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Conserved domains on  [gi|518215315|ref|WP_019385523|]
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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase [Acinetobacter venetianus]

Protein Classification

Mur ligase family protein( domain architecture ID 11433679)

Mur ligase family protein such as MurC, MurD, and MurE, which catalyze consecutive steps in the synthesis of peptidoglycan

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
24-487 0e+00

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: 575.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  24 GFCLDSRKVEAGHIFIALNSFSQpeKTLQFAQNALDAGALIVISEAALGIEKE----WVCPEVRNLMGEWQKQYLQltDP 99
Cdd:COG0769    1 GITYDSRKVKPGDLFVALPGARV--DGHDFIAQAIARGAVAVVTEAPGALLAAgvpvIVVPDPRAALALLAAAFYG--HP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 100 TQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALEAS 179
Cdd:COG0769   77 SQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGGELIPSSLTTPEALDLQRLLAEMVDAGVTHVVMEVS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 180 SHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKF-KTLKAVVINLDDAHANIMLDAAQNnpsqpKILT 258
Cdd:COG0769  157 SHALDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQlGPGGAAVINADDPYGRRLAAAAPA-----RVIT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 259 YSLtQASADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQ 338
Cdd:COG0769  232 YGL-KADADLRATDIELSADGTRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRME 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 339 VIQ-DDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTENPEQI 417
Cdd:COG0769  311 RVDgGQGPTVIVDYAHTPDALENVLEALRPHTKGRLIVVFGCGGDRDRGKRPLMGEIAARLADVVIVTSDNPRSEDPAAI 390
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 418 FADMKQGIHFAQHTmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAA 487
Cdd:COG0769  391 IADILAGIPGAGKV-LVIPDRAEAIRYAIALAKPGDVVLIAGKGHETYQIIGGVKIPFDDREVAREALAE 459
 
Name Accession Description Interval E-value
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
24-487 0e+00

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: 575.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  24 GFCLDSRKVEAGHIFIALNSFSQpeKTLQFAQNALDAGALIVISEAALGIEKE----WVCPEVRNLMGEWQKQYLQltDP 99
Cdd:COG0769    1 GITYDSRKVKPGDLFVALPGARV--DGHDFIAQAIARGAVAVVTEAPGALLAAgvpvIVVPDPRAALALLAAAFYG--HP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 100 TQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALEAS 179
Cdd:COG0769   77 SQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGGELIPSSLTTPEALDLQRLLAEMVDAGVTHVVMEVS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 180 SHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKF-KTLKAVVINLDDAHANIMLDAAQNnpsqpKILT 258
Cdd:COG0769  157 SHALDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQlGPGGAAVINADDPYGRRLAAAAPA-----RVIT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 259 YSLtQASADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQ 338
Cdd:COG0769  232 YGL-KADADLRATDIELSADGTRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRME 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 339 VIQ-DDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTENPEQI 417
Cdd:COG0769  311 RVDgGQGPTVIVDYAHTPDALENVLEALRPHTKGRLIVVFGCGGDRDRGKRPLMGEIAARLADVVIVTSDNPRSEDPAAI 390
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 418 FADMKQGIHFAQHTmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAA 487
Cdd:COG0769  391 IADILAGIPGAGKV-LVIPDRAEAIRYAIALAKPGDVVLIAGKGHETYQIIGGVKIPFDDREVAREALAE 459
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
21-488 0e+00

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 539.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  21 PFKGFCLDSRKVEAGHIFIALNSFSQPEktLQFAQNALDAGALIVISEAALGIEKEW---VCPEVRNLMGEWQKQYLQlt 97
Cdd:PRK00139  14 EITGLTYDSRKVKPGDLFVALPGHKVDG--RDFIAQAIANGAAAVVAEADGEAGTGVpviIVPDLRKALALLAAAFYG-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  98 DPTQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALE 177
Cdd:PRK00139  90 HPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNGIGGELIPSGLTTPDALDLQRLLAELVDAGVTYAAME 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 178 ASSHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAvVINLDDAHANIMLDAAQnnpsqpkil 257
Cdd:PRK00139 170 VSSHALDQGRVDGLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLFSELGLAA-VINADDEVGRRLLALPD--------- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 258 TYSLTQASADYHIADLQYRLSGASFSLITPtgcyaVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRM 337
Cdd:PRK00139 240 AYAVSMAGADLRATDVEYTDSGQTFTLVTE-----VESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRM 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 338 QVIQDDER-LFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTENPEQ 416
Cdd:PRK00139 315 ERVDAGQGpLVIVDYAHTPDALEKVLEALRPHAKGRLICVFGCGGDRDKGKRPLMGAIAERLADVVIVTSDNPRSEDPAA 394
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518215315 417 IFADMKQGIHfaqhtmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAAQ 488
Cdd:PRK00139 395 IIADILAGIY------DVIEDRAEAIRYAIAQAKPGDVVLIAGKGHEDYQIIGGVKIPFDDREVAREALAER 460
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
23-477 3.69e-153

