|
Name |
Accession |
Description |
Interval |
E-value |
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
8-434 |
0e+00 |
|
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440536 [Multi-domain] Cd Length: 451 Bit Score: 528.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 8 YHFVGIKGSGMSSLALVLHEQGLNVQGSDIEKYFFTQRdLEKANITI-LPFNADNVKPGMTIIAGNAFPDSHEEIQRAKE 86
Cdd:COG0773 7 IHFIGIGGIGMSGLAEILLALGYKVSGSDLAESPMTER-LEALGIPVfIGHDAENIDDADLVVVSSAIPRDNPELVAARE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 87 LGLEVIRYHDFIGHFIQNYTSIAVTGSHGKTSTTGLLSHVL--SGVRPTsYLIGD-----GTGHGDPQAEFFSFEACEYR 159
Cdd:COG0773 86 RGIPVLSRAEMLAELMRGKRSIAVAGTHGKTTTTSMLAHILeeAGLDPT-FLIGGilnnfGTNARLGDGDYFVAEADESD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 160 RHFLAYSPDYAIMTNIDFDHPDYYTSIDDVFTAFQTMAGQVKK--AIFAYGDDAYLRKL--KANVPIYYYGVTENDDIQA 235
Cdd:COG0773 165 GSFLHYSPDIAVVTNIEADHLDIYGDLEAIKEAFHEFARNVPFygLLVLCADDPGLRELlpRCGRPVITYGFSEDADYRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 236 RNIERTTSGSAFDVYHGDEFVGHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRFSEKI-VADMTVV 314
Cdd:COG0773 245 ENIRIDGGGSTFDVLRRGEELGEVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALASFKGVKRRFELKGeVGGVTVI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 315 DDYAHHPAEIKATIDGARQKYPDKEIIAVFQPHTFTRTIALMDEFAEALDLADKVYLCDIFGSAREEQGNVKIEDLGAKI 394
Cdd:COG0773 325 DDYAHHPTEIAATLAAAREKYPDRRLVAVFQPHRYSRTRDFLDEFAEALSLADEVILLDIYAAREKPIPGVSSEDLAEAI 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 488225192 395 KK-GGEVIKENNVSPLLDY------HDAVVIFMGAGDVQKFEQAYEK 434
Cdd:COG0773 405 RKrGKDVVYVPDLDELVEAlaeiarPGDVVLTMGAGDIGGLGEKLLE 451
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
8-428 |
1.58e-144 |
|
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273433 [Multi-domain] Cd Length: 448 Bit Score: 419.79 E-value: 1.58e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 8 YHFVGIKGSGMSSLALVLHEQGLNVQGSDIEKYFFTQRdLEKANITIL-PFNADNVKPGMTIIAGNAFPDSHEEIQRAKE 86
Cdd:TIGR01082 2 IHFVGIGGIGMSGIAEILLNRGYQVSGSDIAENATTKR-LEALGIPIYiGHSAENLDDADVVVVSAAIKDDNPEIVEAKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 87 LGLEVIRYHDFIGHFIQNYTSIAVTGSHGKTSTTGLLSHVLSGVRP-TSYLIGDGTGHGDPQA-----EFFSFEACEYRR 160
Cdd:TIGR01082 81 RGIPVIRRAEMLAELMRFRHSIAVAGTHGKTTTTAMIAVILKEAGLdPTVVVGGLVKEAGTNArlgsgEYLVAEADESDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 161 HFLAYSPDYAIMTNIDFDHPD-YYTSIDDVFTAFQTMAGQVKK--AIFAYGDDAYLRKLKAN---VPIYYYGVTENDDIQ 234
Cdd:TIGR01082 161 SFLHLQPNVAIVTNIEPDHLDtYGSSFERLKAAFEKFIHNLPFygLAVICADDPVLRELVPKateQVITYGGSGEDADYR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 235 ARNIERTTSGSAFDVYHGDEFVGHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRFSEKI-VADMTV 313
Cdd:TIGR01082 241 AENIQQSGAEGKFSVRGKGKLYLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQGVKRRFEILGeFGGVLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 314 VDDYAHHPAEIKATIDGARQKYPDKEIIAVFQPHTFTRTIALMDEFAEALDLADKVYLCDIFGSAREEQGNVKIEDLGAK 393
