|
Name |
Accession |
Description |
Interval |
E-value |
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
4-301 |
1.49e-166 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 463.81 E-value: 1.49e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 4 LVNELIEANVGRVLVDEPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRL 83
Cdd:PRK13905 1 LLKELLPALRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 84 GEGLDHLEVEKYKVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDW 163
Cdd:PRK13905 81 GKGLNEIEVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDGEIKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 164 LTHEELEFSYRTSVLQTKRpGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAG 243
Cdd:PRK13905 161 LSNEELGFGYRHSALQEEG-LIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 872563037 244 LRGYQIGGAQISEMHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIGR 301
Cdd:PRK13905 240 LKGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGE 297
|
|
| MurB |
COG0812 |
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ... |
20-299 |
2.85e-132 |
|
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: 376.28 E-value: 2.85e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 20 EPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGeGLDHLEV-EKYKVR 98
Cdd:COG0812 1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLG-RLKGIEVdDGVLVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 99 VGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDWLTHEELEFSYRTSVL 178
Cdd:COG0812 80 AGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 179 QTKRpGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISEMH 258
Cdd:COG0812 160 KRER-YIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKH 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 872563037 259 GNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEII 299
Cdd:COG0812 239 ANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
|
|
| murB |
TIGR00179 |
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ... |
22-300 |
1.26e-117 |
|
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: 339.81 E-value: 1.26e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 22 LARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGEGLDHLEVEKYKVRVGG 101
Cdd:TIGR00179 1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIEDDEGEYVHVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 102 GYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDWLTHEELEFSYRTSVLQTK 181
Cdd:TIGR00179 81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 182 RPGIVLEAEFQLQIGERER-----IVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISE 256
Cdd:TIGR00179 161 YVGLVLKAEFQLTLGFGTRldpetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 872563037 257 MHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIG 300
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
|
|
| MurB_C |
pfam02873 |
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ... |
201-299 |
5.56e-51 |
|
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: 163.29 E-value: 5.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 201 IVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISEMHGNFIINTGEASAQDVLSLIAFI 280
Cdd:pfam02873 1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80
|
90
....*....|....*....
gi 872563037 281 KQTIKDKFGVEMHTEVEII 299
Cdd:pfam02873 81 RERVKEKFGVELEPEVRII 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
4-301 |
1.49e-166 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 463.81 E-value: 1.49e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 4 LVNELIEANVGRVLVDEPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRL 83
Cdd:PRK13905 1 LLKELLPALRGRLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 84 GEGLDHLEVEKYKVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDW 163
Cdd:PRK13905 81 GKGLNEIEVEGNRITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNAGAYGGETADVLESVEVLDRDGEIKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 164 LTHEELEFSYRTSVLQTKRpGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAG 243
Cdd:PRK13905 161 LSNEELGFGYRHSALQEEG-LIVLSATFQLEPGDKEEIKARMDELLARREATQPLEYPSAGSVFKNPPGHFAGKLIEEAG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 872563037 244 LRGYQIGGAQISEMHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIGR 301
Cdd:PRK13905 240 LKGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGE 297
|
|
| MurB |
COG0812 |
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ... |
20-299 |
2.85e-132 |
|
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: 376.28 E-value: 2.85e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 20 EPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGeGLDHLEV-EKYKVR 98
Cdd:COG0812 1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLG-RLKGIEVdDGVLVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 99 VGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDWLTHEELEFSYRTSVL 178
