|
Name |
Accession |
Description |
Interval |
E-value |
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
11-353 |
1.45e-119 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 347.48 E-value: 1.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 11 LSIEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVPSQQSYtsnqienmna 90
Cdd:COG2070 1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPANPR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 91 wlkpyrralhLEEpvvkiteeqqfkcHIDTIIKKQVPVCCFTFGIPnESIIKRLKEANIKLIGTVTSVDEAIANEKAGMD 170
Cdd:COG2070 71 ----------FEE-------------LLEVVLEEGVPVVSTSAGLP-ADLIERLKEAGIKVIPIVTSVREARKAEKAGAD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 171 AIVAQGSEAGGHRGSflkpknqlPMVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFLTSQDSNA 250
Cdd:COG2070 127 AVVAEGAEAGGHRGA--------DEVSTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 251 SELLRDAIINSKETDTVITKAFSGKLARGINNRFIEEMSQYEgDIPDYPIQNELTS--SIRKAAANiGDKELTHMWSGQS 328
Cdd:COG2070 199 HEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGLDLE-AECLYPILEALTAgkRLRAAAAE-GDLEKGLLWAGQG 276
|
330 340
....*....|....*....|....*.
gi 686383795 329 PRLATT-HPANTIMSNIINQINQIMQ 353
Cdd:COG2070 277 AGLIRDiLPAAELVARLVAEAEAALA 302
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
13-280 |
1.32e-103 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 304.41 E-value: 1.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 13 IEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVPSQqsytsnqienmnawl 92
Cdd:cd04730 1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 93 kpyrralhleepvvkiteEQQFKCHIDTIIKKQVPVCCFTFGIPnESIIKRLKEANIKLIGTVTSVDEAIANEKAGMDAI 172
Cdd:cd04730 66 ------------------NPDFEALLEVALEEGVPVVSFSFGPP-AEVVERLKAAGIKVIPTVTSVEEARKAEAAGADAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 173 VAQGSEAGGHRGSFLkpknqlpmVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFLTSQDSNASE 252
Cdd:cd04730 127 VAQGAEAGGHRGTFD--------IGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASP 198
|
250 260
....*....|....*....|....*...
gi 686383795 253 LLRDAIINSKETDTVITKAFSGKLARGI 280
Cdd:cd04730 199 AYKQALLAATAEDTVLTRAFSGRPARGL 226
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
4-327 |
4.81e-100 |
|
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.
Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 298.66 E-value: 4.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 4 KNRLTQMLSIEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVPSqqsytsn 83
Cdd:pfam03060 1 KSLLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYLTPDRLYQEIRKVKALTDKPFGANLFLPK------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 84 qiENMNAWLKPYRRALHLEEPVVKITEEQQFKCHIDTIIKKQVPVCCFTFGIPNESIIKRLKEANIKLIGTVTSVDEAIA 163
Cdd:pfam03060 74 --PDLADPAANYAKILGNNALGYNIEEGVPDYGKVLVDLDEGVNVVSFGFGLPPNDVVFRLHFAGVALIPTISSAKEARI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 164 NEKAGMDAIVAQGSEAGGHRGSFLKPKnqlpmVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:pfam03060 152 AEARGADALIVQGPEAGGHQGTPEYGD-----KGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 244 TSQDSNASELLRDAIINSKETDTVITKAFSGKLARGINNRFIEEMSQYEGDIPDYPIQNELTSSIRKAAANIGDKELTHM 323
Cdd:pfam03060 227 LTKESGAHDAHKQKITEAGEDDTLVTSPFSGRPARALANGFLEELEEPKIATLAYPEAHEMTKPIRAAAVRGGNREEGLL 306
|
....
gi 686383795 324 WSGQ 327
Cdd:pfam03060 307 WAGQ 310
|
|
| enACPred_II |
TIGR03151 |
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ... |
4-352 |
4.27e-73 |
|
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase.