Cdd:TIGR01082 321 IDDYAHHPTEIKATLKAARQGYPDKRIVVVFQPHRYSRTRDLFDDFAKVLSDADELILLDIYAAGEEPINGIDGKSLARK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 488225192 394 IKKGG--EVI-------KENNVSPLLDYHDaVVIFMGAGDVQKF 428
Cdd:TIGR01082 401 ITQLGkiEPYfvpdlaeLVEFLAAVLQSGD-LILTMGAGDIIKL 443
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
8-425 |
1.44e-51 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 185.79 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 8 YHFVGIKGSGMSSLALVLHEQGLNVQGSDIEKYFFTQRDLEKANITILPFNADNVKPGMTIIAGNAFPDSHEEIQRAKEL 87
Cdd:PRK14573 7 YHFIGIGGIGMSALAHILLDRGYSVSGSDLSEGKTVEKLKAKGARFFLGHQEEHVPEDAVVVYSSSISKDNVEYLSAKSR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 88 GLEVIRYHDFIGHFIQNYTSIAVTGSHGKTSTTGLLSHVLSGVRPT-SYLIG----DGTGHGDPQAEFFSFEACEYRRHF 162
Cdd:PRK14573 87 GNRLVHRAELLAELMQEQISILVSGSHGKTTVSSLITAIFQEAKKDpSYAIGglnqEGLNGYSGSSEYFVAEADESDGSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 163 LAYSPDYAIMTNIDFDH-PDYYTSIDDVFTAFQTMAGQVK--KAIFAYGDdayLRKLKANVPIYYYGVTENDDIQARNIE 239
Cdd:PRK14573 167 KHYTPEFSVITNIDNEHlSNFEGDRELLLASIQDFARKVQqiNKCFYNGD---CPRLKGCLQGHSYGFSSSCDLHILSYY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 240 RTTSGSAFDVYHGDEFVGHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRFSEKIVADMTV-VDDYA 318
Cdd:PRK14573 244 QEGWRSYFSAKFLGVVYQDIELNLVGMHNVANAAAAMGIALTLGIDEGAIRNALKGFSGVQRRLERKNSSETFLfLEDYA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 319 HHPAEIKATIDGARQKYPDKEIIAVFQPHTFTRTIALMDEFAEALDLADKVYLCDIFGSAREEQGNVKIEDLGAKIKKGG 398
Cdd:PRK14573 324 HHPSEISCTLRAVRDAVGLRRIIAICQPHRFSRLRECLDSFPSAFQDADEVILTDVYSAGEEPEDSISYQKLAEAISQSS 403
|
410 420 430
....*....|....*....|....*....|....*
gi 488225192 399 EV----IKENNVSPLLD----YHDaVVIFMGAGDV 425
Cdd:PRK14573 404 IVkctyVPFHEIQRYLEqsirVHD-VCVSLGAGNI 437
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
108-344 |
1.85e-30 |
|
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl tripeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440532 [Multi-domain] Cd Length: 459 Bit Score: 122.49 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 108 IAVTGSHGKTSTTGLLSHVLSGV-RPTSYL------IGDG---TGH--GDP-------------QAEFFSFE----ACEY 158
Cdd:COG0769 83 IGVTGTNGKTTTTYLLAQILRALgKKTGLIgtvgngIGGElipSSLttPEAldlqrllaemvdaGVTHVVMEvsshALDQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 159 RR----HFlayspDYAIMTNIDFDHPDYYTSIDDVFTA----FqTMAGQVKKAIFaYGDDAYLRKLKANVP--IYYYGVT 228
Cdd:COG0769 163 GRvdgvRF-----DVAVFTNLTRDHLDYHGTMEAYFAAkarlF-DQLGPGGAAVI-NADDPYGRRLAAAAParVITYGLK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 229 ENDDIQARNIERTTSGSAFDVYHGDEfVGHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRFsEKIV 308
Cdd:COG0769 236 ADADLRATDIELSADGTRFTLVTPGG-EVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRM-ERVD 313
|
250 260 270
....*....|....*....|....*....|....*...
