|
Name |
Accession |
Description |
Interval |
E-value |
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
41-498 |
6.15e-168 |
|
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 480.76 E-value: 6.15e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 41 RELAEIEAELDQRWPeTKIDPSLERIEMLMDILGHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLV 120
Cdd:COG0285 2 TTYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 121 TERIAIDGQPIHPRDYVRIWREIQPYVEMVDAksaekggPQMSKFEVLTAMAYAAFADAPVDVAVVEVGMGGTWDATNVV 200
Cdd:COG0285 81 NERIRINGEPISDEELVEALEEVEPAVEEVDA-------GPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 201 EADVAVICPIGLDHTEYLGDTLAEIAAEKAGIIKsrwnkddlltpPDNVAIVGEQEPEAMDVVLRRAVEMDASVARAGVE 280
Cdd:COG0285 154 DPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIK-----------PGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 281 YGVVSHqlavGGQNLTLKGLAGEYDDLHLPLHGPHQARNAATALAAVEAFFGAGPgrPLNIDAVREGFATVASPGRLERV 360
Cdd:COG0285 223 FSVEER----EGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELGL--PISEEAIREGLANARWPGRLEVL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 361 RSTPTVFIDAAHNPHGARALRTALSAEFDFRRVIGVLSVLGEKDARGLLVELEPYFEEVVITQNTSPRALHYDDLADLAE 440
Cdd:COG0285 297 SRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAR 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2208556948 441 EIfgEERVHRVPTLPSAVELAVALAEETDtgdgivsgsGVIVTGSVVTAGEARTLFGK 498
Cdd:COG0285 377 EL--GLRVEVAPDVEEALEAALELADPDD---------LILVTGSLYLVGEVRALLGR 423
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
63-496 |
2.18e-101 |
|
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273659 [Multi-domain] Cd Length: 397 Bit Score: 309.98 E-value: 2.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 63 LERIEMLMDILGHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLVTERIAIDGQPIHPRDYVRIWRE 142
Cdd:TIGR01499 1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 143 IQPYVEMVDAKSAEkggpqmskFEVLTAMAYAAFADAPVDVAVVEVGMGGTWDATNVVEADVAVICPIGLDHTEYLGDTL 222
Cdd:TIGR01499 81 VRPILESLSQQPTY--------FELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 223 AEIAAEKAGIIKSRwnkddllTPpdnvAIVGEQEPEAMDVVLRRAVEMDASVARAGVEYGVVS---HQLAVGGQNLTLKg 299
Cdd:TIGR01499 153 EEIAWEKAGIIKEG-------VP----IVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSEtdeNYLSFSGANLFLE- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 300 lageydDLHLPLHGPHQARNAATALAAVEAFFGAGPgrPLNIDAVREGFATVASPGRLERVR-STPTVFIDAAHNPHGAR 378
Cdd:TIGR01499 221 ------PLALSLLGDHQQENAALALAALEVLGKQNP--KLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 379 ALRTALSAEFDFRRVIGVLSVLGEKDARGLLVELEPYF-EEVVITQNTSPRALHYDDLADLAEEIFGEERvhrvptlpSA 457
Cdd:TIGR01499 293 ALAEWFKKRFNGRPITLLFGALADKDAAAMLAPLKPVVdKEVFVTPFDYPRADDAADLAAFAEETGKSTV--------ED 364
|
410 420 430
....*....|....*....|....*....|....*....
