|
Name |
Accession |
Description |
Interval |
E-value |
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
57-500 |
4.47e-159 |
|
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: 458.03 E-value: 4.47e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 57 AELRRVEAELLTRWgETEIDPTLDRVRLLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLI 136
Cdd:COG0285 2 TTYQEALAYLESLH-PFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 137 TERIGIDGAPIHPAQFVAIYDQVAPYMELADQHSgqrLSYFEALVCLAYAAFADAPVEVAVVEVGMGGRWDATNVVEADV 216
Cdd:COG0285 81 NERIRINGEPISDEELVEALEEVEPAVEEVDAGP---PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 217 NVIMPIGLDHTDYLGDTLAQIAGEKAGIITnPDSVTIIADQDPEAMRVVLEAAVDTGSAVARLGIEFTVAEatvaVGGQN 296
Cdd:COG0285 158 SVITSIGLDHTDFLGDTLEEIAREKAGIIK-PGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEE----REGAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 297 LTLKGLGGEYTDIFLPLSGPHQARNAAVALAAVEAFHGASseRPLDADTVRRGFAAVESPGRLERVRATPTTFIDATHNP 376
Cdd:COG0285 233 FSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG--LPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 377 HGARALADALANDFDFTRLIGVLGVLGDKDATGILAALEPVFTEVVITQNTSPRAMDAYELAELAREIygDERVHVVTRL 456
Cdd:COG0285 311 AGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAREL--GLRVEVAPDV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 493893808 457 ADAYELAVELAEDalaevgvqsGSGVVITGSVVTAGEARSMFGK 500
Cdd:COG0285 389 EEALEAALELADP---------DDLILVTGSLYLVGEVRALLGR 423
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
79-498 |
2.42e-96 |
|
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: 296.89 E-value: 2.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 79 LDRVRLLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLITERIGIDGAPIHPAQFVAIYDQ 158
Cdd:TIGR01499 1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 159 VAPymeLADQHSgQRLSYFEALVCLAYAAFADAPVEVAVVEVGMGGRWDATNVVEADVNVIMPIGLDHTDYLGDTLAQIA 238
Cdd:TIGR01499 81 VRP---ILESLS-QQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 239 GEKAGIITnPDSVTIIADQDPEAMRVVLEAAVDTGSAVARLGIEFTVAEATvavgGQNLTLKGLGGEYTDIFLPLSGPHQ 318
Cdd:TIGR01499 157 WEKAGIIK-EGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETD----ENYLSFSGANLFLEPLALSLLGDHQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 319 ARNAAVALAAVEAFhgASSERPLDADTVRRGFAAVESPGRLERVR-ATPTTFIDATHNPHGARALADALANDFDFTRLIG 397
Cdd:TIGR01499 232 QENAALALAALEVL--GKQNPKLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALAEWFKKRFNGRPITL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 398 VLGVLGDKDATGILAALEPVFTEVV-ITQNTSPRAMDAYELAELAREiYGDERVhvvtrlaDAYELAVELAEDALAEvgv 476
Cdd:TIGR01499 310 LFGALADKDAAAMLAPLKPVVDKEVfVTPFDYPRADDAADLAAFAEE-TGKSTV-------EDWREALEEALNASAE--- 378
|
410 420
....*....|....*....|..
gi 493893808 477 qsgSGVVITGSVVTAGEARSMF 498
Cdd:TIGR01499 379 ---DDILVTGSLYLVGEVRKLL 397
|
|
| PRK10846 |
PRK10846 |
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional |
75-439 |
2.12e-48 |
|
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
Pssm-ID: 182774 [Multi-domain] Cd Length: 416 Bit Score: 172.18 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 75 IDPTLDRVRLLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLITERIGIDGAPIHPAQFVA 154
Cdd:PRK10846 28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 155 IYdqvapyMELADQHSGQRLSYFEALVCLAYAAFADAPVEVAVVEVGMGGRWDATNVVEADVNVIMPIGLDHTDYLGDTL 234
Cdd:PRK10846 108 SF------AEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 235 AQIAGEKAGI--------ITNPDSVTIIADqdpeamrvvleAAVDTGSAVARLGIEFtvaeaTVAVGGQNLTLKGLGGEY 306
Cdd:PRK10846 182 ESIGREKAGIfraekpavVGEPDMPSTIAD-----------VAQEKGALLQRRGVDW-----NYSVTDHDWAFSDGDGTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 307 TDifLPLSGPHQARNAAVALAAveafhgASSERPLDADTVRRGFAAVESPGRLERVRATPTTFIDATHNPHGARALADAL 386
Cdd:PRK10846 246 EN--LPLPNVPLPNAATALAAL------RASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 493893808 387 ANDFDFTRLIGVLGVLGDKDATGILAALEPVFTEVVITQNTSPRAMDAYELAE 439
Cdd:PRK10846 318 KALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAE 370
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
356-433 |
2.81e-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: 62.36 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 356 PGRLERVRA--TPTTFIDATHNPHGARALADALANDFDFtRLIGVLGVLGDKDAT--GILAALEPVFTEVVITQNTSPRA 431
Cdd:pfam02875 2 PGRLEVVGEnnGVLVIDDYAHNPDAMEAALRALRNLFPG-RLILVFGGMGDRDAEfhALLGRLAAALADVVILTGDYPRA 80
|
..
