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Conserved domains on  [gi|6324815|ref|NP_014884|]
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tetrahydrofolate synthase [Saccharomyces cerevisiae S288C]

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

Graphical summary

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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 ...
100-542 9.28e-138

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: 404.74  E-value: 9.28e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    100 LLEMHEWSRRIGYSAsdfNKLNIVHITGTKGKGSTAAFTSSILgqyKEQLPRIGLYTSPHLKSVRERIRINGEPISEEKF 179
Cdd:TIGR01499   1 LERMKKLLEALGNPQ---DLYPVIHVAGTNGKGSTCAFLESIL---RAAGYKVGLFTSPHLVSFNERIRINGEPISDEEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    180 AKYFFEVWDRLDSTTssldkfphmipgSKPGYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIEkPIVCGVTLLG 259
Cdd:TIGR01499  75 AQAFEQVRPILESLS------------QQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIE-PLVSVITSIG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    260 IDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVEkQPPQGLTILKERAEERKTTLTEVPP---FKQLENVKLGIAGEFQKSN 336
Cdd:TIGR01499 142 LDHTEILGDTLEEIAWEKAGIIKEGVPIVTGE-QEPEALNVLKKKAQEKGAPLFVVGRdfnYSETDENYLSFSGANLFLE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    337 ASLAVMLASEILHTSNILEEKIKCSSNAS---IPEKFIIGLQNTKWEGRCQVL-EKGKNVWyIDGAHTKDSMVAASTWFR 412
Cdd:TIGR01499 221 PLALSLLGDHQQENAALALAALEVLGKQNpklSEEAIRQGLANTIWPGRLEILsEDNPNIL-LDGAHNPHSAEALAEWFK 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    413 dmVRLSKRKKILLFN-QQSRDANALVNNLYSSVSPEitfddvIFTTNVTWKSGSYSADLVSMNTSQEDveklkvqeSLVK 491
Cdd:TIGR01499 300 --KRFNGRPITLLFGaLADKDAAAMLAPLKPVVDKE------VFVTPFDYPRADDAADLAAFAEETGK--------STVE 363
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6324815    492 NWNKIDDNRAKthvtasieeanelietlYDEPADIFVTGSLHLVGGLLVVF 542
Cdd:TIGR01499 364 DWREALEEALN-----------------ASAEDDILVTGSLYLVGEVRKLL 397
 
Name Accession Description Interval E-value
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
100-542 9.28e-138

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: 404.74  E-value: 9.28e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    100 LLEMHEWSRRIGYSAsdfNKLNIVHITGTKGKGSTAAFTSSILgqyKEQLPRIGLYTSPHLKSVRERIRINGEPISEEKF 179
Cdd:TIGR01499   1 LERMKKLLEALGNPQ---DLYPVIHVAGTNGKGSTCAFLESIL---RAAGYKVGLFTSPHLVSFNERIRINGEPISDEEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    180 AKYFFEVWDRLDSTTssldkfphmipgSKPGYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIEkPIVCGVTLLG 259
Cdd:TIGR01499  75 AQAFEQVRPILESLS------------QQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIE-PLVSVITSIG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    260 IDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVEkQPPQGLTILKERAEERKTTLTEVPP---FKQLENVKLGIAGEFQKSN 336
Cdd:TIGR01499 142 LDHTEILGDTLEEIAWEKAGIIKEGVPIVTGE-QEPEALNVLKKKAQEKGAPLFVVGRdfnYSETDENYLSFSGANLFLE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    337 ASLAVMLASEILHTSNILEEKIKCSSNAS---IPEKFIIGLQNTKWEGRCQVL-EKGKNVWyIDGAHTKDSMVAASTWFR 412
Cdd:TIGR01499 221 PLALSLLGDHQQENAALALAALEVLGKQNpklSEEAIRQGLANTIWPGRLEILsEDNPNIL-LDGAHNPHSAEALAEWFK 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    413 dmVRLSKRKKILLFN-QQSRDANALVNNLYSSVSPEitfddvIFTTNVTWKSGSYSADLVSMNTSQEDveklkvqeSLVK 491
Cdd:TIGR01499 300 --KRFNGRPITLLFGaLADKDAAAMLAPLKPVVDKE------VFVTPFDYPRADDAADLAAFAEETGK--------STVE 363
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6324815    492 NWNKIDDNRAKthvtasieeanelietlYDEPADIFVTGSLHLVGGLLVVF 542
Cdd:TIGR01499 364 DWREALEEALN-----------------ASAEDDILVTGSLYLVGEVRKLL 397
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
67-539 2.12e-123

