|
Name |
Accession |
Description |
Interval |
E-value |
| MurB |
COG0812 |
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ... |
20-324 |
2.45e-90 |
|
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: 271.12 E-value: 2.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 20 EPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRaegvKLVGIkgtinK 99
Cdd:COG0812 1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLG----RLKGI-----E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 100 IGKGiksALVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINSH-FEVEkgefLGNRLVSAALFDsKTGQVK 178
Cdd:COG0812 72 VDDG---VLVTAGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGaYGGE----IKDVLESVEVLD-RTGEVR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 179 NVDHEYFNFAYDHSKIQKTGEVVLEAVFRLDNSpDPGALWQKAMDNVKRRNEEQPVGVACSGCTFRNIsvqcakrlktPN 258
Cdd:COG0812 144 TLSAEECGFGYRDSIFKRERYIILSVTFRLKKG-DPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNP----------PG 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818551066 259 ltTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEI 324
Cdd:COG0812 213 --DSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEV 276
|
|
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
15-330 |
1.43e-85 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 259.66 E-value: 1.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 15 RVFENEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRaEGVKLVGIK 94
Cdd:PRK13905 12 RLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRLG-KGLNEIEVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 95 GTInkigkgiksalVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKIN--SHfeveKGEFlGNRLVSAALFDS 172
Cdd:PRK13905 91 GNR-----------ITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNagAY----GGET-ADVLESVEVLDR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 173 KtGQVKNVDHEYFNFAYDHSKIQKTGEVVLEAVFRLDNSpDPGALWQKAMDNVKRRNEEQPVGVACSGCTFRNisvqcak 252
Cdd:PRK13905 155 D-GEIKTLSNEELGFGYRHSALQEEGLIVLSATFQLEPG-DKEEIKARMDELLARREATQPLEYPSAGSVFKN------- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818551066 253 rlkTPNLttSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEIFYVGNF 330
Cdd:PRK13905 226 ---PPGH--FAGKLIEEAGLKGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGEF 298
|
|
| murB |
TIGR00179 |
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ... |
22-328 |
4.95e-50 |
|
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: 168.01 E-value: 4.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 22 LYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRAegvklvGIKGTINKIG 101
Cdd:TIGR00179 1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGK------GIDIEDDEGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 102 KgiksalVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINSH-FEVEkgefLGNRLVSAALFDSKTGQVKnV 180
Cdd:TIGR00179 75 Y------VHVGGGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGaYGVE----ISEVLVYATILLATGKTEW-L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 181 DHEYFNFAYDHSKIQKTGE-VVLEAVFRL----DNSPDPGALWQKAMDNVKRRNEEQPVGVACSGCTFRNisvqcakrlk 255
Cdd:TIGR00179 144 TNEQLGFGYRTSIFQHKYVgLVLKAEFQLtlgfGTRLDPETITAQQVFNKVCRMRTSHYPDPNAGSFFKN---------- 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818551066 256 tpNLTTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEIFYVG 328
Cdd:TIGR00179 214 --PSPNHAGRLIEECGLKGYQIGGAAVSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
|
|
| MurB_C |
pfam02873 |
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ... |
219-324 |
3.98e-29 |
|
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: 107.44 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 219 QKAM-DNVKRRNEEQPVGVACSGCTFRNisvqcakrlktpNLTTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAK 297
Cdd:pfam02873 2 RAAMlELRRRRLAKQPLDPPSAGSFFKN------------PVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGAT 69
|
90 100
....*....|....*....|....*..
