|
Name |
Accession |
Description |
Interval |
E-value |
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
4-301 |
5.43e-165 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 459.96 E-value: 5.43e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 4 LVNELIKANVGRVLVNEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRL 83
Cdd:PRK13905 1 LLKELLPALRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 84 GEGLDHLEVENHRVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTIEW 163
Cdd:PRK13905 81 GKGLNEIEVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDGEIKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 164 LMNSEMEFSYRTSVLQTKRpGIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAG 243
Cdd:PRK13905 161 LSNEELGFGYRHSALQEEG-LIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1208968233 244 LRGYRIGGAQISEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIGR 301
Cdd:PRK13905 240 LKGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGE 297
|
|
| MurB |
COG0812 |
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ... |
20-299 |
2.16e-133 |
|
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440574 [Multi-domain] Cd Length: 279 Bit Score: 379.36 E-value: 2.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 20 EPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGeGLDHLEV-ENHRVR 98
Cdd:COG0812 1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLG-RLKGIEVdDGVLVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 99 VGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTIEWLMNSEMEFSYRTSVL 178
Cdd:COG0812 80 AGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 179 QTKRpGIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQISEMH 258
Cdd:COG0812 160 KRER-YIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKH 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1208968233 259 GNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEII 299
Cdd:COG0812 239 ANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
|
|
| murB |
TIGR00179 |
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ... |
22-300 |
4.97e-119 |
|
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, UDP-N-acetylenolpyruvoylglucosamine reductase, which is also called UDP-N-acetylmuramate dehydrogenase. It is part of the pathway for the biosynthesis of the UDP-N-acetylmuramoyl-pentapeptide that is a precursor of bacterial peptidoglycan. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 272945 [Multi-domain] Cd Length: 284 Bit Score: 343.28 E-value: 4.97e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 22 LARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGEGLDHLEVENHRVRVGG 101
Cdd:TIGR00179 1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIEDDEGEYVHVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 102 GYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTIEWLMNSEMEFSYRTSVLQTK 181
Cdd:TIGR00179 81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 182 RPGIVLEAEFQLQVG-----EREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQISE 256
Cdd:TIGR00179 161 YVGLVLKAEFQLTLGfgtrlDPETITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1208968233 257 MHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIG 300
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
|
|
| MurB_C |
pfam02873 |
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ... |
202-299 |
7.74e-49 |
|
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 460730 [Multi-domain] Cd Length: 99 Bit Score: 157.90 E-value: 7.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 202 IRN-MQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQISEMHGNFIINTGGASAQDVLSLIALI 280
Cdd:pfam02873 1 IRAaMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80
|
90
....*....|....*....
gi 1208968233 281 KHTIKDKFGLDMHTEVEII 299
Cdd:pfam02873 81 RERVKEKFGVELEPEVRII 99
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
4-301 |
5.43e-165 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 459.96 E-value: 5.43e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 4 LVNELIKANVGRVLVNEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRL 83
Cdd:PRK13905 1 LLKELLPALRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 84 GEGLDHLEVENHRVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTIEW 163
Cdd:PRK13905 81 GKGLNEIEVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDGEIKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 164 LMNSEMEFSYRTSVLQTKRpGIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAG 243
Cdd:PRK13905 161 LSNEELGFGYRHSALQEEG-LIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1208968233 244 LRGYRIGGAQISEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIGR 301
Cdd:PRK13905 240 LKGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGE 297
|
|
| MurB |
COG0812 |
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ... |
20-299 |
2.16e-133 |
|
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440574 [Multi-domain] Cd Length: 279 Bit Score: 379.36 E-value: 2.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 20 EPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGeGLDHLEV-ENHRVR 98
