NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1490726398|gb|RLC97393|]
View 

bifunctional folylpolyglutamate synthase/dihydrofolate synthase [Chloroflexi bacterium]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 23-440 0e+00

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: 526.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  23 ERLSRSAVVFDLARIEALLHRSGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGLYTSPHLHTIRERIQIDGSLI 102
Cdd:COG0285    12 ESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNERIRINGEPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 103 SERAFAGLVARLRPHIEYINRtctlGELTTFEILTAMAFSHFEERAVDFQVLETGLGGRLDATNVIRPEVCVITSISLDH 182
Cdd:COG0285    92 SDEELVEALEEVEPAVEEVDA----GPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVITSIGLDH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 183 TEVLGDTIAQIAVEKAGIIKPGTPVVCAPQVPEAASVIEEVCHDRESRLIRVGHDVTWKKTGasdlGQSFRVKGTKGSY- 261
Cdd:COG0285   168 TDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEERE----GAVFSYQGPGGEYe 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 262 DLTVPLLGEHQLENAAA-AVAALEVLAEGTGITPDSIARGLAQVRWPGRLQVMRTRPLFVVDGAHNADSVEKLKQSLRQS 340
Cdd:COG0285   244 DLPLPLLGAHQAENAALaLAALEALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAGARALAETLKEL 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 341 FAFDDSILIVGASRDKNITGIVAGLAPFSRRVIVTQSEHPRAAEVSTLAQEFSKWGIEALIARDTDSAIRAALREAKPTD 420
Cdd:COG0285   324 FPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAARELGLRVEVAPDVEEALEAALELADPDD 403

                         410       420
                  ....*....|....*....|
gi 1490726398 421 LICVTGSLFVVSEALRYFGR 440
Cdd:COG0285   404 LILVTGSLYLVGEVRALLGR 423
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 23-440 0e+00

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: 526.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  23 ERLSRSAVVFDLARIEALLHRSGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGLYTSPHLHTIRERIQIDGSLI 102
Cdd:COG0285    12 ESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNERIRINGEPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 103 SERAFAGLVARLRPHIEYINRtctlGELTTFEILTAMAFSHFEERAVDFQVLETGLGGRLDATNVIRPEVCVITSISLDH 182
Cdd:COG0285    92 SDEELVEALEEVEPAVEEVDA----GPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVITSIGLDH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 183 TEVLGDTIAQIAVEKAGIIKPGTPVVCAPQVPEAASVIEEVCHDRESRLIRVGHDVTWKKTGasdlGQSFRVKGTKGSY- 261
Cdd:COG0285   168 TDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEERE----GAVFSYQGPGGEYe 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 262 DLTVPLLGEHQLENAAA-AVAALEVLAEGTGITPDSIARGLAQVRWPGRLQVMRTRPLFVVDGAHNADSVEKLKQSLRQS 340
Cdd:COG0285   244 DLPLPLLGAHQAENAALaLAALEALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAGARALAETLKEL 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 341 FAFDDSILIVGASRDKNITGIVAGLAPFSRRVIVTQSEHPRAAEVSTLAQEFSKWGIEALIARDTDSAIRAALREAKPTD 420
Cdd:COG0285   324 FPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAARELGLRVEVAPDVEEALEAALELADPDD 403

                         410       420
                  ....*....|....*....|
gi 1490726398 421 LICVTGSLFVVSEALRYFGR 440
Cdd:COG0285   404 LILVTGSLYLVGEVRALLGR 423
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 34-438 4.54e-128

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: 376.24  E-value: 4.54e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  34 LARIEALLHRSGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGLYTSPHLHTIRERIQIDGSLISERAFAGLVAR 113
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 114 LRPHIEYinrtcTLGELTTFEILTAMAFSHFEERAVDFQVLETGLGGRLDATNVIRPEVCVITSISLDHTEVLGDTIAQI 193
Cdd:TIGR01499  81 VRPILES-----LSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 194 AVEKAGIIKPGTPVVCAPQVPEAASVIEEVCHDRESRLIRVGHDVTWKKTGASDLgqSFRVKGTKgSYDLTVPLLGEHQL 273
Cdd:TIGR01499 156 AWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENYL--SFSGANLF-LEPLALSLLGDHQQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 274 ENAAAA-VAALEVLAEGTGITPDSIARGLAQVRWPGRLQVMRTR-PLFVVDGAHNADSVEKLKQSLRQSFAFDDSILIVG 351
Cdd:TIGR01499 233 ENAALAlAALEVLGKQNPKLSEEAIRQGLANTIWPGRLEILSEDnPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFG 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 352 ASRDKNITGIVAGLAP-FSRRVIVTQSEHPRAAEVSTLAQEFSKWGIEalIARDTDSAIRAALReAKPTDLICVTGSLFV 430
Cdd:TIGR01499 313 ALADKDAAAMLAPLKPvVDKEVFVTPFDYPRADDAADLAAFAEETGKS--TVEDWREALEEALN-ASAEDDILVTGSLYL 389