gi 2208556948 458 VELAVALAEETDTGDGIVsgsgviVTGSVVTAGEARTLF 496
Cdd:TIGR01499 365 WREALEEALNASAEDDIL------VTGSLYLVGEVRKLL 397
|
|
| PRK10846 |
PRK10846 |
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional |
59-488 |
1.16e-52 |
|
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
Pssm-ID: 182774 [Multi-domain] Cd Length: 416 Bit Score: 183.74 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 59 IDPSLERIEMLMDILGHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLVTERIAIDGQPIHPRDYVR 138
Cdd:PRK10846 28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 139 IWREIQpyvemvdaksAEKGGPQMSKFEVLTAMAYAAFADAPVDVAVVEVGMGGTWDATNVVEADVAVICPIGLDHTEYL 218
Cdd:PRK10846 108 SFAEIE----------AARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 219 GDTLAEIAAEKAGIIKSrwnkddlltppDNVAIVGEQE-PEAMDVVlrrAVEMDASVARAGVEYgvvshQLAVGGQNLTL 297
Cdd:PRK10846 178 GPDRESIGREKAGIFRA-----------EKPAVVGEPDmPSTIADV---AQEKGALLQRRGVDW-----NYSVTDHDWAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 298 KGLAGEYDDLHLPlHGPHQARNAATALAAVEaffgagpGRPLNIDAVREGFATVASPGRLERVRSTPTVFIDAAHNPHGA 377
Cdd:PRK10846 239 SDGDGTLENLPLP-NVPLPNAATALAALRAS-------GLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 378 RALRTALSAEFDFRRVIGVLSVLGEKDARGLLVELEPYFEEVVITQNTSPRALHYDDLAdlaeEIFGEERVHrvPTLPSA 457
Cdd:PRK10846 311 EYLTGRLKALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLA----EHLGNGKSF--DSVAQA 384
|
410 420 430
....*....|....*....|....*....|.
gi 2208556948 458 VELAVALAEETDTgdgivsgsgVIVTGSVVT 488
Cdd:PRK10846 385 WDAAMADAKPEDT---------VLVCGSFHT 406
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
354-429 |
4.10e-11 |
|
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: 59.28 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 354 PGRLERVRS--TPTVFIDAAHNPHGARALRTALsAEFDFRRVIGVLSVLGEKDA--RGLLVELEPYFEEVVITQNTSPRA 429
Cdd:pfam02875 2 PGRLEVVGEnnGVLVIDDYAHNPDAMEAALRAL-RNLFPGRLILVFGGMGDRDAefHALLGRLAAALADVVILTGDYPRA 80
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
41-498 |
6.15e-168 |
|
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; Folylpolyglutamate synthase/Dihydropteroate synthase is part of the Pathway/BioSystem: Folate biosynthesis
Pssm-ID: 440054 [Multi-domain] Cd Length: 423 Bit Score: 480.76 E-value: 6.15e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 41 RELAEIEAELDQRWPeTKIDPSLERIEMLMDILGHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLV 120
Cdd:COG0285 2 TTYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 121 TERIAIDGQPIHPRDYVRIWREIQPYVEMVDAksaekggPQMSKFEVLTAMAYAAFADAPVDVAVVEVGMGGTWDATNVV 200
Cdd:COG0285 81 NERIRINGEPISDEELVEALEEVEPAVEEVDA-------GPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 201 EADVAVICPIGLDHTEYLGDTLAEIAAEKAGIIKsrwnkddlltpPDNVAIVGEQEPEAMDVVLRRAVEMDASVARAGVE 280
Cdd:COG0285 154 DPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIK-----------PGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 281 YGVVSHqlavGGQNLTLKGLAGEYDDLHLPLHGPHQARNAATALAAVEAFFGAGPgrPLNIDAVREGFATVASPGRLERV 360
Cdd:COG0285 223 FSVEER----EGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELGL--PISEEAIREGLANARWPGRLEVL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 361 RSTPTVFIDAAHNPHGARALRTALSAEFDFRRVIGVLSVLGEKDARGLLVELEPYFEEVVITQNTSPRALHYDDLADLAE 440
Cdd:COG0285 297 SRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAR 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2208556948 441 EIfgEERVHRVPTLPSAVELAVALAEETDtgdgivsgsGVIVTGSVVTAGEARTLFGK 498
