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Conserved domains on  [gi|765340688|ref|WP_044659085|]
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MULTISPECIES: folylpolyglutamate synthase/dihydrofolate synthase family protein [Micrococcus]

Protein Classification

bifunctional folylpolyglutamate synthase/dihydrofolate synthase( domain architecture ID 11416298)

bifunctional folylpolyglutamate synthase (FGPS)/dihydrofolate synthase (DHFS) functions in two distinct reactions of the de novo folate biosynthetic pathway, catalyzing the addition of a glutamate residue to dihydropteroate to form dihydrofolate and the successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives

CATH:  3.40.1190.10|3.90.190.20
EC:  6.3.2.-
Gene Ontology:  GO:0004326|GO:0008841|GO:0005524|GO:0006730|GO:0046872
SCOP:  4000353

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 8-426 2.95e-152

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: 441.47  E-value: 2.95e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688   8 TVEEVYRDLLARAPeNKMQPRLEPMRRVLALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVT 87
Cdd:COG0285    3 TYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  88 ERISIDGAPVADETFVRVWGEILPIVQTVDAEleaagevPLTYFEAVTTLGFAVFADEPvevvvlevglggvT------- 160
Cdd:COG0285   82 ERIRINGEPISDEELVEALEEVEPAVEEVDAG-------PPTFFEVTTAAAFLYFAEAP-------------Vdvavlev 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 161 ------DATNVADAVVSVVTPISLDHTDLLGETEAEIAEEKAGIIKPGGALVSAAQERDAAQVLLEAARAADVPFRFEGV 234
Cdd:COG0285  142 glggrlDATNVIDPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGR 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 235 EFGVLERslavGGQQVSVRGLAAEYRDLFLPLLGEHQAQNLAVAVAALEMFLGGGeRPLDEELLREGLSQVTSPGRLEVL 314
Cdd:COG0285  222 DFSVEER----EGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG-LPISEEAIREGLANARWPGRLEVL 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 315 RTAPTLIVDAAHNPDGVRATARAVQEAFGFTRLSLVVGILQEKDAPGMLAALyrafGDDVEDLAVTQSSSARAIPAGELA 394
Cdd:COG0285  297 SRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAAL----APLADEVIVTTPPSPRALDAEELA 372

                        410       420       430
                 ....*....|....*....|....*....|..
gi 765340688 395 RMAVDAGwpeDDVYATESVPDALEWAVGRAEA 426
Cdd:COG0285  373 EAARELG---LRVEVAPDVEEALEAALELADP 401
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 8-426 2.95e-152

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: 441.47  E-value: 2.95e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688   8 TVEEVYRDLLARAPeNKMQPRLEPMRRVLALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVT 87
Cdd:COG0285    3 TYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  88 ERISIDGAPVADETFVRVWGEILPIVQTVDAEleaagevPLTYFEAVTTLGFAVFADEPvevvvlevglggvT------- 160
Cdd:COG0285   82 ERIRINGEPISDEELVEALEEVEPAVEEVDAG-------PPTFFEVTTAAAFLYFAEAP-------------Vdvavlev 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 161 ------DATNVADAVVSVVTPISLDHTDLLGETEAEIAEEKAGIIKPGGALVSAAQERDAAQVLLEAARAADVPFRFEGV 234
Cdd:COG0285  142 glggrlDATNVIDPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGR 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 235 EFGVLERslavGGQQVSVRGLAAEYRDLFLPLLGEHQAQNLAVAVAALEMFLGGGeRPLDEELLREGLSQVTSPGRLEVL 314
Cdd:COG0285  222 DFSVEER----EGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG-LPISEEAIREGLANARWPGRLEVL 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 315 RTAPTLIVDAAHNPDGVRATARAVQEAFGFTRLSLVVGILQEKDAPGMLAALyrafGDDVEDLAVTQSSSARAIPAGELA 394
Cdd:COG0285  297 SRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAAL----APLADEVIVTTPPSPRALDAEELA 372