Pssm-ID: 132195 Cd Length: 307 Bit Score: 229.25 E-value: 4.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 4 KNRLTQMLSIEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVpsqqsytsn 83
Cdd:TIGR03151 1 KTRLCDLLGIEYPIFQGGMAWVATGSLAAAVSNAGGLGIIGAGNAPPDVVRKEIRKVKELTDKPFGVNIML--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 84 qienmnawLKPYRRALhleepvvkiteeqqfkchIDTIIKKQVPVCCFTFGIPNEsIIKRLKEANIKLIGTVTSVDEAIA 163
Cdd:TIGR03151 72 --------LSPFVDEL------------------VDLVIEEKVPVVTTGAGNPGK-YIPRLKENGVKVIPVVASVALAKR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 164 NEKAGMDAIVAQGSEAGGHRGSflkpknqlpmVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:TIGR03151 125 MEKAGADAVIAEGMESGGHIGE----------LTTMALVPQVVDAVSIPVIAAGGIADGRGMAAAFALGAEAVQMGTRFL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 244 TSQDSNASELLRDAIINSKETDTVITKAFSGKLARGINNRFIEEMSQYEGDIPDYPIQNELTSSIRKAAANIGDKELTHM 323
Cdd:TIGR03151 195 CAKECNVHPNYKEKVLKAKDRDTVVTGASTGHPVRVLKNKLTRKYQELEKEGASPEEFEKLGAGALRRAVVEGDVENGSV 274
|
330 340 350
....*....|....*....|....*....|
gi 686383795 324 WSGQSPRL-ATTHPANTIMSNIINQINQIM 352
Cdd:TIGR03151 275 MAGQIAGLiKEIKPAKEIIEDIMSEAKEVI 304
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
4-316 |
3.22e-06 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 48.50 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 4 KNRLTQMLSIEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGyFNTQQLEDEIDYVR----QLTSNSFGV------NVF 73
Cdd:PRK06843 32 KTQLTKNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKN-MSIEAQRKEIEKVKtykfQKTINTNGDtneqkpEIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 74 VPSQ-------------QSYTSNQIENMNAWLKpYRRALHLEEPVVKITEEQqFKCHIDTIIKKQvpvccfTFGIPNESI 140
Cdd:PRK06843 111 TAKQhleksdayknaehKEDFPNACKDLNNKLR-VGAAVSIDIDTIERVEEL-VKAHVDILVIDS------AHGHSTRII 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 141 --IKRLKEA--NIKLI-GTVTSVDEAIANEKAGMDAIvaqgsEAGGHRGSFLKPK----NQLPMVGTISLVPQIVDVVSI 211
Cdd:PRK06843 183 elVKKIKTKypNLDLIaGNIVTKEAALDLISVGADCL-----KVGIGPGSICTTRivagVGVPQITAICDVYEVCKNTNI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 212 PVIAAGGIMDGRGVLASIVLGAEGVQMGTAFLTSQDSNASELlrdaIINSKETDTVITKAFSGKLARGINNRF------- 284
Cdd:PRK06843 258 CIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEI----IYNGKKFKSYVGMGSISAMKRGSKSRYfqlenne 333
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 686383795 285 --------IEEMSQYEGDIPDypIQNELTSSIRKAAANIG 316
Cdd:PRK06843 334 pkklvpegIEGMVPYSGKLKD--ILTQLKGGLMSGMGYLG 371
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YrpB |
COG2070 |
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ... |
11-353 |
1.45e-119 |
|
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];
Pssm-ID: 441673 [Multi-domain] Cd Length: 302 Bit Score: 347.48 E-value: 1.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 11 LSIEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVPSQQSYtsnqienmna 90
Cdd:COG2070 1 LGIRYPIIQGPMAGVSTPELAAAVSNAGGLGSIAAGNLTPEALREEIRKIRELTDGPFGVNLIVHPANPR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 91 wlkpyrralhLEEpvvkiteeqqfkcHIDTIIKKQVPVCCFTFGIPnESIIKRLKEANIKLIGTVTSVDEAIANEKAGMD 170
Cdd:COG2070 71 ----------FEE-------------LLEVVLEEGVPVVSTSAGLP-ADLIERLKEAGIKVIPIVTSVREARKAEKAGAD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 171 AIVAQGSEAGGHRGSflkpknqlPMVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFLTSQDSNA 250
Cdd:COG2070 127 AVVAEGAEAGGHRGA--------DEVSTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESPA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 251 SELLRDAIINSKETDTVITKAFSGKLARGINNRFIEEMSQYEgDIPDYPIQNELTS--SIRKAAANiGDKELTHMWSGQS 328
Cdd:COG2070 199 HEAYKQALVDAKEEDTVLTRSFTGRPARALRNSFTREGLDLE-AECLYPILEALTAgkRLRAAAAE-GDLEKGLLWAGQG 276
|
330 340
....*....|....*....|....*.
