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Conserved domains on  [gi|2468620722|ref|WP_276847391|]
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folylpolyglutamate synthase/dihydrofolate synthase family protein [Corynebacterium pyruviciproducens]

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]; ...
 32-483 7.06e-153

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: 441.85  E-value: 7.06e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  32 ARLAEVDAEHNERWsEIHIDPSLSRIAKLMDLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLV 111
Cdd:COG0285     2 TTYQEALAYLESLH-PFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 112 TERIGIDGEPIHPADYVRIWEEIKPYVEMVDAEaeyPMSKFEVLTamafaafadapvdvgvvevgmggRWDATNVVHADV 191
Cdd:COG0285    81 NERIRINGEPISDEELVEALEEVEPAVEEVDAG---PPTFFEVTTaaaflyfaeapvdvavlevglggRLDATNVIDPLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 192 SVICPVGLDHQGMLGDTIAEIAGEKAGIIKPKwdptdllrpGPVtVIGKQDPDAMRVILEKAVEEDNSVARLGQEYGVTE 271
Cdd:COG0285   158 SVITSIGLDHTDFLGDTLEEIAREKAGIIKPG---------VPV-VTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 272 stvaVGGQQLTIQGLGGTYEDIFLPLSGAHQAEnaavalaavevffGAGT-----------GHQLDLETVKRGFAQVQSP 340
Cdd:COG0285   228 ----REGAVFSYQGPGGEYEDLPLPLLGAHQAE-------------NAALalaalealrelGLPISEEAIREGLANARWP 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 341 GRLERVRATPTTFIDAAHNPHGAKALAKAIDRDFTFRRLIGVMACLGDKDVDGVLHELEPVLDEVVCTVNTSPRCLPAEE 420
Cdd:COG0285   291 GRLEVLSRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEE 370

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468620722 421 LAEKARAIlgEERVHLAETLPGAVELAVELAEDptegdtvsGGGILITGSVVTAGEARTLFGK 483
Cdd:COG0285   371 LAEAAREL--GLRVEVAPDVEEALEAALELADP--------DDLILVTGSLYLVGEVRALLGR 423
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 32-483 7.06e-153

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: 441.85  E-value: 7.06e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  32 ARLAEVDAEHNERWsEIHIDPSLSRIAKLMDLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLV 111
Cdd:COG0285     2 TTYQEALAYLESLH-PFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 112 TERIGIDGEPIHPADYVRIWEEIKPYVEMVDAEaeyPMSKFEVLTamafaafadapvdvgvvevgmggRWDATNVVHADV 191
Cdd:COG0285    81 NERIRINGEPISDEELVEALEEVEPAVEEVDAG---PPTFFEVTTaaaflyfaeapvdvavlevglggRLDATNVIDPLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 192 SVICPVGLDHQGMLGDTIAEIAGEKAGIIKPKwdptdllrpGPVtVIGKQDPDAMRVILEKAVEEDNSVARLGQEYGVTE 271
Cdd:COG0285   158 SVITSIGLDHTDFLGDTLEEIAREKAGIIKPG---------VPV-VTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 272 stvaVGGQQLTIQGLGGTYEDIFLPLSGAHQAEnaavalaavevffGAGT-----------GHQLDLETVKRGFAQVQSP 340
Cdd:COG0285   228 ----REGAVFSYQGPGGEYEDLPLPLLGAHQAE-------------NAALalaalealrelGLPISEEAIREGLANARWP 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 341 GRLERVRATPTTFIDAAHNPHGAKALAKAIDRDFTFRRLIGVMACLGDKDVDGVLHELEPVLDEVVCTVNTSPRCLPAEE 420
Cdd:COG0285   291 GRLEVLSRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEE 370

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468620722 421 LAEKARAIlgEERVHLAETLPGAVELAVELAEDptegdtvsGGGILITGSVVTAGEARTLFGK 483
Cdd:COG0285   371 LAEAAREL--GLRVEVAPDVEEALEAALELADP--------DDLILVTGSLYLVGEVRALLGR 423
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 54-481 3.76e-87