                  ....*...
gi 1490726398 431 VSEALRYF 438
Cdd:TIGR01499 390 VGEVRKLL 397
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 54-331 3.97e-69

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 228.78  E-value: 3.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  54 VHVAGTKGKGSTSAMIATALTASGHRTGLYTSPHLHTIRERIQIDGSLISERAFAG----LVARLRPHIeyinrTCTLGE 129
Cdd:PLN02881   64 IHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRyfwwCWDRLKEKT-----TEDLPM 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 130 LTTFEILTAMAFSHFEERAVDFQVLETGLGGRLDATNVIR-PEVCVITSISLDHTEVLGDTIAQIAVEKAGIIKPGTPVV 208
Cdd:PLN02881  139 PAYFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQkPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAF 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 209 CAPQVPEAASVIEEvchdresrlirvghdvtwkktGASDLGQSFRVK---GTKGSYDLTVPLLGEHQLEN---------- 275
Cdd:PLN02881  219 TVPQPDEAMRVLEE---------------------RASELGVPLQVVeplDSYGLSGLKLGLAGEHQYLNaglavalcst 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490726398 276 -AAAAVAALEVLAEGTGITPDSIARGLAQVRWPGRLQVMRTRP---------LFVVDGAHNADSVE 331
Cdd:PLN02881  278 wLQRTGHEEFEALLQAGTLPEQFIKGLSTASLQGRAQVVPDSYinsedsgdlVFYLDGAHSPESME 343
Mur_ligase_M pfam08245
Mur ligase middle domain;
56-275 3.26e-10

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 59.24  E-value: 3.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  56 VAGTKGKGSTSAMIATALTASGHRTGlytsphlhTIreriqidGSLISErafaglvarlrphieyinrtctlGELTTFEI 135
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIG--------TI-------GTYIGK-----------------------SGNTTNNA 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 136 LT-AMAFSHFEERAVDFQVLET---GLG-GRLDATnvIRPEVCVITSISLDHTEVLGdTIAQIAVEKAGIIK----PGTP 206
Cdd:pfam08245  43 IGlPLTLAEMVEAGAEYAVLEVsshGLGeGRLSGL--LKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEglpeDGIA 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490726398 207 VV-----CAPQVPEAASVieevchdRESRLIRVG----HDVTWKKTGASDLGQSFRVKGTK-GSYDLTVPLLGEHQLEN 275
Cdd:pfam08245 120 VInaddpYGAFLIAKLKK-------AGVRVITYGiegeADLRAANIELSSDGTSFDLFTVPgGELEIEIPLLGRHNVYN 191
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 23-440 0e+00

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: 526.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  23 ERLSRSAVVFDLARIEALLHRSGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGLYTSPHLHTIRERIQIDGSLI 102
Cdd:COG0285    12 ESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNERIRINGEPI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 103 SERAFAGLVARLRPHIEYINRtctlGELTTFEILTAMAFSHFEERAVDFQVLETGLGGRLDATNVIRPEVCVITSISLDH 182
Cdd:COG0285    92 SDEELVEALEEVEPAVEEVDA----GPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVITSIGLDH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 183 TEVLGDTIAQIAVEKAGIIKPGTPVVCAPQVPEAASVIEEVCHDRESRLIRVGHDVTWKKTGasdlGQSFRVKGTKGSY- 261
Cdd:COG0285   168 TDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEERE----GAVFSYQGPGGEYe 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 262 DLTVPLLGEHQLENAAA-AVAALEVLAEGTGITPDSIARGLAQVRWPGRLQVMRTRPLFVVDGAHNADSVEKLKQSLRQS 340
Cdd:COG0285   244 DLPLPLLGAHQAENAALaLAALEALRELGLPISEEAIREGLANARWPGRLEVLSRGPLVILDGAHNPAGARALAETLKEL 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 341 FAFDDSILIVGASRDKNITGIVAGLAPFSRRVIVTQSEHPRAAEVSTLAQEFSKWGIEALIARDTDSAIRAALREAKPTD 420
Cdd:COG0285   324 FPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAARELGLRVEVAPDVEEALEAALELADPDD 403