gi 686383795 329 PRLATT-HPANTIMSNIINQINQIMQ 353
Cdd:COG2070 277 AGLIRDiLPAAELVARLVAEAEAALA 302
|
|
| NPD_like |
cd04730 |
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ... |
13-280 |
1.32e-103 |
|
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.
Pssm-ID: 240081 [Multi-domain] Cd Length: 236 Bit Score: 304.41 E-value: 1.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 13 IEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVPSQqsytsnqienmnawl 92
Cdd:cd04730 1 IRYPIIQAPMAGVSTPELAAAVSNAGGLGFIGAGYLTPEALRAEIRKIRALTDKPFGVNLLVPSS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 93 kpyrralhleepvvkiteEQQFKCHIDTIIKKQVPVCCFTFGIPnESIIKRLKEANIKLIGTVTSVDEAIANEKAGMDAI 172
Cdd:cd04730 66 ------------------NPDFEALLEVALEEGVPVVSFSFGPP-AEVVERLKAAGIKVIPTVTSVEEARKAEAAGADAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 173 VAQGSEAGGHRGSFLkpknqlpmVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFLTSQDSNASE 252
Cdd:cd04730 127 VAQGAEAGGHRGTFD--------IGTFALVPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESGASP 198
|
250 260
....*....|....*....|....*...
gi 686383795 253 LLRDAIINSKETDTVITKAFSGKLARGI 280
Cdd:cd04730 199 AYKQALLAATAEDTVLTRAFSGRPARGL 226
|
|
| NMO |
pfam03060 |
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ... |
4-327 |
4.81e-100 |
|
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.
Pssm-ID: 367316 [Multi-domain] Cd Length: 331 Bit Score: 298.66 E-value: 4.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 4 KNRLTQMLSIEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVPSqqsytsn 83
Cdd:pfam03060 1 KSLLTDIHTIKPPVQQPMMGGISWPRLAAAVSNAGGLGVLASGYLTPDRLYQEIRKVKALTDKPFGANLFLPK------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 84 qiENMNAWLKPYRRALHLEEPVVKITEEQQFKCHIDTIIKKQVPVCCFTFGIPNESIIKRLKEANIKLIGTVTSVDEAIA 163
Cdd:pfam03060 74 --PDLADPAANYAKILGNNALGYNIEEGVPDYGKVLVDLDEGVNVVSFGFGLPPNDVVFRLHFAGVALIPTISSAKEARI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 164 NEKAGMDAIVAQGSEAGGHRGSFLKPKnqlpmVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:pfam03060 152 AEARGADALIVQGPEAGGHQGTPEYGD-----KGLFRLVPQVPDAVDIPVIAAGGIWDRRGVAAALALGASGVQMGTRFL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 244 TSQDSNASELLRDAIINSKETDTVITKAFSGKLARGINNRFIEEMSQYEGDIPDYPIQNELTSSIRKAAANIGDKELTHM 323
Cdd:pfam03060 227 LTKESGAHDAHKQKITEAGEDDTLVTSPFSGRPARALANGFLEELEEPKIATLAYPEAHEMTKPIRAAAVRGGNREEGLL 306
|
....
gi 686383795 324 WSGQ 327
Cdd:pfam03060 307 WAGQ 310
|
|
| enACPred_II |
TIGR03151 |
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane ... |
4-352 |
4.27e-73 |
|
putative enoyl-[acyl-carrier-protein] reductase II; This oxidoreductase of the 2-nitropropane dioxygenase family (pfam03060) is commonly found in apparent operons with genes involved in fatty acid biosynthesis. Furthermore, this genomic context generally includes the fabG 3-oxoacyl-[ACP] reductase and lacks the fabI enoyl-[ACP] reductase.
