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Conserved domains on  [gi|446534110|ref|WP_000611456|]
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MULTISPECIES: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase [Staphylococcus]

Protein Classification

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase( domain architecture ID 11433680)

UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
2-450 0e+00

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: 558.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   2 INVTLKQIQSWIPCEIEDQfLNQEINGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPIDenvsG 81
Cdd:COG0770    1 ILLTLAEIAEATGGRLIGD-PDLVVTGVSTDSRKIKPGDLFVALKGERFDGHDFVAQALAKGAAAALVSRPLPAD----L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  82 PIIWVEDTLTALQQLAQAYLRHVNPKVIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNNEIGLPLTILELDNDTEIS 161
Cdd:COG0770   76 PLIVVDDTLKALQQLAAAHRARFNIPVIAITGSNGKTTTKEMLAAVLSTKGKVLATPGNFNNEIGVPLTLLRLPEDHEFA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 162 ILEMGMSGFHEIEFLSNLAQPDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVeNAK 241
Cdd:COG0770  156 VLEMGMNHPGEIAYLARIARPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGLPPGGVAVLNADDPLLAALAERA-KAR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 242 CISIGVATDNALVCCVDDRDTTGISFTIN---NKEHYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMR 318
Cdd:COG0770  235 VLTFGLSEDADVRAEDIELDEDGTRFTLHtpgGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 319 MEQHTLENDITVINDAYNASPTSMRAAIDTLSTLT--GRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTFGNEA 396
Cdd:COG0770  315 LEVIEGAGGVTLIDDSYNANPDSMKAALDVLAQLPggGRRIAVLGDMLELGEESEELHREVGELAAELGIDRLFTVGELA 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446534110 397 KYIYDSGqqHVEKAQHFNSKDDMIGVLTSDLKAHDRVLVKGSRGMKLEEVVNAL 450
Cdd:COG0770  395 RAIAEAA--GGERAEHFEDKEELLAALKALLRPGDVVLVKGSRGMGLERVVEAL 446
 
Name Accession Description Interval E-value
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
2-450 0e+00

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: 558.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   2 INVTLKQIQSWIPCEIEDQfLNQEINGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPIDenvsG 81
Cdd:COG0770    1 ILLTLAEIAEATGGRLIGD-PDLVVTGVSTDSRKIKPGDLFVALKGERFDGHDFVAQALAKGAAAALVSRPLPAD----L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  82 PIIWVEDTLTALQQLAQAYLRHVNPKVIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNNEIGLPLTILELDNDTEIS 161
Cdd:COG0770   76 PLIVVDDTLKALQQLAAAHRARFNIPVIAITGSNGKTTTKEMLAAVLSTKGKVLATPGNFNNEIGVPLTLLRLPEDHEFA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 162 ILEMGMSGFHEIEFLSNLAQPDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVeNAK 241
Cdd:COG0770  156 VLEMGMNHPGEIAYLARIARPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGLPPGGVAVLNADDPLLAALAERA-KAR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 242 CISIGVATDNALVCCVDDRDTTGISFTIN---NKEHYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMR 318
Cdd:COG0770  235 VLTFGLSEDADVRAEDIELDEDGTRFTLHtpgGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 319 MEQHTLENDITVINDAYNASPTSMRAAIDTLSTLT--GRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTFGNEA 396
Cdd:COG0770  315 LEVIEGAGGVTLIDDSYNANPDSMKAALDVLAQLPggGRRIAVLGDMLELGEESEELHREVGELAAELGIDRLFTVGELA 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446534110 397 KYIYDSGqqHVEKAQHFNSKDDMIGVLTSDLKAHDRVLVKGSRGMKLEEVVNAL 450
Cdd:COG0770  395 RAIAEAA--GGERAEHFEDKEELLAALKALLRPGDVVLVKGSRGMGLERVVEAL 446
murF TIGR01143
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ...
31-450 1.37e-157

