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Conserved domains on  [gi|520864484|ref|WP_020305070|]
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bifunctional tetrahydrofolate synthase/dihydrofolate synthase [Pseudomonas syringae]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 4-422 3.29e-159

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: 455.72  E-value: 3.29e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   4 TSLGDWLAYLEQLHPSAIDMGLDRSRQVALQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYN 83
Cdd:COG0285    2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  84 ERVKVQGVEATDLELCDAFAAVEAARGDV---TLTYFEMGTLAAFWLFERAQLDAVVLEVGLGGRLDAVNLIDSDLALVT 160
Cdd:COG0285   82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 161 SIGVDHTEYLGDTRESVAFEKAGIFRAGCPALCGDPSPP--EPLLTKARELGCPLLLRGRDFDLS-IGDDSWGWRgvahG 237
Cdd:COG0285  162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEalEVIEERAAELGAPLYRAGRDFSVEeREGAVFSYQ----G 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 238 EQVELRGLPlLDLP----MQNAA---LALQAFALLGYPLQTDAIGQVLAQTRLAGRLDRrtVRwHGKLlnLLLDVGHNPH 310
Cdd:COG0285  238 PGGEYEDLP-LPLLgahqAENAAlalAALEALRELGLPISEEAIREGLANARWPGRLEV--LS-RGPL--VILDGAHNPA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 311 AAHFLQQRLARRPVPGKRFAVFGLLNDKDLDGVVAHLAPAIADWAVTPLSTSRSRPAEELHSALQNLGARVTSYQSVAQA 390
Cdd:COG0285  312 GARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAARELGLRVEVAPDVEEA 391

                        410       420       430
                 ....*....|....*....|....*....|..
gi 520864484 391 LDAQCAHATPDDEILLFGSFYCVAEALEWLAR 422
Cdd:COG0285  392 LEAALELADPDDLILVTGSLYLVGEVRALLGR 423
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 4-422 3.29e-159

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: 455.72  E-value: 3.29e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   4 TSLGDWLAYLEQLHPSAIDMGLDRSRQVALQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYN 83
Cdd:COG0285    2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  84 ERVKVQGVEATDLELCDAFAAVEAARGDV---TLTYFEMGTLAAFWLFERAQLDAVVLEVGLGGRLDAVNLIDSDLALVT 160
Cdd:COG0285   82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 161 SIGVDHTEYLGDTRESVAFEKAGIFRAGCPALCGDPSPP--EPLLTKARELGCPLLLRGRDFDLS-IGDDSWGWRgvahG 237
Cdd:COG0285  162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEalEVIEERAAELGAPLYRAGRDFSVEeREGAVFSYQ----G 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 238 EQVELRGLPlLDLP----MQNAA---LALQAFALLGYPLQTDAIGQVLAQTRLAGRLDRrtVRwHGKLlnLLLDVGHNPH 310
Cdd:COG0285  238 PGGEYEDLP-LPLLgahqAENAAlalAALEALRELGLPISEEAIREGLANARWPGRLEV--LS-RGPL--VILDGAHNPA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 311 AAHFLQQRLARRPVPGKRFAVFGLLNDKDLDGVVAHLAPAIADWAVTPLSTSRSRPAEELHSALQNLGARVTSYQSVAQA 390
Cdd:COG0285  312 GARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAARELGLRVEVAPDVEEA 391

                        410       420       430
                 ....*....|....*....|....*....|..
gi 520864484 391 LDAQCAHATPDDEILLFGSFYCVAEALEWLAR 422
Cdd:COG0285  392 LEAALELADPDDLILVTGSLYLVGEVRALLGR 423
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 4-420 6.75e-150