Pssm-ID: 132195 Cd Length: 307 Bit Score: 229.25 E-value: 4.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 4 KNRLTQMLSIEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVpsqqsytsn 83
Cdd:TIGR03151 1 KTRLCDLLGIEYPIFQGGMAWVATGSLAAAVSNAGGLGIIGAGNAPPDVVRKEIRKVKELTDKPFGVNIML--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 84 qienmnawLKPYRRALhleepvvkiteeqqfkchIDTIIKKQVPVCCFTFGIPNEsIIKRLKEANIKLIGTVTSVDEAIA 163
Cdd:TIGR03151 72 --------LSPFVDEL------------------VDLVIEEKVPVVTTGAGNPGK-YIPRLKENGVKVIPVVASVALAKR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 164 NEKAGMDAIVAQGSEAGGHRGSflkpknqlpmVGTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:TIGR03151 125 MEKAGADAVIAEGMESGGHIGE----------LTTMALVPQVVDAVSIPVIAAGGIADGRGMAAAFALGAEAVQMGTRFL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 244 TSQDSNASELLRDAIINSKETDTVITKAFSGKLARGINNRFIEEMSQYEGDIPDYPIQNELTSSIRKAAANIGDKELTHM 323
Cdd:TIGR03151 195 CAKECNVHPNYKEKVLKAKDRDTVVTGASTGHPVRVLKNKLTRKYQELEKEGASPEEFEKLGAGALRRAVVEGDVENGSV 274
|
330 340 350
....*....|....*....|....*....|
gi 686383795 324 WSGQSPRL-ATTHPANTIMSNIINQINQIM 352
Cdd:TIGR03151 275 MAGQIAGLiKEIKPAKEIIEDIMSEAKEVI 304
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
141-243 |
2.33e-08 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 55.14 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 141 IKRLKEA-NIKLI--GtVTSVDEAIANEKAGMDAIVAqgSEAGGhRgsflkpknQL-PMVGTISLVPQIVDVV--SIPVI 214
Cdd:COG1304 217 IAWLRERwPGPLIvkG-VLSPEDARRAVDAGVDGIDV--SNHGG-R--------QLdGGPPTIDALPEIRAAVggRIPVI 284
|
90 100
....*....|....*....|....*....
gi 686383795 215 AAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:COG1304 285 ADGGIRRGLDVAKALALGADAVGLGRPFL 313
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
17-240 |
3.19e-08 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 53.36 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 17 IIQAGMAGSTTPKLVASVSNS----GGLGTIGAGYFNTQQLEDEIDYVRQLTSNSFGVNVFVpsqqsytsnqienmNAWL 92
Cdd:cd04722 1 VILALLAGGPSGDPVELAKAAaeagADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGV--------------QLAI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 93 KPYRralhleePVVKITEEQQFKCHIDTIIkkqVPVCCFTFGIPNESIIKRLKEANIKLI----GTVTSVDEAIANEKAG 168
Cdd:cd04722 67 NDAA-------AAVDIAAAAARAAGADGVE---IHGAVGYLAREDLELIRELREAVPDVKvvvkLSPTGELAAAAAEEAG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 686383795 169 MDAIVAQGSEAGGHRGSFLKPknqlpmvgTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGT 240
Cdd:cd04722 137 VDEVGLGNGGGGGGGRDAVPI--------ADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
138-242 |
1.58e-07 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 52.00 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 138 ESIIKRLKEAN-----IKLIGTVTSVDE-AIANEKAGMDAIVA-----------------QGSEAGGHRGSFLKPknqlp 194
Cdd:COG0167 146 AELLAAVKAATdkpvlVKLAPDLTDIVEiARAAEEAGADGVIAinttlgraidletrrpvLANEAGGLSGPALKP----- 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 686383795 195 mvgtISL--VPQIVDVV--SIPVIAAGGIMDGRGVLASIVLGAEGVQMGTAF 242
Cdd:COG0167 221 ----IALrmVREVAQAVggDIPIIGVGGISTAEDALEFILAGASAVQVGTAL 268
|
|
| FMN_dh |
pfam01070 |
FMN-dependent dehydrogenase; |
141-243 |
7.94e-07 |
|
FMN-dependent dehydrogenase;
Pssm-ID: 426029 [Multi-domain] Cd Length: 350 Bit Score: 50.22 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 141 IKRLKEA-NIKLI--GtVTSVDEAIANEKAGMDAIVAqgSEAGGHrgsflkpknQL-PMVGTISLVPQIVDVV--SIPVI 214
Cdd:pfam01070 210 LAWLRERwKGPLVvkG-ILSPEDAKRAVEAGVDGIVV--SNHGGR---------QLdGAPATIDALPEIVAAVggRIPVL 277
|
90 100
....*....|....*....|....*....