gi 818551066 298 ASDVIQLIKLIKEKAKRTYNLDLKEEI 324
Cdd:pfam02873 70 AADVLALIEEVRERVKEKFGVELEPEV 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurB |
COG0812 |
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ... |
20-324 |
2.45e-90 |
|
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: 271.12 E-value: 2.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 20 EPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRaegvKLVGIkgtinK 99
Cdd:COG0812 1 EPLAPHTTFRIGGPADLLVEPASEEELAALLRAAREAGLPVLVLGGGSNLLVRDDGFDGLVIRLG----RLKGI-----E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 100 IGKGiksALVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINSH-FEVEkgefLGNRLVSAALFDsKTGQVK 178
Cdd:COG0812 72 VDDG---VLVTAGAGENWHDLVRFALEAGLSGLEFLAGIPGTVGGAPVMNAGaYGGE----IKDVLESVEVLD-RTGEVR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 179 NVDHEYFNFAYDHSKIQKTGEVVLEAVFRLDNSpDPGALWQKAMDNVKRRNEEQPVGVACSGCTFRNIsvqcakrlktPN 258
Cdd:COG0812 144 TLSAEECGFGYRDSIFKRERYIILSVTFRLKKG-DPAEIAAVMDAVLAIRRSKQPLELPSAGSFFKNP----------PG 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818551066 259 ltTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEI 324
Cdd:COG0812 213 --DSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNRGGATAADVLALIEEVQARVKEKFGVELEPEV 276
|
|
| murB |
PRK13905 |
UDP-N-acetylmuramate dehydrogenase; |
15-330 |
1.43e-85 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237553 [Multi-domain] Cd Length: 298 Bit Score: 259.66 E-value: 1.43e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 15 RVFENEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRaEGVKLVGIK 94
Cdd:PRK13905 12 RLLENEPLARYTSFRVGGPADYLVEPADIEDLQEFLKLLKENNIPVTVLGNGSNLLVRDGGIRGVVIRLG-KGLNEIEVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 95 GTInkigkgiksalVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKIN--SHfeveKGEFlGNRLVSAALFDS 172
Cdd:PRK13905 91 GNR-----------ITAGAGAPLIKLARFAAEAGLSGLEFAAGIPGTVGGAVFMNagAY----GGET-ADVLESVEVLDR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 173 KtGQVKNVDHEYFNFAYDHSKIQKTGEVVLEAVFRLDNSpDPGALWQKAMDNVKRRNEEQPVGVACSGCTFRNisvqcak 252
Cdd:PRK13905 155 D-GEIKTLSNEELGFGYRHSALQEEGLIVLSATFQLEPG-DKEEIKARMDELLARREATQPLEYPSAGSVFKN------- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818551066 253 rlkTPNLttSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEIFYVGNF 330
Cdd:PRK13905 226 ---PPGH--FAGKLIEEAGLKGYRIGGAQVSEKHANFIINTGGATAADIEDLIEHVQKTVKEKFGVELEWEVRIIGEF 298
|
|
| PRK14649 |
PRK14649 |
UDP-N-acetylmuramate dehydrogenase; |
14-328 |
5.58e-56 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173112 [Multi-domain] Cd Length: 295 Bit Score: 183.89 E-value: 5.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 14 LRVFENEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRAEGVKLVgI 93
Cdd:PRK14649 1 ITLRENEPLAPYTSWRIGGPARYFVEPTTPDEAIAAAAWAEQRQLPLFWLGGGSNLLVRDEGFDGLVARYRGQRWELH-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 94 KGtinkigkgiKSALVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINSHFeveKGEFLGNRLVSA-ALFDS 172
Cdd:PRK14649 80 HG---------DTAEVWVEAGAPMAGTARRLAAQGWAGLEWAEGLPGTIGGAIYGNAGC---YGGDTATVLIRAwLLLNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 173 KTGQVKNVDHeyFNFAYDHSKIQKTGE--------VVLEAVFRLDNSpDPGALWQKAMDNVKRRNEEQPVGVACsGCTFR 244
Cdd:PRK14649 148 SECVEWSVHD--FAYGYRTSVLKQLRAdgitwrppLVLAARFRLHRD-DPTALAARMEAIAAERKQKTPAGSSC-GSVFK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 245 NISvqcakrlktpnlTTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEI 324
Cdd:PRK14649 224 NPP------------GDSAGRLIEAAGLKGTRIGDAEIATRHANYIINLGGARAADILRLIDLARTRVLAQFGIELELEV 291
|
....