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 431.81  E-value: 6.75e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   4 TSLGDWLAYLEQLHPSAIDMGLDRSRQVALQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYN 83
Cdd:PRK10846  11 SPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  84 ERVKVQGVEATDLELCDAFAAVEAARGDVTLTYFEMGTLAAFWLFERAQLDAVVLEVGLGGRLDAVNLIDSDLALVTSIG 163
Cdd:PRK10846  91 ERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 164 VDHTEYLGDTRESVAFEKAGIFRAGCPALCGDPSPPEPLLTKARELGCPLLLRGRDFDLSIGDDSWGWRgvahGEQVELR 243
Cdd:PRK10846 171 LDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFS----DGDGTLE 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 244 GLPLLDLPMQNAALALQAFALLGYPLQTDAIGQVLAQTRLAGRLdrRTVRWHGKllnLLLDVGHNPHAAHFLQQRLARRP 323
Cdd:PRK10846 247 NLPLPNVPLPNAATALAALRASGLEVSEQAIRDGIASAILPGRF--QIVSESPR---VILDVAHNPHAAEYLTGRLKALP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 324 VPGKRFAVFGLLNDKDLDGVVAHLAPAIADWAVTPLSTSRSRPAEELhsaLQNLGArVTSYQSVAQALDAQCAHATPDDE 403
Cdd:PRK10846 322 KNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQL---AEHLGN-GKSFDSVAQAWDAAMADAKPEDT 397

                        410
                 ....*....|....*..
gi 520864484 404 ILLFGSFYCVAEALEWL 420
Cdd:PRK10846 398 VLVCGSFHTVAHVMEVI 414
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 25-420 1.15e-106

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: 321.15  E-value: 1.15e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   25 LDRSRQVALQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYNERVKVQGVEATDLELCDAFAA 104
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  105 VEAA--RGDVTLTYFEMGTLAAFWLFERAQLDAVVLEVGLGGRLDAVNLIDSDLALVTSIGVDHTEYLGDTRESVAFEKA 182
Cdd:TIGR01499  81 VRPIleSLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  183 GIFRAGCPALCGD--PSPPEPLLTKARELGCPLLLRGRDFDLSIGD-DSWGWRGvAHGEQVELRGLPLLDLPMQNAALAL 259
Cdd:TIGR01499 161 GIIKEGVPIVTGEqePEALNVLKKKAQEKGAPLFVVGRDFNYSETDeNYLSFSG-ANLFLEPLALSLLGDHQQENAALAL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  260 QAFALLG---YPLQTDAIGQVLAQTRLAGRLDRrtVRWHGKllNLLLDVGHNPHAAH----FLQQRLARRPVpgkrFAVF 332
Cdd:TIGR01499 240 AALEVLGkqnPKLSEEAIRQGLANTIWPGRLEI--LSEDNP--NILLDGAHNPHSAEalaeWFKKRFNGRPI----TLLF 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  333 GLLNDKDLDGVVAHLAPAIA-DWAVTPLSTSRSRPAEELHSALQNLGARVtsYQSVAQALDAQcAHATPDDEILLFGSFY 411
Cdd:TIGR01499 312 GALADKDAAAMLAPLKPVVDkEVFVTPFDYPRADDAADLAAFAEETGKST--VEDWREALEEA-LNASAEDDILVTGSLY 388


                  ....*....
gi 520864484  412 CVAEALEWL 420
Cdd:TIGR01499 389 LVGEVRKLL 397
Mur_ligase_M pfam08245
Mur ligase middle domain;
47-185 5.07e-11

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 61.55  E-value: 5.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   47 VTGTNGKGSTCAFVAALLQAQGLK---VGVYSSPHLIRYNERVKVQgveatdlelcdafaaveaargdvtLTYFEMgtla 123
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVigtIGTYIGKSGNTTNNAIGLP------------------------LTLAEM---- 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520864484  124 afwlfERAQLDAVVLEV---GLG-GRLDavNLIDSDLALVTSIGVDHTEYLGdTRESVAFEKAGIF 185
Cdd:pfam08245  53 -----VEAGAEYAVLEVsshGLGeGRLS--GLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELF 110
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 4-422 3.29e-159