gi 488225192 309 ADM--TVVDDYAHHPAEIKATIDGARQkYPDKEIIAVF 344
Cdd:COG0769 314 GGQgpTVIVDYAHTPDALENVLEALRP-HTKGRLIVVF 350
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
110-279 |
2.58e-26 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 105.08 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 110 VTGSHGKTSTTGLLSHVLS---GVRPTSYLIGDGTGHGDP---------------QAEFFSFEACEYRRHFLAYS----P 167
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSlagGVIGTIGTYIGKSGNTTNnaiglpltlaemveaGAEYAVLEVSSHGLGEGRLSgllkP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 168 DYAIMTNIDFDHPDYYTSIDDVFTAF-QTMAGQVKKAIFAY-GDDAYLRKL-----KANVPIYYYGVTENDDIQARNIER 240
Cdd:pfam08245 81 DIAVFTNISPDHLDFHGTMENYAKAKaELFEGLPEDGIAVInADDPYGAFLiaklkKAGVRVITYGIEGEADLRAANIEL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 488225192 241 TTSGSAFDVYHGDEFVGHFTVPAFGKHNILNALGVIAVA 279
Cdd:pfam08245 161 SSDGTSFDLFTVPGGELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
108-316 |
2.37e-24 |
|
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide synthase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440533 [Multi-domain] Cd Length: 451 Bit Score: 104.80 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 108 IAVTGSHGKTSTTGLLSHVLSGVRPT-----SY--LIG--------DgtghgdPQAEFFSFE--AceyrRHF--LAY--- 165
Cdd:COG0770 103 IAITGSNGKTTTKEMLAAVLSTKGKVlatpgNFnnEIGvpltllrlP------EDHEFAVLEmgM----NHPgeIAYlar 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 166 --SPDYAIMTNIDFDHPDYYTSIDDVFTAfqtmagqvKKAIFAY----------GDDAYLRKL--KANVPIYYYGVTEND 231
Cdd:COG0770 173 iaRPDIAVITNIGPAHLEGFGSLEGIARA--------KGEIFEGlppggvavlnADDPLLAALaeRAKARVLTFGLSEDA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 232 DIQARNIERTTSGSAFDVYHGDEFVgHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRF-SEKIVAD 310
Cdd:COG0770 245 DVRAEDIELDEDGTRFTLHTPGGEL-EVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLeVIEGAGG 323
|
....*.
gi 488225192 311 MTVVDD 316
Cdd:COG0770 324 VTLIDD 329
|
|
| murF |
TIGR01143 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ... |
108-329 |
8.03e-21 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273468 [Multi-domain] Cd Length: 417 Bit Score: 93.87 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 108 IAVTGSHGKTSTTGLLSHVLSGVRPTSYLIGDGTGH-GDPQA--------EFFSFEACEYRRHFLAY-----SPDYAIMT 173
Cdd:TIGR01143 77 IGITGSSGKTTTKEMLAAILSHKYKVFATPGNFNNEiGLPLTllrapgdhDYAVLEMGASHPGEIAYlaeiaKPDIAVIT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 174 NIDFDHPDYYTSIDDV-------FTAFQTMAGQVKKAIFAYGDdaYLRKLKANVPIYYYGvTENDDIQARNIERTTSGSA 246
Cdd:TIGR01143 157 NIGPAHLEGFGSLEGIaeakgeiLQGLKENGIAVINADDPAFA--DLAKRLPNRNILSFG-FEGGDFVAKDISYSALGST 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 247 -FDVYHGDEFVGhFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRFSEKIVADMTVVDD-YAHHPAEI 324
Cdd:TIGR01143 234 sFTLVAPGGEFE-VSLPLLGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFEVQTKNGLTLIDDtYNANPDSM 312
|
....*
gi 488225192 325 KATID 329
Cdd:TIGR01143 313 RAALD 317
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
97-344 |
7.72e-19 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 88.27 E-value: 7.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 97 FIGHFIQNYTSIAVTGSHGKTSTTGLLSHVLSGVRPTSYLIG------DG----TGH--GDP---QAEFFSF--EACEY- 158
Cdd:PRK00139 87 FYGHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGtlgngiGGelipSGLttPDAldlQRLLAELvdAGVTYa 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 159 -----------RR----HFlayspDYAIMTNIDFDHPDYYTSIDDVFTA----FQTMAGqvKKAIFAygDDAYLRKLKAN 219
Cdd:PRK00139 167 amevsshaldqGRvdglKF-----DVAVFTNLSRDHLDYHGTMEDYLAAkarlFSELGL--AAVINA--DDEVGRRLLAL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 220 VPIYYYGvTENDDIQARNIERTTSGSAFDvyhgdeFVGHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGV 299