gi 818551066 325 FYVG 328
Cdd:PRK14649 292 RIIG 295
|
|
| murB |
TIGR00179 |
UDP-N-acetylenolpyruvoylglucosamine reductase; This model describes MurB, ... |
22-328 |
4.95e-50 |
|
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: 168.01 E-value: 4.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 22 LYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRAegvklvGIKGTINKIG 101
Cdd:TIGR00179 1 LAEFTTYKIGGNARHIVCPESIEQLVNVLDNAKEEDQPLLILGEGSNLLILDDGRGGVIINLGK------GIDIEDDEGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 102 KgiksalVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINSH-FEVEkgefLGNRLVSAALFDSKTGQVKnV 180
Cdd:TIGR00179 75 Y------VHVGGGENWHKLVKYALKNGLSGLEFLAGIPGTVGGAVIMNAGaYGVE----ISEVLVYATILLATGKTEW-L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 181 DHEYFNFAYDHSKIQKTGE-VVLEAVFRL----DNSPDPGALWQKAMDNVKRRNEEQPVGVACSGCTFRNisvqcakrlk 255
Cdd:TIGR00179 144 TNEQLGFGYRTSIFQHKYVgLVLKAEFQLtlgfGTRLDPETITAQQVFNKVCRMRTSHYPDPNAGSFFKN---------- 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818551066 256 tpNLTTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEIFYVG 328
Cdd:TIGR00179 214 --PSPNHAGRLIEECGLKGYQIGGAAVSKQHANFLVNIDNAKSEDVLDLIEHVKAEVGEKYGILLEPEVKIIG 284
|
|
| PRK14651 |
PRK14651 |
UDP-N-acetylmuramate dehydrogenase; |
18-311 |
2.87e-39 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237776 [Multi-domain] Cd Length: 273 Bit Score: 139.57 E-value: 2.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 18 ENEPLYKYTYFKIGGSARLFFeAKNVEDLKLALETatehkiPFVVLGGGANVLVSDQGFEGLVIRnraegvkLVGIKGTI 97
Cdd:PRK14651 5 ERVPLARYTTLGVGGPAELWT-VETHEQLAEATEA------PYRVLGGGSNLLVSDAGVPERVIR-------LGGEFAEW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 98 NKIGkgiksalvWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINShfevekgeflGNRLvsAALFDS----- 172
Cdd:PRK14651 71 DLDG--------WVGGGVPLPGLVRRAARLGLSGLEGLVGIPAQVGGAVKMNA----------GTRF--GEMADAlhtve 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 173 --KTGQVKNVDHEYFNFAYDHSKIQKtGEVVLEAVFRLDNSPdPGALWQKaMDNVKRRNEEQPvGVACSGCTFRNISVQc 250
Cdd:PRK14651 131 ivHDGGFHQYSPDELGFGYRHSGLPP-GHVVTRVRLKLRPST-PEAVLAK-MALVDAARKGQP-KKKSAGCAFKNPPGD- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818551066 251 akrlktpnlttSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEK 311
Cdd:PRK14651 206 -----------SAGRLIDEAGLKGTRVGDAMISPEHGNFIVNLGGATAADVHALLRRVRAR 255
|
|
| PRK12436 |
PRK12436 |
UDP-N-acetylmuramate dehydrogenase; |
2-328 |
9.75e-36 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 171497 [Multi-domain] Cd Length: 305 Bit Score: 131.28 E-value: 9.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 2 EDFTKIKNILGPLRVFENEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVi 81
Cdd:PRK12436 5 EVYEYLSTVLPEGHVKQDEMLKNHTHIKVGGKADVFVAPTNYDEIQEVIKYANKYNIPVTFLGNGSNVIIKDGGIRGIT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 82 rnraegVKLVGIKGTInkigkgIKSALVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINShfevekGEFLG 161
Cdd:PRK12436 84 ------VSLIHITGVT------VTGTTIVAQCGAAIIDVSRIALDHNLTGLEFACGIPGSVGGALYMNA------GAYGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 162 --NRLVSAALFDSKTGQVKNVDHEYFNFAYDHSKIQKTGEVVLEAVFRLDNSpDPGALWQKAMDNVKRRNEEQPVGVACS 239
Cdd:PRK12436 146 eiSFVLTEAVVMTGDGELRTLTKEAFEFGYRKSVFANNHYIILEARFELEEG-VYEEIKAKMDDLTFKRESKQPLEYPSC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 240 GCTFRnisvqcakrlKTPNltTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLD 319
Cdd:PRK12436 225 GSVFK----------RPPN--NFAGKLIQESGLQGKRIGGVEVSLKHAGFMVNVDNGTAQDYIDLIHFVQKTVEEKFGVK 292
|
....*....