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: 444.45  E-value: 3.69e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315   23 KGFCLDSRKVEAGHIFIALNSfsQPEKTLQFAQNALDAGALIVISEAALGIEKEWVC----PEVRNLMGEWQKQYLQltD 98
Cdd:TIGR01085   5 TGLTLDSREVKPGDLFVAIKG--THVDGHDFIHDAIANGAVAVVVERDVDFYVAPVPviivPDLRHALSSLAAAFYG--H 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315   99 PTQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNL---TPSTHTTLDALQLQSALHDYAKQGASFVA 175
Cdd:TIGR01085  81 PSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDlikNPAALTTPEALTLQSTLAEMVEAGAQYAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  176 LEASSHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHANIMLDAAqnnpsqP 254
Cdd:TIGR01085 161 MEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLFTELGLKRFaVINLDDEYGAQFVKRL------P 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  255 KILTYSLTQASADYHIADLQ-----YRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAG-FALDKLVQFVP 328
Cdd:TIGR01085 235 KDITVSAITQPADGRAQDIKitdsgYSFEGQQFTFETPAGEGHLHTPLIGRFNVYNLLAALATLLHLGgIDLEDIVAALE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  329 QLQGAPGRMQVIQ-DDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSD 407
Cdd:TIGR01085 315 KFRGVPGRMELVDgGQKFLVIVDYAHTPDALEKALRTLRKHKDGRLIVVFGCGGDRDRGKRPLMGAIAEQLADLVILTSD 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  408 NPRTENPEQIFADMKQGIHFAQHTmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDD 477
Cdd:TIGR01085 395 NPRGEDPEQIIADILAGISEKEKV-VIIADRRQAIRYAISNAKAGDVVLIAGKGHEDYQIIGGETIPFDD 463
Mur_ligase_M pfam08245
Mur ligase middle domain;
108-313 2.52e-64

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 207.16  E-value: 2.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  108 VTGTNGKTTISRLIAELITSQhhgCAVMGTTGNGILPnltpSTHTTLDALQLQSALHDYAKQGASFVALEASSHGLEQGR 187
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLA---GGVIGTIGTYIGK----SGNTTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGEGR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  188 LNG-CDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHANIMLDAAQNNPSqpKILTYSLtQAS 265
Cdd:pfam08245  74 LSGlLKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIaVINADDPYGAFLIAKLKKAGV--RVITYGI-EGE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 518215315  266 ADYHIADLQYRLSGASFSLI-TPTGCYAVQSPLLGHFNVENLLASLIAA 313
Cdd:pfam08245 151 ADLRAANIELSSDGTSFDLFtVPGGELEIEIPLLGRHNVYNALAAIAAA 199
 
Name Accession Description Interval E-value
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
24-487 0e+00

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: 575.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  24 GFCLDSRKVEAGHIFIALNSFSQpeKTLQFAQNALDAGALIVISEAALGIEKE----WVCPEVRNLMGEWQKQYLQltDP 99
Cdd:COG0769    1 GITYDSRKVKPGDLFVALPGARV--DGHDFIAQAIARGAVAVVTEAPGALLAAgvpvIVVPDPRAALALLAAAFYG--HP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 100 TQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALEAS 179
Cdd:COG0769   77 SQKLKLIGVTGTNGKTTTTYLLAQILRALGKKTGLIGTVGNGIGGELIPSSLTTPEALDLQRLLAEMVDAGVTHVVMEVS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 180 SHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKF-KTLKAVVINLDDAHANIMLDAAQNnpsqpKILT 258
Cdd:COG0769  157 SHALDQGRVDGVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQlGPGGAAVINADDPYGRRLAAAAPA-----RVIT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 259 YSLtQASADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQ 338
Cdd:COG0769  232 YGL-KADADLRATDIELSADGTRFTLVTPGGEVEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRME 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 339 VIQ-DDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTENPEQI 417
Cdd:COG0769  311 RVDgGQGPTVIVDYAHTPDALENVLEALRPHTKGRLIVVFGCGGDRDRGKRPLMGEIAARLADVVIVTSDNPRSEDPAAI 390
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 418 FADMKQGIHFAQHTmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAA 487
Cdd:COG0769  391 IADILAGIPGAGKV-LVIPDRAEAIRYAIALAKPGDVVLIAGKGHETYQIIGGVKIPFDDREVAREALAE 459
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
21-488 0e+00

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 539.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  21 PFKGFCLDSRKVEAGHIFIALNSFSQPEktLQFAQNALDAGALIVISEAALGIEKEW---VCPEVRNLMGEWQKQYLQlt 97
Cdd:PRK00139  14 EITGLTYDSRKVKPGDLFVALPGHKVDG--RDFIAQAIANGAAAVVAEADGEAGTGVpviIVPDLRKALALLAAAFYG-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  98 DPTQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALE 177
Cdd:PRK00139  90 HPSDKLKLIGVTGTNGKTTTAYLLAQILRLLGEKTALIGTLGNGIGGELIPSGLTTPDALDLQRLLAELVDAGVTYAAME 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 178 ASSHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAvVINLDDAHANIMLDAAQnnpsqpkil 257
Cdd:PRK00139 170 VSSHALDQGRVDGLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLFSELGLAA-VINADDEVGRRLLALPD--------- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 258 TYSLTQASADYHIADLQYRLSGASFSLITPtgcyaVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRM 337
Cdd:PRK00139 240 AYAVSMAGADLRATDVEYTDSGQTFTLVTE-----VESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRM 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 338 QVIQDDER-LFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTENPEQ 416
Cdd:PRK00139 315 ERVDAGQGpLVIVDYAHTPDALEKVLEALRPHAKGRLICVFGCGGDRDKGKRPLMGAIAERLADVVIVTSDNPRSEDPAA 394
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518215315 417 IFADMKQGIHfaqhtmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAAQ 488
Cdd:PRK00139 395 IIADILAGIY------DVIEDRAEAIRYAIAQAKPGDVVLIAGKGHEDYQIIGGVKIPFDDREVAREALAER 460
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
23-477 3.69e-153