                        410       420       430
                 ....*....|....*....|....*....|..
gi 765340688 395 RMAVDAGwpeDDVYATESVPDALEWAVGRAEA 426
Cdd:COG0285  373 EAARELG---LRVEVAPDVEEALEAALELADP 401
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 29-434 4.60e-98

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: 301.89  E-value: 4.60e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688   29 LEPMRRVLALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVTERISIDGAPVADETFVRVWGE 108
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  109 ILPIVQTVDAELeaagevplTYFEAVTTLGFAVFADEPVEVVVLEVGLGGVTDATNVADAVVSVVTPISLDHTDLLGETE 188
Cdd:TIGR01499  81 VRPILESLSQQP--------TYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  189 AEIAEEKAGIIKPGGALVSAAQERDAAQVLLEAARAADVPFRFEGVEFGVLErslaVGGQQVSVRGLAAEYRDLFLPLLG 268
Cdd:TIGR01499 153 EEIAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSE----TDENYLSFSGANLFLEPLALSLLG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  269 EHQAQNLAVAVAALEMfLGGGERPLDEELLREGLSQVTSPGRLEVLRT-APTLIVDAAHNPDGVRATARAVQEAFGFTRL 347
Cdd:TIGR01499 229 DHQQENAALALAALEV-LGKQNPKLSEEAIRQGLANTIWPGRLEILSEdNPNILLDGAHNPHSAEALAEWFKKRFNGRPI 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  348 SLVVGILQEKDAPGMLAALYRAFGDDVedlAVTQSSSARAIPAGELARMAVDAGwpeddvyaTESVPDaleWAVGRAEAL 427
Cdd:TIGR01499 308 TLLFGALADKDAAAMLAPLKPVVDKEV---FVTPFDYPRADDAADLAAFAEETG--------KSTVED---WREALEEAL 373


                  ....*..
gi 765340688  428 ETSADEL 434
Cdd:TIGR01499 374 NASAEDD 380
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 29-366 6.64e-47

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 168.33  E-value: 6.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  29 LEPMRRVLALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVTERISIDGAPVADETFVRVWge 108
Cdd:PRK10846  32 LERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTASF-- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 109 ilpivqtvdAELEAA-GEVPLTYFEAVTTLGFAVFADEPVEVVVLEVGLGGVTDATNVADAVVSVVTPISLDHTDLLGET 187
Cdd:PRK10846 110 ---------AEIEAArGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 188 EAEIAEEKAGIIKPGGALVSAAQER-----DAAQVLLEAARAADVPFRFEgvefgvlerslaVGGQQVSVRGLAAEYRDL 262
Cdd:PRK10846 181 RESIGREKAGIFRAEKPAVVGEPDMpstiaDVAQEKGALLQRRGVDWNYS------------VTDHDWAFSDGDGTLENL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 263 FLPLLgehQAQNLAVAVAALEMflggGERPLDEELLREGLSQVTSPGRLEVLRTAPTLIVDAAHNPDGVRATARAVQEAF 342
Cdd:PRK10846 249 PLPNV---PLPNAATALAALRA----SGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKALP 321

                        330       340
                 ....*....|....*....|....
gi 765340688 343 GFTRLSLVVGILQEKDAPGMLAAL 366
Cdd:PRK10846 322 KNGRVLAVIGMLHDKDIAGTLACL 345
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 308-374 8.40e-09

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: 52.73  E-value: 8.40e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 765340688  308 PGRLEVLRTA--PTLIVDAAHNPDGVRATARAVQEAFGFtRLSLVVGILQEKDA--PGMLAALYRAFGDDV 374
Cdd:pfam02875   2 PGRLEVVGENngVLVIDDYAHNPDAMEAALRALRNLFPG-RLILVFGGMGDRDAefHALLGRLAAALADVV 71
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 8-426 2.95e-152