                         410       420
                  ....*....|....*....|
gi 1490726398 421 LICVTGSLFVVSEALRYFGR 440
Cdd:COG0285   404 LILVTGSLYLVGEVRALLGR 423
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 34-438 4.54e-128

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: 376.24  E-value: 4.54e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  34 LARIEALLHRSGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGLYTSPHLHTIRERIQIDGSLISERAFAGLVAR 113
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 114 LRPHIEYinrtcTLGELTTFEILTAMAFSHFEERAVDFQVLETGLGGRLDATNVIRPEVCVITSISLDHTEVLGDTIAQI 193
Cdd:TIGR01499  81 VRPILES-----LSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 194 AVEKAGIIKPGTPVVCAPQVPEAASVIEEVCHDRESRLIRVGHDVTWKKTGASDLgqSFRVKGTKgSYDLTVPLLGEHQL 273
Cdd:TIGR01499 156 AWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENYL--SFSGANLF-LEPLALSLLGDHQQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 274 ENAAAA-VAALEVLAEGTGITPDSIARGLAQVRWPGRLQVMRTR-PLFVVDGAHNADSVEKLKQSLRQSFAFDDSILIVG 351
Cdd:TIGR01499 233 ENAALAlAALEVLGKQNPKLSEEAIRQGLANTIWPGRLEILSEDnPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFG 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 352 ASRDKNITGIVAGLAP-FSRRVIVTQSEHPRAAEVSTLAQEFSKWGIEalIARDTDSAIRAALReAKPTDLICVTGSLFV 430
Cdd:TIGR01499 313 ALADKDAAAMLAPLKPvVDKEVFVTPFDYPRADDAADLAAFAEETGKS--TVEDWREALEEALN-ASAEDDILVTGSLYL 389


                  ....*...
gi 1490726398 431 VSEALRYF 438
Cdd:TIGR01499 390 VGEVRKLL 397
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 54-331 3.97e-69

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 228.78  E-value: 3.97e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  54 VHVAGTKGKGSTSAMIATALTASGHRTGLYTSPHLHTIRERIQIDGSLISERAFAG----LVARLRPHIeyinrTCTLGE 129
Cdd:PLN02881   64 IHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRyfwwCWDRLKEKT-----TEDLPM 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 130 LTTFEILTAMAFSHFEERAVDFQVLETGLGGRLDATNVIR-PEVCVITSISLDHTEVLGDTIAQIAVEKAGIIKPGTPVV 208
Cdd:PLN02881  139 PAYFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQkPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAF 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 209 CAPQVPEAASVIEEvchdresrlirvghdvtwkktGASDLGQSFRVK---GTKGSYDLTVPLLGEHQLEN---------- 275
Cdd:PLN02881  219 TVPQPDEAMRVLEE---------------------RASELGVPLQVVeplDSYGLSGLKLGLAGEHQYLNaglavalcst 277

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490726398 276 -AAAAVAALEVLAEGTGITPDSIARGLAQVRWPGRLQVMRTRP---------LFVVDGAHNADSVE 331
Cdd:PLN02881  278 wLQRTGHEEFEALLQAGTLPEQFIKGLSTASLQGRAQVVPDSYinsedsgdlVFYLDGAHSPESME 343
PLN02913 PLN02913
dihydrofolate synthetase
 7-440 2.05e-67