Cdd:COG0812 1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLG-RLKGIEVdDGVLVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 99 VGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTIEWLMNSEMEFSYRTSVL 178
Cdd:COG0812 80 AGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 179 QTKRpGIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQISEMH 258
Cdd:COG0812 160 KRER-YIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKH 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1208968233 259 GNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEII 299
Cdd:COG0812 239 ANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
|
|
| murB |
TIGR00179 |
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ... |
22-300 |
4.97e-119 |
|
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, UDP-N-acetylenolpyruvoylglucosamine reductase, which is also called UDP-N-acetylmuramate dehydrogenase. It is part of the pathway for the biosynthesis of the UDP-N-acetylmuramoyl-pentapeptide that is a precursor of bacterial peptidoglycan. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 272945 [Multi-domain] Cd Length: 284 Bit Score: 343.28 E-value: 4.97e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 22 LARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGEGLDHLEVENHRVRVGG 101
Cdd:TIGR00179 1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIEDDEGEYVHVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 102 GYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTIEWLMNSEMEFSYRTSVLQTK 181
Cdd:TIGR00179 81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 182 RPGIVLEAEFQLQVG-----EREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQISE 256
Cdd:TIGR00179 161 YVGLVLKAEFQLTLGfgtrlDPETITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1208968233 257 MHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIG 300
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
|
|
| PRK14649 |
PRK14649 |
UDP-N-acetylmuramate dehydrogenase; |
15-300 |
1.09e-77 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173112 [Multi-domain] Cd Length: 295 Bit Score: 238.59 E-value: 1.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 15 RVLVNEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRL-GEGLD-HLEV 92
Cdd:PRK14649 2 TLRENEPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARYrGQRWElHEHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 93 ENHRVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKA-LILFENGTIEWLMnSEMEF 171
Cdd:PRK14649 82 DTAEVWVEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAwLLLNGSECVEWSV-HDFAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 172 SYRTSVLQ-------TKRPGIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCaGSVFRNPLPDFAGHLVEKAGL 244
Cdd:PRK14649 161 GYRTSVLKqlradgiTWRPPLVLAARFRLHRDDPTALAARMEAIAAERKQKTPAGSSC-GSVFKNPPGDSAGRLIEAAGL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1208968233 245 RGYRIGGAQISEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIG 300
Cdd:PRK14649 240 KGTRIGDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRIIG 295
|
|
| murB |
PRK13906 |
UDP-N-acetylmuramate dehydrogenase; |
18-300 |
7.20e-75 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 184386 [Multi-domain] Cd Length: 307 Bit Score: 231.63 E-value: 7.20e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 18 VNEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLgEGLDHLEVENHRV 97
Cdd:PRK13906 21 VDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISL-LSLDHIEVSDDAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 98 RVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTIEWLMNSEMEFSYRTSV 177
Cdd:PRK13906 100 IAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 178 LQtKRPGIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQISEM 257
Cdd:PRK13906 180 IQ-KEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTK 258
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1208968233 258 HGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIG 300
Cdd:PRK13906 259 HAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
|
|
| PRK14652 |
PRK14652 |
UDP-N-acetylmuramate dehydrogenase; |
14-300 |
2.60e-74 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237777 [Multi-domain] Cd Length: 302 Bit Score: 230.14 E-value: 2.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 14 GRVLVNEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGEGLDHLEVE 93
Cdd:PRK14652 16 GEVLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDFPGESTD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 94 NHRVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTiEWLMNSEMEFSY 173
Cdd:PRK14652 96 GGRLVLGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVTAVELATADGA-GFVPAAALGYAY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 174 RTSVLQTKrpGIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQ 253
Cdd:PRK14652 175 RTCRLPPG--AVITRVEVRLRPGDVAASEALMRADRERRRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVGLKGHRVGGAI 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1208968233 254 ISEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIG 300
Cdd:PRK14652 253 WSPVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLG 299
|
|
| PRK14653 |
PRK14653 |