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: 444.45  E-value: 3.69e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315   23 KGFCLDSRKVEAGHIFIALNSfsQPEKTLQFAQNALDAGALIVISEAALGIEKEWVC----PEVRNLMGEWQKQYLQltD 98
Cdd:TIGR01085   5 TGLTLDSREVKPGDLFVAIKG--THVDGHDFIHDAIANGAVAVVVERDVDFYVAPVPviivPDLRHALSSLAAAFYG--H 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315   99 PTQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNL---TPSTHTTLDALQLQSALHDYAKQGASFVA 175
Cdd:TIGR01085  81 PSKKLKVIGVTGTNGKTTTTSLIAQLLRLLGKKTGLIGTIGYRLGGNDlikNPAALTTPEALTLQSTLAEMVEAGAQYAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  176 LEASSHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHANIMLDAAqnnpsqP 254
Cdd:TIGR01085 161 MEVSSHALAQGRVRGVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLFTELGLKRFaVINLDDEYGAQFVKRL------P 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  255 KILTYSLTQASADYHIADLQ-----YRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAG-FALDKLVQFVP 328
Cdd:TIGR01085 235 KDITVSAITQPADGRAQDIKitdsgYSFEGQQFTFETPAGEGHLHTPLIGRFNVYNLLAALATLLHLGgIDLEDIVAALE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  329 QLQGAPGRMQVIQ-DDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSD 407
Cdd:TIGR01085 315 KFRGVPGRMELVDgGQKFLVIVDYAHTPDALEKALRTLRKHKDGRLIVVFGCGGDRDRGKRPLMGAIAEQLADLVILTSD 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  408 NPRTENPEQIFADMKQGIHFAQHTmHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDD 477
Cdd:TIGR01085 395 NPRGEDPEQIIADILAGISEKEKV-VIIADRRQAIRYAISNAKAGDVVLIAGKGHEDYQIIGGETIPFDD 463
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
27-487 4.22e-139

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: 424.50  E-value: 4.22e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  27 LDSRKVEAGHIFIALNSFSQPEKtlQFAQNALDAGALIVISEA-------ALGIEKEWVcPEVRNLMGEWQKQYLqlTDP 99
Cdd:PRK11929  34 LDSREVQPGDLFVACRGAASDGR--AFIDQALARGAAAVLVEAegedqvaAADALVLPV-ADLRKALGELAARWY--GRP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 100 TQPLRGIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALEAS 179
Cdd:PRK11929 109 SEQLSLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTLGARLDGRLIPGSLTTPDAIILHRILARMRAAGADAVAMEAS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 180 SHGLEQGRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLF-KFKTLKAVVINLDDAHANIMLDAaqnNPSQPKILt 258
Cdd:PRK11929 189 SHGLEQGRLDGLRIAVAGFTNLTRDHLDYHGTMQDYEEAKAALFsKLPGLGAAVINADDPAAARLLAA---LPRGLKVG- 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 259 YSLTQASADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQ 338
Cdd:PRK11929 265 YSPQNAGADVQARDLRATAHGQVFTLATPDGSYQLVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSPVPGRME 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 339 VIQDDER----LFVVDYAHTPDALIQVLTTLK---RHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRT 411
Cdd:PRK11929 345 RVGPTAGaqgpLVVVDYAHTPDALAKALTALRpvaQARNGRLVCVFGCGGDRDKGKRPEMGRIAAELADRVVVTSDNPRS 424
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518215315 412 ENPEQIFADMKQGIHfAQHTMHEIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEIDGVRHWFDDVVEVQSAIAA 487
Cdd:PRK11929 425 EAPEAIIDQILAGIP-AGARVFVISDRAEAIRQAIWMAAPGDVILIAGKGHETYQEIGGRKLFFDDREWARRALLA 499
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
28-472 7.09e-73

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


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 238.78  E-value: 7.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  28 DSRKVEAGHIFIALNSFSQPEktlqFAQNALDAGALIVISEA--ALGIEKEWVcPEVRNLMGEWQKQYLQltDPTQPLRG 105
Cdd:PRK14022  40 DSRTADEGTLFFAKGAYFKHK----FLQNAITQGLKLYVSEKdyEVGIPQVIV-PDIKKAMSLIAMEFYD--NPQHKLKL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNGILPNLTPSTHTTLDALQLQSALHDYAKQGASFVALEASSHGLEQ 185
Cdd:PRK14022 113 LAFTGTKGKTTAAYFAYHILKQLHKPAMLSTMNTTLDGETFFKSALTTPESLDLFKMMAEAVDNGMTHLIMEVSSQAYLV 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 186 GRLNGCDLEIAVYSNLSRDHLDY--HGTLEAYAEAKALLFKFKtlKAVVINLDDAHANIMLDAAQNNPsqpkILTYSLTQ 263
Cdd:PRK14022 193 GRVYGLTFDVGVFLNITPDHIGPieHPTFEDYFYHKRLLMENS--KAVVVNSDMDHFSELLEQVTPQE----HDFYGIDS 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 264 asadyhiaDLQYRLSGAsFSLIT---PTGCYAVQspLLGHFNVENLLASLIAAECAGFALDKLVQFVPQlQGAPGRMQVI 340
Cdd:PRK14022 267 --------ENQIMASNA-FSFEAtgkLAGTYDIQ--LIGKFNQENAMAAGLACLRLGASLEDIQKGIAQ-TPVPGRMEVL 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 341 -QDDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHAN-PVILTSDNPRTENPEQIF 418
Cdd:PRK14022 335 tQSNGAKVFIDYAHNGDSLNKLIDVVEEHQKGKLILLLGAAGNKGESRRPDFGRVANRHPYlQVILTADDPNNEDPKMIT 414
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518215315 419 ADMKQGIHfaqHTMHEIHDRREAIKFVVAQA-RSGDIVVIAGKGHENYQEIDGVR 472
Cdd:PRK14022 415 QEIASHIT---HPVEIIDDRAEAIKHAMSITeGPGDAVIIAGKGADAYQIVPGHR 466
Mur_ligase_M pfam08245
Mur ligase middle domain;
108-313 2.52e-64

