|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-271 |
2.05e-86 |
|
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: 258.45 E-value: 2.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGgFPADEVVVFDRNADKRELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLRG 80
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 81 LAGRIAERRrVVLSIAAGTPLARLESFLttdaapGSDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAVG 160
Cdd:COG0345 82 LAPLLDPDK-LVISIAAGVTLATLEEAL------GGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 161 EVVEIPESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGGT 240
Cdd:COG0345 155 KVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGT 234
|
250 260 270
....*....|....*....|....*....|.
gi 1870254859 241 TVAGLLALEDRGFLSTVAHGVKATIDRDREM 271
Cdd:COG0345 235 TIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-271 |
6.45e-80 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 241.97 E-value: 6.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGgFPADEVVVFDRNADKRELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLRG 80
Cdd:PRK11880 3 KKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 81 LAGRIaerRRVVLSIAAGTPLARLESFLttdaapGSDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAVG 160
Cdd:PRK11880 82 LKGQL---DKLVVSIAAGVTLARLERLL------GADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 161 EVVEIP-ESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGG 239
Cdd:PRK11880 153 KVVWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGG 232
|
250 260 270
....*....|....*....|....*....|..
gi 1870254859 240 TTVAGLLALEDRGFLSTVAHGVKATIDRDREM 271
Cdd:PRK11880 233 TTIAALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
19-270 |
3.57e-69 |
|
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: 214.05 E-value: 3.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 19 MVGSGGFPADEVVVFDRNADKRELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLRGLAGRIAeRRRVVLSIAAG 98
Cdd:TIGR00112 1 LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKG-KDKLLISIAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 99 TPLARLESFLttdaapGSDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAVGEVVEIPESQFSTYTAIAG 178
Cdd:TIGR00112 80 VTLEKLSQLL------GGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 179 SSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGGTTVAGLLALEDRGFLSTVA 258
Cdd:TIGR00112 154 SGPAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVI 233
|
250
....*....|..
gi 1870254859 259 HGVKATIDRDRE 270
Cdd:TIGR00112 234 EAIEAAVRRSRE 245
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
167-270 |
1.85e-33 |
|
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: 117.50 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 167 ESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGGTTVAGLL 246
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1870254859 247 ALEDRGFLSTVAHGVKATIDRDRE 270
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-271 |
2.05e-86 |
|
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: 258.45 E-value: 2.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGgFPADEVVVFDRNADKRELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLRG 80
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 81 LAGRIAERRrVVLSIAAGTPLARLESFLttdaapGSDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAVG 160
Cdd:COG0345 82 LAPLLDPDK-LVISIAAGVTLATLEEAL------GGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 161 EVVEIPESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGGT 240
Cdd:COG0345 155 KVVWVDEELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGT 234
|
250 260 270
....*....|....*....|....*....|.
gi 1870254859 241 TVAGLLALEDRGFLSTVAHGVKATIDRDREM 271
Cdd:COG0345 235 TIAGLKVLEEGGLRAAVIEAVEAAAERSKEL 265
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-271 |
6.45e-80 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 241.97 E-value: 6.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGgFPADEVVVFDRNADKRELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLRG 80
Cdd:PRK11880 3 KKIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 81 LAGRIaerRRVVLSIAAGTPLARLESFLttdaapGSDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAVG 160
Cdd:PRK11880 82 LKGQL---DKLVVSIAAGVTLARLERLL------GADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 161 EVVEIP-ESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGG 239
Cdd:PRK11880 153 KVVWVDdEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGG 232
|
250 260 270
....*....|....*....|....*....|..
gi 1870254859 240 TTVAGLLALEDRGFLSTVAHGVKATIDRDREM 271
Cdd:PRK11880 233 TTIAALRVLEEKGLRAAVIEAVQAAAKRSKEL 264
|
|
| proC |
TIGR00112 |
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ... |
19-270 |
3.57e-69 |
|
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: 214.05 E-value: 3.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 19 MVGSGGFPADEVVVFDRNADKRELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLRGLAGRIAeRRRVVLSIAAG 98
Cdd:TIGR00112 1 LLKAGALAPYDIYVINRSPEKLAALAKELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKG-KDKLLISIAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 99 TPLARLESFLttdaapGSDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAVGEVVEIPESQFSTYTAIAG 178
Cdd:TIGR00112 80 VTLEKLSQLL------GGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 179 SSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGGTTVAGLLALEDRGFLSTVA 258
Cdd:TIGR00112 154 SGPAYVFLFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVI 233
|
250
....*....|..