Cdd:COG0285 377 EL--GLRVEVAPDVEEALEAALELADPDD---------LILVTGSLYLVGEVRALLGR 423
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
63-496 |
2.18e-101 |
|
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of folate pathway proteins. Most examples are bifunctional, active as both folylpolyglutamate synthetase (EC 6.3.2.17) and dihydrofolate synthetase (EC 6.3.2.12). The two activities are similar - ATP + glutamate + dihydropteroate or tetrahydrofolyl-[Glu](n) = ADP + orthophosphate + dihydrofolate or tetrahydrofolyl-[Glu](n+1). A mutation study of the FolC gene of E. coli suggests that both activities belong to the same active site. Because some examples are monofunctional (and these cannot be separated phylogenetically), the model is treated as subfamily, not equivalog. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 273659 [Multi-domain] Cd Length: 397 Bit Score: 309.98 E-value: 2.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 63 LERIEMLMDILGHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLVTERIAIDGQPIHPRDYVRIWRE 142
Cdd:TIGR01499 1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 143 IQPYVEMVDAKSAEkggpqmskFEVLTAMAYAAFADAPVDVAVVEVGMGGTWDATNVVEADVAVICPIGLDHTEYLGDTL 222
Cdd:TIGR01499 81 VRPILESLSQQPTY--------FELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 223 AEIAAEKAGIIKSRwnkddllTPpdnvAIVGEQEPEAMDVVLRRAVEMDASVARAGVEYGVVS---HQLAVGGQNLTLKg 299
Cdd:TIGR01499 153 EEIAWEKAGIIKEG-------VP----IVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSEtdeNYLSFSGANLFLE- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 300 lageydDLHLPLHGPHQARNAATALAAVEAFFGAGPgrPLNIDAVREGFATVASPGRLERVR-STPTVFIDAAHNPHGAR 378
Cdd:TIGR01499 221 ------PLALSLLGDHQQENAALALAALEVLGKQNP--KLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 379 ALRTALSAEFDFRRVIGVLSVLGEKDARGLLVELEPYF-EEVVITQNTSPRALHYDDLADLAEEIFGEERvhrvptlpSA 457
Cdd:TIGR01499 293 ALAEWFKKRFNGRPITLLFGALADKDAAAMLAPLKPVVdKEVFVTPFDYPRADDAADLAAFAEETGKSTV--------ED 364
|
410 420 430
....*....|....*....|....*....|....*....
gi 2208556948 458 VELAVALAEETDTGDGIVsgsgviVTGSVVTAGEARTLF 496
Cdd:TIGR01499 365 WREALEEALNASAEDDIL------VTGSLYLVGEVRKLL 397
|
|
| PRK10846 |
PRK10846 |
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional |
59-488 |
1.16e-52 |
|
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
Pssm-ID: 182774 [Multi-domain] Cd Length: 416 Bit Score: 183.74 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 59 IDPSLERIEMLMDILGHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLVTERIAIDGQPIHPRDYVR 138
Cdd:PRK10846 28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 139 IWREIQpyvemvdaksAEKGGPQMSKFEVLTAMAYAAFADAPVDVAVVEVGMGGTWDATNVVEADVAVICPIGLDHTEYL 218
Cdd:PRK10846 108 SFAEIE----------AARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 219 GDTLAEIAAEKAGIIKSrwnkddlltppDNVAIVGEQE-PEAMDVVlrrAVEMDASVARAGVEYgvvshQLAVGGQNLTL 297
Cdd:PRK10846 178 GPDRESIGREKAGIFRA-----------EKPAVVGEPDmPSTIADV---AQEKGALLQRRGVDW-----NYSVTDHDWAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 298 KGLAGEYDDLHLPlHGPHQARNAATALAAVEaffgagpGRPLNIDAVREGFATVASPGRLERVRSTPTVFIDAAHNPHGA 377
Cdd:PRK10846 239 SDGDGTLENLPLP-NVPLPNAATALAALRAS-------GLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 378 RALRTALSAEFDFRRVIGVLSVLGEKDARGLLVELEPYFEEVVITQNTSPRALHYDDLAdlaeEIFGEERVHrvPTLPSA 457
Cdd:PRK10846 311 EYLTGRLKALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLA----EHLGNGKSF--DSVAQA 384
|
410 420 430
....*....|....*....|....*....|.