UDP-N-acetylmuramate dehydrogenase; |
16-298 |
1.87e-71 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237778 [Multi-domain] Cd Length: 297 Bit Score: 222.79 E-value: 1.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 16 VLVNEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKtKWTVIGRGSNLLVSDKGIEGVVIRLgEGLDHLEVENH 95
Cdd:PRK14653 16 VFINEEMKCHVSFKIGGPVPLFAIPNSTNGFIETINLLKEGI-EVKILGNGTNVLPKDEPMDFVVVST-ERLDDIFVDND 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 96 RVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKaLILFENGTIEWLMNSEMEFSYRT 175
Cdd:PRK14653 94 KIICESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVE-VVAYDGKKIIRLGKNEIKFSYRN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 176 SVLQTKRPGIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCAGSVFRNPLPDF-AGHLVEKAGLRGYRIGGAQI 254
Cdd:PRK14653 173 SIFKEEKDLIILRVTFKLKKGNKNEIYNLMLETMKKRVEKQPLEFPSAGSVFKRPRKDFyVGSAIEKLGLKGFSIGGAQI 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1208968233 255 SEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEI 298
Cdd:PRK14653 253 SEKHAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEIEI 296
|
|
| PRK12436 |
PRK12436 |
UDP-N-acetylmuramate dehydrogenase; |
14-300 |
1.35e-70 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 171497 [Multi-domain] Cd Length: 305 Bit Score: 220.65 E-value: 1.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 14 GRVLVNEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGEgLDHLEVE 93
Cdd:PRK12436 17 GHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIRGITVSLIH-ITGVTVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 94 NHRVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENGTIEWLMNSEMEFSY 173
Cdd:PRK12436 96 GTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEISFVLTEAVVMTGDGELRTLTKEAFEFGY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 174 RTSVLQTKRPgIVLEAEFQLQVGEREEIIRNMQkNKDYRRET-QPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGA 252
Cdd:PRK12436 176 RKSVFANNHY-IILEARFELEEGVYEEIKAKMD-DLTFKRESkQPLEYPSCGSVFKRPPNNFAGKLIQESGLQGKRIGGV 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1208968233 253 QISEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIG 300
Cdd:PRK12436 254 EVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIG 301
|
|
| murB |
PRK13904 |
UDP-N-acetylmuramate dehydrogenase; |
22-299 |
7.12e-63 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 184384 [Multi-domain] Cd Length: 257 Bit Score: 199.38 E-value: 7.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 22 LARYTTMKIGGPADILIvpkhvtgIEKTlqlvKKYKTKWTVIGRGSNLLVSDK----GIegvvirLGEGLDHLEVENHRV 97
Cdd:PRK13904 7 FSKYSSVKIGPPLEVLV-------LEEI----DDFSQDGQIIGGANNLLISPNpknlAI------LGKNFDYIKIDGECL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 98 RVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFEngtieWLMNSEMEFSYRTSV 177
Cdd:PRK13904 70 EIGGATKSGKIFNYAKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLESICTNGG-----WIEKEDIGFGYRSSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 178 LQtkrpGIVLEAEFQLQVGEREEI---IRNMQKNkdyrretQPwNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQI 254
Cdd:PRK13904 145 IN----GVILEARFKKTHGFDEELleaFKSMRKN-------QP-KGPSFGSCFKNPKGDYAGRLIEAVGLKGYCKGGAGF 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1208968233 255 SEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEII 299
Cdd:PRK13904 213 SEEHANFLVNLGGATFEDALDLIELAKKRVLEEFGINLEEEVIIL 257
|
|
| PRK14651 |
PRK14651 |
UDP-N-acetylmuramate dehydrogenase; |
21-300 |
4.06e-56 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237776 [Multi-domain] Cd Length: 273 Bit Score: 182.32 E-value: 4.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 21 PLARYTTMKIGGPADILIVPKHVtgiektlQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGEGLDHLEVENHrvrVG 100
Cdd:PRK14651 8 PLARYTTLGVGGPAELWTVETHE-------QLAEATEAPYRVLGGGSNLLVSDAGVPERVIRLGGEFAEWDLDGW---VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 101 GGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILsKALILFENGTIEWLMNSEMEFSYRTSVLqt 180
Cdd:PRK14651 78 GGVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADAL-HTVEIVHDGGFHQYSPDELGFGYRHSGL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 181 KRPGIVLEAEFQLQVGEREEIIRNMQKnKDYRRETQPWNHpCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQISEMHGN 260
Cdd:PRK14651 155 PPGHVVTRVRLKLRPSTPEAVLAKMAL-VDAARKGQPKKK-SAGCAFKNPPGDSAGRLIDEAGLKGTRVGDAMISPEHGN 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1208968233 261 FIINTGGASAQDVLSLIALikhtIKDKFGLDMHTEVEIIG 300
Cdd:PRK14651 233 FIVNLGGATAADVHALLRR----VRARVGLPLELEWELWP 268
|
|
| MurB_C |
pfam02873 |
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ... |
202-299 |
7.74e-49 |
|
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are UDP-N-acetylenolpyruvoylglucosamine reductase enzymes EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 460730 [Multi-domain] Cd Length: 99 Bit Score: 157.90 E-value: 7.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 202 IRN-MQKNKDYRRETQPWNHPCAGSVFRNPLPDFAGHLVEKAGLRGYRIGGAQISEMHGNFIINTGGASAQDVLSLIALI 280
Cdd:pfam02873 1 IRAaMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80
|
90
....*....|....*....