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 207.16  E-value: 2.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  108 VTGTNGKTTISRLIAELITSQhhgCAVMGTTGNGILPnltpSTHTTLDALQLQSALHDYAKQGASFVALEASSHGLEQGR 187
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLA---GGVIGTIGTYIGK----SGNTTNNAIGLPLTLAEMVEAGAEYAVLEVSSHGLGEGR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  188 LNG-CDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHANIMLDAAQNNPSqpKILTYSLtQAS 265
Cdd:pfam08245  74 LSGlLKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIaVINADDPYGAFLIAKLKKAGV--RVITYGI-EGE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 518215315  266 ADYHIADLQYRLSGASFSLI-TPTGCYAVQSPLLGHFNVENLLASLIAA 313
Cdd:pfam08245 151 ADLRAANIELSSDGTSFDLFtVPGGELEIEIPLLGRHNVYNALAAIAAA 199
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
1-378 2.67e-38

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: 145.24  E-value: 2.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315   1 MSISFQQIHPIsIDAAWYTQP---FKGFCLDSRKVEAGHIFIALnsfsQPEKT--LQFAQNALDAGALIVISEAALGIEK 75
Cdd:COG0770    1 ILLTLAEIAEA-TGGRLIGDPdlvVTGVSTDSRKIKPGDLFVAL----KGERFdgHDFVAQALAKGAAAALVSRPLPADL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  76 E-WVCPEVRNLMGEWQKQYLQLTDPtqPLrgIAVTGTNGKTTISRLIAELITSQHHGCAvmgTTGN-----GiLPnLTps 149
Cdd:COG0770   76 PlIVVDDTLKALQQLAAAHRARFNI--PV--IAITGSNGKTTTKEMLAAVLSTKGKVLA---TPGNfnneiG-VP-LT-- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 150 thttldALQLQSAlHDYAkqgasfVaLEAS-SHGLEQGRLngCDL---EIAVYSNLSRDHLDYHGTLEAYAEAKALLFKF 225
Cdd:COG0770  145 ------LLRLPED-HEFA------V-LEMGmNHPGEIAYL--ARIarpDIAVITNIGPAHLEGFGSLEGIARAKGEIFEG 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 226 ktLKA---VVINLDDAHANIMLDAAQNnpsqpKILTYSLtQASADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFN 302
Cdd:COG0770  209 --LPPggvAVLNADDPLLAALAERAKA-----RVLTFGL-SEDADVRAEDIELDEDGTRFTLHTPGGELEVTLPLPGRHN 280
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518215315 303 VENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQVIQDDERLFVVD--YAHTPDALIQVLTTLKR-HVNGQLWAVFG 378
Cdd:COG0770  281 VSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLEVIEGAGGVTLIDdsYNANPDSMKAALDVLAQlPGGGRRIAVLG 359
murF TIGR01143
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ...
27-459 1.28e-33

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the strictly bacterial MurF gene of peptidoglycan biosynthesis. This enzyme is almost always UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanyl ligase, but in a few species, MurE adds lysine rather than diaminopimelate. This enzyme acts on the product from MurE activity, and so is also subfamily rather than equivalog. Staphylococcus aureus is an example of species in this MurF protein would differ. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273468 [Multi-domain]  Cd Length: 417  Bit Score: 131.62  E-value: 1.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315   27 LDSRKVEAGHIFIAL--NSFSqpekTLQFAQNALDAGAliviseAALGIEKEWVCPEV---------RNLMGEWQKQYLQ 95
Cdd:TIGR01143   1 TDSRAIKPGDLFIALkgERFD----GHDFVEQALAAGA------VAVVVDREVGPDNGlpqilvddtLEALQALARAKRA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315   96 LTdptqPLRGIAVTGTNGKTTISRLIAELItsQHHGcAVMGTTGN-----GILPNLtpsthttldaLQLqSALHDYAkqg 170
Cdd:TIGR01143  71 KF----SGKVIGITGSSGKTTTKEMLAAIL--SHKY-KVFATPGNfnneiGLPLTL----------LRA-PGDHDYA--- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  171 asFVALEASSHGlEQGRLngCDL---EIAVYSNLSRDHLDYHGTLEAYAEAKALLFK-FKTLKAVVINLDDAHaniMLDA 246
Cdd:TIGR01143 130 --VLEMGASHPG-EIAYL--AEIakpDIAVITNIGPAHLEGFGSLEGIAEAKGEILQgLKENGIAVINADDPA---FADL 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  247 AQNNPsQPKILTYSLTqaSADYHIADLQYR-LSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQ 325
Cdd:TIGR01143 202 AKRLP-NRNILSFGFE--GGDFVAKDISYSaLGSTSFTLVAPGGEFEVSLPLLGRHNVMNALAAAALALELGIPLEEIAE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  326 FVPQLQGAPGRMQVIQDDERLFVVD-YAHTPDALIQVLTTLKrHVNGQLWAVFG----CGGDRDRGKRPLMTQAALDHAN 400
Cdd:TIGR01143 279 GLAELKLVKGRFEVQTKNGLTLIDDtYNANPDSMRAALDALA-RFPGKKILVLGdmaeLGEYSEELHAEVGRYANSLGID 357
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 518215315  401 PVILTSDNPRTEnpEQIFAdmKQGIHFAQHTmheihdrrEAIKFVVAQARSGDIVVIAG 459
Cdd:TIGR01143 358 LVFLVGEEAAVI--YDSFG--KQGKHFADKD--------ELLAFLKTLVRKGDVVLVKG 404
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
104-461 3.52e-31

UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440536 [Multi-domain]  Cd Length: 451  Bit Score: 125.18  E-value: 3.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 104 RGIAVTGTNGKTTISRLIAELItsQHHGC---AVMGttgnGILPNLTPSthttldalqlqsalhdyAKQGAS--FVAlEA 178
Cdd:COG0773  105 RSIAVAGTHGKTTTTSMLAHIL--EEAGLdptFLIG----GILNNFGTN-----------------ARLGDGdyFVA-EA 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 179 ----SSHgleqgrlngcdL----EIAVYSNLSRDHLDYHGTLEAYAEA-KALLFKFKTLKAVVINLDDAHANIMLDAAqn 249
Cdd:COG0773  161 desdGSF-----------LhyspDIAVVTNIEADHLDIYGDLEAIKEAfHEFARNVPFYGLLVLCADDPGLRELLPRC-- 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 250 npsQPKILTYSLTqASADYHIADLQYRLSGASFSLITPTGCYA-VQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVP 328
Cdd:COG0773  228 ---GRPVITYGFS-EDADYRAENIRIDGGGSTFDVLRRGEELGeVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALA 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 329 QLQGAPGRMQVIQDDERLFVV-DYAHTPDALIQVLTTLKRHV-NGQLWAVFgcggdrdrgkRP---LMTQA-------AL 396
Cdd:COG0773  304 SFKGVKRRFELKGEVGGVTVIdDYAHHPTEIAATLAAAREKYpDRRLVAVF----------QPhrySRTRDfldefaeAL 373
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518215315 397 DHANPVILTSDNPRTENP------EQIFADMKQGIHFAQHtmheIHDRREAIKFVVAQARSGDIVVIAGKG 461
Cdd:COG0773  374 SLADEVILLDIYAAREKPipgvssEDLAEAIRKRGKDVVY----VPDLDELVEALAEIARPGDVVLTMGAG 440
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
106-455 5.20e-30

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: 121.73  E-value: 5.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELItsQHHGC-AVMGttGN-GilpnlTPsthtTLDALqLQSALHDYakqgasfVALEASSHGL 183
Cdd:COG0771  108 IAITGTNGKTTTTTLIGHIL--KAAGLrVAVG--GNiG-----TP----LLDLL-LEPEPPDV-------YVLELSSFQL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 184 EqgRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKF-KTLKAVVINLDDAHANIMLDAAqnnpsQPKILTYSLT 262
Cdd:COG0771  167 E--TTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANqTPDDYAVLNADDPLTRALAEEA-----KARVVPFSLK 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 263 Q-ASADYHIAD--LQYRLSGASFslitptgCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQV 339
Cdd:COG0771  240 EpLEGGAGLEDgkLVDRASGEEL-------LPVDDLRLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLEF 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 340 I-QDDERLFVVD-YAHTPDALIQVLTTLKRHVngqlwaVFGCGGDrDRG--KRPLMtQAALDHANPVILT-SDNPRtenp 414
Cdd:COG0771  313 VaEINGVRFINDsKATNPDATLAALESFDGPV------VLIAGGL-DKGadFSPLA-PAVAERVKAVVLIgEDAEK---- 380
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 518215315 415 eqiFADMKQGIHFAqhtMHEIHDRREAIKFVVAQARSGDIV 455
Cdd:COG0771  381 ---IAAALAGAGVP---VVIVETMEEAVAAAAELARPGDVV 415
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
106-458 3.41e-28

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: 116.29  E-value: 3.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  106 IAVTGTNGKTTISRLIAELItsQHHGC-AVMGttGN-GILPnltpsthttLDALqlqsalhdyAKQGASFVALEASSHGL 183
Cdd:TIGR01087 105 VAITGTNGKTTTTSLLYHLL--KAAGLkAFLG--GNiGTPA---------LEVL---------DQEGAELYVLELSSFQL 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  184 EqgRLNGCDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHAnimldAAQNNPSQPKILTYSLT 262
Cdd:TIGR01087 163 E--TTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVaVLNADDPRF-----ARLAQKSKAQVIWFSVE 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  263 QAsADYHIADLQYRLSGASFSLItptgcyavqSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRMQVI-Q 341
Cdd:TIGR01087 236 KD-AERGLCIRDGGLYLKPNDLE---------GSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVgQ 305
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  342 DDERLFVVDYAHT-PDALIQVLTTLKRHVNgqlWAVfgCGGDRDRGKRPLMTQAALDHANPVILTSDNPrtenpeQIFAD 420
Cdd:TIGR01087 306 KNGVHFYNDSKATnVHATLAALSAFDNPVI---LIV--GGDDKGADFSPLAPAAAGKVKAVLAIGEDAA------KIAPL 374
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 518215315  421 MKQGIHFAQ--HTMheihdrREAIKFVVAQARSGDIVVIA 458
Cdd:TIGR01087 375 LKEAGLSVYlvESL------EEAVQAAREVASPGDVVLLS 408
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
334-418 1.87e-23