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: 272.62  E-value: 3.76e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  54 LSRIAKLMDLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLVTERIGIDGEPIHPADYVRIWEE 133
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 134 IKPYVEMVDAEAEYpmskFEVLTAMAFAAFADAPVDVGVVEVGMGGRWDATNVVHADVSVICPVGLDHQGMLGDTIAEIA 213
Cdd:TIGR01499  81 VRPILESLSQQPTY----FELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 214 GEKAGIIKPKwdptdllrpGPVtVIGKQDPDAMRVILEKAVEEDNSVARLGQEYGVTESTvavgGQQLTIQGLGGTYEDI 293
Cdd:TIGR01499 157 WEKAGIIKEG---------VPI-VTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETD----ENYLSFSGANLFLEPL 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 294 FLPLSGAHQAENAAVALAAVEVFfgAGTGHQLDLETVKRGFAQVQSPGRLERVR-ATPTTFIDAAHNPHGAKALAKAIDR 372
Cdd:TIGR01499 223 ALSLLGDHQQENAALALAALEVL--GKQNPKLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALAEWFKK 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 373 DFTFRRLIGVMACLGDKDVDGVLHELEPVLDEVV-CTVNTSPRCLPAEELAEKARAILGEERVHLAEtlpgavelAVELA 451
Cdd:TIGR01499 301 RFNGRPITLLFGALADKDAAAMLAPLKPVVDKEVfVTPFDYPRADDAADLAAFAEETGKSTVEDWRE--------ALEEA 372

                         410       420       430
                  ....*....|....*....|....*....|
gi 2468620722 452 EDPTEGDTvsgggILITGSVVTAGEARTLF 481
Cdd:TIGR01499 373 LNASAEDD-----ILVTGSLYLVGEVRKLL 397
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 50-460 7.52e-38

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 143.29  E-value: 7.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  50 IDPSLSRIAKLMDLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLVTERIGIDGEPIHPADYVR 129
Cdd:PRK10846   28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 130 IWEEIKPyvemvdAEAEYPMSKFEVLTAMAFAAFADAPVDVGVVEVGMGGRWDATNVVHADVSVICPVGLDHQGMLGDTI 209
Cdd:PRK10846  108 SFAEIEA------ARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 210 AEIAGEKAGIikpkwdptdlLRPGPVTVIGkqDPDAMRVILEKAVEEDNSVARLGQEYgvtesTVAVGGQQLTIQGLGGT 289
Cdd:PRK10846  182 ESIGREKAGI----------FRAEKPAVVG--EPDMPSTIADVAQEKGALLQRRGVDW-----NYSVTDHDWAFSDGDGT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 290 YEDifLPLSGAHQAenaavalaavevffGAGT--------GHQLDLETVKRGFAQVQSPGRLERVRATPTTFIDAAHNPH 361
Cdd:PRK10846  245 LEN--LPLPNVPLP--------------NAATalaalrasGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPH 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 362 GAKALA---KAIDRDftfRRLIGVMACLGDKDVDGVLHELEPVLDEVVCTVNTSPRCLPAEELAEkarailgeervHLAE 438
Cdd:PRK10846  309 AAEYLTgrlKALPKN---GRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAE-----------HLGN 374

                         410       420
                  ....*....|....*....|....*..
gi 2468620722 439 tlpGAVELAVELA-----EDPTEGDTV 460
Cdd:PRK10846  375 ---GKSFDSVAQAwdaamADAKPEDTV 398
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 340-414 5.06e-11

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: 58.89  E-value: 5.06e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468620722 340 PGRLERVRA--TPTTFIDAAHNPHGAKALAKAIdRDFTFRRLIGVMACLGDKDVD--GVLHELEPVLDEVVCTVNTSPR 414
Cdd:pfam02875   2 PGRLEVVGEnnGVLVIDDYAHNPDAMEAALRAL-RNLFPGRLILVFGGMGDRDAEfhALLGRLAAALADVVILTGDYPR 79
 
Name Accession Description Interval E-value
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
 32-483 7.06e-153