gi 2208556948 458 VELAVALAEETDTgdgivsgsgVIVTGSVVT 488
Cdd:PRK10846 385 WDAAMADAKPEDT---------VLVCGSFHT 406
|
|
| PLN02881 |
PLN02881 |
tetrahydrofolylpolyglutamate synthase |
63-316 |
2.66e-43 |
|
tetrahydrofolylpolyglutamate synthase
Pssm-ID: 215476 Cd Length: 530 Bit Score: 160.60 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 63 LERIEMLMDILGHPER--ATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLVTERIAIDGQPIHPRDYVR-- 138
Cdd:PLN02881 42 FDLLFDYLKILELEEAisRLKVIHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRyf 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 139 --IWREIQpyvemvDAKSAEKGGPQMSKFevLTAMAYAAFADAPVDVAVVEVGMGGTWDATNVVEADVAV-ICPIGLDHT 215
Cdd:PLN02881 122 wwCWDRLK------EKTTEDLPMPAYFRF--LTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCgITSLGYDHM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 216 EYLGDTLAEIAAEKAGIIKSRwnkddllTPpdnvAIVGEQEPEAMDVVLRRAVEMDasvaragveygvVSHQLAvggQNL 295
Cdd:PLN02881 194 EILGDTLGKIAGEKAGIFKPG-------VP----AFTVPQPDEAMRVLEERASELG------------VPLQVV---EPL 247
|
250 260
....*....|....*....|.
gi 2208556948 296 TLKGLageyDDLHLPLHGPHQ 316
Cdd:PLN02881 248 DSYGL----SGLKLGLAGEHQ 264
|
|
| PLN02913 |
PLN02913 |
dihydrofolate synthetase |
63-485 |
1.71e-40 |
|
dihydrofolate synthetase
Pssm-ID: 178501 [Multi-domain] Cd Length: 510 Bit Score: 152.67 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 63 LERIEMLMDILGHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLVTERIAI--DGQPIHPRDYVRIW 140
Cdd:PLN02913 58 LGRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVgkLGKPVSTNTLNDLF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 141 REIQPYVEmvDAKSAEKGgpQMSKFEVLTAMAYAAFADAPVDVAVVEVGMGGTWDATNVVEAD---VAVICPIGLDHTEY 217
Cdd:PLN02913 138 HGIKPILD--EAIQLENG--SLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSSglaASVITTIGEEHLAA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 218 LGDTLAEIAAEKAGIIKSRwnkddllTPpdnVAIVGEQEPEAMDVVLRRAVEMDASVARA---GVEYGVVSHQLAVGG-- 292
Cdd:PLN02913 214 LGGSLESIALAKSGIIKQG-------RP---VVLGGPFLPHIESILRDKASSMNSPVVSAsdpGVRSSIKGIITDNGKpc 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 293 -------QNLTLKGLAGEYDDLHLPLHGPHQARNAATALAAVEAFFGAGpGRpLNIDAVREGFATVASPGRLERVRST-- 363
Cdd:PLN02913 284 qscdiviRVEKDDPLFIELSDVNLRMLGSHQLQNAVTAACAALCLRDQG-WR-ISDASIRAGLENTNLLGRSQFLTSKea 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 364 -------PTVFIDAAHNPHGARALRTALSAEFDFRRVIGVLSVLGEKD----ARGLLVELEPyfEEVVITQ----NTSPR 428
Cdd:PLN02913 362 evlglpgATVLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKDhlafASEFLSGLKP--EAVFLTEadiaGGKSR 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2208556948 429 ALHYDDLAD----LAEEIFGEERVHRVPTLPSAVELAVALAEETDTGDgivSGSGVIVTGS 485
Cdd:PLN02913 440 STSASALKEawikAAPELGIETLLAENNSLLKSLVDASAILRKARTLD---PSSVVCVTGS 497
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
74-470 |
3.01e-13 |
|
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: 71.58 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 74 GHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTSPHLQLVTERIAIDGQPIHPRDYVriwrEIQPYV-EMVDA 152
Cdd:TIGR01085 79 GHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDLIKNPAALTTPEAL----TLQSTLaEMVEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 153 KsaekggpqmskfevltamayaafadapVDVAVVEVGMGG-TWDATNVVEADVAVICPIGLDHTEYLGdTLAEIAAEKAG 231
Cdd:TIGR01085 155 G---------------------------AQYAVMEVSSHAlAQGRVRGVRFDAAVFTNLSRDHLDFHG-TMENYFAAKAS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 232 IIKsrwnkdDLLTPPDNVAIVGEqepeAMDVVLRRAVEMDASVArAGVEYGVVSHQ--------LAVGGQNLTLKGLAGE 303
Cdd:TIGR01085 207 LFT------ELGLKRFAVINLDD----EYGAQFVKRLPKDITVS-AITQPADGRAQdikitdsgYSFEGQQFTFETPAGE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 304 YDdLHLPLHGPHQARNAATALAAVEAFFGAGPgrplniDAVREGFATVAS-PGRLERVRS--TPTVFIDAAHNPHGAR-A 379
Cdd:TIGR01085 276 GH-LHTPLIGRFNVYNLLAALATLLHLGGIDL------EDIVAALEKFRGvPGRMELVDGgqKFLVIVDYAHTPDALEkA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 380 LRTAlsAEFDFRRVIGVLSVLGEKD--ARGLLVELEPYFEEVVITQNTSPRALHYDD-LADLAEEIFGEERVHRVPTLPS 456
Cdd:TIGR01085 349 LRTL--RKHKDGRLIVVFGCGGDRDrgKRPLMGAIAEQLADLVILTSDNPRGEDPEQiIADILAGISEKEKVVIIADRRQ 426
|
410
....*....|....