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: 441.47  E-value: 2.95e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688   8 TVEEVYRDLLARAPeNKMQPRLEPMRRVLALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVT 87
Cdd:COG0285    3 TYQEALAYLESLHP-FGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  88 ERISIDGAPVADETFVRVWGEILPIVQTVDAEleaagevPLTYFEAVTTLGFAVFADEPvevvvlevglggvT------- 160
Cdd:COG0285   82 ERIRINGEPISDEELVEALEEVEPAVEEVDAG-------PPTFFEVTTAAAFLYFAEAP-------------Vdvavlev 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 161 ------DATNVADAVVSVVTPISLDHTDLLGETEAEIAEEKAGIIKPGGALVSAAQERDAAQVLLEAARAADVPFRFEGV 234
Cdd:COG0285  142 glggrlDATNVIDPLVSVITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGR 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 235 EFGVLERslavGGQQVSVRGLAAEYRDLFLPLLGEHQAQNLAVAVAALEMFLGGGeRPLDEELLREGLSQVTSPGRLEVL 314
Cdd:COG0285  222 DFSVEER----EGAVFSYQGPGGEYEDLPLPLLGAHQAENAALALAALEALRELG-LPISEEAIREGLANARWPGRLEVL 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 315 RTAPTLIVDAAHNPDGVRATARAVQEAFGFTRLSLVVGILQEKDAPGMLAALyrafGDDVEDLAVTQSSSARAIPAGELA 394
Cdd:COG0285  297 SRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAAL----APLADEVIVTTPPSPRALDAEELA 372

                        410       420       430
                 ....*....|....*....|....*....|..
gi 765340688 395 RMAVDAGwpeDDVYATESVPDALEWAVGRAEA 426
Cdd:COG0285  373 EAARELG---LRVEVAPDVEEALEAALELADP 401
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 29-434 4.60e-98

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: 301.89  E-value: 4.60e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688   29 LEPMRRVLALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVTERISIDGAPVADETFVRVWGE 108
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  109 ILPIVQTVDAELeaagevplTYFEAVTTLGFAVFADEPVEVVVLEVGLGGVTDATNVADAVVSVVTPISLDHTDLLGETE 188
Cdd:TIGR01499  81 VRPILESLSQQP--------TYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  189 AEIAEEKAGIIKPGGALVSAAQERDAAQVLLEAARAADVPFRFEGVEFGVLErslaVGGQQVSVRGLAAEYRDLFLPLLG 268
Cdd:TIGR01499 153 EEIAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSE----TDENYLSFSGANLFLEPLALSLLG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  269 EHQAQNLAVAVAALEMfLGGGERPLDEELLREGLSQVTSPGRLEVLRT-APTLIVDAAHNPDGVRATARAVQEAFGFTRL 347
Cdd:TIGR01499 229 DHQQENAALALAALEV-LGKQNPKLSEEAIRQGLANTIWPGRLEILSEdNPNILLDGAHNPHSAEALAEWFKKRFNGRPI 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  348 SLVVGILQEKDAPGMLAALYRAFGDDVedlAVTQSSSARAIPAGELARMAVDAGwpeddvyaTESVPDaleWAVGRAEAL 427
Cdd:TIGR01499 308 TLLFGALADKDAAAMLAPLKPVVDKEV---FVTPFDYPRADDAADLAAFAEETG--------KSTVED---WREALEEAL 373


                  ....*..
gi 765340688  428 ETSADEL 434
Cdd:TIGR01499 374 NASAEDD 380
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 29-366 6.64e-47

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 168.33  E-value: 6.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  29 LEPMRRVLALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVTERISIDGAPVADETFVRVWge 108
Cdd:PRK10846  32 LERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTASF-- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 109 ilpivqtvdAELEAA-GEVPLTYFEAVTTLGFAVFADEPVEVVVLEVGLGGVTDATNVADAVVSVVTPISLDHTDLLGET 187
Cdd:PRK10846 110 ---------AEIEAArGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 188 EAEIAEEKAGIIKPGGALVSAAQER-----DAAQVLLEAARAADVPFRFEgvefgvlerslaVGGQQVSVRGLAAEYRDL 262
Cdd:PRK10846 181 RESIGREKAGIFRAEKPAVVGEPDMpstiaDVAQEKGALLQRRGVDWNYS------------VTDHDWAFSDGDGTLENL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 263 FLPLLgehQAQNLAVAVAALEMflggGERPLDEELLREGLSQVTSPGRLEVLRTAPTLIVDAAHNPDGVRATARAVQEAF 342
Cdd:PRK10846 249 PLPNV---PLPNAATALAALRA----SGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGRLKALP 321