gi 493893808 432 MD 433
Cdd:pfam02875 81 ED 82
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FolC |
COG0285 |
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ... |
57-500 |
4.47e-159 |
|
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: 458.03 E-value: 4.47e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 57 AELRRVEAELLTRWgETEIDPTLDRVRLLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLI 136
Cdd:COG0285 2 TTYQEALAYLESLH-PFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 137 TERIGIDGAPIHPAQFVAIYDQVAPYMELADQHSgqrLSYFEALVCLAYAAFADAPVEVAVVEVGMGGRWDATNVVEADV 216
Cdd:COG0285 81 NERIRINGEPISDEELVEALEEVEPAVEEVDAGP---PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 217 NVIMPIGLDHTDYLGDTLAQIAGEKAGIITnPDSVTIIADQDPEAMRVVLEAAVDTGSAVARLGIEFTVAEatvaVGGQN 296
Cdd:COG0285 158 SVITSIGLDHTDFLGDTLEEIAREKAGIIK-PGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEE----REGAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 297 LTLKGLGGEYTDIFLPLSGPHQARNAAVALAAVEAFHGASseRPLDADTVRRGFAAVESPGRLERVRATPTTFIDATHNP 376
Cdd:COG0285 233 FSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG--LPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 377 HGARALADALANDFDFTRLIGVLGVLGDKDATGILAALEPVFTEVVITQNTSPRAMDAYELAELAREIygDERVHVVTRL 456
Cdd:COG0285 311 AGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAAREL--GLRVEVAPDV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 493893808 457 ADAYELAVELAEDalaevgvqsGSGVVITGSVVTAGEARSMFGK 500
Cdd:COG0285 389 EEALEAALELADP---------DDLILVTGSLYLVGEVRALLGR 423
|
|
| folC |
TIGR01499 |
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ... |
79-498 |
2.42e-96 |
|
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: 296.89 E-value: 2.42e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 79 LDRVRLLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLITERIGIDGAPIHPAQFVAIYDQ 158
Cdd:TIGR01499 1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 159 VAPymeLADQHSgQRLSYFEALVCLAYAAFADAPVEVAVVEVGMGGRWDATNVVEADVNVIMPIGLDHTDYLGDTLAQIA 238
Cdd:TIGR01499 81 VRP---ILESLS-QQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 239 GEKAGIITnPDSVTIIADQDPEAMRVVLEAAVDTGSAVARLGIEFTVAEATvavgGQNLTLKGLGGEYTDIFLPLSGPHQ 318
Cdd:TIGR01499 157 WEKAGIIK-EGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETD----ENYLSFSGANLFLEPLALSLLGDHQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 319 ARNAAVALAAVEAFhgASSERPLDADTVRRGFAAVESPGRLERVR-ATPTTFIDATHNPHGARALADALANDFDFTRLIG 397
Cdd:TIGR01499 232 QENAALALAALEVL--GKQNPKLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALAEWFKKRFNGRPITL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 398 VLGVLGDKDATGILAALEPVFTEVV-ITQNTSPRAMDAYELAELAREiYGDERVhvvtrlaDAYELAVELAEDALAEvgv 476
Cdd:TIGR01499 310 LFGALADKDAAAMLAPLKPVVDKEVfVTPFDYPRADDAADLAAFAEE-TGKSTV-------EDWREALEEALNASAE--- 378
|
410 420
....*....|....*....|..