Cdd:COG0812 80 AGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGAYGGEIKDVLESVEVLDRTGEVRTLSAEECGFGYRDSIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 179 QTKRpGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISEMH 258
Cdd:COG0812 160 KRER-YIILSVTFRLKKGDPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNPPGDSAGWLIEQAGLKGYRIGGAQVSEKH 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 872563037 259 GNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEII 299
Cdd:COG0812 239 ANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEVRII 279
|
|
| murB |
TIGR00179 |
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ... |
22-300 |
1.26e-117 |
|
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: 339.81 E-value: 1.26e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 22 LARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGEGLDHLEVEKYKVRVGG 101
Cdd:TIGR00179 1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGKGIDIEDDEGEYVHVGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 102 GYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDWLTHEELEFSYRTSVLQTK 181
Cdd:TIGR00179 81 GENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGAYGVEISEVLVYATILLATGKTEWLTNEQLGFGYRTSIFQHK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 182 RPGIVLEAEFQLQIGERER-----IVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISE 256
Cdd:TIGR00179 161 YVGLVLKAEFQLTLGFGTRldpetITAQQVFNKVCRMRTSHYPDPNAGSFFKNPSPNHAGRLIEECGLKGYQIGGAAVSK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 872563037 257 MHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIG 300
Cdd:TIGR00179 241 QHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
|
|
| murB |
PRK13906 |
UDP-N-acetylmuramate dehydrogenase; |
18-300 |
1.13e-76 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 184386 [Multi-domain] Cd Length: 307 Bit Score: 236.25 E-value: 1.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 18 VDEPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLgEGLDHLEVEKYKV 97
Cdd:PRK13906 21 VDEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISL-LSLDHIEVSDDAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 98 RVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDWLTHEELEFSYRTSV 177
Cdd:PRK13906 100 IAGSGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCIDYALCVNEQGSLIKLTTKELELDYRNSI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 178 LQtKRPGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISEM 257
Cdd:PRK13906 180 IQ-KEHLVVLEAAFTLAPGKMTEIQAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGGVEVSTK 258
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 872563037 258 HGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIG 300
Cdd:PRK13906 259 HAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIG 301
|
|
| PRK14649 |
PRK14649 |
UDP-N-acetylmuramate dehydrogenase; |
15-300 |
3.01e-75 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173112 [Multi-domain] Cd Length: 295 Bit Score: 232.42 E-value: 3.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 15 RVLVDEPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRL-GEGLD-HLEV 92
Cdd:PRK14649 2 TLRENEPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARYrGQRWElHEHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 93 EKYKVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDG-TIDWLTHEeLEF 171
Cdd:PRK14649 82 DTAEVWVEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGCYGGDTATVLIRAWLLLNGSeCVEWSVHD-FAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 172 SYRTSVLQ-------TKRPGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCaGSVFRNPIPYFAGDLIEKAGL 244
Cdd:PRK14649 161 GYRTSVLKqlradgiTWRPPLVLAARFRLHRDDPTALAARMEAIAAERKQKTPAGSSC-GSVFKNPPGDSAGRLIEAAGL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 872563037 245 RGYQIGGAQISEMHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIG 300
Cdd:PRK14649 240 KGTRIGDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEVRIIG 295
|
|
| PRK14652 |
PRK14652 |
UDP-N-acetylmuramate dehydrogenase; |
9-300 |
4.75e-73 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237777 [Multi-domain] Cd Length: 302 Bit Score: 226.68 E-value: 4.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 9 IEANV-GRVLVDEPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGEGL 87
Cdd:PRK14652 10 IARRVrGEVLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 88 DHLEVEKYKVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTiDWLTHE 167
Cdd:PRK14652 90 PGESTDGGRLVLGAGAPISRLPARAHAHGLVGMEFLAGIPGTLGGAVAMNAGTKLGEMKDVVTAVELATADGA-GFVPAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 168 ELEFSYRTSVLQTKrpGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGY 247
Cdd:PRK14652 169 ALGYAYRTCRLPPG--AVITRVEVRLRPGDVAASEALMRADRERRRRTQPLDRPTFGSTFTNPPGDYAGRLVEAVGLKGH 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 872563037 248 QIGGAQISEMHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIG 300
Cdd:PRK14652 247 RVGGAIWSPVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLG 299
|
|
| PRK12436 |
PRK12436 |
UDP-N-acetylmuramate dehydrogenase; |
14-300 |