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 372.84  E-value: 2.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    67 TYRDAVTALNSLQSNyanimaiRQTGDRKNTMTLLE-MHEWSRRIGYSaSDFNKLNIVHITGTKGKGSTAAFTSSILgqy 145
Cdd:PLN02881  15 SYEEALDALSSLITK-------KSRADPSNPGDQFDlLFDYLKILELE-EAISRLKVIHVAGTKGKGSTCTFTESIL--- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   146 KEQLPRIGLYTSPHLKSVRERIRINGEPISEEKFAKYFFEVWDRLDSTTSslDKFPhMipgskPGYFKFLTLLSFHTFIQ 225
Cdd:PLN02881  84 RNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCWDRLKEKTT--EDLP-M-----PAYFRFLTLLAFKIFSA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   226 EDCKSCVYEVGVGGELDSTNIIEKPIVCGVTLLGIDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVeKQPPQGLTILKERA 305
Cdd:PLN02881 156 EQVDVAILEVGLGGRLDATNVVQKPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAFTV-PQPDEAMRVLEERA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   306 EERKTTLTEVPPF--KQLENVKLGIAGEFQKSNASLAVMLASEILHTSNIlEEKIKCSSNASIPEKFIIGLQNTKWEGRC 383
Cdd:PLN02881 235 SELGVPLQVVEPLdsYGLSGLKLGLAGEHQYLNAGLAVALCSTWLQRTGH-EEFEALLQAGTLPEQFIKGLSTASLQGRA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   384 QVL--------EKGKNVWYIDGAHTKDSMVAASTWFRDMVRL------------------------SKRKKILLFNQQS- 430
Cdd:PLN02881 314 QVVpdsyinseDSGDLVFYLDGAHSPESMEACARWFSSAIKGdeqspgsgygphggggksedtesnKISEQILLFNCMSv 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   431 RDANALVNNLYSSVSPEIT-FDDVIFTTNVtwksgSYSADLVSMNTSQEDVEKLKVQESLVKNWNKIDDNRAKTHVTASI 509
Cdd:PLN02881 394 RDPQLLLPPLANTCASNGVpFKKALFVPNI-----SVYNKVGSGLPVDDPQVDLSWQFTLQRVWESLIRGKAGAPADAVC 468
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6324815   510 EEANE------------------------LIETLYDEPA---DIFVTGSLHLVGGLL 539
Cdd:PLN02881 469 EESASsglndgksdensavfpslplaikwLRDCARENPSlrfQVLVTGSLHLVGDVL 525
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
118-539 1.26e-91