                        330       340
                 ....*....|....*....|....
gi 765340688 343 GFTRLSLVVGILQEKDAPGMLAAL 366
Cdd:PRK10846 322 KNGRVLAVIGMLHDKDIAGTLACL 345
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 28-336 2.18e-45

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 166.76  E-value: 2.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  28 RLEPMRRVLALLG--DPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVTERISIDGAPVADETFVR- 104
Cdd:PLN02881  41 QFDLLFDYLKILEleEAISRLKVIHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRy 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 105 ---VWGEIlpivqtvdAElEAAGEVPL-TYFEAVTTLGFAVFADEPVEVVVLEVGLGGVTDATNVADA-VVSVVTPISLD 179
Cdd:PLN02881 121 fwwCWDRL--------KE-KTTEDLPMpAYFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKpVVCGITSLGYD 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 180 HTDLLGETEAEIAEEKAGIIKPGGALVSAAQERDAAQVLLEAARAADVPFrfegvefgvlerslavggqQVsVRGL-AAE 258
Cdd:PLN02881 192 HMEILGDTLGKIAGEKAGIFKPGVPAFTVPQPDEAMRVLEERASELGVPL-------------------QV-VEPLdSYG 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 259 YRDLFLPLLGEHQAQNLAVAVAALEMFL---GGGERPLDE------ELLREGLSQVTSPGRLEVL-------RTAPTLI- 321
Cdd:PLN02881 252 LSGLKLGLAGEHQYLNAGLAVALCSTWLqrtGHEEFEALLqagtlpEQFIKGLSTASLQGRAQVVpdsyinsEDSGDLVf 331

                        330
                 ....*....|....*.
gi 765340688 322 -VDAAHNPDGVRATAR 336
Cdd:PLN02881 332 yLDGAHSPESMEACAR 347
PLN02913 PLN02913
dihydrofolate synthetase
 32-358 4.28e-38

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 146.12  E-value: 4.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  32 MRRVLALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPHLQRVTERISI--DGAPVADETFVRVWGEI 109
Cdd:PLN02913  61 MRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVgkLGKPVSTNTLNDLFHGI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 110 LPIVQTVdAELEAAGevpLTYFEAVTTLGFAVFADEPVEVVVLEVGLGGVTDATNVADA---VVSVVTPISLDHTDLLGE 186
Cdd:PLN02913 141 KPILDEA-IQLENGS---LTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSsglAASVITTIGEEHLAALGG 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 187 TEAEIAEEKAGIIKPGGALVSAAQ-ERDAAQVLLEAARAADVPF----------------RFEGVEFGVLERSLAVGGQQ 249
Cdd:PLN02913 217 SLESIALAKSGIIKQGRPVVLGGPfLPHIESILRDKASSMNSPVvsasdpgvrssikgiiTDNGKPCQSCDIVIRVEKDD 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 250 vsvrGLAAEYRDLFLPLLGEHQAQNLAVAV-AALEMFLGGGERPldEELLREGLSQVTSPGRLEVLR---------TAPT 319
Cdd:PLN02913 297 ----PLFIELSDVNLRMLGSHQLQNAVTAAcAALCLRDQGWRIS--DASIRAGLENTNLLGRSQFLTskeaevlglPGAT 370

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 765340688 320 LIVDAAHNPDGVRATARAVQEAFGFTRLSLVVGILQEKD 358
Cdd:PLN02913 371 VLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKD 409
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 33-352 4.81e-17