gi 686383795 215 AAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:pfam01070 278 VDGGIRRGTDVLKALALGADAVLLGRPFL 306
|
|
| alpha_hydroxyacid_oxid_FMN |
cd02809 |
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ... |
141-243 |
8.44e-07 |
|
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.
Pssm-ID: 239203 [Multi-domain] Cd Length: 299 Bit Score: 49.75 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 141 IKRLKEA-NIKLI--GtVTSVDEAIANEKAGMDAIVAqgSEAGGhrgsflkpkNQL-PMVGTISLVPQIVDVV--SIPVI 214
Cdd:cd02809 164 LAWLRSQwKGPLIlkG-ILTPEDALRAVDAGADGIVV--SNHGG---------RQLdGAPATIDALPEIVAAVggRIEVL 231
|
90 100
....*....|....*....|....*....
gi 686383795 215 AAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:cd02809 232 LDGGIRRGTDVLKALALGADAVLIGRPFL 260
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
138-241 |
1.22e-06 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 49.47 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 138 ESIIKRLKEAN-----IKLIGTVTSVDE-AIANEKAGMDAIVA-----------------QGSEAGGHRGSFLKPknqlp 194
Cdd:cd04740 143 AEIVKAVKKATdvpviVKLTPNVTDIVEiARAAEEAGADGLTLintlkgmaidietrkpiLGNVTGGLSGPAIKP----- 217
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 686383795 195 mvgtISL--VPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTA 241
Cdd:cd04740 218 ----IALrmVYQVYKAVEIPIIGVGGIASGEDALEFLMAGASAVQVGTA 262
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
140-241 |
1.60e-06 |
|
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.
Pssm-ID: 130109 [Multi-domain] Cd Length: 300 Bit Score: 48.96 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 140 IIKRLKEAN-----IKLIGTVTSVDE-AIANEKAGMDAIVAQGS-----------------EAGGHRGSFLKPKnqlpmv 196
Cdd:TIGR01037 148 VVKAVKDKTdvpvfAKLSPNVTDITEiAKAAEEAGADGLTLINTlrgmkidiktgkpilanKTGGLSGPAIKPI------ 221
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 686383795 197 gTISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTA 241
Cdd:TIGR01037 222 -ALRMVYDVYKMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTA 265
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
4-316 |
3.22e-06 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 48.50 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 4 KNRLTQMLSIEFPIIQAGMAGSTTPKLVASVSNSGGLGTIGAGyFNTQQLEDEIDYVR----QLTSNSFGV------NVF 73
Cdd:PRK06843 32 KTQLTKNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKN-MSIEAQRKEIEKVKtykfQKTINTNGDtneqkpEIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 74 VPSQ-------------QSYTSNQIENMNAWLKpYRRALHLEEPVVKITEEQqFKCHIDTIIKKQvpvccfTFGIPNESI 140
Cdd:PRK06843 111 TAKQhleksdayknaehKEDFPNACKDLNNKLR-VGAAVSIDIDTIERVEEL-VKAHVDILVIDS------AHGHSTRII 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 141 --IKRLKEA--NIKLI-GTVTSVDEAIANEKAGMDAIvaqgsEAGGHRGSFLKPK----NQLPMVGTISLVPQIVDVVSI 211
Cdd:PRK06843 183 elVKKIKTKypNLDLIaGNIVTKEAALDLISVGADCL-----KVGIGPGSICTTRivagVGVPQITAICDVYEVCKNTNI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 212 PVIAAGGIMDGRGVLASIVLGAEGVQMGTAFLTSQDSNASELlrdaIINSKETDTVITKAFSGKLARGINNRF------- 284