gi 1208968233 281 KHTIKDKFGLDMHTEVEII 299
Cdd:pfam02873 81 RERVKEKFGVELEPEVRII 99
|
|
| PRK14650 |
PRK14650 |
UDP-N-acetylmuramate dehydrogenase; |
1-300 |
5.60e-46 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173113 [Multi-domain] Cd Length: 302 Bit Score: 157.31 E-value: 5.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 1 MEQLVNELIKANVGRVLVNepLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKG-IEGV 79
Cdd:PRK14650 2 LKNINNFLKKINIKPQTKN--LANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILINDEEeIDFP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 80 VIRLGEgLDHLEVENHRVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALILFENG 159
Cdd:PRK14650 80 IIYTGH-LNKIEIHDNQIVAECGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCFGNEISEILDKITFIDEKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 160 TIEWLMNSEMEFSYRTSVLQTKRPgIVLEAEFQLQVGEREEIIRNMQKNKDYRRETQPWNHPCAGSVFRN--PLPDFAGH 237
Cdd:PRK14650 159 KTICKKFKKEEFKYKISPFQNKNT-FILKATLNLKKGNKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKNnkAFLKPTGQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1208968233 238 LVEKAGLRGYRIGGAQISEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFGLDMHTEVEIIG 300
Cdd:PRK14650 238 IIEECKLKGLSIGGATVSHYHGNFIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
|
|
| murB |
PRK13903 |
UDP-N-acetylmuramate dehydrogenase; |
21-300 |
2.00e-44 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237552 [Multi-domain] Cd Length: 363 Bit Score: 154.73 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 21 PLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLG-EGLDhLEVENHRVRV 99
Cdd:PRK13903 20 PLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDGFDGTVVRVAtRGVT-VDCGGGLVRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 100 GGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALIL-FENGTIEWLMNSEMEFSYRTSVL 178
Cdd:PRK13903 99 EAGAVWDDVVARTVEAGLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTITRVRLLdRRTGEVRWVPAADLGFGYRTSVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 179 QTKRPGIVLEAEFQLQVGERE------EIIRNMQKNKDYR------RET------------QPWNHPC--AGSVFRNPL- 231
Cdd:PRK13903 179 KHSDRAVVLEVEFQLDPSGLSaplrygELARALGVEPGERvppaavREAvlalragkgmvlDPADHDTwsAGSFFTNPVv 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 232 --------------------PDF----------AGHLVEKAGL-RGYRIGG--AQISEMHGNFIINTGGASAQDVLSLIA 278
Cdd:PRK13903 259 spavaerlaarvaerlgdpvPRYpagdggvklsAAWLIERAGFgKGYPGGGapARLSTKHTLALTNRGGATTADLVALAR 338
|
330 340
....*....|....*....|..