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: 83.59  E-value: 4.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  33 RRVLALL-----GDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGrytsphlqrvteriSIdGApvadeTFVRVWG 107
Cdd:COG0769   62 RAALALLaaafyGHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTG--------------LI-GT-----VGNGIGG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 108 EILPIVQTVdaeleaagevPltyfEAVTTLG-FAVFADEpvevvvlevglggvtDATNVA-------------DAV---V 170
Cdd:COG0769  122 ELIPSSLTT----------P----EALDLQRlLAEMVDA---------------GVTHVVmevsshaldqgrvDGVrfdV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 171 SVVTPISLDHTDLLGeTEAEIAEEKAGII----KPGGALVSAAQERdaAQVLLEAARAADVPFRFEG-VEFGVLERSLAV 245
Cdd:COG0769  173 AVFTNLTRDHLDYHG-TMEAYFAAKARLFdqlgPGGAAVINADDPY--GRRLAAAAPARVITYGLKAdADLRATDIELSA 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 246 GGQQVSVRGLAAEYRdLFLPLLGEHQAQNLAVAVAALemfLGGGerpLDEELLREGLSQVTS-PGRLEVLRTA--PTLIV 322
Cdd:COG0769  250 DGTRFTLVTPGGEVE-VRLPLIGRFNVYNALAAIAAA---LALG---IDLEEILAALEKLKGvPGRMERVDGGqgPTVIV 322

                        330       340       350
                 ....*....|....*....|....*....|..
gi 765340688 323 DAAHNPDGVRATARAVQEafgFT--RLSLVVG 352
Cdd:COG0769  323 DYAHTPDALENVLEALRP---HTkgRLIVVFG 351
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 33-352 1.26e-13

UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 72.86  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  33 RRVLALL-----GDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGrytsphLqrvterISIDGapvadetfVRVWG 107
Cdd:PRK00139  77 RKALALLaaafyGHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTA------L------IGTLG--------NGIGG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 108 EILPivqtvdaeleaageVPLTYFEAVTTLG-FAVFADEpvevvvlevglggvtDATNVA-------------DAV---V 170
Cdd:PRK00139 137 ELIP--------------SGLTTPDALDLQRlLAELVDA---------------GVTYAAmevsshaldqgrvDGLkfdV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 171 SVVTPISLDHtdlLGE--TEAEIAEEKAGIIKPGG--ALVSAaqERDAAQVLLEAARAadVPFRFEGVEFGVLERSLAVG 246
Cdd:PRK00139 188 AVFTNLSRDH---LDYhgTMEDYLAAKARLFSELGlaAVINA--DDEVGRRLLALPDA--YAVSMAGADLRATDVEYTDS 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 247 GQQVSVRGlaaeyrDLFLPLLGEHQAQNLAVAVAALeMFLGggerpLDEELLREGLSQVTS-PGRLEVLRTA--PTLIVD 323
Cdd:PRK00139 261 GQTFTLVT------EVESPLIGRFNVSNLLAALAAL-LALG-----VPLEDALAALAKLQGvPGRMERVDAGqgPLVIVD 328

                        330       340       350
                 ....*....|....*....|....*....|.
gi 765340688 324 AAHNPDGVRATARAVQEafgFT--RLSLVVG 352
Cdd:PRK00139 329 YAHTPDALEKVLEALRP---HAkgRLICVFG 356
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 170-419 1.89e-11

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: 65.89  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 170 VSVVTPISLDHTDLLGeTEAEIAEEKAGII---KPGG--------ALVSAAQERDAAQVLL----EAA--RAADVPFRFE 232
Cdd:COG0770  178 IAVITNIGPAHLEGFG-SLEGIARAKGEIFeglPPGGvavlnaddPLLAALAERAKARVLTfglsEDAdvRAEDIELDED 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 233 GVEFgvlerSLAVGGQQVSVRglaaeyrdlfLPLLGEHQAQNlAVAVAALEMFLGggerpLDEELLREGLSQVT-SPGRL 311
Cdd:COG0770  257 GTRF-----TLHTPGGELEVT----------LPLPGRHNVSN-ALAAAAVALALG-----LDLEEIAAGLAAFQpVKGRL 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 312 EVLRTAP--TLIVDA--AhNPDGVRATARAVQEAFGFTRLSLVVGilqekdapGML------AALYRAFGDDVEDLAVtq 381
Cdd:COG0770  316 EVIEGAGgvTLIDDSynA-NPDSMKAALDVLAQLPGGGRRIAVLG--------DMLelgeesEELHREVGELAAELGI-- 384