gi 493893808 477 qsgSGVVITGSVVTAGEARSMF 498
Cdd:TIGR01499 379 ---DDILVTGSLYLVGEVRKLL 397
|
|
| PRK10846 |
PRK10846 |
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional |
75-439 |
2.12e-48 |
|
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
Pssm-ID: 182774 [Multi-domain] Cd Length: 416 Bit Score: 172.18 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 75 IDPTLDRVRLLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLITERIGIDGAPIHPAQFVA 154
Cdd:PRK10846 28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 155 IYdqvapyMELADQHSGQRLSYFEALVCLAYAAFADAPVEVAVVEVGMGGRWDATNVVEADVNVIMPIGLDHTDYLGDTL 234
Cdd:PRK10846 108 SF------AEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 235 AQIAGEKAGI--------ITNPDSVTIIADqdpeamrvvleAAVDTGSAVARLGIEFtvaeaTVAVGGQNLTLKGLGGEY 306
Cdd:PRK10846 182 ESIGREKAGIfraekpavVGEPDMPSTIAD-----------VAQEKGALLQRRGVDW-----NYSVTDHDWAFSDGDGTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 307 TDifLPLSGPHQARNAAVALAAveafhgASSERPLDADTVRRGFAAVESPGRLERVRATPTTFIDATHNPHGARALADAL 386
Cdd:PRK10846 246 EN--LPLPNVPLPNAATALAAL------RASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 493893808 387 ANDFDFTRLIGVLGVLGDKDATGILAALEPVFTEVVITQNTSPRAMDAYELAE 439
Cdd:PRK10846 318 KALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAE 370
|
|
| PLN02913 |
PLN02913 |
dihydrofolate synthetase |
79-487 |
4.09e-39 |
|
dihydrofolate synthetase
Pssm-ID: 178501 [Multi-domain] Cd Length: 510 Bit Score: 148.81 E-value: 4.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 79 LDRVRLLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLITERI--GIDGAPIHPAQFVAIY 156
Cdd:PLN02913 58 LGRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERIsvGKLGKPVSTNTLNDLF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 157 DQVAPYMELADQHSGQRLSYFEALVCLAYAAFADAPVEVAVVEVGMGGRWDATNVVEAD---VNVIMPIGLDHTDYLGDT 233
Cdd:PLN02913 138 HGIKPILDEAIQLENGSLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSSglaASVITTIGEEHLAALGGS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 234 LAQIAGEKAGIITN-----------PDSVTIIADQdPEAMRVVLEAAVDTGSAVARLGIE------FTVAEATVAVGGQN 296
Cdd:PLN02913 218 LESIALAKSGIIKQgrpvvlggpflPHIESILRDK-ASSMNSPVVSASDPGVRSSIKGIItdngkpCQSCDIVIRVEKDD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 297 ltlkGLGGEYTDIFLPLSGPHQARNAAVALAAVEAFHGASSERPlDAdTVRRGFAAVESPGRLERVRAT---------PT 367
Cdd:PLN02913 297 ----PLFIELSDVNLRMLGSHQLQNAVTAACAALCLRDQGWRIS-DA-SIRAGLENTNLLGRSQFLTSKeaevlglpgAT 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 368 TFIDATHNPHGARALADALANDFDFTRLIGVLGVLGDKD----ATGILAALEP---VFTEVVITQNTSpRAMDAYELA-- 438
Cdd:PLN02913 371 VLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKDhlafASEFLSGLKPeavFLTEADIAGGKS-RSTSASALKea 449
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 493893808 439 ------ELAREIYGDERVHVVTRLADAYELAVELAedalaevGVQSGSGVVITGS 487
Cdd:PLN02913 450 wikaapELGIETLLAENNSLLKSLVDASAILRKAR-------TLDPSSVVCVTGS 497
|
|
| PLN02881 |
PLN02881 |
tetrahydrofolylpolyglutamate synthase |
80-318 |
1.08e-38 |
|
tetrahydrofolylpolyglutamate synthase
Pssm-ID: 215476 Cd Length: 530 Bit Score: 147.88 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 80 DRVRLLMDYLG-----EPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLITERIGIDGAPIHPAQFVA 154
Cdd:PLN02881 40 DQFDLLFDYLKileleEAISRLKVIHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 155 ----IYDQVApymeladQHSGQRL---SYFEALVCLAYAAFADAPVEVAVVEVGMGGRWDATNVVEADVNV-IMPIGLDH 226
Cdd:PLN02881 120 yfwwCWDRLK-------EKTTEDLpmpAYFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCgITSLGYDH 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 227 TDYLGDTLAQIAGEKAGIItNPDSVTIIADQDPEAMRVVLEAAvdtgsavARLGIEFTVAEAtvavggqnLTLKGLGGey 306
Cdd:PLN02881 193 MEILGDTLGKIAGEKAGIF-KPGVPAFTVPQPDEAMRVLEERA-------SELGVPLQVVEP--------LDSYGLSG-- 254
|
250
....*....|..