gi 1208968233 279 LIKHTIKDKFGLDMHTEVEIIG 300
Cdd:PRK13903 339 EVRDGVRDAFGVTLVPEPVLVG 360
|
|
| PRK14648 |
PRK14648 |
UDP-N-acetylmuramate dehydrogenase; |
19-296 |
2.01e-33 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173111 [Multi-domain] Cd Length: 354 Bit Score: 125.61 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 19 NEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGEgLDHLEVENHR-- 96
Cdd:PRK14648 15 NVPLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLRR-FRSLHTQTQRdg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 97 ---VRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISSILSKALIL------------------ 155
Cdd:PRK14648 94 svlVHAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARTLvlhpvrsrakelpevrkn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 156 ---------------FENGTIEWLMNSEMEFSYRTSVLQTKRpGIVLEAE--------FQLQVGEREEIIRNMQKNKDYR 212
Cdd:PRK14648 174 aqdkrgeclgldggpFTCSSFQTVFARAGDWGYKRSPFQSPH-GVELHAGrrlilslcVRLTPGNPAQIRKHMQEKIADR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 213 RETQPWNHPCAGSVFRNPlPDF---AGHLVEKAGLRGYRIGGAQISEMHGNFIINTGGASAQDVLSLIALIKHTIKDKFG 289
Cdd:PRK14648 253 ISKGQFRFPSAGSAFKNN-PAFgkpSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQRVFETHG 331
|
....*..
gi 1208968233 290 LDMHTEV 296
Cdd:PRK14648 332 VWLEREI 338
|
|
| murB |
PRK00046 |
UDP-N-acetylmuramate dehydrogenase; |
19-299 |
1.28e-26 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 234593 [Multi-domain] Cd Length: 334 Bit Score: 106.77 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 19 NEPLARYTTMKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKgIEGVVIRLG-EGLDHLEV--ENH 95
Cdd:PRK00046 6 NHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTED-FDGTVLLNRiKGIEVLSEddDAW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 96 RVRVGGG---YPLIKLSTllsRQGLAGLEFASGIPGSVGGAVYMNAGAH----KSDISSIlsKALILfENGTIEWLMNSE 168
Cdd:PRK00046 85 YLHVGAGenwHDLVLWTL---QQGMPGLENLALIPGTVGAAPIQNIGAYgvelKDVCDYV--EALDL-ATGEFVRLSAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 169 MEFSYRTSVLQTKRPG--IVLEAEFQLQvgereeiiRNMQKNKDY---RRETQ----------------------PWNHP 221
Cdd:PRK00046 159 CRFGYRDSIFKHEYPDryAITAVGFRLP--------KQWQPVLDYgdlARLDPdtvtaqdvfdavcairrsklpdPKVLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 222 CAGSVFRNPL-------------PDF-------------AGHLVEKAGLRGYRIGGAQISEMHGNFIINTGGASAQDVLS 275
Cdd:PRK00046 231 NAGSFFKNPVvsaeqfeallaqyPDIphypqadgsvklaAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGADVLA 310
|
330 340
....*....|....*....|....
gi 1208968233 276 LIALIKHTIKDKFGLDMHTEVEII 299
Cdd:PRK00046 311 LARHIQQDVREKFGVELEPEPRFI 334
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
34-164 |
1.44e-20 |
|
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
Pssm-ID: 426326 [Multi-domain] Cd Length: 139 Bit Score: 85.72 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 34 ADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNLLVSDKGIEGVVIRLGE--GLDHLEVENHRVRVGGGYPLIKLSTL 111
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLSRlnGILEIDPEDGTATVEAGVTLGDLVRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1208968233 112 LSRQGLA-GLEFASGIPGSVGGAVYMNAGAHKS----DISSILSKALILFENGTIEWL 164
Cdd:pfam01565 81 LAAKGLLlGLDPGSGIPGTVGGAIATNAGGYGSekygLTRDNVLGLEVVLADGEVVRL 138
|
|
| GlcD |
COG0277 |
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion]; |
1-139 |
8.09e-05 |
|
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
Pssm-ID: 440046 [Multi-domain] Cd Length: 462 Bit Score: 43.73 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1208968233 1 MEQLVNELIKANVGRVLVNEP-LARYTT---MKIGGPADILIVPKHVTGIEKTLQLVKKYKTKWTVIGRGSNL---LVSD 73
Cdd:COG0277 3 TAALLAALRAILAGRVLTDPAdRAAYARdgnSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLaggAVPL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1208968233 74 KGieGVVIRLGE--GLDHLEVENHRVRVGGGYPLIKLSTLLSRQGLA-GLEFASGIPGSVGGAVYMNAG 139
Cdd:COG0277 83 DG--GVVLDLSRmnRILEVDPEDRTATVEAGVTLADLNAALAPHGLFfPPDPSSQGTATIGGNIATNAG 149
|
|
|