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: 93.95  E-value: 1.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  334 PGRMQVIQDDER-LFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMTQAALDHANPVILTSDNPRTE 412
Cdd:pfam02875   2 PGRLEVVGENNGvLVIDDYAHNPDAMEAALRALRNLFPGRLILVFGGMGDRDAEFHALLGRLAAALADVVILTGDYPRAE 81

                  ....*.
gi 518215315  413 NPEQIF 418
Cdd:pfam02875  82 DPGAII 87
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
96-459 7.52e-23

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: 100.56  E-value: 7.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  96 LTDPTQPLRGIAVTGTNGKTTISRLIAELItsQHHGCavmgTTG------------------------------------ 139
Cdd:COG0285   33 LGNPQRKLPVIHVAGTNGKGSTAAMLESIL--RAAGY----RVGlytsphlvrfneriringepisdeelvealeevepa 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 140 NGILPNLTPST--HTTLDALQLqsalhdYAKQGASFVALEAsshGLEqGRL---NGCDLEIAVYSNLSRDHLDYHG-TLE 213
Cdd:COG0285  107 VEEVDAGPPTFfeVTTAAAFLY------FAEAPVDVAVLEV---GLG-GRLdatNVIDPLVSVITSIGLDHTDFLGdTLE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 214 AYAEAKALLFKFKTlKAVVINLDDAHANIMLDAAQNNPSQpkiltysLTQASADYHIADLQyrlsGASFSLITPTGCYA- 292
Cdd:COG0285  177 EIAREKAGIIKPGV-PVVTGDQQPEALEVIEERAAELGAP-------LYRAGRDFSVEERE----GAVFSYQGPGGEYEd 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 293 VQSPLLGHFNVENLLASLIAAEcagfALDKLVQFVPQ------LQGA--PGRMQVIQDDeRLFVVDYAHTPDALIQVLTT 364
Cdd:COG0285  245 LPLPLLGAHQAENAALALAALE----ALRELGLPISEeairegLANArwPGRLEVLSRG-PLVILDGAHNPAGARALAET 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 365 LKRH-VNGQLWAVFGCGGDRDRGKrplMTQAALDHANPVILTS-DNPRTENPEQIFADMKQgihfAQHTMHEIHDRREAI 442
Cdd:COG0285  320 LKELfPFRKLHLVFGMLADKDIEG---MLAALAPLADEVIVTTpPSPRALDAEELAEAARE----LGLRVEVAPDVEEAL 392
                        410
                 ....*....|....*..
gi 518215315 443 KFVVAQARSGDIVVIAG 459
Cdd:COG0285  393 EAALELADPDDLILVTG 409
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
28-367 4.29e-22

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: 100.16  E-value: 4.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  28 DSRKVEAGHIFIAL--NSFSQPEktlqFAQNALDAGAliviseAALGIEKEW--------VCPEVRNLMGEWQKQYL-QL 96
Cdd:PRK11929 532 DSRSVGRGELFVALrgENFDGHD----YLPQAFAAGA------CAAVVERQVadvdlpqiVVDDTRAALGRLATAWRaRF 601
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  97 TDPTqplrgIAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGNgiLPNLT--PsthttLDALQLQsalhdyAKQGASFV 174
Cdd:PRK11929 602 SLPV-----VAITGSNGKTTTKEMIAAILAAWQGEDRVLATEGN--FNNEIgvP-----LTLLRLR------AQHRAAVF 663
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 175 ALEASSHGlEQGRLNG-CDLEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAV-VINLDDAHANIMLDAAqnnpS 252
Cdd:PRK11929 664 ELGMNHPG-EIAYLAAiAAPTVALVTNAQREHQEFMHSVEAVARAKGEIIAALPEDGVaVVNGDDPYTAIWAKLA----G 738
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 253 QPKILTYSLTQASADYH---IADLQ-YRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVP 328
Cdd:PRK11929 739 ARRVLRFGLQPGADVYAekiAKDISvGEAGGTRCQVVTPAGSAEVYLPLIGEHNLRNALAAIACALAAGASLKQIRAGLE 818
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 518215315 329 QLQGAPGRMQVIQDDERLFVVD--YAHTPDAL---IQVLTTLKR 367
Cdd:PRK11929 819 RFQPVAGRMQRRRLSCGTRIIDdtYNANPDSMraaIDVLAELPN 862
cya_phycin_syn TIGR02068
cyanophycin synthetase; Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and ...
106-474 2.90e-21

cyanophycin synthetase; Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and energy, found in most Cyanobacteria. The polymer has a backbone of L-aspartic acid, with most Asp side chain carboxyl groups attached to L-arginine. The polymer is made by this enzyme, cyanophycin synthetase, and degraded by cyanophycinase. Heterologously expressed cyanophycin synthetase in E. coli produces a closely related, water-soluble polymer with some Arg replaced by Lys. It is unclear whether enzymes that produce soluble cyanophycin-like polymers in vivo in non-Cyanobacterial species should be designated as cyanophycin synthetase itself or as a related enzyme. This model makes the designation as cyanophycin synthetase. Cyanophycin synthesis is analogous to polyhydroxyalkanoic acid (PHA) biosynthesis, except that PHA polymers lack nitrogen and may be made under nitrogen-limiting conditions. [Cellular processes, Biosynthesis of natural products]