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: 455.72  E-value: 3.29e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   4 TSLGDWLAYLEQLHPSAIDMGLDRSRQVALQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYN 83
Cdd:COG0285    2 TTYQEALAYLESLHPFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRFN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  84 ERVKVQGVEATDLELCDAFAAVEAARGDV---TLTYFEMGTLAAFWLFERAQLDAVVLEVGLGGRLDAVNLIDSDLALVT 160
Cdd:COG0285   82 ERIRINGEPISDEELVEALEEVEPAVEEVdagPPTFFEVTTAAAFLYFAEAPVDVAVLEVGLGGRLDATNVIDPLVSVIT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 161 SIGVDHTEYLGDTRESVAFEKAGIFRAGCPALCGDPSPP--EPLLTKARELGCPLLLRGRDFDLS-IGDDSWGWRgvahG 237
Cdd:COG0285  162 SIGLDHTDFLGDTLEEIAREKAGIIKPGVPVVTGDQQPEalEVIEERAAELGAPLYRAGRDFSVEeREGAVFSYQ----G 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 238 EQVELRGLPlLDLP----MQNAA---LALQAFALLGYPLQTDAIGQVLAQTRLAGRLDRrtVRwHGKLlnLLLDVGHNPH 310
Cdd:COG0285  238 PGGEYEDLP-LPLLgahqAENAAlalAALEALRELGLPISEEAIREGLANARWPGRLEV--LS-RGPL--VILDGAHNPA 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 311 AAHFLQQRLARRPVPGKRFAVFGLLNDKDLDGVVAHLAPAIADWAVTPLSTSRSRPAEELHSALQNLGARVTSYQSVAQA 390
Cdd:COG0285  312 GARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEELAEAARELGLRVEVAPDVEEA 391

                        410       420       430
                 ....*....|....*....|....*....|..
gi 520864484 391 LDAQCAHATPDDEILLFGSFYCVAEALEWLAR 422
Cdd:COG0285  392 LEAALELADPDDLILVTGSLYLVGEVRALLGR 423
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 4-420 6.75e-150

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 431.81  E-value: 6.75e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   4 TSLGDWLAYLEQLHPSAIDMGLDRSRQVALQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYN 83
Cdd:PRK10846  11 SPLASWLSYLENLHSKTIDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  84 ERVKVQGVEATDLELCDAFAAVEAARGDVTLTYFEMGTLAAFWLFERAQLDAVVLEVGLGGRLDAVNLIDSDLALVTSIG 163
Cdd:PRK10846  91 ERVRIQGQELPESAHTASFAEIEAARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 164 VDHTEYLGDTRESVAFEKAGIFRAGCPALCGDPSPPEPLLTKARELGCPLLLRGRDFDLSIGDDSWGWRgvahGEQVELR 243
Cdd:PRK10846 171 LDHTDWLGPDRESIGREKAGIFRAEKPAVVGEPDMPSTIADVAQEKGALLQRRGVDWNYSVTDHDWAFS----DGDGTLE 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 244 GLPLLDLPMQNAALALQAFALLGYPLQTDAIGQVLAQTRLAGRLdrRTVRWHGKllnLLLDVGHNPHAAHFLQQRLARRP 323
Cdd:PRK10846 247 NLPLPNVPLPNAATALAALRASGLEVSEQAIRDGIASAILPGRF--QIVSESPR---VILDVAHNPHAAEYLTGRLKALP 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 324 VPGKRFAVFGLLNDKDLDGVVAHLAPAIADWAVTPLSTSRSRPAEELhsaLQNLGArVTSYQSVAQALDAQCAHATPDDE 403
Cdd:PRK10846 322 KNGRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQL---AEHLGN-GKSFDSVAQAWDAAMADAKPEDT 397

                        410
                 ....*....|....*..
gi 520864484 404 ILLFGSFYCVAEALEWL 420
Cdd:PRK10846 398 VLVCGSFHTVAHVMEVI 414
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 25-420 1.15e-106

