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Conserved domains on  [gi|545668916|ref|WP_021775232|]
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folylpolyglutamate synthase/dihydrofolate synthase family protein [Streptococcus pyogenes]

Protein Classification

folylpolyglutamate synthase/dihydrofolate synthase family protein( domain architecture ID 11492710)

folylpolyglutamate synthase/dihydrofolate synthase family protein similar to Saccharomyces cerevisiae folylpolyglutamate synthase that catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis

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

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List of domain hits

 Name Accession Description Interval E-value
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 22-413 1.20e-165

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: 471.00  E-value: 1.20e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916   22 LKRMLWVLGQLGNPQKNVKGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKERISINGRMISEKDLVIAANR 101
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  102 IRPLTERLVQetdfgEVTEFEVITLIMFLYFGDmHPVDIAIIEAGLGGLYDSTNVFQAMVVVCPSIGLDHQAILGETYAD 181
Cdd:TIGR01499  81 VRPILESLSQ-----QPTYFELLTLLAFLYFAQ-AQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  182 IAAQKAGVLEGGETLVFAVENPSAREVFLTKAEQVGASIWEWQEQFQMAENASGY-RFTSPLGVISDIHIAMPGHHQVSN 260
Cdd:TIGR01499 155 IAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENYlSFSGANLFLEPLALSLLGDHQQEN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  261 AALAIMTCLTLQDRYPRLTPDHIREGLANSLWLGRTELLA---PNLMIDGAHNNESVAALVAVLKNNYNDKKLHILFGAI 337
Cdd:TIGR01499 235 AALALAALEVLGKQNPKLSEEAIRQGLANTIWPGRLEILSednPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFGAL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  338 DTKPIVDMLVALEQI--GDLQVTSFHYPNAYPLEKYPER-----FGRVADFKDFLALRKHAKADDFFVITGSLYFISEIR 410
Cdd:TIGR01499 315 ADKDAAAMLAPLKPVvdKEVFVTPFDYPRADDAADLAAFaeetgKSTVEDWREALEEALNASAEDDILVTGSLYLVGEVR 394


                  ...
gi 545668916  411 RYW 413
Cdd:TIGR01499 395 KLL 397
 
Name Accession Description Interval E-value
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 22-413 1.20e-165

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: 471.00  E-value: 1.20e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916   22 LKRMLWVLGQLGNPQKNVKGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKERISINGRMISEKDLVIAANR 101
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  102 IRPLTERLVQetdfgEVTEFEVITLIMFLYFGDmHPVDIAIIEAGLGGLYDSTNVFQAMVVVCPSIGLDHQAILGETYAD 181
Cdd:TIGR01499  81 VRPILESLSQ-----QPTYFELLTLLAFLYFAQ-AQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  182 IAAQKAGVLEGGETLVFAVENPSAREVFLTKAEQVGASIWEWQEQFQMAENASGY-RFTSPLGVISDIHIAMPGHHQVSN 260
Cdd:TIGR01499 155 IAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENYlSFSGANLFLEPLALSLLGDHQQEN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  261 AALAIMTCLTLQDRYPRLTPDHIREGLANSLWLGRTELLA---PNLMIDGAHNNESVAALVAVLKNNYNDKKLHILFGAI 337
Cdd:TIGR01499 235 AALALAALEVLGKQNPKLSEEAIRQGLANTIWPGRLEILSednPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFGAL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  338 DTKPIVDMLVALEQI--GDLQVTSFHYPNAYPLEKYPER-----FGRVADFKDFLALRKHAKADDFFVITGSLYFISEIR 410
Cdd:TIGR01499 315 ADKDAAAMLAPLKPVvdKEVFVTPFDYPRADDAADLAAFaeetgKSTVEDWREALEEALNASAEDDILVTGSLYLVGEVR 394


                  ...
gi 545668916  411 RYW 413
Cdd:TIGR01499 395 KLL 397
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 2-415 1.30e-163