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 223.54  E-value: 2.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398   7 MDFQGAVDYVLSFADYERL-------SRSAVVFDLARIEALLHRSGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHR 79
Cdd:PLN02913   24 PELGDFLRYLDSLKNYEKSgvpkdagTDSDDGFDLGRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  80 TGLYTSPHLHTIRERIQI--DGSLISERAFAGLVARLRPH----IEYINrtctlGELTTFEILTAMAFSHFEERAVDFQV 153
Cdd:PLN02913  104 VGCYTSPHLRSIRERISVgkLGKPVSTNTLNDLFHGIKPIldeaIQLEN-----GSLTHFEVLTALAFKLFAQENVDIAV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 154 LETGLGGRLDATNVIRPE---VCVITSISLDHTEVLGDTIAQIAVEKAGIIKPGTPVVCAPQVpeaASVIEEVCHDRESR 230
Cdd:PLN02913  179 IEAGLGGARDATNVIDSSglaASVITTIGEEHLAALGGSLESIALAKSGIIKQGRPVVLGGPF---LPHIESILRDKASS 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 231 lirvghdVTWKKTGASDLGQSFRVKGTKGS------------------------YDLTVPLLGEHQLENAAAAV-AALEV 285
Cdd:PLN02913  256 -------MNSPVVSASDPGVRSSIKGIITDngkpcqscdivirvekddplfielSDVNLRMLGSHQLQNAVTAAcAALCL 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 286 LAEGTGITPDSIARGLAQVRWPGRLQVMRTRPLFV---------VDGAHNADSVEKLKQSLRQSFAFDDSILIVGASRDK 356
Cdd:PLN02913  329 RDQGWRISDASIRAGLENTNLLGRSQFLTSKEAEVlglpgatvlLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDK 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 357 N----ITGIVAGLAPfsRRVIVTQSE----HPRAAEVSTLAQEFSK----WGIEALIARDTDS--AIRAALREAK----- 417
Cdd:PLN02913  409 DhlafASEFLSGLKP--EAVFLTEADiaggKSRSTSASALKEAWIKaapeLGIETLLAENNSLlkSLVDASAILRkartl 486

                         490       500
                  ....*....|....*....|....
gi 1490726398 418 -PTDLICVTGSLFVVSEALRYFGR 440
Cdd:PLN02913  487 dPSSVVCVTGSLHIVSAVLASLQG 510
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 23-435 2.18e-59

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 199.92  E-value: 2.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  23 ERLSRSAVVFDLARIEALLHRSGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGLYTSPHLHTIRERIQIDGSLI 102
Cdd:PRK10846   21 ENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 103 SE----RAFAGLVARlRPHIEyinrtctlgeLTTFEILTAMAFSHFEERAVDFQVLETGLGGRLDATNVIRPEVCVITSI 178
Cdd:PRK10846  101 PEsahtASFAEIEAA-RGDIS----------LTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 179 SLDHTEVLGDTIAQIAVEKAGIIKPGTP-VVCAPQVPeaaSVIEEVCHDRESRLIRVGHDVTWkktgaSDLGQSFRVKGT 257
Cdd:PRK10846  170 ALDHTDWLGPDRESIGREKAGIFRAEKPaVVGEPDMP---STIADVAQEKGALLQRRGVDWNY-----SVTDHDWAFSDG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 258 KGSY-DLTVPLLgehQLENaaAAVAALEVLAEGTGITPDSIARGLAQVRWPGRLQVMRTRPLFVVDGAHNADSVEKLKQS 336
Cdd:PRK10846  242 DGTLeNLPLPNV---PLPN--AATALAALRASGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPHAAEYLTGR 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 337 LRQSFAFDDSILIVGASRDKNITGIVAGLAPFSRRVIVTQSEHPRAAEVSTLAQEFSKWGIEAliarDTDSAIRAALREA 416
Cdd:PRK10846  317 LKALPKNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAEHLGNGKSFD----SVAQAWDAAMADA 392

                         410       420
                  ....*....|....*....|..
gi 1490726398 417 KPTDLICVTGSLFVVS---EAL 435
Cdd:PRK10846  393 KPEDTVLVCGSFHTVAhvmEVI 414
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 56-426 2.98e-22