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: 287.00  E-value: 1.26e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  118 NKLNIVHITGTKGKGSTAAFTSSILGQ--YkeqlpRIGLYTSPHLKSVRERIRINGEPISEEKFAKYFFEVWDRLDstts 195
Cdd:COG0285  38 RKLPVIHVAGTNGKGSTAAMLESILRAagY-----RVGLYTSPHLVRFNERIRINGEPISDEELVEALEEVEPAVE---- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  196 sldkfphMIPGSKPGYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIeKPIVCGVTLLGIDHTFMLGDTIEEIAW 275
Cdd:COG0285 109 -------EVDAGPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI-DPLVSVITSIGLDHTDFLGDTLEEIAR 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  276 NKGGIFKSGAPAFTVEkQPPQGLTILKERAEERKTTLTEVP-----------------PFKQLENVKLGIAGEFQKSNAS 338
Cdd:COG0285 181 EKAGIIKPGVPVVTGD-QQPEALEVIEERAAELGAPLYRAGrdfsveeregavfsyqgPGGEYEDLPLPLLGAHQAENAA 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  339 LAVMlASEILHTSNIleekikcssnaSIPEKFII-GLQNTKWEGRCQVLEKGKNVWyIDGAHTKDSMVAASTWFRDMvrL 417
Cdd:COG0285 260 LALA-ALEALRELGL-----------PISEEAIReGLANARWPGRLEVLSRGPLVI-LDGAHNPAGARALAETLKEL--F 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  418 SKRKKILLFN-QQSRDANALVNNLyssvsPEItFDDVIFTTNvtwkSGSYSAdlvsmntsqeDVEKLKvqeslvknwNKI 496
Cdd:COG0285 325 PFRKLHLVFGmLADKDIEGMLAAL-----APL-ADEVIVTTP----PSPRAL----------DAEELA---------EAA 375
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 6324815  497 DDNRAKTHVTASIEEANELIETLYDEPADIFVTGSLHLVGGLL 539
Cdd:COG0285 376 RELGLRVEVAPDVEEALEAALELADPDDLILVTGSLYLVGEVR 418
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
379-426 5.11e-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: 36.17  E-value: 5.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 6324815    379 WEGRCQVL-EKGKNVWYIDGAHTKDSMVAASTWFRDMVrlsKRKKILLF 426
Cdd:pfam02875   1 VPGRLEVVgENNGVLVIDDYAHNPDAMEAALRALRNLF---PGRLILVF 46
 
Name Accession Description Interval E-value
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
100-542 9.28e-138

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: 404.74  E-value: 9.28e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    100 LLEMHEWSRRIGYSAsdfNKLNIVHITGTKGKGSTAAFTSSILgqyKEQLPRIGLYTSPHLKSVRERIRINGEPISEEKF 179
Cdd:TIGR01499   1 LERMKKLLEALGNPQ---DLYPVIHVAGTNGKGSTCAFLESIL---RAAGYKVGLFTSPHLVSFNERIRINGEPISDEEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    180 AKYFFEVWDRLDSTTssldkfphmipgSKPGYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIEkPIVCGVTLLG 259
Cdd:TIGR01499  75 AQAFEQVRPILESLS------------QQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIE-PLVSVITSIG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    260 IDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVEkQPPQGLTILKERAEERKTTLTEVPP---FKQLENVKLGIAGEFQKSN 336
Cdd:TIGR01499 142 LDHTEILGDTLEEIAWEKAGIIKEGVPIVTGE-QEPEALNVLKKKAQEKGAPLFVVGRdfnYSETDENYLSFSGANLFLE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    337 ASLAVMLASEILHTSNILEEKIKCSSNAS---IPEKFIIGLQNTKWEGRCQVL-EKGKNVWyIDGAHTKDSMVAASTWFR 412
Cdd:TIGR01499 221 PLALSLLGDHQQENAALALAALEVLGKQNpklSEEAIRQGLANTIWPGRLEILsEDNPNIL-LDGAHNPHSAEALAEWFK 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    413 dmVRLSKRKKILLFN-QQSRDANALVNNLYSSVSPEitfddvIFTTNVTWKSGSYSADLVSMNTSQEDveklkvqeSLVK 491
Cdd:TIGR01499 300 --KRFNGRPITLLFGaLADKDAAAMLAPLKPVVDKE------VFVTPFDYPRADDAADLAAFAEETGK--------STVE 363
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6324815    492 NWNKIDDNRAKthvtasieeanelietlYDEPADIFVTGSLHLVGGLLVVF 542
Cdd:TIGR01499 364 DWREALEEALN-----------------ASAEDDILVTGSLYLVGEVRKLL 397
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
67-539 2.12e-123