gi 2208556948 457 AVELAVALAEETDT 470
Cdd:TIGR01085 427 AIRYAISNAKAGDV 440
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
354-429 |
4.10e-11 |
|
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: 59.28 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 354 PGRLERVRS--TPTVFIDAAHNPHGARALRTALsAEFDFRRVIGVLSVLGEKDA--RGLLVELEPYFEEVVITQNTSPRA 429
Cdd:pfam02875 2 PGRLEVVGEnnGVLVIDDYAHNPDAMEAALRAL-RNLFPGRLILVFGGMGDRDAefHALLGRLAAALADVVILTGDYPRA 80
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
74-475 |
5.49e-11 |
|
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: 64.71 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 74 GHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGR--TTsphlqlvteriaidgqpihprdYVRIWREIQPYV---- 147
Cdd:COG0769 74 GHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLigTV----------------------GNGIGGELIPSSlttp 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 148 ----------EMVDAKsaekggpqmskfevltamayaafadapVDVAVVEV-----------GmggtwdatnvVEADVAV 206
Cdd:COG0769 132 ealdlqrllaEMVDAG---------------------------VTHVVMEVsshaldqgrvdG----------VRFDVAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 207 ICPIGLDHTEYLGdTLAEIAAEKAGIIKsrwnkddlLTPPDNVAIVGeqepeAMDVVLRRAVEM-DASV----ARAGVEY 281
Cdd:COG0769 175 FTNLTRDHLDYHG-TMEAYFAAKARLFD--------QLGPGGAAVIN-----ADDPYGRRLAAAaPARVitygLKADADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 282 GVVSHQLAVGGQNLTLKGLAGEYdDLHLPLHGphqarnaatalaaveAF--------FGAGPGRPLNIDAVREGFATVAS 353
Cdd:COG0769 241 RATDIELSADGTRFTLVTPGGEV-EVRLPLIG---------------RFnvynalaaIAAALALGIDLEEILAALEKLKG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 354 -PGRLERVRST--PTVFIDAAHNPhgaRALRTALSA--EFDFRRVIGVLSVLGEKDA--RGLLVE-LEPYFEEVVIT--- 422
Cdd:COG0769 305 vPGRMERVDGGqgPTVIVDYAHTP---DALENVLEAlrPHTKGRLIVVFGCGGDRDRgkRPLMGEiAARLADVVIVTsdn 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2208556948 423 -QNTSPRALhyddLADLAEEIFGEERVHRVPTLPSAVELAVALAEEtdtGDGIV 475
Cdd:COG0769 382 pRSEDPAAI----IADILAGIPGAGKVLVIPDRAEAIRYAIALAKP---GDVVL 428
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
74-406 |
1.94e-09 |
|
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: 60.10 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 74 GHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTS-----PHLQLVTERIAIDGQPIHprdyvRIWREiqpyve 148
Cdd:PRK11929 106 GRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTlgarlDGRLIPGSLTTPDAIILH-----RILAR------ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 149 MVDAKsaekggpqmskfevltamayaafadapVDVAVVEVG--------MGGtwdatnvVEADVAVICPIGLDHTEYLGd 220
Cdd:PRK11929 175 MRAAG---------------------------ADAVAMEASshgleqgrLDG-------LRIAVAGFTNLTRDHLDYHG- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 221 TLAEIAAEKAGIIkSRWnkddlltPPDNVAIVGEQEPEA--MDVVLRRAVEMDASVARAGVEygVVSHQLAVG--GQNLT 296
Cdd:PRK11929 220 TMQDYEEAKAALF-SKL-------PGLGAAVINADDPAAarLLAALPRGLKVGYSPQNAGAD--VQARDLRATahGQVFT 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 297 LKGLAGEYDdLHLPLHGPHQARNAatalaaveaFFGAGPGRPLNI--DAVREGFATVAS-PGRLERVRST-----PTVFI 368
