4 GFIGAGQLACALARGFTAAGvlsAHKI-IASSPEMDLpTVSALRRMGVNLT-RSNKDTVRHSDVLFLAVKPHIIPFILDE 81
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAG---PHEVvVANSRNPEK-AEELAEEYGVGATaVDNEEAAEEADVVFLAVKPEDAPDVLSE 76
|
90
....*....|....*..
gi 1211453920 82 IgADVQDRHIVVSCAAG 98
Cdd:pfam03807 77 L-SDLLKGKIVISIAAG 92
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
3-238 |
3.98e-12 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 65.56 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 3 VGFIGAGQLACALARGFTAAGVLSAHKI-IASSPEMDLPTVSALRRMGVNLTRSNKDTVRHSDVLFLAVKP-HIIPfILD 80
Cdd:PRK06928 4 IGFIGYGSMADMIATKLLETEVATPEEIiLYSSSKNEHFNQLYDKYPTVELADNEAEIFTKCDHSFICVPPlAVLP-LLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 81 EIGADVQ-DRHiVVSCAAGVTISsvekKLMVFQPAPKVIRCMTNTPVVVREGATVYATGTHALVEDGKLLEQLMSSVGFC 159
Cdd:PRK06928 83 DCAPVLTpDRH-VVSIAAGVSLD----DLLEITPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSHV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 160 TEVEEDLIDAITGLSGSGPAYAFMALDALADGGVKMG-VPRRLAVRLGAQALLGAAKMLLDSEDHPGQLKDNVCSPGGAT 238
Cdd:PRK06928 158 MTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGIT 237
|
|
| PRK06476 |
PRK06476 |
pyrroline-5-carboxylate reductase; Reviewed |
1-266 |
9.98e-10 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235812 [Multi-domain] Cd Length: 258 Bit Score: 58.10 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFtAAGVLSAHKIIASSPEMDLPTVSALRRMGVNLTRSNKDTVRHSDVLFLAVKPhiipfild 80
Cdd:PRK06476 1 MKIGFIGTGAITEAMVTGL-LTSPADVSEIIVSPRNAQIAARLAERFPKVRIAKDNQAVVDRSDVVFLAVRP-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 81 EIGADV------QDRHIVVSCAAGVTISSVEKKLmvfQPAPKVIRCMTNTPVVVREGAT-VYAtgTHALVEDgkLLEQLM 153
Cdd:PRK06476 72 QIAEEVlralrfRPGQTVISVIAATDRAALLEWI---GHDVKLVRAIPLPFVAERKGVTaIYP--PDPFVAA--LFDALG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 154 SSVGFCTEVEEDLIDAITGLsgSGPAYAFMalDALADGGVKMGVPRRLAVRLGAQALLGAAKMLLDSEDHP-GQLKDNVC 232
Cdd:PRK06476 145 TAVECDSEEEYDLLAAASAL--MATYFGIL--ETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFS 220
|
250 260 270
....*....|....*....|....*....|....
gi 1211453920 233 SPGGATIHALHFLESGGFRSLLINAVEASCIRTR 266
Cdd:PRK06476 221 TKGGLNEQVLNDFSRQGGYAALTDALDRVLRRIN 254
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
3-96 |
4.34e-06 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 46.70 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 3 VGFIGAGQLACALARGFTAAGvlsaHK-IIAS-SPEmdlpTVSAL-RRMGVNLT-RSNKDTVRHSDVLFLAVKPHIIPFI 78
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAG----HEvVIGSrDPE----KAAALaAELGPGARaGTNAEAAAAADVVVLAVPYEAVPDV 72
|
90
....*....|....*...
gi 1211453920 79 LDEIGADVQDRhIVVSCA 96
Cdd:COG2085 73 LESLGDALAGK-IVIDAT 89
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-114 |
1.67e-05 |
|
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];
Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 45.57 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGV-LSAhkIIASSPEmdlptvSALR---RMGVNLTRSNKDTVRHSDVLFLAVKPHIIP 76
Cdd:COG5495 4 MKIGIIGAGRVGTALAAALRAAGHeVVG--VYSRSPA------SAERaaaLLGAVPALDLEELAAEADLVLLAVPDDAIA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1211453920 77 FILDEIGA--DVQDRHIVVSCAAGVTISsvekklmVFQPA 114
Cdd:COG5495 76 EVAAGLAAagALRPGQLVVHTSGALGSD-------VLAPA 108
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
1-92 |
5.94e-03 |
|
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: 37.80 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211453920 1 MSVGFIGAGQLACALARGFTAAGVlsAHKIIASSPemDLPTVSALRRMGV--NLTRSNKDTVRHSDVLFLAVKPHIIPFI 78
Cdd:COG0287 2 MRIAIIGLGLIGGSLALALKRAGL--AHEVVGVDR--SPETLERALELGVidRAATDLEEAVADADLVVLAVPVGATIEV 77
|
90
....*....|....
gi 1211453920 79 LDEIGADVQDRHIV 92
Cdd:COG0287 78 LAELAPHLKPGAIV 91
|
|
|