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: 321.15  E-value: 1.15e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   25 LDRSRQVALQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYNERVKVQGVEATDLELCDAFAA 104
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  105 VEAA--RGDVTLTYFEMGTLAAFWLFERAQLDAVVLEVGLGGRLDAVNLIDSDLALVTSIGVDHTEYLGDTRESVAFEKA 182
Cdd:TIGR01499  81 VRPIleSLSQQPTYFELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIAWEKA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  183 GIFRAGCPALCGD--PSPPEPLLTKARELGCPLLLRGRDFDLSIGD-DSWGWRGvAHGEQVELRGLPLLDLPMQNAALAL 259
Cdd:TIGR01499 161 GIIKEGVPIVTGEqePEALNVLKKKAQEKGAPLFVVGRDFNYSETDeNYLSFSG-ANLFLEPLALSLLGDHQQENAALAL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  260 QAFALLG---YPLQTDAIGQVLAQTRLAGRLDRrtVRWHGKllNLLLDVGHNPHAAH----FLQQRLARRPVpgkrFAVF 332
Cdd:TIGR01499 240 AALEVLGkqnPKLSEEAIRQGLANTIWPGRLEI--LSEDNP--NILLDGAHNPHSAEalaeWFKKRFNGRPI----TLLF 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  333 GLLNDKDLDGVVAHLAPAIA-DWAVTPLSTSRSRPAEELHSALQNLGARVtsYQSVAQALDAQcAHATPDDEILLFGSFY 411
Cdd:TIGR01499 312 GALADKDAAAMLAPLKPVVDkEVFVTPFDYPRADDAADLAAFAEETGKST--VEDWREALEEA-LNASAEDDILVTGSLY 388


                  ....*....
gi 520864484  412 CVAEALEWL 420
Cdd:TIGR01499 389 LVGEVRKLL 397
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 44-213 3.71e-46

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 166.76  E-value: 3.71e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  44 VITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYNERVKVQGVEATDlelcDAFAAV---------EAARGDVTL 114
Cdd:PLN02881  63 VIHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISE----EKFLRYfwwcwdrlkEKTTEDLPM 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 115 -TYFEMGTLAAFWLFERAQLDAVVLEVGLGGRLDAVNLIDSDLAL-VTSIGVDHTEYLGDTRESVAFEKAGIFRAGCPAL 192
Cdd:PLN02881 139 pAYFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQKPVVCgITSLGYDHMEILGDTLGKIAGEKAGIFKPGVPAF 218

                        170       180
                 ....*....|....*....|....
gi 520864484 193 CGdPSPPEP---LLTKARELGCPL 213
Cdd:PLN02881 219 TV-PQPDEAmrvLEERASELGVPL 241
PLN02913 PLN02913
dihydrofolate synthetase
 6-199 1.43e-33

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 131.87  E-value: 1.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   6 LGDWLAYLEQLH-------PSAI----DMGLD--RSRQVALQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVG 72
Cdd:PLN02913  26 LGDFLRYLDSLKnyeksgvPKDAgtdsDDGFDlgRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  73 VYSSPHLIRYNERVKV--QGVEATDLELCDAF--------AAVEAARGdvTLTYFEMGTLAAFWLFERAQLDAVVLEVGL 142
Cdd:PLN02913 106 CYTSPHLRSIRERISVgkLGKPVSTNTLNDLFhgikpildEAIQLENG--SLTHFEVLTALAFKLFAQENVDIAVIEAGL 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 143 GGRLDAVNLIDS-DLA--LVTSIGVDHTEYLGDTRESVAFEKAGIFRAGCPALCGDPSPP 199
Cdd:PLN02913 184 GGARDATNVIDSsGLAasVITTIGEEHLAALGGSLESIALAKSGIIKQGRPVVLGGPFLP 243
Mur_ligase_M pfam08245
Mur ligase middle domain;
47-185 5.07e-11

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 61.55  E-value: 5.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   47 VTGTNGKGSTCAFVAALLQAQGLK---VGVYSSPHLIRYNERVKVQgveatdlelcdafaaveaargdvtLTYFEMgtla 123
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVigtIGTYIGKSGNTTNNAIGLP------------------------LTLAEM---- 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520864484  124 afwlfERAQLDAVVLEV---GLG-GRLDavNLIDSDLALVTSIGVDHTEYLGdTRESVAFEKAGIF 185
Cdd:pfam08245  53 -----VEAGAEYAVLEVsshGLGeGRLS--GLLKPDIAVFTNISPDHLDFHG-TMENYAKAKAELF 110
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 40-339 5.71e-09