Cdd:PRK00139 238 PDAYAVS-MAGADLRATDVEYTDSGQTFT------LVTEVESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGV 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488225192 300 KRRFsEKIVA--DMTVVDDYAHHPAEIKATIDGARQkYPDKEIIAVF 344
Cdd:PRK00139 311 PGRM-ERVDAgqGPLVIVDYAHTPDALEKVLEALRP-HAKGRLICVF 355
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
52-373 |
1.58e-18 |
|
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. An exception is Staphylococcus aureus, in which diaminopimelate is replaced by lysine in the peptidoglycan and MurE is EC 6.3.2.7. The Mycobacteria, part of the closest neighboring branch outside of the low-GC Gram-positive bacteria, use diaminopimelate. A close homolog, scoring just below the trusted cutoff, is found (with introns) in Arabidopsis thaliana. Its role is unknown. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273435 [Multi-domain] Cd Length: 464 Bit Score: 87.37 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 52 ITILPFNADNVKPGMTIIA--GNAFpDSHEEIQRAKELG----------------LEVIRYHD-----------FIGHFI 102
Cdd:TIGR01085 4 VTGLTLDSREVKPGDLFVAikGTHV-DGHDFIHDAIANGavavvverdvdfyvapVPVIIVPDlrhalsslaaaFYGHPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 103 QNYTSIAVTGSHGKTSTTGLLSHVL------SGVRPTSY-------LIGDGTGHGDPQA---------------EFFSFE 154
Cdd:TIGR01085 83 KKLKVIGVTGTNGKTTTTSLIAQLLrllgkkTGLIGTIGyrlggndLIKNPAALTTPEAltlqstlaemveagaQYAVME 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 155 AC-----EYRRHFLAYspDYAIMTNIDFDHPDYYTSIDDVFTA----FQTMAGQVKKAIFAygDDAYLRKLKANVP---- 221
Cdd:TIGR01085 163 VSshalaQGRVRGVRF--DAAVFTNLSRDHLDFHGTMENYFAAkaslFTELGLKRFAVINL--DDEYGAQFVKRLPkdit 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 222 ---IYYYGVTENDDIQARNIERTTSGSAFDVYHGDEfVGHFTVPAFGKHNILNALGVIAVA-YFEKLDLKEVAEEMLTFP 297
Cdd:TIGR01085 239 vsaITQPADGRAQDIKITDSGYSFEGQQFTFETPAG-EGHLHTPLIGRFNVYNLLAALATLlHLGGIDLEDIVAALEKFR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 298 GVKRRFsEKI--VADMTVVDDYAHHP-AEIKATIdgARQKYPDKEIIAVF----QPHTFTRtiALMDEFAEalDLADKVY 370
Cdd:TIGR01085 318 GVPGRM-ELVdgGQKFLVIVDYAHTPdALEKALR--TLRKHKDGRLIVVFgcggDRDRGKR--PLMGAIAE--QLADLVI 390
|
...
gi 488225192 371 LCD 373
Cdd:TIGR01085 391 LTS 393
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
4-316 |
1.72e-18 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 87.06 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 4 QNKLYHFVGIKGSGMSsLALVLHEQGLNVQGSDIEKYF-FTQRDLEKANITI--------LPFNADN-VK-PGMtiiagn 72
Cdd:COG0771 3 KGKKVLVLGLGKSGLA-AARLLAKLGAEVTVSDDRPAPeLAAAELEAPGVEVvlgehpeeLLDGADLvVKsPGI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 73 afPDSHEEIQRAKELGLEVI-------RYHDfiGHFIqnytsiAVTGSHGKTSTTGLLSHVL--SGVR---------PTS 134
Cdd:COG0771 76 --PPDHPLLKAARAAGIPVIgeielayRLSP--APII------AITGTNGKTTTTTLIGHILkaAGLRvavggnigtPLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 135 YLIGDGTghgDPQ---AEFFSF--EACEyrrHFlaySPDYAIMTNIDFDHPDYYTSIDDVFTAfqtmagqvKKAIFAY-- 207
Cdd:COG0771 146 DLLLEPE---PPDvyvLELSSFqlETTP---SL---RPDVAVILNITPDHLDRHGSMEAYAAA--------KARIFANqt 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 208 --------GDDAYLRKL--KANVPIYYYGVTE--NDDIQARNierttsGSAFDVYHGDEF--VGHFTVPafGKHNILNAL 273
Cdd:COG0771 209 pddyavlnADDPLTRALaeEAKARVVPFSLKEplEGGAGLED------GKLVDRASGEELlpVDDLRLP--GRHNLENAL 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488225192 274 GVIAVAYFEKLDLKEVAEEMLTFPGVKRRFsEKI--VADMTVVDD 316
Cdd:COG0771 281 AALAAARALGVPPEAIREALRSFKGLPHRL-EFVaeINGVRFIND 324
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
11-303 |
1.45e-16 |
|