Cdd:PRK11929 290 LATPDGSYQ-LVTRLLGRFNVSNL---------LLVAAALKKLGLplAQIARALAAVSPvPGRMERVGPTagaqgPLVVV 359
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2208556948 369 DAAHNPHgarALRTALSA-----EFDFRRVIGVLSVLGEKDAR 406
Cdd:PRK11929 360 DYAHTPD---ALAKALTAlrpvaQARNGRLVCVFGCGGDRDKG 399
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
81-233 |
8.78e-09 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 57.86 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 81 PVIHVAGTNGKTSTVRMIESLVRALGRRTGRTTsphlqlvTERIAIDGQPIHPRDyvriwreiqpyveMVDAKSAEKggp 160
Cdd:PRK14016 481 PIVAVTGTNGKTTTTRLIAHILKLSGKRVGMTT-------TDGVYIDGRLIDKGD-------------CTGPKSARR--- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 161 qmskfeVLTAMAyaafadapVDVAVVEVGMGG------TWDatnvvEADVAVICPIGLDHteyLG----DTLAEIAAEKA 230
Cdd:PRK14016 538 ------VLMNPD--------VEAAVLETARGGilreglAYD-----RCDVGVVTNIGEDH---LGlggiNTLEDLAKVKR 595
|
...
gi 2208556948 231 GII 233
Cdd:PRK14016 596 VVV 598
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
85-304 |
3.11e-07 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 50.77 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 85 VAGTNGKTSTVRMIESLVRALGRRTGrttsphlqlvTERIAIDGQPIHPRDYVRIWREIQpyvEMVDAKsaekggpqmsk 164
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGVIG----------TIGTYIGKSGNTTNNAIGLPLTLA---EMVEAG----------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 165 fevltamayaafadapVDVAVVEVGMGGTWDA--TNVVEADVAVICPIGLDHTEYLGdTLAEIAAEKAGIIKSrwnkddl 242
Cdd:pfam08245 57 ----------------AEYAVLEVSSHGLGEGrlSGLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEG------- 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2208556948 243 lTPPDNVAIVGEQEPEAMDVVLRRAV----------EMDASVARAGVEY---GVVSHQLAVGGQNLTLK-GLAGEY 304
Cdd:pfam08245 113 -LPEDGIAVINADDPYGAFLIAKLKKagvrvitygiEGEADLRAANIELssdGTSFDLFTVPGGELEIEiPLLGRH 187
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
74-386 |
5.14e-07 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 52.06 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 74 GHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTGrttsphlqLV-TERIAIDGQPIHPR----DYVRIWREIQpyvE 148
Cdd:PRK00139 89 GHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTA--------LIgTLGNGIGGELIPSGlttpDALDLQRLLA---E 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 149 MVDAKsaekggpqmskfevltamayaafadapVDVAVVEV---GMggtwdATNVVEA---DVAVICPIGLDHTEYLGdTL 222
Cdd:PRK00139 158 LVDAG---------------------------VTYAAMEVsshAL-----DQGRVDGlkfDVAVFTNLSRDHLDYHG-TM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 223 AEIAAEKAGiiksrwnkddLLTPPDNVAIVGEQEPEAMDVVLRRAVemdASVARAGVEYGVVSHQLAVGGQNLTLKGlag 302
Cdd:PRK00139 205 EDYLAAKAR----------LFSELGLAAVINADDEVGRRLLALPDA---YAVSMAGADLRATDVEYTDSGQTFTLVT--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 303 eydDLHLPLHGPHQARnaatalaaveaffgagpgrplNI--------------DAVREGFATVAS-PGRLERVRST--PT 365
Cdd:PRK00139 269 ---EVESPLIGRFNVS---------------------NLlaalaallalgvplEDALAALAKLQGvPGRMERVDAGqgPL 324
|
330 340
....*....|....*....|.