gi 1870254859 259 HGVKATIDRDRE 270
Cdd:TIGR00112 234 EAIEAAVRRSRE 245
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
1-271 |
3.49e-57 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 184.00 E-value: 3.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGGFPADEVVVFDRNADKRELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLRG 80
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 81 LAGRIAERRrVVLSIAAGTPLARLEsflttDAAPGSdsAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAVG 160
Cdd:PLN02688 81 LRPLLSKDK-LLVSVAAGITLADLQ-----EWAGGR--RVVRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 161 EVVEIPESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGGT 240
Cdd:PLN02688 153 KIWVVDEKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGT 232
|
250 260 270
....*....|....*....|....*....|.
gi 1870254859 241 TVAGLLALEDRGFLSTVAHGVKATIDRDREM 271
Cdd:PLN02688 233 TIAGVHELEKGGFRAALMNAVVAAAKRSREL 263
|
|
| P5CR_dimer |
pfam14748 |
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ... |
167-270 |
1.85e-33 |
|
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: 117.50 E-value: 1.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 167 ESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGGTTVAGLL 246
Cdd:pfam14748 1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80
|
90 100
....*....|....*....|....
gi 1870254859 247 ALEDRGFLSTVAHGVKATIDRDRE 270
Cdd:pfam14748 81 VLEEGGFRGAVIEAVEAATKRAKE 104
|
|
| PTZ00431 |
PTZ00431 |
pyrroline carboxylate reductase; Provisional |
3-271 |
1.04e-31 |
|
pyrroline carboxylate reductase; Provisional
Pssm-ID: 173621 [Multi-domain] Cd Length: 260 Bit Score: 117.75 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 3 VGFIGTGNMANAIVRGMVGSGgfpadevVVFDRNADKRELLGADLGVQVAGSAEDLVDASDVVVVAVKPQgipallrgLA 82
Cdd:PTZ00431 6 VGFIGLGKMGSALAYGIENSN-------IIGKENIYYHTPSKKNTPFVYLQSNEELAKTCDIIVLAVKPD--------LA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 83 GRIAER------RRVVLSIAAGTPLARLESFLttdaapGSDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIF 156
Cdd:PTZ00431 71 GKVLLEikpylgSKLLISICGGLNLKTLEEMV------GVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 157 QAVGEVVEIPESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCS 236
Cdd:PTZ00431 145 SACGIIQEIKEKDMDIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCS 224
|
250 260 270
....*....|....*....|....*....|....*
gi 1870254859 237 PGGTTVAGLLALEDRGFLSTVAHGVKATIDRDREM 271
Cdd:PTZ00431 225 PGGITIVGLYTLEKHAFKYTVMDAVESACQKSKSM 259
|
|
| PRK07679 |
PRK07679 |
pyrroline-5-carboxylate reductase; Reviewed |
1-271 |
8.66e-31 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 181079 [Multi-domain] Cd Length: 279 Bit Score: 116.02 E-value: 8.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGGFPADEVVVFDRNADKR-ELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLR 79
Cdd:PRK07679 4 QNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNRSNETRlQELHQKYGVKGTHNKKELLTDANILFLAMKPKDVAEALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 80 GLAGRIAERRrVVLSIAAGTPLARLESFLttdaapGSDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAV 159
Cdd:PRK07679 84 PFKEYIHNNQ-LIISLLAGVSTHSIRNLL------QKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 160 GEVVEIPESQFSTYTAIAGSSPAFTYLFIDALSRAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPGG 239
Cdd:PRK07679 157 GLVSVVEEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGG 236
|
250 260 270
....*....|....*....|....*....|..