gi 818551066 320 LKEEIFYVG 328
Cdd:PRK12436 293 LEREVRIIG 301
|
|
| PRK14652 |
PRK14652 |
UDP-N-acetylmuramate dehydrogenase; |
16-330 |
3.55e-35 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237777 [Multi-domain] Cd Length: 302 Bit Score: 129.61 E-value: 3.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 16 VFENEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRAEGVKLVGIKG 95
Cdd:PRK14652 18 VLRDAPLAPRTAVRVGGPADLLVRPADPDALSALLRAVRELGVPLSILGGGANTLVADAGVRGVVLRLPQDFPGESTDGG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 96 TINkIGKGIKSALVWTASGTlmnqlgrftmdQGLEGLEFLLSIPGTVGGGIKINShfevekGEFLGN--RLVSAALFDSK 173
Cdd:PRK14652 98 RLV-LGAGAPISRLPARAHA-----------HGLVGMEFLAGIPGTLGGAVAMNA------GTKLGEmkDVVTAVELATA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 174 TGqVKNVDHEYFNFAYDHSKIqKTGEVVLEAVFRLdnSPDPGALWQKAMD-NVKRRNEEQPVGVACSGCTFRNISVQCAK 252
Cdd:PRK14652 160 DG-AGFVPAAALGYAYRTCRL-PPGAVITRVEVRL--RPGDVAASEALMRaDRERRRRTQPLDRPTFGSTFTNPPGDYAG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818551066 253 RLktpnlttsagyiIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEIFYVGNF 330
Cdd:PRK14652 236 RL------------VEAVGLKGHRVGGAIWSPVHANFVTNLGGATARDVLALVRLARARVKERFGIALETEVRLLGEF 301
|
|
| murB |
PRK13906 |
UDP-N-acetylmuramate dehydrogenase; |
19-329 |
3.21e-33 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 184386 [Multi-domain] Cd Length: 307 Bit Score: 124.55 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 19 NEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIrnraEGVKLVGIKGTIN 98
Cdd:PRK13906 22 DEPLKRYTYTKTGGNADFYITPTKNEEVQAVVKYAYQNEIPVTYLGNGSNIIIREGGIRGIVI----SLLSLDHIEVSDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 99 KIGKGiksalvwtaSGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINShfevekGEFLG--NRLVSAALFDSKTGQ 176
Cdd:PRK13906 98 AIIAG---------SGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNA------GAYGGevKDCIDYALCVNEQGS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 177 VKNVDHEYFNFAYDHSKIQKTGEVVLEAVFRLdnspDPGAL--WQKAMDNV-KRRNEEQPVGVACSGCTFRnisvqcakr 253
Cdd:PRK13906 163 LIKLTTKELELDYRNSIIQKEHLVVLEAAFTL----APGKMteIQAKMDDLtERRESKQPLEYPSCGSVFQ--------- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818551066 254 lKTPNltTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEIFYVGN 329
Cdd:PRK13906 230 -RPPG--HFAGKLIQDSNLQGHRIGGVEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE 302
|
|
| PRK14653 |
PRK14653 |
UDP-N-acetylmuramate dehydrogenase; |
16-324 |
8.41e-32 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237778 [Multi-domain] Cd Length: 297 Bit Score: 120.71 E-value: 8.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 16 VFENEPLYKYTYFKIGGSARLFFEAKNVEdlkLALETAT--EHKIPFVVLGGGANVLVSDQGFEGLVIRNRaegvKLVGI 93
Cdd:PRK14653 16 VFINEEMKCHVSFKIGGPVPLFAIPNSTN---GFIETINllKEGIEVKILGNGTNVLPKDEPMDFVVVSTE----RLDDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 94 KGTINKIGKGiksalvwtaSGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINS-HFEVEKGEFlgnrLVSAALFDS 172