gi 493893808 307 tdIFLPLSGPHQ 318
Cdd:PLN02881 255 --LKLGLAGEHQ 264
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
90-486 |
1.77e-12 |
|
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: 69.34 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 90 GEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGrttsphlqLI-TERIGIDGAPIHP--------------AQFVA 154
Cdd:COG0769 74 GHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTG--------LIgTVGNGIGGELIPSslttpealdlqrllAEMVD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 155 I-YDQVApyME-----LaDQHsgqRLSYfealVCLAYAAFadapvevavvevgmggrwdaTNvveadvnvimpIGLDHTD 228
Cdd:COG0769 146 AgVTHVV--MEvsshaL-DQG---RVDG----VRFDVAVF--------------------TN-----------LTRDHLD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 229 YLGdTLAQIAGEKAGIITN--PDSVTII-ADqDPEAMRVVLEAAVdtgsAVARLGIE----FTVAEATVAVGGQNLTLKG 301
Cdd:COG0769 185 YHG-TMEAYFAAKARLFDQlgPGGAAVInAD-DPYGRRLAAAAPA----RVITYGLKadadLRATDIELSADGTRFTLVT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 302 LGGEYtDIFLPLSGphqarnaavalaaveAFH--------GASSERPLDADTVRRGFAAVES-PGRLERVRAT--PTTFI 370
Cdd:COG0769 259 PGGEV-EVRLPLIG---------------RFNvynalaaiAAALALGIDLEEILAALEKLKGvPGRMERVDGGqgPTVIV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 371 DATHNPhgaRALADAL--ANDFDFTRLIGVLGVLGDKDAT------GILAALepvFTEVVITqNTSPRAMDAYE-LAELA 441
Cdd:COG0769 323 DYAHTP---DALENVLeaLRPHTKGRLIVVFGCGGDRDRGkrplmgEIAARL---ADVVIVT-SDNPRSEDPAAiIADIL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 493893808 442 REIYGDERVHVVTRLADAYELAVELAedalaevgvQSGSGVVITG 486
Cdd:COG0769 396 AGIPGAGKVLVIPDRAEAIRYAIALA---------KPGDVVLIAG 431
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
84-467 |
2.63e-12 |
|
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: 69.35 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 84 LLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRttsphlqliterIGIDGApIHPAQFVAIyDQVAPym 163
Cdd:PRK11929 100 LAARWYGRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGS------------IGTLGA-RLDGRLIPG-SLTTP-- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 164 elaDQHSGQRLsyFEALVclayAAFADAPVEVAVVEVGMGGRWDAtnvVEADVNVIMPIGLDHTDYLGdTLAQIAGEKAG 243
Cdd:PRK11929 164 ---DAIILHRI--LARMR----AAGADAVAMEASSHGLEQGRLDG---LRIAVAGFTNLTRDHLDYHG-TMQDYEEAKAA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 244 IITN--PDSVTIIADQDPEAMRV--VLEAAVDTGSAVARLGIEFTVAEATVAVGGQNLTLKGLGGEYTdIFLPLSGPHQA 319
Cdd:PRK11929 231 LFSKlpGLGAAVINADDPAAARLlaALPRGLKVGYSPQNAGADVQARDLRATAHGQVFTLATPDGSYQ-LVTRLLGRFNV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 320 RNAAVALaaveafhGASSERPLDADTVRRGFAAVES-PGRLERVRAT-----PTTFIDATHNPHgarALADALAN----- 388
Cdd:PRK11929 310 SNLLLVA-------AALKKLGLPLAQIARALAAVSPvPGRMERVGPTagaqgPLVVVDYAHTPD---ALAKALTAlrpva 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 389 DFDFTRLIGVLGVLGDKDATG--ILAALEPVFTEVVITQNTSPRAMDAYE-LAELAREIYGDERVHVVTRLADAYELAVE 465
Cdd:PRK11929 380 QARNGRLVCVFGCGGDRDKGKrpEMGRIAAELADRVVVTSDNPRSEAPEAiIDQILAGIPAGARVFVISDRAEAIRQAIW 459
|
..