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: 441.85  E-value: 7.06e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  32 ARLAEVDAEHNERWsEIHIDPSLSRIAKLMDLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLV 111
Cdd:COG0285     2 TTYQEALAYLESLH-PFGIKLGLERIRALLERLGNPQRKLPVIHVAGTNGKGSTAAMLESILRAAGYRVGLYTSPHLVRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 112 TERIGIDGEPIHPADYVRIWEEIKPYVEMVDAEaeyPMSKFEVLTamafaafadapvdvgvvevgmggRWDATNVVHADV 191
Cdd:COG0285    81 NERIRINGEPISDEELVEALEEVEPAVEEVDAG---PPTFFEVTTaaaflyfaeapvdvavlevglggRLDATNVIDPLV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 192 SVICPVGLDHQGMLGDTIAEIAGEKAGIIKPKwdptdllrpGPVtVIGKQDPDAMRVILEKAVEEDNSVARLGQEYGVTE 271
Cdd:COG0285   158 SVITSIGLDHTDFLGDTLEEIAREKAGIIKPG---------VPV-VTGDQQPEALEVIEERAAELGAPLYRAGRDFSVEE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 272 stvaVGGQQLTIQGLGGTYEDIFLPLSGAHQAEnaavalaavevffGAGT-----------GHQLDLETVKRGFAQVQSP 340
Cdd:COG0285   228 ----REGAVFSYQGPGGEYEDLPLPLLGAHQAE-------------NAALalaalealrelGLPISEEAIREGLANARWP 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 341 GRLERVRATPTTFIDAAHNPHGAKALAKAIDRDFTFRRLIGVMACLGDKDVDGVLHELEPVLDEVVCTVNTSPRCLPAEE 420
Cdd:COG0285   291 GRLEVLSRGPLVILDGAHNPAGARALAETLKELFPFRKLHLVFGMLADKDIEGMLAALAPLADEVIVTTPPSPRALDAEE 370

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468620722 421 LAEKARAIlgEERVHLAETLPGAVELAVELAEDptegdtvsGGGILITGSVVTAGEARTLFGK 483
Cdd:COG0285   371 LAEAAREL--GLRVEVAPDVEEALEAALELADP--------DDLILVTGSLYLVGEVRALLGR 423
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
 54-481 3.76e-87

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: 272.62  E-value: 3.76e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  54 LSRIAKLMDLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLVTERIGIDGEPIHPADYVRIWEE 133
Cdd:TIGR01499   1 LERMKKLLEALGNPQDLYPVIHVAGTNGKGSTCAFLESILRAAGYKVGLFTSPHLVSFNERIRINGEPISDEELAQAFEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 134 IKPYVEMVDAEAEYpmskFEVLTAMAFAAFADAPVDVGVVEVGMGGRWDATNVVHADVSVICPVGLDHQGMLGDTIAEIA 213
Cdd:TIGR01499  81 VRPILESLSQQPTY----FELLTLLAFLYFAQAQVDVAVLEVGLGGRLDATNVIEPLVSVITSIGLDHTEILGDTLEEIA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 214 GEKAGIIKPKwdptdllrpGPVtVIGKQDPDAMRVILEKAVEEDNSVARLGQEYGVTESTvavgGQQLTIQGLGGTYEDI 293
Cdd:TIGR01499 157 WEKAGIIKEG---------VPI-VTGEQEPEALNVLKKKAQEKGAPLFVVGRDFNYSETD----ENYLSFSGANLFLEPL 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 294 FLPLSGAHQAENAAVALAAVEVFfgAGTGHQLDLETVKRGFAQVQSPGRLERVR-ATPTTFIDAAHNPHGAKALAKAIDR 372
Cdd:TIGR01499 223 ALSLLGDHQQENAALALAALEVL--GKQNPKLSEEAIRQGLANTIWPGRLEILSeDNPNILLDGAHNPHSAEALAEWFKK 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 373 DFTFRRLIGVMACLGDKDVDGVLHELEPVLDEVV-CTVNTSPRCLPAEELAEKARAILGEERVHLAEtlpgavelAVELA 451
Cdd:TIGR01499 301 RFNGRPITLLFGALADKDAAAMLAPLKPVVDKEVfVTPFDYPRADDAADLAAFAEETGKSTVEDWRE--------ALEEA 372