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: 466.50  E-value: 1.30e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916   2 TYEETLEWIHDHLVFGIKPGLKRMLWVLGQLGNPQKNVKGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKE 81
Cdd:COG0285    3 TYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  82 RISINGRMISEKDLVIAANRIRPlterLVQETDFGEVTEFEVITLIMFLYFGDmHPVDIAIIEAGLGGLYDSTNVFQAMV 161
Cdd:COG0285   83 RIRINGEPISDEELVEALEEVEP----AVEEVDAGPPTFFEVTTAAAFLYFAE-APVDVAVLEVGLGGRLDATNVIDPLV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 162 VVCPSIGLDHQAILGETYADIAAQKAGVLEGGETLVFAVENPSAREVFLTKAEQVGASIWEWQEQFQMAENASGY-RFTS 240
Cdd:COG0285  158 SVITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEEREGAVfSYQG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 241 PLGVISDIHIAMPGHHQVSNAALAIMTCLTLQDRYPRLTPDHIREGLANSLWLGRTELL--APNLMIDGAHNNESVAALV 318
Cdd:COG0285  238 PGGEYEDLPLPLLGAHQAENAALALAALEALRELGLPISEEAIREGLANARWPGRLEVLsrGPLVILDGAHNPAGARALA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 319 AVLKNNYNDKKLHILFGAIDTKPIVDMLVALEQIGD-LQVTSFHYPNAYPLEKYPERFGRV-------ADFKDFL-ALRK 389
Cdd:COG0285  318 ETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADeVIVTTPPSPRALDAEELAEAARELglrvevaPDVEEALeAALE 397

                        410       420
                 ....*....|....*....|....*.
gi 545668916 390 HAKADDFFVITGSLYFISEIRRYWKK 415
Cdd:COG0285  398 LADPDDLILVTGSLYLVGEVRALLGR 423
PLN02913 PLN02913
dihydrofolate synthetase
 22-330 2.75e-59

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 201.59  E-value: 2.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  22 LKRMLWVLGQLGNPQKNVKGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKERISIN--GRMISEKDLVIAA 99
Cdd:PLN02913  58 LGRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVGklGKPVSTNTLNDLF 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 100 NRIRPLTERLVQETDfGEVTEFEVITLIMFLYFGDmHPVDIAIIEAGLGGLYDSTNVFQ-----AMVVVcpSIGLDHQAI 174
Cdd:PLN02913 138 HGIKPILDEAIQLEN-GSLTHFEVLTALAFKLFAQ-ENVDIAVIEAGLGGARDATNVIDssglaASVIT--TIGEEHLAA 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 175 LGETYADIAAQKAGVLEGGETLVFAVE-NPSAREVFLTKAEQVGAS----------------IWEWQEQFQMAENASGYR 237
Cdd:PLN02913 214 LGGSLESIALAKSGIIKQGRPVVLGGPfLPHIESILRDKASSMNSPvvsasdpgvrssikgiITDNGKPCQSCDIVIRVE 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 238 FTSPLGV-ISDIHIAMPGHHQVSNAALAIMTCLTLQDRYPRLTPDHIREGLANSLWLGRTELLAP-----------NLMI 305
Cdd:PLN02913 294 KDDPLFIeLSDVNLRMLGSHQLQNAVTAACAALCLRDQGWRISDASIRAGLENTNLLGRSQFLTSkeaevlglpgaTVLL 373

                        330       340
                 ....*....|....*....|....*
gi 545668916 306 DGAHNNESVAALVAVLKNNYNDKKL 330
Cdd:PLN02913 374 DGAHTKESAKALVDTIKTAFPEARL 398
Mur_ligase_M pfam08245
Mur ligase middle domain;
44-265 4.11e-05

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 44.22  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916   44 IVGTNGKGSTVNHLQHIFTTAGYEVGTftspyimdfkerisiNGRMISEKDLviaanrirplterlvqetdfgevTEFEV 123
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIGT---------------IGTYIGKSGN-----------------------TTNNA 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  124 ITLIMFLYFGDMHPVDIAIIEAGLGGLYDS--TNVFQAMVVVCPSIGLDHQAILGeTYADIAAQKAGVLEG---GETLVF 198
Cdd:pfam08245  43 IGLPLTLAEMVEAGAEYAVLEVSSHGLGEGrlSGLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGlpeDGIAVI 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545668916  199 AVENPSAREvFLTKAEQVGASIWE-------WQEQFQMAENASGYRFT--SPLGVISDIHIAMPGHHQVSNAALAI 265
Cdd:pfam08245 122 NADDPYGAF-LIAKLKKAGVRVITygiegeaDLRAANIELSSDGTSFDlfTVPGGELEIEIPLLGRHNVYNALAAI 196
 