Cdd:PRK14653 89 FVDNDKIICE---------SGLSLKKLCLVAAKNGLSGFENAYGIPGSVGGAVYMNAgAYGWETAEN----IVEVVAYDG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 173 KtgQVKNVDHEYFNFAYDHSKIQKTGE-VVLEAVFRLDNSpDPGALWQKAMDNVKRRNEEQPVGVACSGCTFrnisvqca 251
Cdd:PRK14653 156 K--KIIRLGKNEIKFSYRNSIFKEEKDlIILRVTFKLKKG-NKNEIYNLMLETMKKRVEKQPLEFPSAGSVF-------- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818551066 252 krlKTPNLTTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEI 324
Cdd:PRK14653 225 ---KRPRKDFYVGSAIEKLGLKGFSIGGAQISEKHAGFIINYNNAKAEDVLKLIEYVKDKIYENYNVELETEI 294
|
|
| MurB_C |
pfam02873 |
UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain; Members of this family are ... |
219-324 |
3.98e-29 |
|
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: 107.44 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 219 QKAM-DNVKRRNEEQPVGVACSGCTFRNisvqcakrlktpNLTTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAK 297
Cdd:pfam02873 2 RAAMlELRRRRLAKQPLDPPSAGSFFKN------------PVGHSAGWLIEQAGLKGYRIGGAQVSEKHANFLVNTGGAT 69
|
90 100
....*....|....*....|....*..
gi 818551066 298 ASDVIQLIKLIKEKAKRTYNLDLKEEI 324
Cdd:pfam02873 70 AADVLALIEEVRERVKEKFGVELEPEV 96
|
|
| PRK14650 |
PRK14650 |
UDP-N-acetylmuramate dehydrogenase; |
18-328 |
1.34e-28 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173113 [Multi-domain] Cd Length: 302 Bit Score: 112.25 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 18 ENEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRnraegvklvgIKGTI 97
Cdd:PRK14650 17 QTKNLANYTTYKIGGISKLFLTPKTIKDAEHIFKAAIEEKIKIFILGGGSNILINDEEEIDFPII----------YTGHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 98 NKIGkgIKSALVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINSH-FEVEKGEFLgnrlvSAALFDSKTGQ 176
Cdd:PRK14650 87 NKIE--IHDNQIVAECGTNFEDLCKFALQNELSGLEFIYGLPGTLGGAIWMNARcFGNEISEIL-----DKITFIDEKGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 177 VKNVDHEYFNFAYDHSKIQKTGEVVLEAVFRLDNSpDPGALWQKAMDNVKRRNEEQPVGVACSGCTFRNisvqcakrlkT 256
Cdd:PRK14650 160 TICKKFKKEEFKYKISPFQNKNTFILKATLNLKKG-NKKHIEEIMKQNKQIRINKGHYLFPSSGSTFKN----------N 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818551066 257 PNLTTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEIFYVG 328
Cdd:PRK14650 229 KAFLKPTGQIIEECKLKGLSIGGATVSHYHGNFIININNATSKDIKTLIEKVKTEVQIKTGFLLEEEVLYIG 300
|
|
| murB |
PRK00046 |
UDP-N-acetylmuramate dehydrogenase; |
18-323 |
1.10e-27 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 234593 [Multi-domain] Cd Length: 334 Bit Score: 110.24 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 18 ENEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQgFEGLVIRNRAEGVKLVGIKGTi 97
Cdd:PRK00046 5 MNHSLKPLNTFGIDARARHLVEAESEEQLLEALADARAAGLPVLVLGGGSNVLFTED-FDGTVLLNRIKGIEVLSEDDD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 98 nkigkgikSALVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVG----------GgikinshfeVEkgefLGNRLVSA 167