gi 1870254859 240 TTVAGLLALEDRGFLSTVAHGVKATIDRDREM 271
Cdd:PRK07679 237 TTEAGIEVLQEHRFQQALISCITQATQRSHNL 268
|
|
| PRK07680 |
PRK07680 |
late competence protein ComER; Validated |
1-250 |
7.93e-16 |
|
late competence protein ComER; Validated
Pssm-ID: 181080 [Multi-domain] Cd Length: 273 Bit Score: 75.39 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGGFPADEVVVFDRNADK-RELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLR 79
Cdd:PRK07680 1 MNIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKaYHIKERYPGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 80 GLAGRIAERRRVVlSIAAGTPLARLESFLttdaapgsDSAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAV 159
Cdd:PRK07680 81 KLAPHLTDEHCLV-SITSPISVEQLETLV--------PCQVARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 160 GEVVEIPESQFSTYTAIAGSSPAF-TYL---FIDAlsrAAVAGGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVC 235
Cdd:PRK07680 152 STPLVIEEDITRVSSDIVSCGPAFfSYLlqrFIDA---AVEETNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVC 228
|
250
....*....|....*
gi 1870254859 236 SPGGTTVAGLLALED 250
Cdd:PRK07680 229 VKGGITGEGIKVLEE 243
|
|
| PRK06928 |
PRK06928 |
pyrroline-5-carboxylate reductase; Reviewed |
2-244 |
2.26e-15 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235888 [Multi-domain] Cd Length: 277 Bit Score: 74.03 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 2 TVGFIGTGNMANAIVRGMVGSGGFPADEVVVFDRNADKR--ELLGADLGVQVAGSAEDLVDASDVVVVAVKPQGIPALLR 79
Cdd:PRK06928 3 KIGFIGYGSMADMIATKLLETEVATPEEIILYSSSKNEHfnQLYDKYPTVELADNEAEIFTKCDHSFICVPPLAVLPLLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 80 GLAGRIAERRRVVlSIAAGTPLARLesfltTDAAPGSdsAVVRVMPNVNAMIGAGMSAVTGNAAATADDVATVVAIFQAV 159
Cdd:PRK06928 83 DCAPVLTPDRHVV-SIAAGVSLDDL-----LEITPGL--QVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 160 GEVVEIPESQFSTYTAIAGSSPAFTYLFIDALSRAAVA-GGMPKAQATQIAAQAVLGSAKMVRESPKSPWDLIDTVCSPG 238
Cdd:PRK06928 155 SHVMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRnSSLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKG 234
|
....*.
gi 1870254859 239 GTTVAG 244
Cdd:PRK06928 235 GITAEG 240
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
4-98 |
1.74e-09 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 53.77 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 4 GFIGTGNMANAIVRGMVGSGgfPADEVVVFDRNADKRELLGADLGVQV-AGSAEDLVDASDVVVVAVKPQGIPALLRGLA 82
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAG--PHEVVVANSRNPEKAEELAEEYGVGAtAVDNEEAAEEADVVFLAVKPEDAPDVLSELS 78
|
90
....*....|....*.
gi 1870254859 83 GriAERRRVVLSIAAG 98
Cdd:pfam03807 79 D--LLKGKIVISIAAG 92
|
|
| PRK06476 |
PRK06476 |
pyrroline-5-carboxylate reductase; Reviewed |
1-125 |
6.41e-09 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 235812 [Multi-domain] Cd Length: 258 Bit Score: 55.41 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSgGFPADEVVVFDRNADKRELLGADLG-VQVAGSAEDLVDASDVVVVAVKPQGIPALLR 79
Cdd:PRK06476 1 MKIGFIGTGAITEAMVTGLLTS-PADVSEIIVSPRNAQIAARLAERFPkVRIAKDNQAVVDRSDVVFLAVRPQIAEEVLR 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1870254859 80 GLAGRiaeRRRVVLSIAAGTPLARLESFLttdaapGSDSAVVRVMP 125
Cdd:PRK06476 80 ALRFR---PGQTVISVIAATDRAALLEWI------GHDVKLVRAIP 116
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
1-58 |
4.70e-06 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 47.03 E-value: 4.70e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGgfpaDEVVVFDRNADKRELLgADLGVQVAGSAEDL 58
Cdd:COG2084 2 MKVGFIGLGAMGAPMARNLLKAG----HEVTVWNRTPAKAEAL-VAAGARVAASPAEA 54
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-58 |
4.37e-05 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 44.14 E-value: 4.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGGFpadEVV-VFDRNADKRELLGADLGVQVAGSAEDL 58
Cdd:COG0673 4 LRVGIIGAGGIGRAHAPALAALPGV---ELVaVADRDPERAEAFAEEYGVRVYTDYEEL 59
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
2-58 |
4.72e-05 |
|
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: 42.84 E-value: 4.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1870254859 2 TVGFIGTGNMANAIVRGMVGSGgfpaDEVVVFDRNADKRELLgADLGVQVAGSAEDL 58
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAG----YTVTVYNRTPEKVEEL-VAAGAIAAASPAEF 52
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
1-58 |
6.02e-04 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 40.50 E-value: 6.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1870254859 1 MTVGFIGTGNMANAIVRGMVGSGgfpaDEVVVFDRNADKRELLgADLGVQVAGSAEDL 58
Cdd:PRK09599 1 MQLGMIGLGRMGGNMARRLLRGG----HEVVGYDRNPEAVEAL-AEEGATGADSLEEL 53
|
|
|