Name Accession Description Interval E-value
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 22-413 1.20e-165

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: 471.00  E-value: 1.20e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916   22 LKRMLWVLGQLGNPQKNVKGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKERISINGRMISEKDLVIAANR 101
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  102 IRPLTERLVQetdfgEVTEFEVITLIMFLYFGDmHPVDIAIIEAGLGGLYDSTNVFQAMVVVCPSIGLDHQAILGETYAD 181
Cdd:TIGR01499  81 VRPILESLSQ-----QPTYFELLTLLAFLYFAQ-AQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  182 IAAQKAGVLEGGETLVFAVENPSAREVFLTKAEQVGASIWEWQEQFQMAENASGY-RFTSPLGVISDIHIAMPGHHQVSN 260
Cdd:TIGR01499 155 IAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDENYlSFSGANLFLEPLALSLLGDHQQEN 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  261 AALAIMTCLTLQDRYPRLTPDHIREGLANSLWLGRTELLA---PNLMIDGAHNNESVAALVAVLKNNYNDKKLHILFGAI 337
Cdd:TIGR01499 235 AALALAALEVLGKQNPKLSEEAIRQGLANTIWPGRLEILSednPNILLDGAHNPHSAEALAEWFKKRFNGRPITLLFGAL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  338 DTKPIVDMLVALEQI--GDLQVTSFHYPNAYPLEKYPER-----FGRVADFKDFLALRKHAKADDFFVITGSLYFISEIR 410
Cdd:TIGR01499 315 ADKDAAAMLAPLKPVvdKEVFVTPFDYPRADDAADLAAFaeetgKSTVEDWREALEEALNASAEDDILVTGSLYLVGEVR 394


                  ...
gi 545668916  411 RYW 413
Cdd:TIGR01499 395 KLL 397
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 2-415 1.30e-163

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: 466.50  E-value: 1.30e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916   2 TYEETLEWIHDHLVFGIKPGLKRMLWVLGQLGNPQKNVKGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKE 81
Cdd:COG0285    3 TYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  82 RISINGRMISEKDLVIAANRIRPlterLVQETDFGEVTEFEVITLIMFLYFGDmHPVDIAIIEAGLGGLYDSTNVFQAMV 161
Cdd:COG0285   83 RIRINGEPISDEELVEALEEVEP----AVEEVDAGPPTFFEVTTAAAFLYFAE-APVDVAVLEVGLGGRLDATNVIDPLV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 162 VVCPSIGLDHQAILGETYADIAAQKAGVLEGGETLVFAVENPSAREVFLTKAEQVGASIWEWQEQFQMAENASGY-RFTS 240
Cdd:COG0285  158 SVITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEEREGAVfSYQG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 241 PLGVISDIHIAMPGHHQVSNAALAIMTCLTLQDRYPRLTPDHIREGLANSLWLGRTELL--APNLMIDGAHNNESVAALV 318
Cdd:COG0285  238 PGGEYEDLPLPLLGAHQAENAALALAALEALRELGLPISEEAIREGLANARWPGRLEVLsrGPLVILDGAHNPAGARALA 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 319 AVLKNNYNDKKLHILFGAIDTKPIVDMLVALEQIGD-LQVTSFHYPNAYPLEKYPERFGRV-------ADFKDFL-ALRK 389
Cdd:COG0285  318 ETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADeVIVTTPPSPRALDAEELAEAARELglrvevaPDVEEALeAALE 397