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 372.84  E-value: 2.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    67 TYRDAVTALNSLQSNyanimaiRQTGDRKNTMTLLE-MHEWSRRIGYSaSDFNKLNIVHITGTKGKGSTAAFTSSILgqy 145
Cdd:PLN02881  15 SYEEALDALSSLITK-------KSRADPSNPGDQFDlLFDYLKILELE-EAISRLKVIHVAGTKGKGSTCTFTESIL--- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   146 KEQLPRIGLYTSPHLKSVRERIRINGEPISEEKFAKYFFEVWDRLDSTTSslDKFPhMipgskPGYFKFLTLLSFHTFIQ 225
Cdd:PLN02881  84 RNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCWDRLKEKTT--EDLP-M-----PAYFRFLTLLAFKIFSA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   226 EDCKSCVYEVGVGGELDSTNIIEKPIVCGVTLLGIDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVeKQPPQGLTILKERA 305
Cdd:PLN02881 156 EQVDVAILEVGLGGRLDATNVVQKPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAFTV-PQPDEAMRVLEERA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   306 EERKTTLTEVPPF--KQLENVKLGIAGEFQKSNASLAVMLASEILHTSNIlEEKIKCSSNASIPEKFIIGLQNTKWEGRC 383
Cdd:PLN02881 235 SELGVPLQVVEPLdsYGLSGLKLGLAGEHQYLNAGLAVALCSTWLQRTGH-EEFEALLQAGTLPEQFIKGLSTASLQGRA 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   384 QVL--------EKGKNVWYIDGAHTKDSMVAASTWFRDMVRL------------------------SKRKKILLFNQQS- 430
Cdd:PLN02881 314 QVVpdsyinseDSGDLVFYLDGAHSPESMEACARWFSSAIKGdeqspgsgygphggggksedtesnKISEQILLFNCMSv 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   431 RDANALVNNLYSSVSPEIT-FDDVIFTTNVtwksgSYSADLVSMNTSQEDVEKLKVQESLVKNWNKIDDNRAKTHVTASI 509
Cdd:PLN02881 394 RDPQLLLPPLANTCASNGVpFKKALFVPNI-----SVYNKVGSGLPVDDPQVDLSWQFTLQRVWESLIRGKAGAPADAVC 468
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6324815   510 EEANE------------------------LIETLYDEPA---DIFVTGSLHLVGGLL 539
Cdd:PLN02881 469 EESASsglndgksdensavfpslplaikwLRDCARENPSlrfQVLVTGSLHLVGDVL 525
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
118-539 1.26e-91

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: 287.00  E-value: 1.26e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  118 NKLNIVHITGTKGKGSTAAFTSSILGQ--YkeqlpRIGLYTSPHLKSVRERIRINGEPISEEKFAKYFFEVWDRLDstts 195
Cdd:COG0285  38 RKLPVIHVAGTNGKGSTAAMLESILRAagY-----RVGLYTSPHLVRFNERIRINGEPISDEELVEALEEVEPAVE---- 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  196 sldkfphMIPGSKPGYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIeKPIVCGVTLLGIDHTFMLGDTIEEIAW 275
Cdd:COG0285 109 -------EVDAGPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVI-DPLVSVITSIGLDHTDFLGDTLEEIAR 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  276 NKGGIFKSGAPAFTVEkQPPQGLTILKERAEERKTTLTEVP-----------------PFKQLENVKLGIAGEFQKSNAS 338
Cdd:COG0285 181 EKAGIIKPGVPVVTGD-QQPEALEVIEERAAELGAPLYRAGrdfsveeregavfsyqgPGGEYEDLPLPLLGAHQAENAA 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  339 LAVMlASEILHTSNIleekikcssnaSIPEKFII-GLQNTKWEGRCQVLEKGKNVWyIDGAHTKDSMVAASTWFRDMvrL 417
Cdd:COG0285 260 LALA-ALEALRELGL-----------PISEEAIReGLANARWPGRLEVLSRGPLVI-LDGAHNPAGARALAETLKEL--F 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815  418 SKRKKILLFN-QQSRDANALVNNLyssvsPEItFDDVIFTTNvtwkSGSYSAdlvsmntsqeDVEKLKvqeslvknwNKI 496
Cdd:COG0285 325 PFRKLHLVFGmLADKDIEGMLAAL-----APL-ADEVIVTTP----PSPRAL----------DAEELA---------EAA 375
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 6324815  497 DDNRAKTHVTASIEEANELIETLYDEPADIFVTGSLHLVGGLL 539
Cdd:COG0285 376 RELGLRVEVAPDVEEALEAALELADPDDLILVTGSLYLVGEVR 418
PLN02913 PLN02913
dihydrofolate synthetase
69-539 1.81e-41