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: 452.11  E-value: 1.37e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   31 IDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPIDENVsgPIIWVEDTLTALQQLAQAYLRHVNPKVIA 110
Cdd:TIGR01143   1 TDSRAIKPGDLFIALKGERFDGHDFVEQALAAGAVAVVVDREVGPDNGL--PQILVDDTLEALQALARAKRAKFSGKVIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  111 VTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNNEIGLPLTILELDNDTEISILEMGMSGFHEIEFLSNLAQPDIAVITNI 190
Cdd:TIGR01143  79 ITGSSGKTTTKEMLAAILSHKYKVFATPGNFNNEIGLPLTLLRAPGDHDYAVLEMGASHPGEIAYLAEIAKPDIAVITNI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  191 GESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVENAKCISIGvATDNALVC---CVDDRDTTGISF 267
Cdd:TIGR01143 159 GPAHLEGFGSLEGIAEAKGEILQGLKENGIAVINADDPAFADLAKRLPNRNILSFG-FEGGDFVAkdiSYSALGSTSFTL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  268 TINNKE-HYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRMEqHTLENDITVINDAYNASPTSMRAAI 346
Cdd:TIGR01143 238 VAPGGEfEVSLPLLGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFE-VQTKNGLTLIDDTYNANPDSMRAAL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  347 DTLSTLTGRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTFGNEAKYIYDSGQqhvEKAQHFNSKDDMIGVLTSD 426
Cdd:TIGR01143 317 DALARFPGKKILVLGDMAELGEYSEELHAEVGRYANSLGIDLVFLVGEEAAVIYDSFG---KQGKHFADKDELLAFLKTL 393
                         410       420
                  ....*....|....*....|....
gi 446534110  427 LKAHDRVLVKGSRGMKLEEVVNAL 450
Cdd:TIGR01143 394 VRKGDVVLVKGSRSVKLEKVVEAL 417
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
26-451 1.85e-122

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: 379.05  E-value: 1.85e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  26 INGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPideNVSGPIIWVEDTLTALQQLAQAYLRHVN 105
Cdd:PRK11929 526 AGAVSTDSRSVGRGELFVALRGENFDGHDYLPQAFAAGACAAVVERQVA---DVDLPQIVVDDTRAALGRLATAWRARFS 602
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 106 PKVIAVTGSNGKTTTKDMIESVLHT---EFKVKKTQGNYNNEIGLPLTILELDNDTEISILEMGMSGFHEIEFLSNLAQP 182
Cdd:PRK11929 603 LPVVAITGSNGKTTTKEMIAAILAAwqgEDRVLATEGNFNNEIGVPLTLLRLRAQHRAAVFELGMNHPGEIAYLAAIAAP 682
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 183 DIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVENAKCISIGV--ATDNALVCCVDDR 260
Cdd:PRK11929 683 TVALVTNAQREHQEFMHSVEAVARAKGEIIAALPEDGVAVVNGDDPYTAIWAKLAGARRVLRFGLqpGADVYAEKIAKDI 762
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 261 DT---TGISFTIN-NKEHYD--LPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRMEQHTLENDITVINDA 334
Cdd:PRK11929 763 SVgeaGGTRCQVVtPAGSAEvyLPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSCGTRIIDDT 842
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 335 YNASPTSMRAAIDTLSTL-TGRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTFGNEAKYIYDSGQQHveKAQHF 413
Cdd:PRK11929 843 YNANPDSMRAAIDVLAELpNGPRALVLGDMLELGDNGPAMHREVGKYARQLGIDALITLGEAARDAAAAFGAG--ARGVC 920
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 446534110 414 NSKDDMIGVLTSDLKAHDRVLVKGSRGMKLEEVVNALI 451
Cdd:PRK11929 921 ASVDEIIAALRGALPEGDSVLIKGSRFMRLERVVDALS 958
Mur_ligase_M pfam08245
Mur ligase middle domain;
111-295 8.81e-45

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 154.77  E-value: 8.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  111 VTGSNGKTTTKDMIESVLHTEFKVKKTQG--------NYNNEIGLPLTILEL-DNDTEISILEMGMSGFHEiEFLSNLAQ 181
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIGTIGtyigksgnTTNNAIGLPLTLAEMvEAGAEYAVLEVSSHGLGE-GRLSGLLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  182 PDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVENAKC--ISIGVATDNALVCC--- 256
Cdd:pfam08245  80 PDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIAVINADDPYGAFLIAKLKKAGVrvITYGIEGEADLRAAnie 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 446534110  257 VDDRDTTGISFTINNKEH-YDLPILGKHNMKNATIAIAVG 295
Cdd:pfam08245 160 LSSDGTSFDLFTVPGGELeIEIPLLGRHNVYNALAAIAAA 199
F430_CfbE NF033197
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ...
107-361 8.41e-05

coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis.