                        410       420
                 ....*....|....*....|....*.
gi 545668916 390 HAKADDFFVITGSLYFISEIRRYWKK 415
Cdd:COG0285  398 LADPDDLILVTGSLYLVGEVRALLGR 423
PLN02913 PLN02913
dihydrofolate synthetase
 22-330 2.75e-59

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 201.59  E-value: 2.75e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  22 LKRMLWVLGQLGNPQKNVKGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKERISIN--GRMISEKDLVIAA 99
Cdd:PLN02913  58 LGRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVGklGKPVSTNTLNDLF 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 100 NRIRPLTERLVQETDfGEVTEFEVITLIMFLYFGDmHPVDIAIIEAGLGGLYDSTNVFQ-----AMVVVcpSIGLDHQAI 174
Cdd:PLN02913 138 HGIKPILDEAIQLEN-GSLTHFEVLTALAFKLFAQ-ENVDIAVIEAGLGGARDATNVIDssglaASVIT--TIGEEHLAA 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 175 LGETYADIAAQKAGVLEGGETLVFAVE-NPSAREVFLTKAEQVGAS----------------IWEWQEQFQMAENASGYR 237
Cdd:PLN02913 214 LGGSLESIALAKSGIIKQGRPVVLGGPfLPHIESILRDKASSMNSPvvsasdpgvrssikgiITDNGKPCQSCDIVIRVE 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 238 FTSPLGV-ISDIHIAMPGHHQVSNAALAIMTCLTLQDRYPRLTPDHIREGLANSLWLGRTELLAP-----------NLMI 305
Cdd:PLN02913 294 KDDPLFIeLSDVNLRMLGSHQLQNAVTAACAALCLRDQGWRISDASIRAGLENTNLLGRSQFLTSkeaevlglpgaTVLL 373

                        330       340
                 ....*....|....*....|....*
gi 545668916 306 DGAHNNESVAALVAVLKNNYNDKKL 330
Cdd:PLN02913 374 DGAHTKESAKALVDTIKTAFPEARL 398
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 40-316 7.04e-44

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 160.60  E-value: 7.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  40 KGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKERISINGRMISEKDLVI----AANRIRpltERLvqETDF 115
Cdd:PLN02881  62 KVIHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRyfwwCWDRLK---EKT--TEDL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 116 GEVTEFEVITLIMFLYFGDmHPVDIAIIEAGLGGLYDSTNVFQAmVVVC--PSIGLDHQAILGETYADIAAQKAGVLEGG 193
Cdd:PLN02881 137 PMPAYFRFLTLLAFKIFSA-EQVDVAILEVGLGGRLDATNVVQK-PVVCgiTSLGYDHMEILGDTLGKIAGEKAGIFKPG 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 194 eTLVFAVENPS-AREVFLTKAEQVGASIwewqeqfQMAEnasgyrftsPL--GVISDIHIAMPGHHQVSNAALAIMTCLT 270
Cdd:PLN02881 215 -VPAFTVPQPDeAMRVLEERASELGVPL-------QVVE---------PLdsYGLSGLKLGLAGEHQYLNAGLAVALCST 277

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545668916 271 LQDRYPRLT----------PDHIREGLANSLWLGRTEL---------LAPNLM--IDGAHNNESVAA 316
Cdd:PLN02881 278 WLQRTGHEEfeallqagtlPEQFIKGLSTASLQGRAQVvpdsyinseDSGDLVfyLDGAHSPESMEA 344
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 18-404 1.40e-31