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: 98.93  E-value: 2.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  56 VAGTKGKGSTSAMIATALTASGHRTGLytsphLHTIRERIqIDGSLISERAfaglvarlrphieyinrtctlgELTTFEI 135
Cdd:TIGR01085  90 VTGTNGKTTTTSLIAQLLRLLGKKTGL-----IGTIGYRL-GGNDLIKNPA----------------------ALTTPEA 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 136 LTAMA-FSHFEERAVDFQVLET---GLG-GRLDATNVirpEVCVITSISLDHTEVLGdTIAQIAVEKAGIIK----PGTP 206
Cdd:TIGR01085 142 LTLQStLAEMVEAGAQYAVMEVsshALAqGRVRGVRF---DAAVFTNLSRDHLDFHG-TMENYFAAKASLFTelglKRFA 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 207 VVCAPQvPEAASVIEEVCHDRESRLIRVGHDvtWKKT-------GASDLGQSFRVKGTKGSYDLTVPLLGEHQLENAAAA 279
Cdd:TIGR01085 218 VINLDD-EYGAQFVKRLPKDITVSAITQPAD--GRAQdikitdsGYSFEGQQFTFETPAGEGHLHTPLIGRFNVYNLLAA 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 280 VAALEVLaegTGITPDSIARGLAQVRW-PGRLQV--MRTRPLFVVDGAHNADSVEKLKQSLRqsfAFDDSILIV----GA 352
Cdd:TIGR01085 295 LATLLHL---GGIDLEDIVAALEKFRGvPGRMELvdGGQKFLVIVDYAHTPDALEKALRTLR---KHKDGRLIVvfgcGG 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 353 SRDKN---ITGIVAglAPFSRRVIVTqSEHPRAAEVSTLAQEFSKwGI----EALIARDTDSAIRAALREAKPTDLICVT 425
Cdd:TIGR01085 369 DRDRGkrpLMGAIA--EQLADLVILT-SDNPRGEDPEQIIADILA-GIsekeKVVIIADRRQAIRYAISNAKAGDVVLIA 444


                  .
gi 1490726398 426 G 426
Cdd:TIGR01085 445 G 445
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 34-426 4.60e-20

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: 92.06  E-value: 4.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  34 LARIEALLHrsGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGLytsphLHTIRerIQIDGSLISerafaglvar 113
Cdd:COG0769    65 LALLAAAFY--GHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGL-----IGTVG--NGIGGELIP---------- 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 114 lrphieyinrtctlGELTTFEILTAMA-FSHFEERAVDFQVLET---GLG-GRLDAtnvIRPEVCVITSISLDHtevLgD 188
Cdd:COG0769   126 --------------SSLTTPEALDLQRlLAEMVDAGVTHVVMEVsshALDqGRVDG---VRFDVAVFTNLTRDH---L-D 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 189 ---TIAQIAVEKAGII----KPGTPVVCApQVPEAASVIEEVchdrESRLIRVG----HDVTWKKTGASDLGQSFRVKGT 257
Cdd:COG0769   185 yhgTMEAYFAAKARLFdqlgPGGAAVINA-DDPYGRRLAAAA----PARVITYGlkadADLRATDIELSADGTRFTLVTP 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 258 KGSYDLTVPLLGEHQLENaaaaVAALEVLAEGTGITPDSIARGLAQVRW-PGRLQVMRT--RPLFVVDGAHNADSVEKLK 334
Cdd:COG0769   260 GGEVEVRLPLIGRFNVYN----ALAAIAAALALGIDLEEILAALEKLKGvPGRMERVDGgqGPTVIVDYAHTPDALENVL 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 335 QSLRQsFAFDDSILIVGAS--RDKN----ITGIVAGLAPfsrRVIVTqSEHPR----AAEVSTLAQEFSKwGIEALIARD 404
Cdd:COG0769   336 EALRP-HTKGRLIVVFGCGgdRDRGkrplMGEIAARLAD---VVIVT-SDNPRsedpAAIIADILAGIPG-AGKVLVIPD 409

                         410       420
                  ....*....|....*....|..
gi 1490726398 405 TDSAIRAALREAKPTDLICVTG 426
Cdd:COG0769   410 RAEAIRYAIALAKPGDVVLIAG 431
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 45-426 3.29e-19