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 765340688 382 sssARAIPAGELARMAVDAgWPEDDVYATESVPDALEW 419
Cdd:COG0770  385 ---DRLFTVGELARAIAEA-AGGERAEHFEDKEELLAA 418
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 37-352 9.52e-11

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: 63.87  E-value: 9.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688   37 ALLGDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTsphlqrvTERISIDGAPVADETFVRVWGEiLPIVQTV 116
Cdd:TIGR01085  76 AFYGHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIG-------TIGYRLGGNDLIKNPAALTTPE-ALTLQST 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  117 DAELEAAGeVPLTYFEaVTTLGFAvfadepvevvvlevglggvTDATNVADAVVSVVTPISLDHTDLLGETEAEIAEeKA 196
Cdd:TIGR01085 148 LAEMVEAG-AQYAVME-VSSHALA-------------------QGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAA-KA 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  197 GIIKPGGALVSAAQERDA--AQVLLEAArAADVPFRFEGVEFGVLERSLAVGGQQVSVRGLA------AEYRDLFLPLLG 268
Cdd:TIGR01085 206 SLFTELGLKRFAVINLDDeyGAQFVKRL-PKDITVSAITQPADGRAQDIKITDSGYSFEGQQftfetpAGEGHLHTPLIG 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  269 EHQAQNLAVAVAALEMFLGggerpLDEELLREGLSQVTS-PGRLEV--LRTAPTLIVDAAHNPDGVRATARAVQEAFGfT 345
Cdd:TIGR01085 285 RFNVYNLLAALATLLHLGG-----IDLEDIVAALEKFRGvPGRMELvdGGQKFLVIVDYAHTPDALEKALRTLRKHKD-G 358


                  ....*..
gi 765340688  346 RLSLVVG 352
Cdd:TIGR01085 359 RLIVVFG 365
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 308-374 8.40e-09

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: 52.73  E-value: 8.40e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 765340688  308 PGRLEVLRTA--PTLIVDAAHNPDGVRATARAVQEAFGFtRLSLVVGILQEKDA--PGMLAALYRAFGDDV 374
Cdd:pfam02875   2 PGRLEVVGENngVLVIDDYAHNPDAMEAALRALRNLFPG-RLILVFGGMGDRDAefHALLGRLAAALADVV 71
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
 170-425 2.82e-07

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: 52.76  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 170 VSVVTPISLDHTDLLGeTEAEIAE---EKAGIIKPGGALVSAAQErdaaQVLLEAARAADVPFRF----EGVEFGVLERS 242
Cdd:COG0773  174 IAVVTNIEADHLDIYG-DLEAIKEafhEFARNVPFYGLLVLCADD----PGLRELLPRCGRPVITygfsEDADYRAENIR 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 243 LAVGGQQVSVRGLAAEYRDLFLPLLGEHQAQNLAVAVAALeMFLGggerpLDEELLREGLSQVTSPG-RLEVLRTAP--T 319
Cdd:COG0773  249 IDGGGSTFDVLRRGEELGEVELNLPGRHNVLNALAAIAVA-LELG-----VDPEAIAEALASFKGVKrRFELKGEVGgvT 322

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 320 LIVDAAHNPDGVRATARAVQEAFGFTRLslvVGILQekdaP---GMLAALYRAFG---DDVEDLAVTQSSSARAIPAGEL 393
Cdd:COG0773  323 VIDDYAHHPTEIAATLAAAREKYPDRRL---VAVFQ----PhrySRTRDFLDEFAealSLADEVILLDIYAAREKPIPGV 395