Pssm-ID: 273950 [Multi-domain]  Cd Length: 864  Bit Score: 97.54  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  106 IAVTGTNGKTTISRLIAELItsQHHGCAVMGTTGNGIL---------PNLTPST------HTTLDALQLQSALHDYAKQG 170
Cdd:TIGR02068 482 VSVTGTNGKTTTTRLVAHIL--KQTGKVVGMTTTDGVYigkylvekgDNTGPASarrilmDPTVDAAVLETARGGILREG 559
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  171 ASFvaleasshgleqgrlNGCDleIAVYSNLSRDHL--DYHGTLEAYAEAKALLFKF-KTLKAVVINLDDAHANIMLDAA 247
Cdd:TIGR02068 560 LAF---------------DRCD--VGVVTNIAGDHLgiGDINTIEDLADVKRVVVEVvLPDGYAVLNADDPMVAAMAEKC 622
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  248 QN-------NPSQPKILTYSLTQASADYHIADlqyRLSGASFSLITPTGcYAVQSPL-LGH---FNVENLLASLIAAECA 316
Cdd:TIGR02068 623 KGkiayfsmDPNNPTVAAHIADGGRAVYYENG---YIVIARGGDEVAIA-RIAAIPLtMGGrvaFQIENALAAVAAAWAL 698
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  317 GFALDKLVQ----FVPQLQGAPGRMQVIQDDERLFVVDYAHTPDALIQVLTTLKRHVNGQLWAVFGCGGDRDRGKRPLMT 392
Cdd:TIGR02068 699 GVPIELIRAgirtFDADAAQAPGRFNLFNLGGAHVLVDYGHNPAAIEAVGAAIRNWPARRRIGVIGGPGDRRDEDLVEQG 778
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  393 QAALDHANPVILTSDNPRTENPE-QIFADMKQGIHFAQHTMH--EIHDRREAIKFVVAQARSGDIVVIAGKGHENYQEID 469
Cdd:TIGR02068 779 ELLGGAFDQIILKEDDDVRGRPRgEAAALLRQGLRQSARKAAieDILDETEAIAAALDDLRAGDLVVIFPESVERAIKLI 858

                  ....*
gi 518215315  470 GVRHW 474
Cdd:TIGR02068 859 LVRVW 863
murF PRK10773
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
28-350 5.99e-19

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed


Pssm-ID: 182718 [Multi-domain]  Cd Length: 453  Bit Score: 89.32  E-value: 5.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  28 DSRKVEAGHIFIALnsfsQPEK--TLQFAQNALDAGALIVISEAALGIEkewvCPEV-----RNLMGE---WQKQylqlt 97
Cdd:PRK10773  30 DTRKVTPGCLFVAL----KGERfdAHDFADDAKAAGAGALLVSRPLDID----LPQLvvkdtRLAFGQlaaWVRQ----- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  98 dpTQPLRGIAVTGTNGKTTISRLIAElITSQhhgCA-VMGTTGN-----GI---LPNLTPSthttldalqlqsalHDYA- 167
Cdd:PRK10773  97 --QVPARVVALTGSSGKTSVKEMTAA-ILRQ---CGnTLYTAGNlnndiGVpltLLRLTPE--------------HDYAv 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 168 -KQGASFVALEASSHGLEQGrlngcdlEIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKAVVI-NLDD---AHAni 242
Cdd:PRK10773 157 iELGANHQGEIAYTVSLTRP-------EAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPENGIAImNADSndwLNW-- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 243 mldaaQNNPSQPKILTYSLTQA-SADYHIADLQYRLSGASFSLITPTGCYAVQSPLLGHFNVENLLASLIAAECAGFALD 321
Cdd:PRK10773 228 -----QSVIGSKTVWRFSPNAAnSVDFTATNIHVTSHGTEFTLHTPTGSVDVLLPLPGRHNIANALAAAALAMSVGATLD 302
                        330       340
                 ....*....|....*....|....*....
gi 518215315 322 KLVQFVPQLQGAPGRMQVIQDDERLFVVD 350
Cdd:PRK10773 303 AVKAGLANLKAVPGRLFPIQLAEGQLLLD 331
murC TIGR01082
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ...
104-461 4.72e-15

UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial peptidoglycan (murein) biosynthesis. In a few species (Mycobacterium leprae, the Chlamydia), the amino acid may be L-serine or glycine instead of L-alanine. A related protein, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (murein tripeptide ligase) is described by model TIGR01081. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273433 [Multi-domain]  Cd Length: 448  Bit Score: 77.35  E-value: 4.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  104 RGIAVTGTNGKTTISRLIAELItsQHHG---CAVMGttgnGILPNLTPSTHTtldalqlqsalhdyaKQGASFV--ALEA 178
Cdd:TIGR01082 100 HSIAVAGTHGKTTTTAMIAVIL--KEAGldpTVVVG----GLVKEAGTNARL---------------GSGEYLVaeADES 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  179 SSHGLEQGRlngcdlEIAVYSNLSRDHLD-YHGTLEAYAEAkalLFKF----KTLKAVVINLDDAHANIMLDAAQNnpsq 253
Cdd:TIGR01082 159 DASFLHLQP------NVAIVTNIEPDHLDtYGSSFERLKAA---FEKFihnlPFYGLAVICADDPVLRELVPKATE---- 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  254 pKILTYSLTQASADYHIADLQYRLSGASFSLITP-TGCYAVQSPLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQG 332
Cdd:TIGR01082 226 -QVITYGGSGEDADYRAENIQQSGAEGKFSVRGKgKLYLEFTLNLPGRHNVLNALAAIAVALELGIDFEAILRALANFQG 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  333 APGRMQVIQDDERLFVVD-YAHTPDALIQVLTTLKRHVNGQ-LWAVFgcggdrdRGKRPLMTQA-------ALDHANPVI 403
Cdd:TIGR01082 305 VKRRFEILGEFGGVLLIDdYAHHPTEIKATLKAARQGYPDKrIVVVF-------QPHRYSRTRDlfddfakVLSDADELI 377
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518215315  404 LTSDNPRTENP------EQIFADMKQGIHFaqhTMHEIHDRREAIKFVVAQARSGDIVVIAGKG 461
Cdd:TIGR01082 378 LLDIYAAGEEPingidgKSLARKITQLGKI---EPYFVPDLAELVEFLAAVLQSGDLILTMGAG 438
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
106-367 8.29e-13