Pssm-ID: 467992 [Multi-domain]  Cd Length: 419  Bit Score: 44.62  E-value: 8.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 107 KVIAVTGSNGKTTTKDMIESVLHTEFKVKKT-QGNYNNEIGL--------PLTILE-LDNDTEISILEMGMSGFhEIEfL 176
Cdd:NF033197  93 KFIEITGVKGKTTTAELLAHILSDEYVLLHTsRGTERYPEGElsnkgsitPASILNaLELAEEIGIDDYGFLIF-EVS-L 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 177 SNLAQPDIAVITNIGESHmqdlgsreGIAK-------AKSEIT-------IGLKDNGTFIYDGDEPLLKPHVKEVENAKC 242
Cdd:NF033197 171 GGTGAGDVGIITNILEDY--------PIAGgkrsasaAKLQSLknakvgsINVADLGIYINGKNKLVITVAGVEILSKYP 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 243 IsigvatdnalvccVDDRDTTGISFtiNNKehydlpILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRMEQH 322
Cdd:NF033197 243 L-------------RFKYGNTEFEF--NPL------LFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMAVK 301
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446534110 323 TLENdITVINdayNASP-TSMRA---AIDTLSTLTGRRILILG 361
Cdd:NF033197 302 KEGG-VVIVD---NINPgLNVKAieyALDDALELLGDGTLVIG 340
 
Name Accession Description Interval E-value
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
2-450 0e+00

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: 558.18  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   2 INVTLKQIQSWIPCEIEDQfLNQEINGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPIDenvsG 81
Cdd:COG0770    1 ILLTLAEIAEATGGRLIGD-PDLVVTGVSTDSRKIKPGDLFVALKGERFDGHDFVAQALAKGAAAALVSRPLPAD----L 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  82 PIIWVEDTLTALQQLAQAYLRHVNPKVIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNNEIGLPLTILELDNDTEIS 161
Cdd:COG0770   76 PLIVVDDTLKALQQLAAAHRARFNIPVIAITGSNGKTTTKEMLAAVLSTKGKVLATPGNFNNEIGVPLTLLRLPEDHEFA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 162 ILEMGMSGFHEIEFLSNLAQPDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVeNAK 241
Cdd:COG0770  156 VLEMGMNHPGEIAYLARIARPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGLPPGGVAVLNADDPLLAALAERA-KAR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 242 CISIGVATDNALVCCVDDRDTTGISFTIN---NKEHYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMR 318
Cdd:COG0770  235 VLTFGLSEDADVRAEDIELDEDGTRFTLHtpgGELEVTLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 319 MEQHTLENDITVINDAYNASPTSMRAAIDTLSTLT--GRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTFGNEA 396
Cdd:COG0770  315 LEVIEGAGGVTLIDDSYNANPDSMKAALDVLAQLPggGRRIAVLGDMLELGEESEELHREVGELAAELGIDRLFTVGELA 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446534110 397 KYIYDSGqqHVEKAQHFNSKDDMIGVLTSDLKAHDRVLVKGSRGMKLEEVVNAL 450
Cdd:COG0770  395 RAIAEAA--GGERAEHFEDKEELLAALKALLRPGDVVLVKGSRGMGLERVVEAL 446
murF TIGR01143
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ...
31-450 1.37e-157

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: 452.11  E-value: 1.37e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   31 IDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPIDENVsgPIIWVEDTLTALQQLAQAYLRHVNPKVIA 110
Cdd:TIGR01143   1 TDSRAIKPGDLFIALKGERFDGHDFVEQALAAGAVAVVVDREVGPDNGL--PQILVDDTLEALQALARAKRAKFSGKVIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  111 VTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNNEIGLPLTILELDNDTEISILEMGMSGFHEIEFLSNLAQPDIAVITNI 190
Cdd:TIGR01143  79 ITGSSGKTTTKEMLAAILSHKYKVFATPGNFNNEIGLPLTLLRAPGDHDYAVLEMGASHPGEIAYLAEIAKPDIAVITNI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  191 GESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVENAKCISIGvATDNALVC---CVDDRDTTGISF 267
Cdd:TIGR01143 159 GPAHLEGFGSLEGIAEAKGEILQGLKENGIAVINADDPAFADLAKRLPNRNILSFG-FEGGDFVAkdiSYSALGSTSFTL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  268 TINNKE-HYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRMEqHTLENDITVINDAYNASPTSMRAAI 346
Cdd:TIGR01143 238 VAPGGEfEVSLPLLGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFE-VQTKNGLTLIDDTYNANPDSMRAAL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  347 DTLSTLTGRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTFGNEAKYIYDSGQqhvEKAQHFNSKDDMIGVLTSD 426
Cdd:TIGR01143 317 DALARFPGKKILVLGDMAELGEYSEELHAEVGRYANSLGIDLVFLVGEEAAVIYDSFG---KQGKHFADKDELLAFLKTL 393
                         410       420
                  ....*....|....*....|....
gi 446534110  427 LKAHDRVLVKGSRGMKLEEVVNAL 450
Cdd:TIGR01143 394 VRKGDVVLVKGSRSVKLEKVVEAL 417
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
26-451 1.85e-122