Cdd:PRK00046 83 --------AWYLHVGAGENWHDLVLWTLQQGMPGLENLALIPGTVGaapiqnigayG---------VE----LKDVCDYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 168 ALFDSKTGQVKNVDHEYFNFAYDHS--KIQKTGEVVLEAV-FRLDNSPDP----GALWQKAMDNV----------KRRNE 230
Cdd:PRK00046 142 EALDLATGEFVRLSAAECRFGYRDSifKHEYPDRYAITAVgFRLPKQWQPvldyGDLARLDPDTVtaqdvfdavcAIRRS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 231 EQP----VGVAcsGCTFRN--ISVQCAKRLKT--PNLTT----------SAGYIIESLGLKGTKIDGVQISTHHANFIIN 292
Cdd:PRK00046 222 KLPdpkvLGNA--GSFFKNpvVSAEQFEALLAqyPDIPHypqadgsvklAAGWLIDQCGLKGFQIGGAAVHEKQALVLVN 299
|
330 340 350
....*....|....*....|....*....|.
gi 818551066 293 TGGAKASDVIQLIKLIKEKAKRTYNLDLKEE 323
Cdd:PRK00046 300 YGNATGADVLALARHIQQDVREKFGVELEPE 330
|
|
| murB |
PRK13904 |
UDP-N-acetylmuramate dehydrogenase; |
24-324 |
5.31e-26 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 184384 [Multi-domain] Cd Length: 257 Bit Score: 103.85 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 24 KYTYFKIGGSarlfFEAKNVEDLKlalETATEHkipfVVLGGGANVLVSDQGFEGLVIRNRAEGVKlvgIKGTINKIGKG 103
Cdd:PRK13904 9 KYSSVKIGPP----LEVLVLEEID---DFSQDG----QIIGGANNLLISPNPKNLAILGKNFDYIK---IDGECLEIGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 104 IKSALVWtasgtlmnqlgRFTMDQGLEGLEFLLSIPGTVGGGIKINSHFeveKGEFLGNRLVSAALFDsktGQVKNvdhE 183
Cdd:PRK13904 75 TKSGKIF-----------NYAKKNNLGGFEFLGKLPGTLGGLVKMNAGL---KEYEISNNLESICTNG---GWIEK---E 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 184 YFNFAYDHSKIQktgEVVLEAVFRLDNSPDPGALwqkAMDNVKRRNeeQPVGVACSGCtFRNisvqcakrlkTPNltTSA 263
Cdd:PRK13904 135 DIGFGYRSSGIN---GVILEARFKKTHGFDEELL---EAFKSMRKN--QPKGPSFGSC-FKN----------PKG--DYA 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818551066 264 GYIIESLGLKGTKIDGVQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEI 324
Cdd:PRK13904 194 GRLIEAVGLKGYCKGGAGFSEEHANFLVNLGGATFEDALDLIELAKKRVLEEFGINLEEEV 254
|
|
| PRK14648 |
PRK14648 |
UDP-N-acetylmuramate dehydrogenase; |
19-328 |
1.80e-24 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 173111 [Multi-domain] Cd Length: 354 Bit Score: 101.72 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 19 NEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRaegvKLVGIKGTIN 98
Cdd:PRK14648 15 NVPLAERCSFRIGGAAQFWAEPRSCTQLRALIEEAQRARIPLSLIGGGSNVLIADEGVPGLMLSLR----RFRSLHTQTQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 99 KIGkgikSALVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVGGGIKINSHFeveKGEFLGNRLVSAALF-------- 170
Cdd:PRK14648 91 RDG----SVLVHAGAGLPVAALLAFCAHHALRGLETFAGLPGSVGGAAYMNARC---YGRAIADCFHSARTLvlhpvrsr 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 171 -----------DSKTGQVKNVDHEYF-------------NFAYDHSKIQKTGEVVLEAVFRLDNS-------PDPGALWQ 219
Cdd:PRK14648 164 akelpevrknaQDKRGECLGLDGGPFtcssfqtvfaragDWGYKRSPFQSPHGVELHAGRRLILSlcvrltpGNPAQIRK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 220 KAMDNVKRRNEEQPVGVACSGCTFRNisvqcakrlkTPNLTTSAGYIIESLGLKGTKIDGVQISTHHANFIINTGGAKAS 299
Cdd:PRK14648 244 HMQEKIADRISKGQFRFPSAGSAFKN----------NPAFGKPSGILIEEAGLRGTSCGAAQVAPWHGNLIINTGNATAH 313
|
330 340
....*....|....*....|....*....