5.07e-72 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 171497 [Multi-domain] Cd Length: 305 Bit Score: 224.50 E-value: 5.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 14 GRVLVDEPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGEgLDHLEVE 93
Cdd:PRK12436 17 GHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIRGITVSLIH-ITGVTVT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 94 KYKVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDWLTHEELEFSY 173
Cdd:PRK12436 96 GTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNAGAYGGEISFVLTEAVVMTGDGELRTLTKEAFEFGY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 174 RTSVLQTKRPgIVLEAEFQLQIGERERIVSVMQkNKDYRRET-QPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGA 252
Cdd:PRK12436 176 RKSVFANNHY-IILEARFELEEGVYEEIKAKMD-DLTFKRESkQPLEYPSCGSVFKRPPNNFAGKLIQESGLQGKRIGGV 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 872563037 253 QISEMHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIG 300
Cdd:PRK12436 254 EVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVKLEREVRIIG 301
|
|
| PRK14653 |
PRK14653 |
UDP-N-acetylmuramate dehydrogenase; |
16-298 |
1.03e-68 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237778 [Multi-domain] Cd Length: 297 Bit Score: 215.47 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 16 VLVDEPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKtKWTVIGRGSNLLVSDLGIEGVVIRLgEGLDHLEVEKY 95
Cdd:PRK14653 16 VFINEEMKCHVSFKIGGPVPLFAIPNSTNGFIETINLLKEGI-EVKILGNGTNVLPKDEPMDFVVVST-ERLDDIFVDND 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 96 KVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKaLILFEDGTIDWLTHEELEFSYRT 175
Cdd:PRK14653 94 KIICESGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAGAYGWETAENIVE-VVAYDGKKIIRLGKNEIKFSYRN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 176 SVLQTKRPGIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPIP-YFAGDLIEKAGLRGYQIGGAQI 254
Cdd:PRK14653 173 SIFKEEKDLIILRVTFKLKKGNKNEIYNLMLETMKKRVEKQPLEFPSAGSVFKRPRKdFYVGSAIEKLGLKGFSIGGAQI 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 872563037 255 SEMHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEI 298
Cdd:PRK14653 253 SEKHAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEIEI 296
|
|
| murB |
PRK13904 |
UDP-N-acetylmuramate dehydrogenase; |
22-299 |
4.38e-60 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 184384 [Multi-domain] Cd Length: 257 Bit Score: 192.06 E-value: 4.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 22 LARYTTMKIGGPADILIvpkhvagIEKTlqlvKKYKTKWTVIGRGSNLLVS----DLGIegvvirLGEGLDHLEVEKYKV 97
Cdd:PRK13904 7 FSKYSSVKIGPPLEVLV-------LEEI----DDFSQDGQIIGGANNLLISpnpkNLAI------LGKNFDYIKIDGECL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 98 RVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEdgtidWLTHEELEFSYRTSV 177
Cdd:PRK13904 70 EIGGATKSGKIFNYAKKNNLGGFEFLGKLPGTLGGLVKMNAGLKEYEISNNLESICTNGG-----WIEKEDIGFGYRSSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 178 LQtkrpGIVLEAEFQLQIGERERIVSVMQKnkdyRRETQPwNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISEM 257
Cdd:PRK13904 145 IN----GVILEARFKKTHGFDEELLEAFKS----MRKNQP-KGPSFGSCFKNPKGDYAGRLIEAVGLKGYCKGGAGFSEE 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 872563037 258 HGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEII 299
Cdd:PRK13904 216 HANFLVNLGGATFEDALDLIELAKKRVLEEFGINLEEEVIIL 257
|
|
| PRK14651 |
PRK14651 |
UDP-N-acetylmuramate dehydrogenase; |
21-300 |
9.93e-55 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237776 [Multi-domain] Cd Length: 273 Bit Score: 178.86 E-value: 9.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 21 PLARYTTMKIGGPADILIVPKHVagiektlQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGEGLDHLEVEKYkvrVG 100
Cdd:PRK14651 8 PLARYTTLGVGGPAELWTVETHE-------QLAEATEAPYRVLGGGSNLLVSDAGVPERVIRLGGEFAEWDLDGW---VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 101 GGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVsKALILFEDGTIDWLTHEELEFSYRTSVLqt 180
Cdd:PRK14651 78 GGVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNAGTRFGEMADAL-HTVEIVHDGGFHQYSPDELGFGYRHSGL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 181 KRPGIVLEAEFQLQIGERERIVSVMQKnKDYRRETQPWNHpCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISEMHGN 260
Cdd:PRK14651 155 PPGHVVTRVRLKLRPSTPEAVLAKMAL-VDAARKGQPKKK-SAGCAFKNPPGDSAGRLIDEAGLKGTRVGDAMISPEHGN 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 872563037 261 FIINTGEASAQDVLSLIAFIKQtikdKFGVEMHTEVEIIG 300
Cdd:PRK14651 233 FIVNLGGATAADVHALLRRVRA----RVGLPLELEWELWP 268
|
|
| MurB_C |
pfam02873 |
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ... |
201-299 |
5.56e-51 |
|
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: 163.29 E-value: 5.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 201 IVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYFAGDLIEKAGLRGYQIGGAQISEMHGNFIINTGEASAQDVLSLIAFI 280
Cdd:pfam02873 1 IRAAMLELRRRRLAKQPLDPPSAGSFFKNPVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGATAADVLALIEEV 80
|
90
....*....|....*....