gi 2208556948 366 VFIDAAHNPHgarALRTALSA 386
Cdd:PRK00139 325 VIVDYAHTPD---ALEKVLEA 342
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
182-470 |
1.12e-05 |
|
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: 47.79 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 182 DVAVVEVGMGG------TwdaTNVVEADVAVICPIGLDHTEYLGdTLAEIAAEKAGIIKSrwnkddllTPPDNVAIVGEQ 255
Cdd:COG0770 153 EFAVLEMGMNHpgeiayL---ARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIFEG--------LPPGGVAVLNAD 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 256 EPEAMdvvlRRAVEMDASVAR----AGVEYGVVSHQLAVGGQNLTLKGLAGEYDdLHLPLHGPHQarnaatalaaveaF- 330
Cdd:COG0770 221 DPLLA----ALAERAKARVLTfglsEDADVRAEDIELDEDGTRFTLHTPGGELE-VTLPLPGRHN-------------Vs 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 331 -----------FGagpgrpLNIDAVREGFATV-ASPGRLERVRSTPTV-FIDAAHN--PHGAR-ALRTALSAEFDFRRVI 394
Cdd:COG0770 283 nalaaaavalaLG------LDLEEIAAGLAAFqPVKGRLEVIEGAGGVtLIDDSYNanPDSMKaALDVLAQLPGGGRRIA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 395 gvlsVLGEkdarglLVEL----EPYFEEVVitqnTSPRALHYD------DLADLAEEIFGEERVHRVPTLPSAVELAVAL 464
Cdd:COG0770 357 ----VLGD------MLELgeesEELHREVG----ELAAELGIDrlftvgELARAIAEAAGGERAEHFEDKEELLAALKAL 422
|
....*.
gi 2208556948 465 AEETDT 470
Cdd:COG0770 423 LRPGDV 428
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
66-110 |
1.96e-03 |
|
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: 40.45 E-value: 1.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2208556948 66 IEMLMDI-LGHPERATPVIHVAGTNGKTSTVRMIESLVRALGRRTG 110
Cdd:COG0771 90 IPVIGEIeLAYRLSPAPIIAITGTNGKTTTTTLIGHILKAAGLRVA 135
|
|
| PRK14022 |
PRK14022 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; |
340-442 |
2.31e-03 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
Pssm-ID: 237588 [Multi-domain] Cd Length: 481 Bit Score: 40.41 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208556948 340 NIDAVREGFATVASPGRLERVrsTPT----VFIDAAHNPHGARALRTALSaEFDFRRVIGVLSVLGEKDAR-----GLLV 410
Cdd:PRK14022 314 SLEDIQKGIAQTPVPGRMEVL--TQSngakVFIDYAHNGDSLNKLIDVVE-EHQKGKLILLLGAAGNKGESrrpdfGRVA 390
|
90 100 110
....*....|....*....|....*....|..
gi 2208556948 411 ELEPYFEevVITQNTSPralHYDDLADLAEEI 442
Cdd:PRK14022 391 NRHPYLQ--VILTADDP---NNEDPKMITQEI 417
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
78-120 |
3.26e-03 |
|
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: 40.02 E-value: 3.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2208556948 78 RATPVIHVAGTNGKTSTVRMIESLVRALGRRT---GRTTSPHLQLV 120
Cdd:TIGR01087 100 VPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAflgGNIGTPALEVL 145
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
61-106 |
5.57e-03 |
|
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: 39.21 E-value: 5.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2208556948 61 PSLERIEMLMDILghpeRATPVIHVAGTNGKTSTVRMIESLVRALG 106
Cdd:TIGR01082 84 PVIRRAEMLAELM----RFRHSIAVAGTHGKTTTTAMIAVILKEAG 125
|
|
| |