                        250       260       270
                 ....*....|....*....|....*....|....
gi 765340688 394 -ARMAVDA-GWPEDDVYATESVPDALEWAVGRAE 425
Cdd:COG0773  396 sSEDLAEAiRKRGKDVVYVPDLDELVEALAEIAR 429
Mur_ligase_M pfam08245
Mur ligase middle domain;
52-282 3.66e-06

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 47.68  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688   52 TGTNGKTSTARMVEAVLRAYGLRTG-RYTSPHLQRVTERISIdGAPVADETFVRVWGEIlpivqtvdAELE----AAGEV 126
Cdd:pfam08245   2 TGTNGKTTTTELIAAILSLAGGVIGtIGTYIGKSGNTTNNAI-GLPLTLAEMVEAGAEY--------AVLEvsshGLGEG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  127 PLTyfeavttlGFAVFAdepvevvvlevglggvtdatnvadavVSVVTPISLDHTDLLGeTEAEIAEEKAGIIK---PGG 203
Cdd:pfam08245  73 RLS--------GLLKPD--------------------------IAVFTNISPDHLDFHG-TMENYAKAKAELFEglpEDG 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  204 ALVSAAQErDAAQVLLEAARAADVPFRFEGVE----FGVLERSLAVGGQQVSVRGLAAEYRDLFLPLLGEHQAQNLAVAV 279
Cdd:pfam08245 118 IAVINADD-PYGAFLIAKLKKAGVRVITYGIEgeadLRAANIELSSDGTSFDLFTVPGGELEIEIPLLGRHNVYNALAAI 196


                  ...
gi 765340688  280 AAL 282
Cdd:pfam08245 197 AAA 199
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
296-358 5.67e-06

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 48.88  E-value: 5.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 765340688 296 ELLREGLSQVTSPGRLEVL-RTAP-TLIVDAAHNPDGVRATARAVQEaFGFTRLSLVVGILQEKD 358
Cdd:PRK14022 316 EDIQKGIAQTPVPGRMEVLtQSNGaKVFIDYAHNGDSLNKLIDVVEE-HQKGKLILLLGAAGNKG 379
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 40-339 1.39e-05

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: 47.78  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  40 GDPQHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRytsphlqrvterISIDGApvadetfvRVWGEILP-------- 111
Cdd:PRK11929 106 GRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGS------------IGTLGA--------RLDGRLIPgslttpda 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 112 -IVQTVDAELEAAGevpltyfeavttlgfavfADEPVEVVVLEVGLGGVTDATNVAdavVSVVTPISLDHTDLLGETEAe 190
Cdd:PRK11929 166 iILHRILARMRAAG------------------ADAVAMEASSHGLEQGRLDGLRIA---VAGFTNLTRDHLDYHGTMQD- 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 191 IAEEKAGI---IKPGGALVSAAQERDAAQVLLEAARAADVPFRFEGVEFGVLERSLAVG--GQQVSVRGLAAEYRdLFLP 265
Cdd:PRK11929 224 YEEAKAALfskLPGLGAAVINADDPAAARLLAALPRGLKVGYSPQNAGADVQARDLRATahGQVFTLATPDGSYQ-LVTR 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 266 LLGEHQAQNLAVAVAALEMfLGggerpLDEELLREGLSQVTS-PGRLEVL-----RTAPTLIVDAAHNPDgvrATARAVQ 339
Cdd:PRK11929 303 LLGRFNVSNLLLVAAALKK-LG-----LPLAQIARALAAVSPvPGRMERVgptagAQGPLVVVDYAHTPD---ALAKALT 373
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 46-378 1.58e-05