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273436 [Multi-domain] Cd Length: 433 Bit Score: 81.23 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 11 VGIKGSGMS--SLALVLHEQGLNVQGSDIEkyFFTQRD-----LEKANITILPFNADNVKPGM--TIIAGNAFPDSHEEI 81
Cdd:TIGR01087 2 ILILGLGKTgrAVARFLHKKGAEVTVTDLK--PNEELEpsmgqLRLNEGSVLHTGLHLEDLNNadLVVKSPGIPPDHPLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 82 QRAKELGLEVIRYHDFIGHFIQnYTSIAVTGSHGKTSTTGLLSHVLSGVRPTSYLIGD-GTghgdPQAEFFSFEACEYR- 159
Cdd:TIGR01087 80 QAAAKRGIPVVGDIELFLRLVP-LPVVAITGTNGKTTTTSLLYHLLKAAGLKAFLGGNiGT----PALEVLDQEGAELYv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 160 ---RHF-LAYS----PDYAIMTNIDFDHPDYYTSIDDVFTAFQTM-AGQVKKAIFAYG-DDAYLRKLKAN--VPIYYYGV 227
Cdd:TIGR01087 155 lelSSFqLETTeslrPEIALILNISEDHLDWHGSFEDYVAAKLKIfARQTEGDVAVLNaDDPRFARLAQKskAQVIWFSV 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488225192 228 TENDDiqaRNIERTTSGSAFdvyhgdeFVGHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRF 303
Cdd:TIGR01087 235 EKDAE---RGLCIRDGGLYL-------KPNDLEGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRL 300
|
|
| Mur_ligase |
pfam01225 |
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes ... |
8-106 |
1.65e-16 |
|
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460121 [Multi-domain] Cd Length: 84 Bit Score: 74.19 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 8 YHFVGIKGSGMSSLALVLHEQGLNVQGSDIEKYfftqrdLEKANITILPFNAdnvkpgmtiiAGNAFPDSHEEIQRAKEL 87
Cdd:pfam01225 2 IHFVGIDGRGMSPGALFLALKGYRVDGSDFIES------LIALGAAAVVGHD----------AANNISPDNPELEAAKVP 65
|
90
....*....|....*....
gi 488225192 88 GLEVIRYHDFIGHFIQNYT 106
Cdd:pfam01225 66 GIPVIDRREALAELAAAFY 84
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
108-373 |
1.28e-14 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 76.28 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 108 IAVTGSHGKTSTTGLLSHVLS------GVRPT-SYLIGD---GTGHGDPQAEFFS------------FEACEYRRHFLAY 165
Cdd:PRK11929 115 VAVTGTNGKTSCAQLLAQLLTrlgkpcGSIGTlGARLDGrliPGSLTTPDAIILHrilarmraagadAVAMEASSHGLEQ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 166 SP------DYAIMTNIDFDHPDYYTSIDDVFTAFQTMAGQVKKAIFAY--GDDAYLRKLKANVP----IYYYGVTENDDI 233
Cdd:PRK11929 195 GRldglriAVAGFTNLTRDHLDYHGTMQDYEEAKAALFSKLPGLGAAVinADDPAAARLLAALPrglkVGYSPQNAGADV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 234 QARNIERTTSGSAFDVYHGDEFVgHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRFsEKIVADMT- 312
Cdd:PRK11929 275 QARDLRATAHGQVFTLATPDGSY-QLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSPVPGRM-ERVGPTAGa 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488225192 313 ----VVDDYAHHPAEIKATIDGAR--QKYPDKEIIAVF----------QPhtftrtiaLMDEFAEAldLADKVYLCD 373
Cdd:PRK11929 353 qgplVVVDYAHTPDALAKALTALRpvAQARNGRLVCVFgcggdrdkgkRP--------EMGRIAAE--LADRVVVTS 419
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
299-381 |
1.68e-12 |
|
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase enzymes which have EC numbers 6.3.2.*. This family includes: MurC, MurD, MurE, MurF, Mpl and FolC. MurC, MurD, Mure and MurF catalyze consecutive steps in the synthesis of peptidoglycan. Peptidoglycan consists of a sheet of two sugar derivatives, with one of these N-acetylmuramic acid attaching to a small pentapeptide. The pentapeptide is is made of L-alanine, D-glutamic acid, Meso-diaminopimelic acid and D-alanyl alanine. The peptide moiety is synthesized by successively adding these amino acids to UDP-N-acetylmuramic acid. MurC transfers the L-alanine, MurD transfers the D-glutamate, MurE transfers the diaminopimelic acid, and MurF transfers the D-alanyl alanine. This family also includes Folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate.