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 124.42  E-value: 1.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  18 IKPGLKRMLWVLGQLGNPQKNVKGVHIVGTNGKGSTVNHLQHIFTTAGYEVGTFTSPYIMDFKERISINGRMISEKDLVI 97
Cdd:PRK10846  28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  98 AANRIrplterlvqETDFGEV--TEFEVITLIMFLYFGDMHpVDIAIIEAGLGGLYDSTNVFQAMVVVCPSIGLDHQAIL 175
Cdd:PRK10846 108 SFAEI---------EAARGDIslTYFEYGTLSALWLFKQAQ-LDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 176 GETYADIAAQKAGVLEGGETLVfaVENPSAREVFLTKAEQVGASI------WEWQEQfqmaenASGYRFTSPLGVISDIH 249
Cdd:PRK10846 178 GPDRESIGREKAGIFRAEKPAV--VGEPDMPSTIADVAQEKGALLqrrgvdWNYSVT------DHDWAFSDGDGTLENLP 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 250 I-AMPghhqVSNA--ALAIMTCLTLQdryprLTPDHIREGLANSLWLGRTELL--APNLMIDGAHNNESVAALVAVLKNN 324
Cdd:PRK10846 250 LpNVP----LPNAatALAALRASGLE-----VSEQAIRDGIASAILPGRFQIVseSPRVILDVAHNPHAAEYLTGRLKAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 325 YNDKKLHILFGAIDTKPIVDMLVAL-EQIGDLQVTSFHYPNAYPLEKYPERFGRVADFKDFLALRKHAKAD----DFFVI 399
Cdd:PRK10846 321 PKNGRVLAVIGMLHDKDIAGTLACLkSVVDDWYCAPLEGPRGATAEQLAEHLGNGKSFDSVAQAWDAAMADakpeDTVLV 400


                 ....*
gi 545668916 400 TGSLY 404
Cdd:PRK10846 401 CGSFH 405
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 233-336 1.92e-06

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: 49.69  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 233 ASGYRFT--SPLGVIsDIHIAMPGHHQVSNAALAIMTCLTLQdryprLTPDHIREGLANslwL----GRTELLA----PN 302
Cdd:COG0769  249 ADGTRFTlvTPGGEV-EVRLPLIGRFNVYNALAAIAAALALG-----IDLEEILAALEK---LkgvpGRMERVDggqgPT 319

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 545668916 303 LMIDGAHNnesVAALVAVLK--NNYNDKKLHILFGA 336
Cdd:COG0769  320 VIVDYAHT---PDALENVLEalRPHTKGRLIVVFGC 352
Mur_ligase_M pfam08245
Mur ligase middle domain;
44-265 4.11e-05

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 44.22  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916   44 IVGTNGKGSTVNHLQHIFTTAGYEVGTftspyimdfkerisiNGRMISEKDLviaanrirplterlvqetdfgevTEFEV 123
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIGT---------------IGTYIGKSGN-----------------------TTNNA 42

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  124 ITLIMFLYFGDMHPVDIAIIEAGLGGLYDS--TNVFQAMVVVCPSIGLDHQAILGeTYADIAAQKAGVLEG---GETLVF 198
Cdd:pfam08245  43 IGLPLTLAEMVEAGAEYAVLEVSSHGLGEGrlSGLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELFEGlpeDGIAVI 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545668916  199 AVENPSAREvFLTKAEQVGASIWE-------WQEQFQMAENASGYRFT--SPLGVISDIHIAMPGHHQVSNAALAI 265
Cdd:pfam08245 122 NADDPYGAF-LIAKLKKAGVRVITygiegeaDLRAANIELSSDGTSFDlfTVPGGELEIEIPLLGRHNVYNALAAI 196
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
 157-289 7.61e-05

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: 44.67  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 157 FQAMVVVCPSIGLDHQailgETYADIAAQK------AGVLEGGETLVFAVENPSAREVfltkAEQVGASIW--------E 222
Cdd:COG0773  170 YSPDIAVVTNIEADHL----DIYGDLEAIKeafhefARNVPFYGLLVLCADDPGLREL----LPRCGRPVItygfsedaD 241

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545668916 223 WQ-EQFQMAENASGYRFTSPLGVISDIHIAMPGHHQVSNAALAIMTCLTLQdryprLTPDHIREGLAN 289
Cdd:COG0773  242 YRaENIRIDGGGSTFDVLRRGEELGEVELNLPGRHNVLNALAAIAVALELG-----VDPEAIAEALAS 304
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 232-336 1.53e-04

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 43.97  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 232 NASGYRFTsplgVISDIHIAMPGHHQVSNAALAIMTCLTLQdryprLTPDHIREGLANslwL----GRTELLA----PNL 303
Cdd:PRK00139 258 TDSGQTFT----LVTEVESPLIGRFNVSNLLAALAALLALG-----VPLEDALAALAK---LqgvpGRMERVDagqgPLV 325