gi 493893808 466 LA 467
Cdd:PRK11929 460 MA 461
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
356-433 |
2.81e-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: 62.36 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 356 PGRLERVRA--TPTTFIDATHNPHGARALADALANDFDFtRLIGVLGVLGDKDAT--GILAALEPVFTEVVITQNTSPRA 431
Cdd:pfam02875 2 PGRLEVVGEnnGVLVIDDYAHNPDAMEAALRALRNLFPG-RLILVFGGMGDRDAEfhALLGRLAAALADVVILTGDYPRA 80
|
..
gi 493893808 432 MD 433
Cdd:pfam02875 81 ED 82
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
88-486 |
6.36e-10 |
|
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: 61.18 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 88 YLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPHLQLITERIGIDGAPIHPAQFVAIYDQVApymELAD 167
Cdd:TIGR01085 77 FYGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDLIKNPAALTTPEALTLQSTLA---EMVE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 168 QHsgqrlsyfealvcLAYAAFadapvevAVVEVGMG-GRWDATNVveaDVNVIMPIGLDHTDYLGdTLAQIAGEKAGIIT 246
Cdd:TIGR01085 154 AG-------------AQYAVM-------EVSSHALAqGRVRGVRF---DAAVFTNLSRDHLDFHG-TMENYFAAKASLFT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 247 N---PDSVTIIADqDPEAMRVVLEAAVDTGSAVARLGIEFTVA-----EATVAVGGQNLTLKGLGGEYtDIFLPLSGPHQ 318
Cdd:TIGR01085 210 ElglKRFAVINLD-DEYGAQFVKRLPKDITVSAITQPADGRAQdikitDSGYSFEGQQFTFETPAGEG-HLHTPLIGRFN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 319 ARNAAVALAAVEAFHGasserpLDADTVRRGFAAVES-PGRLERV--RATPTTFIDATHNPHgarALADALANDFDFT-- 393
Cdd:TIGR01085 288 VYNLLAALATLLHLGG------IDLEDIVAALEKFRGvPGRMELVdgGQKFLVIVDYAHTPD---ALEKALRTLRKHKdg 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 394 RLIGVLGVLGDKDAT--GILAALEPVFTEVVITQNTSPRAMDAYE-LAELAREIYGDERVHVVTRLADAYELAVELAEDa 470
Cdd:TIGR01085 359 RLIVVFGCGGDRDRGkrPLMGAIAEQLADLVILTSDNPRGEDPEQiIADILAGISEKEKVVIIADRRQAIRYAISNAKA- 437
|
410
....*....|....*.