                         410       420       430
                  ....*....|....*....|....*....|
gi 2468620722 452 EDPTEGDTvsgggILITGSVVTAGEARTLF 481
Cdd:TIGR01499 373 LNASAEDD-----ILVTGSLYLVGEVRKLL 397
PRK10846 PRK10846
bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional
 50-460 7.52e-38

bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional


Pssm-ID: 182774 [Multi-domain]  Cd Length: 416  Bit Score: 143.29  E-value: 7.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  50 IDPSLSRIAKLMDLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLVTERIGIDGEPIHPADYVR 129
Cdd:PRK10846   28 IDLGLERVSQVAARLDLLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYRVGVYSSPHLVRYTERVRIQGQELPESAHTA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 130 IWEEIKPyvemvdAEAEYPMSKFEVLTAMAFAAFADAPVDVGVVEVGMGGRWDATNVVHADVSVICPVGLDHQGMLGDTI 209
Cdd:PRK10846  108 SFAEIEA------ARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 210 AEIAGEKAGIikpkwdptdlLRPGPVTVIGkqDPDAMRVILEKAVEEDNSVARLGQEYgvtesTVAVGGQQLTIQGLGGT 289
Cdd:PRK10846  182 ESIGREKAGI----------FRAEKPAVVG--EPDMPSTIADVAQEKGALLQRRGVDW-----NYSVTDHDWAFSDGDGT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 290 YEDifLPLSGAHQAenaavalaavevffGAGT--------GHQLDLETVKRGFAQVQSPGRLERVRATPTTFIDAAHNPH 361
Cdd:PRK10846  245 LEN--LPLPNVPLP--------------NAATalaalrasGLEVSEQAIRDGIASAILPGRFQIVSESPRVILDVAHNPH 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 362 GAKALA---KAIDRDftfRRLIGVMACLGDKDVDGVLHELEPVLDEVVCTVNTSPRCLPAEELAEkarailgeervHLAE 438
Cdd:PRK10846  309 AAEYLTgrlKALPKN---GRVLAVIGMLHDKDIAGTLACLKSVVDDWYCAPLEGPRGATAEQLAE-----------HLGN 374

                         410       420
                  ....*....|....*....|....*..
gi 2468620722 439 tlpGAVELAVELA-----EDPTEGDTV 460
Cdd:PRK10846  375 ---GKSFDSVAQAwdaamADAKPEDTV 398
PLN02913 PLN02913
dihydrofolate synthetase
 54-470 3.41e-30

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 123.01  E-value: 3.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  54 LSRIAKLMDLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLVTERI--GIDGEPIHPADYVRIW 131
Cdd:PLN02913   58 LGRMRRLMDRLGNPHSKFKAVHVAGTKGKGSTAAFLSNILRAQGYSVGCYTSPHLRSIRERIsvGKLGKPVSTNTLNDLF 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 132 EEIKPYVEMVDAEAEYPMSKFEVLTAMAFAAFADAPVDVGVVEVGMGGRWDATNVVHAD---VSVICPVGLDHQGMLGDT 208
Cdd:PLN02913  138 HGIKPILDEAIQLENGSLTHFEVLTALAFKLFAQENVDIAVIEAGLGGARDATNVIDSSglaASVITTIGEEHLAALGGS 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 209 IAEIAGEKAGIIKpkwdptdllRPGPVTVIGKQDPDAMRVILEKAVEEDNSVarlgqeygVTESTVAVGGqqlTIQGL-- 286
Cdd:PLN02913  218 LESIALAKSGIIK---------QGRPVVLGGPFLPHIESILRDKASSMNSPV--------VSASDPGVRS---SIKGIit 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 287 --GGTYE-------------------DIFLPLSGAHQAENAAVALAAVEVFfgAGTGHQLDLETVKRGFAQVQSPGRLER 345
Cdd:PLN02913  278 dnGKPCQscdivirvekddplfielsDVNLRMLGSHQLQNAVTAACAALCL--RDQGWRISDASIRAGLENTNLLGRSQF 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 346 VRAT---------PTTFIDAAHNPHGAKALAKAIDRDFTFRRLIGVMACLGDKD--------VDGVlhELEPVLDEVVCT 408
Cdd:PLN02913  356 LTSKeaevlglpgATVLLDGAHTKESAKALVDTIKTAFPEARLALVVAMASDKDhlafasefLSGL--KPEAVFLTEADI 433