gi 872563037 281 KQTIKDKFGVEMHTEVEII 299
Cdd:pfam02873 81 RERVKEKFGVELEPEVRII 99
|
|
| PRK14650 |
PRK14650 |
UDP-N-acetylmuramate dehydrogenase; |
22-300 |
2.95e-46 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173113 [Multi-domain] Cd Length: 302 Bit Score: 157.70 E-value: 2.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 22 LARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLG-IEGVVIRLGEgLDHLEVEKYKVRVG 100
Cdd:PRK14650 21 LANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILINDEEeIDFPIIYTGH-LNKIEIHDNQIVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 101 GGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALILFEDGTIDWLTHEELEFSYRTSVLQT 180
Cdd:PRK14650 100 CGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARCFGNEISEILDKITFIDEKGKTICKKFKKEEFKYKISPFQN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 181 KRPgIVLEAEFQLQIGERERIVSVMQKNKDYRRETQPWNHPCAGSVFRNPIPYF--AGDLIEKAGLRGYQIGGAQISEMH 258
Cdd:PRK14650 180 KNT-FILKATLNLKKGNKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKNNKAFLkpTGQIIEECKLKGLSIGGATVSHYH 258
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 872563037 259 GNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEMHTEVEIIG 300
Cdd:PRK14650 259 GNFIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
|
|
| murB |
PRK13903 |
UDP-N-acetylmuramate dehydrogenase; |
14-300 |
1.41e-44 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237552 [Multi-domain] Cd Length: 363 Bit Score: 155.12 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 14 GRVLVDEPLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGEGLDHLEVE 93
Cdd:PRK13903 13 AEVAEDVPLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDGFDGTVVRVATRGVTVDCG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 94 KYKVRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALIL-FEDGTIDWLTHEELEFS 172
Cdd:PRK13903 93 GGLVRAEAGAVWDDVVARTVEAGLGGLECLSGIPGSAGATPVQNVGAYGQEVSDTITRVRLLdRRTGEVRWVPAADLGFG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 173 YRTSVLQTKRPGIVLEAEFQL--------------------QIGERERIVSVMQKNKDYRR-------ETQP--WNhpcA 223
Cdd:PRK13903 173 YRTSVLKHSDRAVVLEVEFQLdpsglsaplrygelaralgvEPGERVPPAAVREAVLALRAgkgmvldPADHdtWS---A 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 224 GSVFRNPI----------------------PYFAGD---------LIEKAGL-RGYQIGG--AQISEMHGNFIINTGEAS 269
Cdd:PRK13903 250 GSFFTNPVvspavaerlaarvaerlgdpvpRYPAGDggvklsaawLIERAGFgKGYPGGGapARLSTKHTLALTNRGGAT 329
|
330 340 350
....*....|....*....|....*....|.