Pssm-ID: 460731 [Multi-domain] Cd Length: 87 Bit Score: 62.75 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 299 VKRRFsEKI--VADMTVVDDYAHHPAEIKATIDGARQKYPdKEIIAVFQPHTfTRTIALMDEFAEAL-DLADKVYLCDIF 375
Cdd:pfam02875 1 VPGRL-EVVgeNNGVLVIDDYAHNPDAMEAALRALRNLFP-GRLILVFGGMG-DRDAEFHALLGRLAaALADVVILTGDY 77
|
....*.
gi 488225192 376 GSAREE 381
Cdd:pfam02875 78 PRAEDP 83
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
108-329 |
3.86e-11 |
|
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;
Pssm-ID: 237025 [Multi-domain] Cd Length: 958 Bit Score: 65.50 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 108 IAVTGSHGKTSTTGLLSHVLS------GVRPTSYLIGDGTG------HGDPQAEFFSFEACEYRRHFLAY-----SPDYA 170
Cdd:PRK11929 606 VAITGSNGKTTTKEMIAAILAawqgedRVLATEGNFNNEIGvpltllRLRAQHRAAVFELGMNHPGEIAYlaaiaAPTVA 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 171 IMTNIDFDHPDYYTSIDDVFTAfqtmagqvKKAIFAY----------GDDAYLRKLKA-----NVPIYYYGVTEN---DD 232
Cdd:PRK11929 686 LVTNAQREHQEFMHSVEAVARA--------KGEIIAAlpedgvavvnGDDPYTAIWAKlagarRVLRFGLQPGADvyaEK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 233 IQARNIERTTSGSAFDVYHGDEfVGHFTVPAFGKHNILNALGVIAVAYFEKLDLKEVAEEMLTFPGVKRRFSEKIVAD-M 311
Cdd:PRK11929 758 IAKDISVGEAGGTRCQVVTPAG-SAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSCgT 836
|
250
....*....|....*....
gi 488225192 312 TVVDD-YAHHPAEIKATID 329
Cdd:PRK11929 837 RIIDDtYNANPDSMRAAID 855
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
1-302 |
1.98e-09 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 59.21 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 1 MENQNKLYHFVGIKGSGMSsLALVLHEQGLNVQGSDIEKYFFTQRDLEKANitilpfnadnvKPGMTIIAGnAFPDSHEE 80
Cdd:PRK14106 1 MELKGKKVLVVGAGVSGLA-LAKFLKKLGAKVILTDEKEEDQLKEALEELG-----------ELGIELVLG-EYPEEFLE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 81 -----------------IQRAKELGLEVIRYHDFIGHFIQNYTsIAVTGSHGKTSTTGLLSHVL--SGVR---------P 132
Cdd:PRK14106 68 gvdlvvvspgvpldsppVVQAHKKGIEVIGEVELAYRFSKAPI-VAITGTNGKTTTTTLLGEIFknAGRKtlvagnigyP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 133 TSYLIGDGTGHGDPQAEFFSFEaCEYRRHFlaySPDYAIMTNIDFDHPDYYTSIDDVFTAfqtmagqvKKAIFA------ 206
Cdd:PRK14106 147 LIDAVEEYGEDDIIVAEVSSFQ-LETIKEF---KPKVGCILNITPDHLDRHKTMENYIKA--------KARIFEnqrpsd 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 207 -----YgDDAYLRKLKANVP----------IYYYGV-TENDDIQARniertTSGSAFDVYHGDEfvghftVPAFGKHNIL 270
Cdd:PRK14106 215 ytvlnY-DDPRTRSLAKKAKarviffsrksLLEEGVfVKNGKIVIS-----LGGKEEEVIDIDE------IFIPGEHNLE 282
|
330 340 350
....*....|....*....|....*....|..