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468620722 409 VNTSPRCLPAEELAE---KARAILGEERVHLAE-TLPGAVELAVELAEDPTEGDtvSGGGILITGS 470
Cdd:PLN02913  434 AGGKSRSTSASALKEawiKAAPELGIETLLAENnSLLKSLVDASAILRKARTLD--PSSVVCVTGS 497
PLN02881 PLN02881
tetrahydrofolylpolyglutamate synthase
 54-302 6.17e-28

tetrahydrofolylpolyglutamate synthase


Pssm-ID: 215476  Cd Length: 530  Bit Score: 116.68  E-value: 6.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  54 LSRIAKLMDLLGHPEQASPM--IHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLVTERIGIDGEPIHPADYVR-- 129
Cdd:PLN02881   42 FDLLFDYLKILELEEAISRLkvIHVAGTKGKGSTCTFTESILRNCGFRTGLFTSPHLIDVRERFRLDGVDISEEKFLRyf 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 130 --IWEEIKPyvemvDAEAEYPM-SKFEVLTAMAFAAFADAPVDVGVVEVGMGGRWDATNVVHAdvSVICPV---GLDHQG 203
Cdd:PLN02881  122 wwCWDRLKE-----KTTEDLPMpAYFRFLTLLAFKIFSAEQVDVAILEVGLGGRLDATNVVQK--PVVCGItslGYDHME 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 204 MLGDTIAEIAGEKAGIIKPKWdPTdllrpgpVTVigKQDPDAMRVILEKAveednsvarlgQEYGVTESTVavggQQLTI 283
Cdd:PLN02881  195 ILGDTLGKIAGEKAGIFKPGV-PA-------FTV--PQPDEAMRVLEERA-----------SELGVPLQVV----EPLDS 249

                         250
                  ....*....|....*....
gi 2468620722 284 QGLGGtyedIFLPLSGAHQ 302
Cdd:PLN02881  250 YGLSG----LKLGLAGEHQ 264
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 54-390 7.93e-12

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: 67.03  E-value: 7.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  54 LSRIAKLmdLLGHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGrttsphlqLV-TERIGIDGEpIHPA-----DY 127
Cdd:COG0769    65 LALLAAA--FYGHPSQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTG--------LIgTVGNGIGGE-LIPSslttpEA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 128 VRIWEEIKpyvEMVDAEAEYpmskfevltamafaafadapvdvgvvevgmggrwdatnVV-----HA-----------DV 191
Cdd:COG0769   134 LDLQRLLA---EMVDAGVTH--------------------------------------VVmevssHAldqgrvdgvrfDV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 192 SVICPVGLDHqgmLgD---TIAEIAGEKAGIIkpkwdptDLLRPGPVTVIGKQDPDAmRVILEKAveeDNSVARLGQE-- 266
Cdd:COG0769   173 AVFTNLTRDH---L-DyhgTMEAYFAAKARLF-------DQLGPGGAAVINADDPYG-RRLAAAA---PARVITYGLKad 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 267 --YGVTESTVAVGGQQLTIQGLGGTYEdIFLPLSGAHQaenaavalaavevffgA-------GTGHQL--DLETVKRGFA 335
Cdd:COG0769   238 adLRATDIELSADGTRFTLVTPGGEVE-VRLPLIGRFN----------------VynalaaiAAALALgiDLEEILAALE 300

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 336 QVQS-PGRLERVRAT--PTTFIDAAHNPhgaKALAKAID--RDFTFRRLIGVMACLGDKD 390
Cdd:COG0769   301 KLKGvPGRMERVDGGqgPTVIVDYAHTP---DALENVLEalRPHTKGRLIVVFGCGGDRD 357
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
 340-414 5.06e-11