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: 90.53  E-value: 3.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  45 GDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGlytsphlhTIreriqidgsliserafAGLVARLRPHIEYINRT 124
Cdd:PRK11929  106 GRPSEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCG--------SI----------------GTLGARLDGRLIPGSLT 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 125 cTLGELTTFEILTAMAfshfeERAVDFQVLET---GLG-GRLDAtnvIRPEVCVITSISLDHTEVLGdTIAQIAVEKAGI 200
Cdd:PRK11929  162 -TPDAIILHRILARMR-----AAGADAVAMEAsshGLEqGRLDG---LRIAVAGFTNLTRDHLDYHG-TMQDYEEAKAAL 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 201 ---IKPGTPVVCAPQVPEAASVIEEVCH--DRESRLIRVGHDVTWKKTGASDLGQSFRVKGTKGSYDLTVPLLGEHQLEN 275
Cdd:PRK11929  232 fskLPGLGAAVINADDPAAARLLAALPRglKVGYSPQNAGADVQARDLRATAHGQVFTLATPDGSYQLVTRLLGRFNVSN 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 276 aaaaVAALEVLAEGTGITPDSIARGLAQVR-WPGRLQVM-----RTRPLFVVDGAHNADSVEKLKQSLRQSFAFDDSILI 349
Cdd:PRK11929  312 ----LLLVAAALKKLGLPLAQIARALAAVSpVPGRMERVgptagAQGPLVVVDYAHTPDALAKALTALRPVAQARNGRLV 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 350 V----GASRDKN---ITGIVAglAPFSRRVIVTqSEHPRAAEVSTLAQEFSKwGIEA----LIARDTDSAIRAALREAKP 418
Cdd:PRK11929  388 CvfgcGGDRDKGkrpEMGRIA--AELADRVVVT-SDNPRSEAPEAIIDQILA-GIPAgarvFVISDRAEAIRQAIWMAAP 463


                  ....*...
gi 1490726398 419 TDLICVTG 426
Cdd:PRK11929  464 GDVILIAG 471
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 10-426 2.39e-16

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 80.95  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  10 QGAVDYVLSFADYERLSRSAVVFD-----LARIEALLHrsGDPHLAARAVHVAGTKGKGSTSAMIATALTASGHRTGLyt 84
Cdd:PRK00139   51 NGAAAVVAEADGEAGTGVPVIIVPdlrkaLALLAAAFY--GHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTAL-- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  85 sphLHTIRerIQIDGSLISerafaglvarlrphieyinrtctlGELTTFEILTAMA-FSHFEERAVDFQVLET---GLG- 159
Cdd:PRK00139  127 ---IGTLG--NGIGGELIP------------------------SGLTTPDALDLQRlLAELVDAGVTYAAMEVsshALDq 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 160 GRLDATNVirpEVCVITSISLDHtevLG--DTIAQIAVEKAGIIKPGTP--VVCA-----PQVPEAASVIEEVCHDRESR 230
Cdd:PRK00139  178 GRVDGLKF---DVAVFTNLSRDH---LDyhGTMEDYLAAKARLFSELGLaaVINAddevgRRLLALPDAYAVSMAGADLR 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 231 LIRVGHDVTwkktgasdlGQSFRVkgtkgSYDLTVPLLGEHQLENAAAAVAALEVlaegTGITPDSIARGLAQVRW-PGR 309
Cdd:PRK00139  252 ATDVEYTDS---------GQTFTL-----VTEVESPLIGRFNVSNLLAALAALLA----LGVPLEDALAALAKLQGvPGR 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 310 LQVMRTR--PLFVVDGAHNADSVEKLKQSLRQsFAFDDSILIVGAS--RDKN---ITGIVAglAPFSRRVIVTqSEHPR- 381
Cdd:PRK00139  314 MERVDAGqgPLVIVDYAHTPDALEKVLEALRP-HAKGRLICVFGCGgdRDKGkrpLMGAIA--ERLADVVIVT-SDNPRs 389

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1490726398 382 ------AAEVstLAqefskwGIEALIArDTDSAIRAALREAKPTDLICVTG 426
Cdd:PRK00139  390 edpaaiIADI--LA------GIYDVIE-DRAEAIRYAIAQAKPGDVVLIAG 431
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 165-436 1.47e-12

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: 68.98  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 165 TNVIRPEVCVITSISLDHTEVLGdTIAQIAVEKAGII----KPGTPVVCA--PQVPEAASVIEevchdreSRLIRVG--- 235
Cdd:COG0770   171 ARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIFeglpPGGVAVLNAddPLLAALAERAK-------ARVLTFGlse 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 236 -HDVTWKKTGASDLGQSFRVKGTKGSYDLTVPLLGEHQLENAAAAVAALEVLaegtGITPDSIARGLAQVR-WPGRLQVM 313
Cdd:COG0770   243 dADVRAEDIELDEDGTRFTLHTPGGELEVTLPLPGRHNVSNALAAAAVALAL----GLDLEEIAAGLAAFQpVKGRLEVI 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 314 RTRP-LFVVDGAHNA--DSVEKLKQSLRQSFAFDDSILIVGAsrdknitgiVAGLAPFSRRvivtqsEHpraAEVSTLAQ 390
Cdd:COG0770   319 EGAGgVTLIDDSYNAnpDSMKAALDVLAQLPGGGRRIAVLGD---------MLELGEESEE------LH---REVGELAA 380