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: 47.34  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688   46 APVIHLTGTNGKTSTARMVEAVLRAYGLRtgrytsphlqrvterisidgAPVAdetfvrvwGEI-LPIVQTVDAELEAAG 124
Cdd:TIGR01087 102 LPVVAITGTNGKTTTTSLLYHLLKAAGLK--------------------AFLG--------GNIgTPALEVLDQEGAELY 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  125 EVPLTYFEAVTTLGFavfadepvevvvlevglggvtdatnvaDAVVSVVTPISLDHTDLLGETEAEIAeEKAGIIK--PG 202
Cdd:TIGR01087 154 VLELSSFQLETTESL---------------------------RPEIALILNISEDHLDWHGSFEDYVA-AKLKIFArqTE 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  203 GALVSAAQERDAAQVLLEAARAADVPFRfegvEFGVLERSLAVGGQQVSVRGlaaeyRDLFLPLLGEHQAQNLAVAVA-A 281
Cdd:TIGR01087 206 GDVAVLNADDPRFARLAQKSKAQVIWFS----VEKDAERGLCIRDGGLYLKP-----NDLEGSLLGLHNAENILAAIAlA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  282 LEMFlgggerpLDEELLREGLSQVTS-PGRLEVLRTAP--TLIVD-AAHNPDGVRATARAVQEafgftRLSLVV-GILQE 356
Cdd:TIGR01087 277 KSLG-------LNLEAILEALRSFKGlPHRLEYVGQKNgvHFYNDsKATNVHATLAALSAFDN-----PVILIVgGDDKG 344

                         330       340
                  ....*....|....*....|....*...
gi 765340688  357 KDAPGMLAAL------YRAFGDDVEDLA 378
Cdd:TIGR01087 345 ADFSPLAPAAagkvkaVLAIGEDAAKIA 372
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 47-80 4.57e-05

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 46.30  E-value: 4.57e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 765340688  47 PVIHLTGTNGKTSTARMVEAVLRAYGLRTGrYTS 80
Cdd:PRK14016 481 PIVAVTGTNGKTTTTRLIAHILKLSGKRVG-MTT 513
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 45-76 2.33e-04

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: 43.53  E-value: 2.33e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 765340688  45 AAPVIHLTGTNGKTSTARMVEAVLRAYGLRTG 76
Cdd:COG0771  104 PAPIIAITGTNGKTTTTTLIGHILKAAGLRVA 135
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 43-419 1.18e-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: 41.61  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688  43 QHAAPVIHLTGTNGKTSTARMVEAVLRAYGLRTGRYTSPhlqrvterisidgapvadETFVRVWGeilpivqtvdaelea 122
Cdd:PRK11929 600 RFSLPVVAITGSNGKTTTKEMIAAILAAWQGEDRVLATE------------------GNFNNEIG--------------- 646

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 123 ageVPLTYFEAVTTLGFAVF---ADEPVEVVVLEVglggvtdatnVADAVVSVVTPISLDHTDLLGETEAeIAEEKAGII 199
Cdd:PRK11929 647 ---VPLTLLRLRAQHRAAVFelgMNHPGEIAYLAA----------IAAPTVALVTNAQREHQEFMHSVEA-VARAKGEII 712

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 200 ---KPGGALVSAAQERDAAQVLLEAARAADVPFRFEGVEFGVLER------SLAVGGQQVSVRgLAAEYRDLFLPLLGEH 270
Cdd:PRK11929 713 aalPEDGVAVVNGDDPYTAIWAKLAGARRVLRFGLQPGADVYAEKiakdisVGEAGGTRCQVV-TPAGSAEVYLPLIGEH 791

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765340688 271 QAQNLAVAVAALemfLGGGERPLDEELLREGLSQVtsPGRLEVLRTA-PTLIVDAAH--NPDGVRATARAVQEAFGFTRL 347
Cdd:PRK11929 792 NLRNALAAIACA---LAAGASLKQIRAGLERFQPV--AGRMQRRRLScGTRIIDDTYnaNPDSMRAAIDVLAELPNGPRA 866

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765340688 348 sLVVGILQEKDAPGmlAALYRAFGDDVEDLAVtqsssARAIPAGELARMAVdAGWPEDDVYATESVPDALEW 419
Cdd:PRK11929 867 -LVLGDMLELGDNG--PAMHREVGKYARQLGI-----DALITLGEAARDAA-AAFGAGARGVCASVDEIIAA 929
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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