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: 58.89  E-value: 5.06e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468620722 340 PGRLERVRA--TPTTFIDAAHNPHGAKALAKAIdRDFTFRRLIGVMACLGDKDVD--GVLHELEPVLDEVVCTVNTSPR 414
Cdd:pfam02875   2 PGRLEVVGEnnGVLVIDDYAHNPDAMEAALRAL-RNLFPGRLILVFGGMGDRDAEfhALLGRLAAALADVVILTGDYPR 79
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
 65-390 9.51e-10

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 60.53  E-value: 9.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  65 GHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGrttsphlqLV-TERIGIDGEPIHPA----DYVRIWEEIKpyvE 139
Cdd:PRK00139   89 GHPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTA--------LIgTLGNGIGGELIPSGlttpDALDLQRLLA---E 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 140 MVDAEAEY-PMskfEV----LtamafaafadapvdvgvvevgMGGRWDATNVvhaDVSVICPVGLDHqgmLG--DTIAEI 212
Cdd:PRK00139  158 LVDAGVTYaAM---EVsshaL---------------------DQGRVDGLKF---DVAVFTNLSRDH---LDyhGTMEDY 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 213 AGEKAGIIKpkwdptdllRPGPVTVIGKQDPDAMRVILEKAVeedNSVARLGQEYGVTESTVAVGGQQLTIQGlggtyeD 292
Cdd:PRK00139  208 LAAKARLFS---------ELGLAAVINADDEVGRRLLALPDA---YAVSMAGADLRATDVEYTDSGQTFTLVT------E 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 293 IFLPLSGAHQAENAAValaavevffGAGTGHQL--DLETVKRGFAQVQS-PGRLERVRAT--PTTFIDAAHNPhgaKALA 367
Cdd:PRK00139  270 VESPLIGRFNVSNLLA---------ALAALLALgvPLEDALAALAKLQGvPGRMERVDAGqgPLVIVDYAHTP---DALE 337

                         330       340
                  ....*....|....*....|....*
gi 2468620722 368 KAID--RDFTFRRLIGVMACLGDKD 390
Cdd:PRK00139  338 KVLEalRPHAKGRLICVFGCGGDRD 362
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
 65-469 2.32e-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: 59.25  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722  65 GHPEQASPMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTSPHLQLVTERIGIDGEPIHPADYVRIWEEIKpyvEMVDAE 144
Cdd:TIGR01085  79 GHPSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDLIKNPAALTTPEALTLQSTLA---EMVEAG 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 145 AEYPMskFEVltamafaafadapvdvgVVEVGMGGRWDATNVvhaDVSVICPVGLDHQGMLGdTIAEIAGEKAGIIKPKW 224
Cdd:TIGR01085 156 AQYAV--MEV-----------------SSHALAQGRVRGVRF---DAAVFTNLSRDHLDFHG-TMENYFAAKASLFTELG 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 225 DPTDllrpgpvTVIGKQDP--DAMRVILEKA-------VEEDNSVARLGQeygvTESTVAVGGQQLTIQGLGGTYEdIFL 295
Cdd:TIGR01085 213 LKRF-------AVINLDDEygAQFVKRLPKDitvsaitQPADGRAQDIKI----TDSGYSFEGQQFTFETPAGEGH-LHT 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 296 PLSGAHQAENAAVALAAVEVFFGagtghqLDLETVKRGFAQVQS-PGRLERV--RATPTTFIDAAHNPhgaKALAKA--I 370
Cdd:TIGR01085 281 PLIGRFNVYNLLAALATLLHLGG------IDLEDIVAALEKFRGvPGRMELVdgGQKFLVIVDYAHTP---DALEKAlrT 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 371 DRDFTFRRLIGVMACLGDKDVdgvlhELEPVL--------DEVVCTvNTSPRCLPAEE-LAEKARAILGEERVHLAETLP 441
Cdd:TIGR01085 352 LRKHKDGRLIVVFGCGGDRDR-----GKRPLMgaiaeqlaDLVILT-SDNPRGEDPEQiIADILAGISEKEKVVIIADRR 425