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 391 EFskwGIEALIA--------------------RDTDSAIRAALREAKPTDLICVTGSLFV----VSEALR 436
Cdd:COG0770   381 EL---GIDRLFTvgelaraiaeaaggeraehfEDKEELLAALKALLRPGDVVLVKGSRGMglerVVEALK 447
Mur_ligase_M pfam08245
Mur ligase middle domain;
56-275 3.26e-10

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 59.24  E-value: 3.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398  56 VAGTKGKGSTSAMIATALTASGHRTGlytsphlhTIreriqidGSLISErafaglvarlrphieyinrtctlGELTTFEI 135
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIG--------TI-------GTYIGK-----------------------SGNTTNNA 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 136 LT-AMAFSHFEERAVDFQVLET---GLG-GRLDATnvIRPEVCVITSISLDHTEVLGdTIAQIAVEKAGIIK----PGTP 206
Cdd:pfam08245  43 IGlPLTLAEMVEAGAEYAVLEVsshGLGeGRLSGL--LKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEglpeDGIA 119

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490726398 207 VV-----CAPQVPEAASVieevchdRESRLIRVG----HDVTWKKTGASDLGQSFRVKGTK-GSYDLTVPLLGEHQLEN 275
Cdd:pfam08245 120 VInaddpYGAFLIAKLKK-------AGVRVITYGiegeADLRAANIELSSDGTSFDLFTVPgGELEIEIPLLGRHNVYN 191
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
251-426 2.97e-09

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


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 58.90  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 251 SFRVKGT-KGSYDLTvpLLGEHQLENAAAAVAALEvlaeGTGITPDSIARGLAQVRWPGRLQVMrTRPL---FVVDGAHN 326
Cdd:PRK14022  277 SFEATGKlAGTYDIQ--LIGKFNQENAMAAGLACL----RLGASLEDIQKGIAQTPVPGRMEVL-TQSNgakVFIDYAHN 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 327 ADSVEKLKQSLrQSFAFDDSILIVGASRDKNIT-----GIVAGLAPFSrRVIVTqSEHPRAAEVSTLAQEfskwgIEALI 401
Cdd:PRK14022  350 GDSLNKLIDVV-EEHQKGKLILLLGAAGNKGESrrpdfGRVANRHPYL-QVILT-ADDPNNEDPKMITQE-----IASHI 421

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1490726398 402 AR------DTDSAIRAALREA-KPTDLICVTG 426
Cdd:PRK14022  422 THpveiidDRAEAIKHAMSITeGPGDAVIIAG 453
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 306-384 5.19e-08

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: 50.04  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 306 WPGRLQVMRT--RPLFVVDGAHNADSVEKLKQSLRQSFAFdDSILIVGASRDKNIT--GIVAGLAPFSRRVIVTQSEHPR 381
Cdd:pfam02875   1 VPGRLEVVGEnnGVLVIDDYAHNPDAMEAALRALRNLFPG-RLILVFGGMGDRDAEfhALLGRLAAALADVVILTGDYPR 79


                  ...
gi 1490726398 382 AAE 384
Cdd:pfam02875  80 AED 82
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 150-332 1.85e-07

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: 53.55  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 150 DFQVLETGLGG-----RLDAtnVIRPEVCVITSISLDHTEVLGDtIAQIAVEKAGII----KPGTPVVCA--PQVPEAAS 218
Cdd:PRK11929  659 RAAVFELGMNHpgeiaYLAA--IAAPTVALVTNAQREHQEFMHS-VEAVARAKGEIIaalpEDGVAVVNGddPYTAIWAK 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726398 219 VIE--EVCHDRESRLIRVGHDVTWKKTGASDLGQ-SFRVKGTKGSYDLTVPLLGEHQLENAAAAVAALEVLaegtGITPD 295
Cdd:PRK11929  736 LAGarRVLRFGLQPGADVYAEKIAKDISVGEAGGtRCQVVTPAGSAEVYLPLIGEHNLRNALAAIACALAA----GASLK 811

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1490726398 296 SIARGLAQVRWP-GRLQVMRT-RPLFVVDGAHNA--DSVEK 332
Cdd:PRK11929  812 QIRAGLERFQPVaGRMQRRRLsCGTRIIDDTYNAnpDSMRA 852
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH