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Conserved domains on  [gi|530390857|ref|XP_005251921|]
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folylpolyglutamate synthase, mitochondrial isoform X2 [Homo sapiens]

Protein Classification

folylpolyglutamate synthase( domain architecture ID 1000681)

folylpolyglutamate synthase (FPGS) catalyzes the addition of glutamate residues to folates, forming polyglutamate derivatives which is essential for the metabolism of folate

EC:  6.3.2.17
Gene Ontology:  GO:0005524|GO:0046872|GO:0004326
PubMed:  7721888

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02881 super family cl47075
tetrahydrofolylpolyglutamate synthase
42-441 1.90e-152

tetrahydrofolylpolyglutamate synthase


The actual alignment was detected with superfamily member PLN02881:

Pssm-ID: 481415  Cd Length: 530  Bit Score: 445.26  E-value: 1.90e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  42 SMEYQDAVRMLNTLQTnagyleqvKRQRGDPQT---QLEAMELYLARSGLQvEDLDRLNIIHVTGTKGKGSTCAFTECIL 118
Cdd:PLN02881  13 SDSYEEALDALSSLIT--------KKSRADPSNpgdQFDLLFDYLKILELE-EAISRLKVIHVAGTKGKGSTCTFTESIL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 119 RSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGScVSMPPYFRFLTLMAFHVFLQEKVDLAV 198
Cdd:PLN02881  84 RNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCWDRLKEKTTED-LPMPAYFRFLTLLAFKIFSAEQVDVAI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 199 VEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLY 278
Cdd:PLN02881 163 LEVGLGGRLDATNVVQKPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAFTVPQPDEAMRVLEERASELGVPLQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 279 LCPMLEAleEGGPPLTLGLEGEHQRSNAALALQLAHCWLQRQDRHGAGEPKASRPgllwqLPlapvfqptSHMRLGLRNT 358
Cdd:PLN02881 243 VVEPLDS--YGLSGLKLGLAGEHQYLNAGLAVALCSTWLQRTGHEEFEALLQAGT-----LP--------EQFIKGLSTA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 359 EWPGRTQVL--------RRGPLTWYLDGAHTASSAQACVRWFRQALQGRE------------------RPSGGPEVRVLL 412
Cdd:PLN02881 308 SLQGRAQVVpdsyinseDSGDLVFYLDGAHSPESMEACARWFSSAIKGDEqspgsgygphggggksedTESNKISEQILL 387
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 530390857 413 FNATGDRDPAALL-KLLQPC-----QFDYAVFCPN 441
Cdd:PLN02881 388 FNCMSVRDPQLLLpPLANTCasngvPFKKALFVPN 422
 
Name Accession Description Interval E-value
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
42-441 1.90e-152

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 445.26  E-value: 1.90e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  42 SMEYQDAVRMLNTLQTnagyleqvKRQRGDPQT---QLEAMELYLARSGLQvEDLDRLNIIHVTGTKGKGSTCAFTECIL 118
Cdd:PLN02881  13 SDSYEEALDALSSLIT--------KKSRADPSNpgdQFDLLFDYLKILELE-EAISRLKVIHVAGTKGKGSTCTFTESIL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 119 RSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGScVSMPPYFRFLTLMAFHVFLQEKVDLAV 198
Cdd:PLN02881  84 RNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCWDRLKEKTTED-LPMPAYFRFLTLLAFKIFSAEQVDVAI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 199 VEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLY 278
Cdd:PLN02881 163 LEVGLGGRLDATNVVQKPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAFTVPQPDEAMRVLEERASELGVPLQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 279 LCPMLEAleEGGPPLTLGLEGEHQRSNAALALQLAHCWLQRQDRHGAGEPKASRPgllwqLPlapvfqptSHMRLGLRNT 358
Cdd:PLN02881 243 VVEPLDS--YGLSGLKLGLAGEHQYLNAGLAVALCSTWLQRTGHEEFEALLQAGT-----LP--------EQFIKGLSTA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 359 EWPGRTQVL--------RRGPLTWYLDGAHTASSAQACVRWFRQALQGRE------------------RPSGGPEVRVLL 412
Cdd:PLN02881 308 SLQGRAQVVpdsyinseDSGDLVFYLDGAHSPESMEACARWFSSAIKGDEqspgsgygphggggksedTESNKISEQILL 387
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 530390857 413 FNATGDRDPAALL-KLLQPC-----QFDYAVFCPN 441
Cdd:PLN02881 388 FNCMSVRDPQLLLpPLANTCasngvPFKKALFVPN 422
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
76-443 7.92e-120

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: 356.98  E-value: 7.92e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857   76 LEAMELYLARSGLQvEDLdrLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKY 155
Cdd:TIGR01499   1 LERMKKLLEALGNP-QDL--YPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  156 FWRLYHRLEETkdgscVSMPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIrKPVVCGVSSLGIDHTSLLGDT 235
Cdd:TIGR01499  78 FEQVRPILESL-----SQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVI-EPLVSVITSIGLDHTEILGDT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  236 VEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGP-------------PLTLGLEGEHQ 302
Cdd:TIGR01499 152 LEEIAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDEnylsfsganlflePLALSLLGDHQ 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  303 RSNAALALQLAHcWLQRQdrhgagEPKASRPgllwqlplapvfqptsHMRLGLRNTEWPGRTQVLRRGPLTWYLDGAHTA 382
Cdd:TIGR01499 232 QENAALALAALE-VLGKQ------NPKLSEE----------------AIRQGLANTIWPGRLEILSEDNPNILLDGAHNP 288
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530390857  383 SSAQACVRWFRQALQGRErpsggpevRVLLFNATGDRDPAALLKLLQPcQFDYAVFCPNLT 443
Cdd:TIGR01499 289 HSAEALAEWFKKRFNGRP--------ITLLFGALADKDAAAMLAPLKP-VVDKEVFVTPFD 340
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
61-441 3.76e-112

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: 338.23  E-value: 3.76e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  61 YLEQVKRQRGDPQtqLEAMELYLARSGL-QvedlDRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRER 139
Cdd:COG0285   10 YLESLHPFGIKLG--LERIRALLERLGNpQ----RKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 140 IRINGQPISPELFTKYFWRLYHRLEETKDGScvsmPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRkPVVC 219
Cdd:COG0285   84 IRINGEPISDEELVEALEEVEPAVEEVDAGP----PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVID-PLVS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 220 GVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLC-PMLEALEEGG-------- 290
Cdd:COG0285  159 VITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAgRDFSVEEREGavfsyqgp 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 291 ----PPLTLGLEGEHQRSNAALALQLAHCWLqrqdrhgagepkasrpGLLWQLPLApvfqptsHMRLGLRNTEWPGRTQV 366
Cdd:COG0285  239 ggeyEDLPLPLLGAHQAENAALALAALEALR----------------ELGLPISEE-------AIREGLANARWPGRLEV 295
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530390857 367 LRRGPLTWyLDGAHTASSAQACVRWFRQALQGRErpsggpevRVLLFNATGDRDPAALLKLLQPCqFDYAVFCPN 441
Cdd:COG0285  296 LSRGPLVI-LDGAHNPAGARALAETLKELFPFRK--------LHLVFGMLADKDIEGMLAALAPL-ADEVIVTTP 360
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
360-441 3.03e-05

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: 42.33  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  360 WPGRTQVLRR-GPLTWYLDGAHTASSAQACVRWFRQALQGRerpsggpevRVLLFNATGDRDPA--ALLKLLQPCQFDYA 436
Cdd:pfam02875   1 VPGRLEVVGEnNGVLVIDDYAHNPDAMEAALRALRNLFPGR---------LILVFGGMGDRDAEfhALLGRLAAALADVV 71

                  ....*
gi 530390857  437 VFCPN 441
Cdd:pfam02875  72 ILTGD 76
 
Name Accession Description Interval E-value
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
42-441 1.90e-152

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 445.26  E-value: 1.90e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  42 SMEYQDAVRMLNTLQTnagyleqvKRQRGDPQT---QLEAMELYLARSGLQvEDLDRLNIIHVTGTKGKGSTCAFTECIL 118
Cdd:PLN02881  13 SDSYEEALDALSSLIT--------KKSRADPSNpgdQFDLLFDYLKILELE-EAISRLKVIHVAGTKGKGSTCTFTESIL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 119 RSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGScVSMPPYFRFLTLMAFHVFLQEKVDLAV 198
Cdd:PLN02881  84 RNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRYFWWCWDRLKEKTTED-LPMPAYFRFLTLLAFKIFSAEQVDVAI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 199 VEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLY 278
Cdd:PLN02881 163 LEVGLGGRLDATNVVQKPVVCGITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAFTVPQPDEAMRVLEERASELGVPLQ 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 279 LCPMLEAleEGGPPLTLGLEGEHQRSNAALALQLAHCWLQRQDRHGAGEPKASRPgllwqLPlapvfqptSHMRLGLRNT 358
Cdd:PLN02881 243 VVEPLDS--YGLSGLKLGLAGEHQYLNAGLAVALCSTWLQRTGHEEFEALLQAGT-----LP--------EQFIKGLSTA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 359 EWPGRTQVL--------RRGPLTWYLDGAHTASSAQACVRWFRQALQGRE------------------RPSGGPEVRVLL 412
Cdd:PLN02881 308 SLQGRAQVVpdsyinseDSGDLVFYLDGAHSPESMEACARWFSSAIKGDEqspgsgygphggggksedTESNKISEQILL 387
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 530390857 413 FNATGDRDPAALL-KLLQPC-----QFDYAVFCPN 441
Cdd:PLN02881 388 FNCMSVRDPQLLLpPLANTCasngvPFKKALFVPN 422
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
76-443 7.92e-120

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: 356.98  E-value: 7.92e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857   76 LEAMELYLARSGLQvEDLdrLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKY 155
Cdd:TIGR01499   1 LERMKKLLEALGNP-QDL--YPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  156 FWRLYHRLEETkdgscVSMPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIrKPVVCGVSSLGIDHTSLLGDT 235
Cdd:TIGR01499  78 FEQVRPILESL-----SQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVI-EPLVSVITSIGLDHTEILGDT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  236 VEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGP-------------PLTLGLEGEHQ 302
Cdd:TIGR01499 152 LEEIAWEKAGIIKEGVPIVTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETDEnylsfsganlflePLALSLLGDHQ 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  303 RSNAALALQLAHcWLQRQdrhgagEPKASRPgllwqlplapvfqptsHMRLGLRNTEWPGRTQVLRRGPLTWYLDGAHTA 382
Cdd:TIGR01499 232 QENAALALAALE-VLGKQ------NPKLSEE----------------AIRQGLANTIWPGRLEILSEDNPNILLDGAHNP 288
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530390857  383 SSAQACVRWFRQALQGRErpsggpevRVLLFNATGDRDPAALLKLLQPcQFDYAVFCPNLT 443
Cdd:TIGR01499 289 HSAEALAEWFKKRFNGRP--------ITLLFGALADKDAAAMLAPLKP-VVDKEVFVTPFD 340
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
61-441 3.76e-112

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: 338.23  E-value: 3.76e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  61 YLEQVKRQRGDPQtqLEAMELYLARSGL-QvedlDRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRER 139
Cdd:COG0285   10 YLESLHPFGIKLG--LERIRALLERLGNpQ----RKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFNER 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 140 IRINGQPISPELFTKYFWRLYHRLEETKDGScvsmPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRkPVVC 219
Cdd:COG0285   84 IRINGEPISDEELVEALEEVEPAVEEVDAGP----PTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVID-PLVS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 220 GVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLC-PMLEALEEGG-------- 290
Cdd:COG0285  159 VITSIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEALEVIEERAAELGAPLYRAgRDFSVEEREGavfsyqgp 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 291 ----PPLTLGLEGEHQRSNAALALQLAHCWLqrqdrhgagepkasrpGLLWQLPLApvfqptsHMRLGLRNTEWPGRTQV 366
Cdd:COG0285  239 ggeyEDLPLPLLGAHQAENAALALAALEALR----------------ELGLPISEE-------AIREGLANARWPGRLEV 295
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530390857 367 LRRGPLTWyLDGAHTASSAQACVRWFRQALQGRErpsggpevRVLLFNATGDRDPAALLKLLQPCqFDYAVFCPN 441
Cdd:COG0285  296 LSRGPLVI-LDGAHNPAGARALAETLKELFPFRK--------LHLVFGMLADKDIEGMLAALAPL-ADEVIVTTP 360
PLN02913 PLN02913
dihydrofolate synthetase
98-449 7.06e-49

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 175.78  E-value: 7.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  98 IIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRERIRIN--GQPISPELFTKYFWRLYHRLEET--KDGSCVS 173
Cdd:PLN02913  77 AVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERISVGklGKPVSTNTLNDLFHGIKPILDEAiqLENGSLT 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 174 mppYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCG--VSSLGIDHTSLLGDTVEKIAWQKGGIFKQGV 251
Cdd:PLN02913 157 ---HFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSSGLAAsvITTIGEEHLAALGGSLESIALAKSGIIKQGR 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 252 PafTVLQpeGPLA-----VLRDRAQQISCPLY-----------------------LCPMLEALEEGGPP------LTLGL 297
Cdd:PLN02913 234 P--VVLG--GPFLphiesILRDKASSMNSPVVsasdpgvrssikgiitdngkpcqSCDIVIRVEKDDPLfielsdVNLRM 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 298 EGEHQRSNAALALQLAHCwLQRQDrhgagepkasrpgllWQLPLAPVfqptshmRLGLRNTEWPGRTQ--------VLRR 369
Cdd:PLN02913 310 LGSHQLQNAVTAACAALC-LRDQG---------------WRISDASI-------RAGLENTNLLGRSQfltskeaeVLGL 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 370 GPLTWYLDGAHTASSAQACVRWFRQALqgrerpsggPEVRVLLFNATG-DRDPAALLKLLQPCQFDYAVFcpnLTEVSST 448
Cdd:PLN02913 367 PGATVLLDGAHTKESAKALVDTIKTAF---------PEARLALVVAMAsDKDHLAFASEFLSGLKPEAVF---LTEADIA 434