gi 493893808 471 laevgvqsGSGVVITG 486
Cdd:TIGR01085 438 --------GDVVLIAG 445
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
101-318 |
3.00e-07 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 50.77 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 101 VAGTNGKTSTTRMIDSLLRAFGHRVG----------RTTSPHLQLiterigidgapihPAQFVAIYDQVAPY--MELADQ 168
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLAGGVIGtigtyigksgNTTNNAIGL-------------PLTLAEMVEAGAEYavLEVSSH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 169 HSGQRLSYFEalvclayaafadapvevavvevgmggrwdatnvVEADVNVIMPIGLDHTDYLGdTLAQIAGEKAGIITN- 247
Cdd:pfam08245 68 GLGEGRLSGL---------------------------------LKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGl 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493893808 248 -PDSVTII-ADqDPEAMRVVLEAAVdTGSAVARLGIE----FTVAEATVAVGGQNLTLKGLGGEYTDIFLPLSGPHQ 318
Cdd:pfam08245 114 pEDGIAVInAD-DPYGAFLIAKLKK-AGVRVITYGIEgeadLRAANIELSSDGTSFDLFTVPGGELEIEIPLLGRHN 188
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
88-408 |
5.25e-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: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 88 YLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGrttsphlqLI-TERIGIDGAPIHP--------------AQF 152
Cdd:PRK00139 87 FYGHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTA--------LIgTLGNGIGGELIPSglttpdaldlqrllAEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 153 VaiyDQVAPY--MELA----DQHsgqRLSYfealVCLAYAAFadapvevavvevgmggrwdaTNvveadvnvimpIGLDH 226
Cdd:PRK00139 159 V---DAGVTYaaMEVSshalDQG---RVDG----LKFDVAVF--------------------TN-----------LSRDH 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 227 TDYLGdTLAQIAGEKAGIITNPDSVTIIADQDPEAMRVvleAAVDTGSAVARLGIEFTVAEATVAVGGQNLTLkglggeY 306
Cdd:PRK00139 198 LDYHG-TMEDYLAAKARLFSELGLAAVINADDEVGRRL---LALPDAYAVSMAGADLRATDVEYTDSGQTFTL------V 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 307 TDIFLPLSGphqarnaavalaaveAFH--------GASSERPLDADTVRRGFAAVES-PGRLERVRAT--PTTFIDATHN 375
Cdd:PRK00139 268 TEVESPLIG---------------RFNvsnllaalAALLALGVPLEDALAALAKLQGvPGRMERVDAGqgPLVIVDYAHT 332
|
330 340 350
....*....|....*....|....*....|....*....
gi 493893808 376 PhgaralaDALANDFDFTR------LIGVLGVLGDKDAT 408
Cdd:PRK00139 333 P-------DALEKVLEALRphakgrLICVFGCGGDRDKG 364
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
101-130 |
3.97e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 49.38 E-value: 3.97e-06
10 20 30
....*....|....*....|....*....|
gi 493893808 101 VAGTNGKTSTTRMIDSLLRAFGHRVGRTTS 130
Cdd:PRK14016 485 VTGTNGKTTTTRLIAHILKLSGKRVGMTTT 514
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
82-122 |
3.68e-04 |
|
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: 43.06 E-value: 3.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 493893808 82 VRLLMDYLGEPQKSFRTIHVAGTNGKTSTTRMIDSLLRAFG 122
Cdd:TIGR01082 85 VIRRAEMLAELMRFRHSIAVAGTHGKTTTTAMIAVILKEAG 125
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
93-404 |
2.67e-03 |
|
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: 40.46 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 93 QKSFRTIHVAGTNGKTSTTRMIDSLLRAFGHRVGRTTSPhlQLITERIGIdgaPIHPAQFVAIYDqvAPYMELADQHSGQ 172
Cdd:PRK11929 600 RFSLPVVAITGSNGKTTTKEMIAAILAAWQGEDRVLATE--GNFNNEIGV---PLTLLRLRAQHR--AAVFELGMNHPGE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 173 rlsyfealvcLAYAAfadapvevavvevgmggrwdatNVVEADVNVIMPIGLDHTDYLGDtLAQIAGEKAGIITN--PDS 250
Cdd:PRK11929 673 ----------IAYLA----------------------AIAAPTVALVTNAQREHQEFMHS-VEAVARAKGEIIAAlpEDG 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 251 VTIIADQDPeamRVVLEAAVDTGSAVARLGI--------EFTVAEATVAVGGQNLTLKGLGGEYTDIFLPLSGPHQARNA 322
Cdd:PRK11929 720 VAVVNGDDP---YTAIWAKLAGARRVLRFGLqpgadvyaEKIAKDISVGEAGGTRCQVVTPAGSAEVYLPLIGEHNLRNA 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493893808 323 AVALAAVEAFhGASserpldADTVRRGFAAVESP-GRLERVR-ATPTTFIDATH--NPHGARALADALAnDFDFTRLIGV 398
Cdd:PRK11929 797 LAAIACALAA-GAS------LKQIRAGLERFQPVaGRMQRRRlSCGTRIIDDTYnaNPDSMRAAIDVLA-ELPNGPRALV 868
|
....*.
gi 493893808 399 LGVLGD 404
Cdd:PRK11929 869 LGDMLE 874
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
103-126 |
4.23e-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: 39.68 E-value: 4.23e-03
10 20
....*....|....*....|....
gi 493893808 103 GTNGKTSTTRMIDSLLRAFGHRVG 126
Cdd:COG0771 112 GTNGKTTTTTLIGHILKAAGLRVA 135
|
|
| |