gi 872563037 270 AQDVLSLIAFIKQTIKDKFGVEMHTEVEIIG 300
Cdd:PRK13903 330 TADLVALAREVRDGVRDAFGVTLVPEPVLVG 360
|
|
| PRK14648 |
PRK14648 |
UDP-N-acetylmuramate dehydrogenase; |
21-296 |
1.09e-30 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173111 [Multi-domain] Cd Length: 354 Bit Score: 118.29 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 21 PLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGEGLD-HLEVEK---YK 96
Cdd:PRK14648 17 PLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLRRFRSlHTQTQRdgsVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 97 VRVGGGYPLIKLSTLLSRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISNIVSKALIL--------------------- 155
Cdd:PRK14648 97 VHAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARCYGRAIADCFHSARTLvlhpvrsrakelpevrknaqd 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 156 ------------FEDGTIDWLTHEELEFSYRTSVLQTKRpGIVLEAEFQLQI--------GERERIVSVMQKNKDYRRET 215
Cdd:PRK14648 177 krgeclgldggpFTCSSFQTVFARAGDWGYKRSPFQSPH-GVELHAGRRLILslcvrltpGNPAQIRKHMQEKIADRISK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 216 QPWNHPCAGSVFRNPiPYF---AGDLIEKAGLRGYQIGGAQISEMHGNFIINTGEASAQDVLSLIAFIKQTIKDKFGVEM 292
Cdd:PRK14648 256 GQFRFPSAGSAFKNN-PAFgkpSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAHQVRTLLRVVRQRVFETHGVWL 334
|
....
gi 872563037 293 HTEV 296
Cdd:PRK14648 335 EREI 338
|
|
| murB |
PRK00046 |
UDP-N-acetylmuramate dehydrogenase; |
21-299 |
9.49e-30 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 234593 [Multi-domain] Cd Length: 334 Bit Score: 114.86 E-value: 9.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 21 PLARYTTMKIGGPADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSN-LLVSDlgIEGVVIRLG-EGLDHLEVEK--YK 96
Cdd:PRK00046 8 SLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNvLFTED--FDGTVLLNRiKGIEVLSEDDdaWY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 97 VRVGGG---YPLIKLSTllsRQGLAGLEFASGIPGSVGGAVYMNAGAHKSDISN-IVSKALILFEDGTIDWLTHEELEFS 172
Cdd:PRK00046 86 LHVGAGenwHDLVLWTL---QQGMPGLENLALIPGTVGAAPIQNIGAYGVELKDvCDYVEALDLATGEFVRLSAAECRFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 173 YRTSVLQTKRPG--IVLEAEFQL--------------QIGERE--------RIVSVmqknkdyRRET--QPWNHPCAGSV 226
Cdd:PRK00046 163 YRDSIFKHEYPDryAITAVGFRLpkqwqpvldygdlaRLDPDTvtaqdvfdAVCAI-------RRSKlpDPKVLGNAGSF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 227 FRNPI----------------PYF----------AGDLIEKAGLRGYQIGGAQISEMHGNFIINTGEASAQDVLSLIAFI 280
Cdd:PRK00046 236 FKNPVvsaeqfeallaqypdiPHYpqadgsvklaAGWLIDQCGLKGFQIGGAAVHEKQALVLVNYGNATGADVLALARHI 315
|
330
....*....|....*....
gi 872563037 281 KQTIKDKFGVEMHTEVEII 299
Cdd:PRK00046 316 QQDVREKFGVELEPEPRFI 334
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
34-161 |
6.01e-21 |
|
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: 86.49 E-value: 6.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872563037 34 ADILIVPKHVAGIEKTLQLVKKYKTKWTVIGRGSNLLVSDLGIEGVVIRLGE--GLDHLEVEKYKVRVGGGYPLIKLSTL 111
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLSRlnGILEIDPEDGTATVEAGVTLGDLVRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 872563037 112 LSRQGLA-GLEFASGIPGSVGGAVYMNAGAHKS----DISNIVSKALILFEDGTI 161
Cdd:pfam01565 81 LAAKGLLlGLDPGSGIPGTVGGAIATNAGGYGSekygLTRDNVLGLEVVLADGEV 135
|
|
| |