                 .
gi 530390857 449 G 449
Cdd:PLN02913 435 G 435
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
77-385 2.35e-38

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 144.84  E-value: 2.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  77 EAMELYLARSGLQVEDLDRLN----IIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELF 152
Cdd:PRK10846  26 KTIDLGLERVSQVAARLDLLKpapfVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAH 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 153 TKYFwrlyHRLEETKDGSCVSmppYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIrKPVVCGVSSLGIDHTSLL 232
Cdd:PRK10846 106 TASF----AEIEAARGDISLT---YFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIV-DADVAVVTSIALDHTDWL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 233 GDTVEKIAWQKGGIFKQGVPAfTVLQPEGPLAVlRDRAQQISCPLYLCpmlealeegGPPLTLGLEGEHQRsnaalalql 312
Cdd:PRK10846 178 GPDRESIGREKAGIFRAEKPA-VVGEPDMPSTI-ADVAQEKGALLQRR---------GVDWNYSVTDHDWA--------- 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857 313 ahcWlQRQDRHGAGEPkasrpglLWQLPLA----------PVFQPTSH--MRLGLRNTEWPGRTQVLRRGPLTwYLDGAH 380
Cdd:PRK10846 238 ---F-SDGDGTLENLP-------LPNVPLPnaatalaalrASGLEVSEqaIRDGIASAILPGRFQIVSESPRV-ILDVAH 305

                 ....*
gi 530390857 381 TASSA 385
Cdd:PRK10846 306 NPHAA 310
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
360-441 3.03e-05

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: 42.33  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  360 WPGRTQVLRR-GPLTWYLDGAHTASSAQACVRWFRQALQGRerpsggpevRVLLFNATGDRDPA--ALLKLLQPCQFDYA 436
Cdd:pfam02875   1 VPGRLEVVGEnNGVLVIDDYAHNPDAMEAALRALRNLFPGR---------LILVFGGMGDRDAEfhALLGRLAAALADVV 71

                  ....*
gi 530390857  437 VFCPN 441
Cdd:pfam02875  72 ILTGD 76
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
94-201 1.75e-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: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  94 DRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSphlVQVreriRINGQPISPELFTkyfwrlyhrleetkdgscvs 173
Cdd:PRK00139  93 DKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGT---LGN----GIGGELIPSGLTT-------------------- 145
                         90       100
                 ....*....|....*....|....*....
gi 530390857 174 mPPYfrfLTLMA-FHVFLQEKVDLAVVEV 201
Cdd:PRK00139 146 -PDA---LDLQRlLAELVDAGVTYAAMEV 170
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
94-129 3.46e-04

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: 43.14  E-value: 3.46e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 530390857  94 DRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFS 129
Cdd:COG0769   78 QKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIG 113
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
94-421 4.25e-04

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: 42.69  E-value: 4.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857   94 DRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSphlvqvreriringqpispelftkyfwrLYHRL---EETKDGS 170
Cdd:TIGR01085  83 KKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGT----------------------------IGYRLggnDLIKNPA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  171 CVSMPPYFRFLTLmaFHVFLQEKVDLAVVEVG---------IGGAYD---CTNIIRkpvvcgvsslgiDHTSLLGdTVEK 238
Cdd:TIGR01085 135 ALTTPEALTLQST--LAEMVEAGAQYAVMEVSshalaqgrvRGVRFDaavFTNLSR------------DHLDFHG-TMEN 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  239 IAWQKGGIFKQ-GVPAFTVLQPEGPL-AVLRDRAQQ----------------------ISCPLYLCPMLEALEEGGPPLT 294
Cdd:TIGR01085 200 YFAAKASLFTElGLKRFAVINLDDEYgAQFVKRLPKditvsaitqpadgraqdikitdSGYSFEGQQFTFETPAGEGHLH 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390857  295 LGLEGEHQRSNAALALQLAHCWLQRqdrhgagEPKASRPGLlwqlplaPVFQPTshmrlglrntewPGRTQVLRRGP-LT 373
Cdd:TIGR01085 280 TPLIGRFNVYNLLAALATLLHLGGI-------DLEDIVAAL-------EKFRGV------------PGRMELVDGGQkFL 333
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 530390857  374 WYLDGAHTASSaqacvrwFRQALQGRERPSGGpevRVL-LFNATGDRDP 421
Cdd:TIGR01085 334 VIVDYAHTPDA-------LEKALRTLRKHKDG---RLIvVFGCGGDRDR 372
 
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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