gi 488225192 271 NALGVIAVAYFEKLDLKEVAEEMLTFPGVKRR 302
Cdd:PRK14106 283 NALAATAAAYLLGISPDVIANTLKTFKGVEHR 314
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
108-280 |
7.04e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 48.61 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 108 IAVTGSHGKTSTTGLLSHVL--SGVRP--TS--------YLI--GDGTGHG-------DPQAEFFSFE-AceyR----RH 161
Cdd:PRK14016 483 VAVTGTNGKTTTTRLIAHILklSGKRVgmTTtdgvyidgRLIdkGDCTGPKsarrvlmNPDVEAAVLEtA---RggilRE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 162 FLAYS-PDYAIMTNIDFDH--PDYYTSIDDVFTAFQTMAGQVKKAIFAY--GDDAYLRKLKANVP--IYYYGVTENDDIQ 234
Cdd:PRK14016 560 GLAYDrCDVGVVTNIGEDHlgLGGINTLEDLAKVKRVVVEAVKPDGYAVlnADDPMVAAMAERCKgkVIFFSMDPDNPVI 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488225192 235 ARNIERttSGSAFdVYHGDEFV---GHFTVPAF----------GK--HNILNALGVIAVAY 280
Cdd:PRK14016 640 AEHRAQ--GGRAV-YVEGDYIVlaeGGWEIRIIsladipltlgGKagFNIENALAAIAAAW 697
|
|
| PRK14022 |
PRK14022 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; |
95-329 |
6.42e-04 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
Pssm-ID: 237588 [Multi-domain] Cd Length: 481 Bit Score: 41.95 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 95 HDFIGHFIQNYTSIAVTGSHGKTSTTGLLSHVLSGV-RPTSYLIGDGTGHGDpqaEFFS---------------FEACEY 158
Cdd:PRK14022 100 MEFYDNPQHKLKLLAFTGTKGKTTAAYFAYHILKQLhKPAMLSTMNTTLDGE---TFFKsalttpesldlfkmmAEAVDN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 159 -RRHFL------AYSP--------DYAIMTNIDFDH--PDYYTSIDDVFTAFQTMAGQVKKAIFAYGDDAYlRKLKANV- 220
Cdd:PRK14022 177 gMTHLImevssqAYLVgrvygltfDVGVFLNITPDHigPIEHPTFEDYFYHKRLLMENSKAVVVNSDMDHF-SELLEQVt 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 221 --PIYYYGVTENDDIQARNierttsgsAFDVYHGDEFVGHFTVPAFGKHNILNALGV-IAV----AYFEklDLKEVAEEM 293
Cdd:PRK14022 256 pqEHDFYGIDSENQIMASN--------AFSFEATGKLAGTYDIQLIGKFNQENAMAAgLAClrlgASLE--DIQKGIAQT 325
|
250 260 270
....*....|....*....|....*....|....*.
gi 488225192 294 lTFPGVKRRFSEKIVADMTVvdDYAHHPAEIKATID 329
Cdd:PRK14022 326 -PVPGRMEVLTQSNGAKVFI--DYAHNGDSLNKLID 358
|
|
| PAPS_reduct |
pfam01507 |
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine ... |
326-437 |
9.35e-03 |
|
Phosphoadenosine phosphosulfate reductase family; This domain is found in phosphoadenosine phosphosulfate (PAPS) reductase enzymes or PAPS sulfotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP). It is also found in NodP nodulation protein P from Rhizobium which has ATP sulfurylase activity (sulfate adenylate transferase).
Pssm-ID: 396201 [Multi-domain] Cd Length: 173 Bit Score: 36.89 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488225192 326 ATIDGARQKYPDKEIIAVFQPHTFTRTIALMDEFAEALDLADKVYLCDIfgsaREEQGNVKIEDLGAKIKKGGEVIKenn 405
Cdd:pfam01507 14 VLLHLASKAFPPGPVIFIDTGYEFPETYEFVDELEEKYGLNLKVYLPED----SFAEGINPEGIPSSLYRRCCRLRK--- 86
|
90 100 110
....*....|....*....|....*....|....*
gi 488225192 406 VSPL---LDYHDAVVIFMGAGDVQKFEQAYEKLLS 437
Cdd:pfam01507 87 VEPLkraLKELGFDAWFTGLRRDESPSRAKLPIVS 121
|
|
| |