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: 57.71  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484   40 PARR--VITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSphliRYNErvkvqgveatdlelcdaFAAVEAARGDVTLTYF 117
Cdd:TIGR01085  81 PSKKlkVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGT----IGYR-----------------LGGNDLIKNPAALTTP 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  118 EMGTL-AAFWLFERAQLDAVVLEV---GLG-GRLDAVNLidsDLALVTSIGVDHTEYLGdTRESVAFEKAGIFRA-GCPA 191
Cdd:TIGR01085 140 EALTLqSTLAEMVEAGAQYAVMEVsshALAqGRVRGVRF---DAAVFTNLSRDHLDFHG-TMENYFAAKASLFTElGLKR 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  192 ---LCGDpSPPEPLLTKARELGCPLLLRGRDF-----DLSIGDDSWGWRGVaHGEQVELRGLPLLDLPM------QNAAL 257
Cdd:TIGR01085 216 favINLD-DEYGAQFVKRLPKDITVSAITQPAdgraqDIKITDSGYSFEGQ-QFTFETPAGEGHLHTPLigrfnvYNLLA 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  258 A-LQAFALLGYPLqtDAIGQVLAQTR-LAGRLDRrtVRwHGKLLNLLLDVGHNPHAahfLQQRL--ARRPVPGKRFAVFG 333
Cdd:TIGR01085 294 AlATLLHLGGIDL--EDIVAALEKFRgVPGRMEL--VD-GGQKFLVIVDYAHTPDA---LEKALrtLRKHKDGRLIVVFG 365


                  ....*.
gi 520864484  334 LLNDKD 339
Cdd:TIGR01085 366 CGGDRD 371
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 43-408 1.26e-05

bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase MurF;


Pssm-ID: 237025 [Multi-domain]  Cd Length: 958  Bit Score: 47.78  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  43 RVITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSPHLIRYNERVKVQGVEATDLELCDAFAAVEAargdvtltyfemgtl 122
Cdd:PRK11929 113 SLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTLGARLDGRLIPGSLTTPDAIILHRILARMRA--------------- 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 123 aafwlferAQLDAVVLEV---GLG-GRLDAVNLidsDLALVTSIGVDHTEYLGdTRESVAFEKAGIFRAGCP---ALCGD 195
Cdd:PRK11929 178 --------AGADAVAMEAsshGLEqGRLDGLRI---AVAGFTNLTRDHLDYHG-TMQDYEEAKAALFSKLPGlgaAVINA 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 196 PSPPEPLLTKARELGCPLLLRGRDFDLSIgdDSWGWRGVAHGEQVEL---RGLPLLDLPM------QNAALALQAFALLG 266
Cdd:PRK11929 246 DDPAAARLLAALPRGLKVGYSPQNAGADV--QARDLRATAHGQVFTLatpDGSYQLVTRLlgrfnvSNLLLVAAALKKLG 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 267 YPLqtDAIGQVLAQTR-LAGRLDRRTVRWHGKLLNLLLDVGHNPHAahfLQQRL-ARRPVP----GKRFAVFGLLNDKDL 340
Cdd:PRK11929 324 LPL--AQIARALAAVSpVPGRMERVGPTAGAQGPLVVVDYAHTPDA---LAKALtALRPVAqarnGRLVCVFGCGGDRDK 398

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520864484 341 DG--VVAHLAPAIADWAVTPLSTSRSRPAEELHSAL-----QNLGARVTSyqSVAQALDAQCAHATPDDEILLFG 408
Cdd:PRK11929 399 GKrpEMGRIAAELADRVVVTSDNPRSEAPEAIIDQIlagipAGARVFVIS--DRAEAIRQAIWMAAPGDVILIAG 471
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 39-73 3.46e-05

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: 45.84  E-value: 3.46e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 520864484  39 RPAR--RVITVTGTNGKGSTCAFVAALLQAQGLKVGV 73
Cdd:COG0769   75 HPSQklKLIGVTGTNGKTTTTYLLAQILRALGKKTGL 111
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 29-73 2.01e-04