Cdd:PRK06843 258 CIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEI----IYNGKKFKSYVGMGSISAMKRGSKSRYfqlenne 333
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 686383795 285 --------IEEMSQYEGDIPDypIQNELTSSIRKAAANIG 316
Cdd:PRK06843 334 pkklvpegIEGMVPYSGKLKD--ILTQLKGGLMSGMGYLG 371
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
138-241 |
7.95e-06 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 47.07 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 138 ESIIKRLKEAN-----IKLIGTVTS-VDEAIANEKAGMDAIVA-----------------QGSEAGGHRGSFLKPknqlp 194
Cdd:PRK07259 146 YEVVKAVKEVVkvpviVKLTPNVTDiVEIAKAAEEAGADGLSLintlkgmaidiktrkpiLANVTGGLSGPAIKP----- 220
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 686383795 195 mVGtISLVPQIVDVVSIPVIAAGGIMDGRGVLASIVLGAEGVQMGTA 241
Cdd:PRK07259 221 -IA-LRMVYQVYQAVDIPIIGMGGISSAEDAIEFIMAGASAVQVGTA 265
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
154-258 |
4.01e-05 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 43.86 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 154 TVTSVDEAIANEKAGMDAIVAqgseagGH---RGSflkpKNQLPMVGtISLVPQIVDVVSIPVIAAGGIMDG--RGVLAS 228
Cdd:PRK07695 101 SVHSLEEAIQAEKNGADYVVY------GHvfpTDC----KKGVPARG-LEELSDIARALSIPVIAIGGITPEntRDVLAA 169
|
90 100 110
....*....|....*....|....*....|.
gi 686383795 229 ivlGAEGVQMGTAFLTSQDSN-ASELLRDAI 258
Cdd:PRK07695 170 ---GVSGIAVMSGIFSSANPYsKAKRYAESI 197
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
141-243 |
5.50e-05 |
|
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.
Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 44.84 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 141 IKRLKEAN------IKLIGTVTSVDEAIANEKAGMDAIVAQGSEAGGHrGSFLKPKNQ--LPMVGTISLVPQIV------ 206
Cdd:cd02808 205 IEDLREATggkpigVKLVAGHGEGDIAAGVAAAGADFITIDGAEGGTG-AAPLTFIDHvgLPTELGLARAHQALvknglr 283
|
90 100 110
....*....|....*....|....*....|....*..
gi 686383795 207 DVVSIpvIAAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:cd02808 284 DRVSL--IASGGLRTGADVAKALALGADAVGIGTAAL 318
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
150-258 |
1.03e-04 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 42.86 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 150 KLIG-TVTSVDEAIANEKAGMDAIVAqgseagGH-RGSFLKPKNQLPMvgTISLVPQIVDVVSIPVIAAGGIM--DGRGV 225
Cdd:COG0352 101 LIIGvSCHSLEEALRAEEAGADYVGF------GPvFPTPTKPGAPPPL--GLEGLAWWAELVEIPVVAIGGITpeNAAEV 172
|
90 100 110
....*....|....*....|....*....|....
gi 686383795 226 LASivlGAEGVQMGTAFLTSQD-SNASELLRDAI 258
Cdd:COG0352 173 LAA---GADGVAVISAIWGAPDpAAAARELRAAL 203
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
141-245 |
8.68e-04 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 40.78 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 141 IKRLKEAN------IKLIGTVTSVDEAIANEKAGMDAIVAQGSEaGGHRGSFLKPKNQ--LPMVGTISLVPQIV------ 206
Cdd:pfam01645 193 IYDLKEINpkapisVKLVSGHGVGTIAAGVAKAGADIILIDGYD-GGTGASPKTSIKHagLPWELALAEAHQTLkenglr 271
|
90 100 110
....*....|....*....|....*....|....*....