gi 818551066 300 DVIQLIKLIKEKAKRTYNLDLKEEIFYVG 328
Cdd:PRK14648 314 QVRTLLRVVRQRVFETHGVWLEREIIFSG 342
|
|
| murB |
PRK13903 |
UDP-N-acetylmuramate dehydrogenase; |
11-328 |
3.84e-23 |
|
UDP-N-acetylmuramate dehydrogenase;
Pssm-ID: 237552 [Multi-domain] Cd Length: 363 Bit Score: 98.11 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 11 LGPLRVFENEPLYKYTYFKIGGSARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRAEGVKL 90
Cdd:PRK13903 10 FAGAEVAEDVPLAPLTTLRVGGPARRLVTCTSTEELVAAVRELDAAGEPLLVLGGGSNLVIADDGFDGTVVRVATRGVTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 91 VGIKGtinkigkgiksaLVWTASGTLMNQLGRFTMDQGLEGLEFLLSIPGTVG-------GGikinshFEVEKGEFlgnr 163
Cdd:PRK13903 90 DCGGG------------LVRAEAGAVWDDVVARTVEAGLGGLECLSGIPGSAGatpvqnvGA------YGQEVSDT---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 164 LVSAALFDSKTGQVKNVDHEYFNFAYDHSKIQKTGE-VVLEAVFRLDNSP----------------DPGALW--QKAMDN 224
Cdd:PRK13903 148 ITRVRLLDRRTGEVRWVPAADLGFGYRTSVLKHSDRaVVLEVEFQLDPSGlsaplrygelaralgvEPGERVppAAVREA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 225 VK--RR------NEEQP----VGvacSGCT--------FRNISVQCAKRLKTP---------NLTTSAGYIIESLGL-KG 274
Cdd:PRK13903 228 VLalRAgkgmvlDPADHdtwsAG---SFFTnpvvspavAERLAARVAERLGDPvprypagdgGVKLSAAWLIERAGFgKG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 818551066 275 TKIDG--VQISTHHANFIINTGGAKASDVIQLIKLIKEKAKRTYNLDLKEEIFYVG 328
Cdd:PRK13903 305 YPGGGapARLSTKHTLALTNRGGATTADLVALAREVRDGVRDAFGVTLVPEPVLVG 360
|
|
| FAD_binding_4 |
pfam01565 |
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ... |
34-151 |
4.33e-12 |
|
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: 62.60 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818551066 34 ARLFFEAKNVEDLKLALETATEHKIPFVVLGGGANVLVSDQGFEGLVIRNRaegvKLVGIKgTINKIGKgiksaLVWTAS 113
Cdd:pfam01565 1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQTGGIVLDLS----RLNGIL-EIDPEDG-----TATVEA 70
|
90 100 110
....*....|....*....|....*....|....*....
gi 818551066 114 GTLMNQLGRFTMDQGLE-GLEFLLSIPGTVGGGIKINSH 151
Cdd:pfam01565 71 GVTLGDLVRALAAKGLLlGLDPGSGIPGTVGGAIATNAG 109
|
|
| |