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 43.58  E-value: 2.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 520864484  29 RQVALQMGLM------RPARR--VITVTGTNGKGSTCAFVAALLQAQGLKVGV 73
Cdd:PRK00139  74 PDLRKALALLaaafygHPSDKlkLIGVTGTNGKTTTAYLLAQILRLLGEKTAL 126
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 40-73 2.06e-04

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 43.53  E-value: 2.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 520864484  40 PARRVITVTGTNGKGSTCAFVAALLQAQGLKVGV 73
Cdd:COG0771  103 SPAPIIAITGTNGKTTTTTLIGHILKAAGLRVAV 136
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 43-409 6.59e-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: 42.01  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  43 RVITVTGTNGKGSTCAFVAALLQAQGlkvGVYSSP-----HLirynervkvqgveatdlelcdafaaveaarGdVTLTYF 117
Cdd:COG0770  101 PVIAITGSNGKTTTKEMLAAVLSTKG---KVLATPgnfnnEI------------------------------G-VPLTLL 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 118 EMgtlaafwlfeRAQLDAVVLEVG---LG--GRLdaVNLIDSDLALVTSIGVDHTEYLGdTRESVAFEKAGIFrAGCPA- 191
Cdd:COG0770  147 RL----------PEDHEFAVLEMGmnhPGeiAYL--ARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIF-EGLPPg 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 192 ----LCGDpsppEPLLTKARE-LGCPLL---------LRGRDFDLSigDDSWGWRGVAHGEQVELRgLPLLDLPM-QNAA 256
Cdd:COG0770  213 gvavLNAD----DPLLAALAErAKARVLtfglsedadVRAEDIELD--EDGTRFTLHTPGGELEVT-LPLPGRHNvSNAL 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 257 LALQAFALLGYPLqtDAIGQVLAQTRL-AGRLDRRTVRWHGKLLN-----------LLLDVghnphaahflqqrLARRPV 324
Cdd:COG0770  286 AAAAVALALGLDL--EEIAAGLAAFQPvKGRLEVIEGAGGVTLIDdsynanpdsmkAALDV-------------LAQLPG 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484 325 PGKRFAVFGllnD-KDL--------DGVVAHLAPAIAD--WAVTPLstsrsrpAEELHSALqnLGARVTSYQSVAQALDA 393
Cdd:COG0770  351 GGRRIAVLG---DmLELgeeseelhREVGELAAELGIDrlFTVGEL-------ARAIAEAA--GGERAEHFEDKEELLAA 418

                        410
                 ....*....|....*.
gi 520864484 394 QCAHATPDDEILLFGS 409
Cdd:COG0770  419 LKALLRPGDVVLVKGS 434
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 44-182 8.16e-04

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 41.68  E-value: 8.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520864484  44 VITVTGTNGKGSTCAFVAALLQAQGLKVGVYSSphlirynERVKVQG--VEATDlelCDAFAAveaargdvtltyfemgt 121
Cdd:PRK14016 482 IVAVTGTNGKTTTTRLIAHILKLSGKRVGMTTT-------DGVYIDGrlIDKGD---CTGPKS----------------- 534

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520864484 122 lAAFWLFERAqLDAVVLEVGLGGRLD---AVNLidSDLALVTSIGVDHteyLG----DTRESVAFEKA 182
Cdd:PRK14016 535 -ARRVLMNPD-VEAAVLETARGGILReglAYDR--CDVGVVTNIGEDH---LGlggiNTLEDLAKVKR 595
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 33-73 9.56e-04

UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273436 [Multi-domain]  Cd Length: 433  Bit Score: 41.17  E-value: 9.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 520864484   33 LQMGLMRPARRVITVTGTNGKGSTCAFVAALLQAQGLKVGV 73
Cdd:TIGR01087  93 IELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFL 133
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 285-353 4.69e-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: 4.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520864484  285 GRLDRrtVRWHGKLLnLLLDVGHNPHAAHFLQQrLARRPVPGKRFAVFGLLNDKDLD--GVVAHLAPAIAD 353
Cdd:pfam02875   3 GRLEV--VGENNGVL-VIDDYAHNPDAMEAALR-ALRNLFPGRLILVFGGMGDRDAEfhALLGRLAAALAD 69
 
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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