                         90       100       110
                 ....*....|....*....|....*....|...
gi 545668916 304 MIDGAHNNESVAALVAVLKNNYNdKKLHILFGA 336
Cdd:PRK00139 326 IVDYAHTPDALEKVLEALRPHAK-GRLICVFGC 357
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 42-288 2.13e-04

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 43.61  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916  42 VHIVGTNGKGSTVNHLQHIFTTAGYEVGtFTSpyimdfKERISINGRMISEKDlviAANrirPLTERLVqetdfgevtef 121
Cdd:PRK14016 483 VAVTGTNGKTTTTRLIAHILKLSGKRVG-MTT------TDGVYIDGRLIDKGD---CTG---PKSARRV----------- 538

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 122 evitLimflyfgdMHP-VDIAIIEAGLGGL------YDStnvfqAMVVVCPSIGLDHQAILG-ETYADIAAQKAGVLE-- 191
Cdd:PRK14016 539 ----L--------MNPdVEAAVLETARGGIlreglaYDR-----CDVGVVTNIGEDHLGLGGiNTLEDLAKVKRVVVEav 601

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 192 ---G-------------------GETLVFAV--ENPsareVFLTKAEQVGASIWEWQEQFQMAENAsgyrFTSPLGVISD 247
Cdd:PRK14016 602 kpdGyavlnaddpmvaamaerckGKVIFFSMdpDNP----VIAEHRAQGGRAVYVEGDYIVLAEGG----WEIRIISLAD 673

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 545668916 248 IHIAMPGH--HQVSNAALAIMTCLTLQdryprLTPDHIREGLA 288
Cdd:PRK14016 674 IPLTLGGKagFNIENALAAIAAAWALG-----IDIELIRAGLR 711
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 139-323 2.76e-04

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: 43.17  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 139 DIAIIEAG---LGGLYDSTNVFQAMVVVCPSIGLDHQAILGeTYADIAAQKAGVLEG---GETLVFAVENPSAREvfltK 212
Cdd:COG0770  153 EFAVLEMGmnhPGEIAYLARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIFEGlppGGVAVLNADDPLLAA----L 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 213 AEQVGASIWEW---------QEQFQMAENASGYRFTSPLGVIsDIHIAMPGHHQVSNAALAIMTCLTLQdryprLTPDHI 283
Cdd:COG0770  228 AERAKARVLTFglsedadvrAEDIELDEDGTRFTLHTPGGEL-EVTLPLPGRHNVSNALAAAAVALALG-----LDLEEI 301

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 545668916 284 REGLANslwL----GRTELL---APNLMIDGAHNN--ESVAALVAVLKN 323
Cdd:COG0770  302 AAGLAA---FqpvkGRLEVIegaGGVTLIDDSYNAnpDSMKAALDVLAQ 347
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
231-336 3.18e-04

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


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 42.72  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545668916 231 ENASGYRFTSPLGVISDIHIAMPGHHQVSNAALAIMTCLT----LQDryprltpdhIREGLANSLWLGRTELLAPN---- 302
Cdd:PRK14022 271 MASNAFSFEATGKLAGTYDIQLIGKFNQENAMAAGLACLRlgasLED---------IQKGIAQTPVPGRMEVLTQSngak 341

                         90       100       110
                 ....*....|....*....|....*....|....
gi 545668916 303 LMIDGAHNNESVAALVAVLKnNYNDKKLHILFGA 336
Cdd:PRK14022 342 VFIDYAHNGDSLNKLIDVVE-EHQKGKLILLLGA 374
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 294-365 2.52e-03

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: 36.94  E-value: 2.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545668916  294 GRTELL----APNLMIDGAHNNESVAALVAVLKnNYNDKKLHILFGAIDTKP---IVDMLVALEQIGDLQVTSFHYPNA 365
Cdd:pfam02875   3 GRLEVVgennGVLVIDDYAHNPDAMEAALRALR-NLFPGRLILVFGGMGDRDaefHALLGRLAAALADVVILTGDYPRA 80
 
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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