                         410       420
                  ....*....|....*....|....*...
gi 2468620722 442 GAVELAVELAEDpteGDTVsgggiLITG 469
Cdd:TIGR01085 426 QAIRYAISNAKA---GDVV-----LIAG 445
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
 184-470 4.95e-06

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: 48.94  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 184 TNVVHADVSVICPVGLDHQGMLGdTIAEIAGEKAGIIKPkwdptdlLRPGPVTVIGKQDPDAMRVIlEKAveeDNSVARL 263
Cdd:COG0770   171 ARIARPDIAVITNIGPAHLEGFG-SLEGIARAKGEIFEG-------LPPGGVAVLNADDPLLAALA-ERA---KARVLTF 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 264 GQE----YGVTESTVAVGGQQLTIQGLGGTYEdIFLPLSGAHQaenaavalaavevF------FGAGTGHQLDLETVKRG 333
Cdd:COG0770   239 GLSedadVRAEDIELDEDGTRFTLHTPGGELE-VTLPLPGRHN-------------VsnalaaAAVALALGLDLEEIAAG 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 334 FAQVQ-SPGRLERVRATPT-TFIDAAHN--PHGAKAlakAIDrdfTFRRL---------IGVMACLGDKDVDgvLHE--- 397
Cdd:COG0770   305 LAAFQpVKGRLEVIEGAGGvTLIDDSYNanPDSMKA---ALD---VLAQLpgggrriavLGDMLELGEESEE--LHRevg 376

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468620722 398 ---LEPVLDEVVCTVntsprclpaeELAEKARAILGEERVHLAETLPgavELAVELAEDPTEGDTVsgggiLITGS 470
Cdd:COG0770   377 elaAELGIDRLFTVG----------ELARAIAEAAGGERAEHFEDKE---ELLAALKALLRPGDVV-----LVKGS 434
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
 318-392 1.71e-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: 47.39  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468620722 318 GAGTGHQLDLETVKRGFAQVQS-PGRLERVRAT-----PTTFIDAAHNPhgaKALAKAID-----RDFTFRRLIGVMACL 386
Cdd:PRK11929  317 AALKKLGLPLAQIARALAAVSPvPGRMERVGPTagaqgPLVVVDYAHTP---DALAKALTalrpvAQARNGRLVCVFGCG 393


                  ....*.
gi 2468620722 387 GDKDVD 392
Cdd:PRK11929  394 GDRDKG 399
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 72-126 2.33e-05

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 47.07  E-value: 2.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2468620722  72 PMIHVAGTNGKTSTVRMIESLLRAFSRRTGRTTsphlqlvTERIGIDGEPIHPAD 126
Cdd:PRK14016  481 PIVAVTGTNGKTTTTRLIAHILKLSGKRVGMTT-------TDGVYIDGRLIDKGD 528
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
 72-111 2.99e-03

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: 40.02  E-value: 2.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2468620722  72 PMIHVAGTNGKTSTVRMIESLLRAFSRRT---GRTTSPHLQLV 111
Cdd:TIGR01087 103 PVVAITGTNGKTTTTSLLYHLLKAAGLKAflgGNIGTPALEVL 145
Mur_ligase_M pfam08245
Mur ligase middle domain;
76-101 3.16e-03

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 38.82  E-value: 3.16e-03
                          10        20
                  ....*....|....*....|....*.
gi 2468620722  76 VAGTNGKTSTVRMIESLLRAFSRRTG 101
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIG 26
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
327-390 5.46e-03

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


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 39.25  E-value: 5.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468620722 327 LETVKRGFAQVQSPGRLERVraTPTT----FIDAAHNPHGAKALAKAIDrDFTFRRLIGVMACLGDKD 390
Cdd:PRK14022  315 LEDIQKGIAQTPVPGRMEVL--TQSNgakvFIDYAHNGDSLNKLIDVVE-EHQKGKLILLLGAAGNKG 379
 
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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