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 156.13  E-value: 1.81e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815    69 RDAVTALNSLqSNYANIMAIRQTG-DRKNTMTLLEMHEWSRRIGYSASDFNklnIVHITGTKGKGSTAAFTSSILgqyKE 147
Cdd:PLN02913  27 GDFLRYLDSL-KNYEKSGVPKDAGtDSDDGFDLGRMRRLMDRLGNPHSKFK---AVHVAGTKGKGSTAAFLSNIL---RA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   148 QLPRIGLYTSPHLKSVRERIRIN--GEPISEEKFAKYFFEVWDRLDSTTSSLDkfphmipGSKpGYFKFLTLLSFHTFIQ 225
Cdd:PLN02913 100 QGYSVGCYTSPHLRSIRERISVGklGKPVSTNTLNDLFHGIKPILDEAIQLEN-------GSL-THFEVLTALAFKLFAQ 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   226 EDCKSCVYEVGVGGELDSTNIIEKPIVCG--VTLLGIDHTFMLGDTIEEIAWNKGGIFKSGAPAFTVEKQPPQGLTILKE 303
Cdd:PLN02913 172 ENVDIAVIEAGLGGARDATNVIDSSGLAAsvITTIGEEHLAALGGSLESIALAKSGIIKQGRPVVLGGPFLPHIESILRD 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   304 RAEERKTTLT---------------------------------EVPPFKQLENVKLGIAGEFQKSNASLAVMLASeilht 350
Cdd:PLN02913 252 KASSMNSPVVsasdpgvrssikgiitdngkpcqscdivirvekDDPLFIELSDVNLRMLGSHQLQNAVTAACAAL----- 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   351 snILEEKIKCSSNASIPekfiIGLQNTKWEGRCQVLEK---------GKNVwYIDGAHTKDSMVAASTWFRdMVRLSKRK 421
Cdd:PLN02913 327 --CLRDQGWRISDASIR----AGLENTNLLGRSQFLTSkeaevlglpGATV-LLDGAHTKESAKALVDTIK-TAFPEARL 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   422 KILLFNQQSRDANALVNNLYSSVSPEitfddVIFTTNVT---WKSGSYSADLVSMNTSQEdVEKLKVQESLVKNwnkidd 498
Cdd:PLN02913 399 ALVVAMASDKDHLAFASEFLSGLKPE-----AVFLTEADiagGKSRSTSASALKEAWIKA-APELGIETLLAEN------ 466
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 6324815   499 nrakTHVTASIEEANELIE--TLYDEPADIFVTGSLHLVGGLL 539
Cdd:PLN02913 467 ----NSLLKSLVDASAILRkaRTLDPSSVVCVTGSLHIVSAVL 505
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
109-296 8.70e-23

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 100.92  E-value: 8.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   109 RIGYSASDFNKLN----IVHITGTKGKGSTAAFTSSIL---GQykeqlpRIGLYTSPHLKSVRERIRINGEPISEEKFAK 181
Cdd:PRK10846  34 RVSQVAARLDLLKpapfVFTVAGTNGKGTTCRTLESILmaaGY------RVGVYSSPHLVRYTERVRIQGQELPESAHTA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324815   182 YFFEVWDRLDSTTSSldkfphmipgskpgYFKFLTLLSFHTFIQEDCKSCVYEVGVGGELDSTNIIEkPIVCGVTLLGID 261
Cdd:PRK10846 108 SFAEIEAARGDISLT--------------YFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVD-ADVAVVTSIALD 172
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6324815   262 HTFMLGDTIEEIAWNKGGIFKSGAPAFTVEKQPPQ 296
Cdd:PRK10846 173 HTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPS 207
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
379-426 5.11e-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: 36.17  E-value: 5.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 6324815    379 WEGRCQVL-EKGKNVWYIDGAHTKDSMVAASTWFRDMVrlsKRKKILLF 426
Cdd:pfam02875   1 VPGRLEVVgENNGVLVIDDYAHNPDAMEAALRALRNLF---PGRLILVF 46
 
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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