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 70.38  E-value: 8.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELITSQHHGCAVMGTTGngilpnltpsthttldaLQLQSALHDYAKQGAsFVAlEASSHGLE- 184
Cdd:PRK14106 111 VAITGTNGKTTTTTLLGEIFKNAGRKTLVAGNIG-----------------YPLIDAVEEYGEDDI-IVA-EVSSFQLEt 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 185 --QGRLNgcdleIAVYSNLSRDHLDYHGTLEAYAEAKALLFKFKTLKA-VVINLDDAhanIMLDAAQNNPSQpkILTYSL 261
Cdd:PRK14106 172 ikEFKPK-----VGCILNITPDHLDRHKTMENYIKAKARIFENQRPSDyTVLNYDDP---RTRSLAKKAKAR--VIFFSR 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 262 TqasadyHIADLQYRLSGASFSLITPTGCYAVQS----PLLGHFNVENLLASLIAAECAGFALDKLVQFVPQLQGAPGRM 337
Cdd:PRK14106 242 K------SLLEEGVFVKNGKIVISLGGKEEEVIDideiFIPGEHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRI 315
                        250       260       270
                 ....*....|....*....|....*....|..
gi 518215315 338 QVIQDDER-LFVVDYAHT-PDALIQVLTTLKR 367
Cdd:PRK14106 316 EFVAEINGvKFINDSKGTnPDAAIKALEAYET 347
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
91-384 3.59e-09

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: 58.45  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315   91 KQYLQ-LTDPTQPLRGIAVTGTNGKTTISRLIAELI----------TSQHhgcaVMGTTG----NGIlpNLTPSTHT--- 152
Cdd:TIGR01499   5 KKLLEaLGNPQDLYPVIHVAGTNGKGSTCAFLESILraagykvglfTSPH----LVSFNEririNGE--PISDEELAqaf 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  153 -----TLDALQLQ---------SALHDYAKQGASFVALEAsshGLeQGRL---NGCDLEIAVYSNLSRDHLDYHG-TLEA 214
Cdd:TIGR01499  79 eqvrpILESLSQQptyfelltlLAFLYFAQAQVDVAVLEV---GL-GGRLdatNVIEPLVSVITSIGLDHTEILGdTLEE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  215 YAEAKALLFKFKTlKAVVINLDDAHANIMLDAAQNNPSQpkiltysLTQASADYHI--ADLQYRLSGASFSLITPtgcya 292
Cdd:TIGR01499 155 IAWEKAGIIKEGV-PIVTGEQEPEALNVLKKKAQEKGAP-------LFVVGRDFNYseTDENYLSFSGANLFLEP----- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315  293 VQSPLLGHFNVENLLASLIAAECAGFALDKL-VQFVPQ-LQGA--PGRMQVIQDDERLFVVDYAHTPDALIQVLTTLKRH 368
Cdd:TIGR01499 222 LALSLLGDHQQENAALALAALEVLGKQNPKLsEEAIRQgLANTiwPGRLEILSEDNPNILLDGAHNPHSAEALAEWFKKR 301
                         330
                  ....*....|....*..
gi 518215315  369 VNGQ-LWAVFGCGGDRD 384
Cdd:TIGR01499 302 FNGRpITLLFGALADKD 318
PRK14016 PRK14016
cyanophycin synthetase; Provisional
106-339 5.14e-09

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 58.63  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 106 IAVTGTNGKTTISRLIAELITSQHHgcaVMG-TTGNGILPN--LTPSTHTTldalQLQSA---LHDYAKQGAsfvALEAS 179
Cdd:PRK14016 483 VAVTGTNGKTTTTRLIAHILKLSGK---RVGmTTTDGVYIDgrLIDKGDCT----GPKSArrvLMNPDVEAA---VLETA 552
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 180 SHG-LEQGrL--NGCDleIAVYSNLSRDHLDYHG--TLEAYAEAKALLFK-FKTLKAVVINLDDAHANIMLDAAQN---- 249
Cdd:PRK14016 553 RGGiLREG-LayDRCD--VGVVTNIGEDHLGLGGinTLEDLAKVKRVVVEaVKPDGYAVLNADDPMVAAMAERCKGkvif 629
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518215315 250 ---NPSQPKILTY---------------SLTQASADYHIADLqyrlsgasfSLITPTgcyavqspLLGH--FNVENLLAS 309
Cdd:PRK14016 630 fsmDPDNPVIAEHraqggravyvegdyiVLAEGGWEIRIISL---------ADIPLT--------LGGKagFNIENALAA 692
                        250       260       270
                 ....*....|....*....|....*....|....
gi 518215315 310 LIAAECAGFALDK----LVQFVPQLQGAPGRMQV 339
Cdd:PRK14016 693 IAAAWALGIDIELiragLRTFVSDAAQAPGRFNL 726
 
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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