gi 686383795 207 DVVSIpvIAAGGIMDGRGVLASIVLGAEGVQMGTAFLTS 245
Cdd:pfam01645 272 DRVSL--IADGGLRTGADVAKAAALGADAVYIGTAALIA 308
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
195-272 |
2.98e-03 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 39.23 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 195 MVG--TISLVPQIVDVVSIPVIAAGGImDGRGVLASIVLGAEGVQMGTAFLTSQD-SNASELLRDAIINSKETDTVITKA 271
Cdd:PRK07028 145 MLGkdPLELLKEVSEEVSIPIAVAGGL-DAETAAKAVAAGADIVIVGGNIIKSADvTEAARKIREAIDSGKPVKIDKFKK 223
|
.
gi 686383795 272 F 272
Cdd:PRK07028 224 S 224
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
150-255 |
3.07e-03 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 38.27 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 150 KLIG-TVTSVDEAIANEKAGMDAIVAqgseagGH-RGSFLKPkNQLPMVGtISLVPQIVDVVSIPVIAAGGIM--DGRGV 225
Cdd:cd00564 96 LIIGvSTHSLEEALRAEELGADYVGF------GPvFPTPTKP-GAGPPLG-LELLREIAELVEIPVVAIGGITpeNAAEV 167
|
90 100 110
....*....|....*....|....*....|..
gi 686383795 226 LASivlGAEGVQMGTAFLTSQD--SNASELLR 255
Cdd:cd00564 168 LAA---GADGVAVISAITGADDpaAAARELLA 196
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
149-241 |
3.61e-03 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 39.16 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 149 IKLIGTVTSVDEaiaNEKAGMDAIVAQGSEaGGHRGSFLKPKnQLPMVGTISLVPQivdVVSIPVIAAGGIMDGRGVLAS 228
Cdd:PRK08318 200 INTINSITGVDL---DRMIPMPIVNGKSSH-GGYCGPAVKPI-ALNMVAEIARDPE---TRGLPISGIGGIETWRDAAEF 271
|
90
....*....|...
gi 686383795 229 IVLGAEGVQMGTA 241
Cdd:PRK08318 272 ILLGAGTVQVCTA 284
|
|
| lldD |
PRK11197 |
L-lactate dehydrogenase; Provisional |
168-243 |
3.71e-03 |
|
L-lactate dehydrogenase; Provisional
Pssm-ID: 183033 Cd Length: 381 Bit Score: 38.85 E-value: 3.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 686383795 168 GMDAIVAqgSEAGGHrgsflkpknQLPMV-GTISLVPQIVDVVS--IPVIAAGGIMDGRGVLASIVLGAEGVQMGTAFL 243
Cdd:PRK11197 266 GADGIVV--SNHGGR---------QLDGVlSSARALPAIADAVKgdITILADSGIRNGLDVVRMIALGADTVLLGRAFV 333
|
|
| NanE |
cd04729 |
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ... |
134-241 |
6.00e-03 |
|
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.
Pssm-ID: 240080 [Multi-domain] Cd Length: 219 Bit Score: 37.55 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 134 GIPNESIIKRLKEA-NIKLIGTVTSVDEAIANEKAGMDAIvaqGSEAGGHRGSflKPKNQLPmvgTISLVPQIVDVVSIP 212
Cdd:cd04729 108 GETLAELIKRIHEEyNCLLMADISTLEEALNAAKLGFDII---GTTLSGYTEE--TAKTEDP---DFELLKELRKALGIP 179
|
90 100
....*....|....*....|....*....
gi 686383795 213 VIAAGGIMDGRGVLASIVLGAEGVQMGTA 241
Cdd:cd04729 180 VIAEGRINSPEQAAKALELGADAVVVGSA 208
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
165-243 |
8.04e-03 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 37.55 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686383795 165 EKAGMDAIvaqgseaggH--RGSFLKPKNQLPMVGT-----ISLVPQIVDVVSIPVIAAGGIMDG---RGVLASIvlGAE 234
Cdd:cd02803 238 EEAGVDAL---------HvsGGSYESPPPIIPPPYVpegyfLELAEKIKKAVKIPVIAVGGIRDPevaEEILAEG--KAD 306
|
....*....
gi 686383795 235 GVQMGTAFL 243
Cdd:cd02803 307 LVALGRALL 315
|
|
| |