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: 379.05  E-value: 1.85e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  26 INGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPideNVSGPIIWVEDTLTALQQLAQAYLRHVN 105
Cdd:PRK11929 526 AGAVSTDSRSVGRGELFVALRGENFDGHDYLPQAFAAGACAAVVERQVA---DVDLPQIVVDDTRAALGRLATAWRARFS 602
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 106 PKVIAVTGSNGKTTTKDMIESVLHT---EFKVKKTQGNYNNEIGLPLTILELDNDTEISILEMGMSGFHEIEFLSNLAQP 182
Cdd:PRK11929 603 LPVVAITGSNGKTTTKEMIAAILAAwqgEDRVLATEGNFNNEIGVPLTLLRLRAQHRAAVFELGMNHPGEIAYLAAIAAP 682
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 183 DIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVENAKCISIGV--ATDNALVCCVDDR 260
Cdd:PRK11929 683 TVALVTNAQREHQEFMHSVEAVARAKGEIIAALPEDGVAVVNGDDPYTAIWAKLAGARRVLRFGLqpGADVYAEKIAKDI 762
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 261 DT---TGISFTIN-NKEHYD--LPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRMEQHTLENDITVINDA 334
Cdd:PRK11929 763 SVgeaGGTRCQVVtPAGSAEvyLPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSCGTRIIDDT 842
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 335 YNASPTSMRAAIDTLSTL-TGRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTFGNEAKYIYDSGQQHveKAQHF 413
Cdd:PRK11929 843 YNANPDSMRAAIDVLAELpNGPRALVLGDMLELGDNGPAMHREVGKYARQLGIDALITLGEAARDAAAAFGAG--ARGVC 920
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 446534110 414 NSKDDMIGVLTSDLKAHDRVLVKGSRGMKLEEVVNALI 451
Cdd:PRK11929 921 ASVDEIIAALRGALPEGDSVLIKGSRFMRLERVVDALS 958
murF PRK10773
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
1-450 9.42e-82

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


Pssm-ID: 182718 [Multi-domain]  Cd Length: 453  Bit Score: 259.58  E-value: 9.42e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   1 MINVTLKQIQSWIPCEIEDQflNQEINGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPIDenvs 80
Cdd:PRK10773   1 MISVTLSQLADILNGELQGA--DITIDAVTTDTRKVTPGCLFVALKGERFDAHDFADDAKAAGAGALLVSRPLDID---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  81 GPIIWVEDTLTALQQLAqAYLR-HVNPKVIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNNEIGLPLTILELDNDTE 159
Cdd:PRK10773  75 LPQLVVKDTRLAFGQLA-AWVRqQVPARVVALTGSSGKTSVKEMTAAILRQCGNTLYTAGNLNNDIGVPLTLLRLTPEHD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 160 ISILEMGMSGFHEIEFLSNLAQPDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLkPHVKEVEN 239
Cdd:PRK10773 154 YAVIELGANHQGEIAYTVSLTRPEAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPENGIAIMNADSNDW-LNWQSVIG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 240 AKCI---SIGvATDNALVCCVDDRDTT-GISFTINN---KEHYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNV 312
Cdd:PRK10773 233 SKTVwrfSPN-AANSVDFTATNIHVTShGTEFTLHTptgSVDVLLPLPGRHNIANALAAAALAMSVGATLDAVKAGLANL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 313 SLTGMRMEQHTLENDITVINDAYNASPTSMRAAIDTLSTLTGRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTF 392
Cdd:PRK10773 312 KAVPGRLFPIQLAEGQLLLDDSYNANVGSMTAAAQVLAEMPGYRVMVVGDMAELGAESEACHRQVGEAAKAAGIDKVLSV 391
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446534110 393 GNEAKYIYD-SGqqhveKAQHFNSKDDMIGVLTSDLKAHD--RVLVKGSRGMKLEEVVNAL 450
Cdd:PRK10773 392 GKLSHAISEaSG-----VGEHFADKTALIARLKALLAEHQviTILVKGSRSAAMEEVVRAL 447
PRK14093 PRK14093
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ...
22-450 8.26e-65

UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional


Pssm-ID: 184501 [Multi-domain]  Cd Length: 479  Bit Score: 216.18  E-value: 8.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  22 LNQEINGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPIDENVSGPIIWVEDTLTALQQLAQAYL 101
Cdd:PRK14093  24 LPRDVTGISIDSRTLAPGDAYFAIKGDVHDGHAFVAAALKAGAALAVVERAQRDKFAADAPLLVVDDVLAALRDLGRAAR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 102 RHVNPKVIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNNEIGLPLTILELDNDTEISILEMGMSGFHEIEFLSNLAQ 181
Cdd:PRK14093 104 ARLEAKVIAVTGSVGKTSTKEALRGVLGAQGETHASVASFNNHWGVPLSLARCPADARFAVFEIGMNHAGEIEPLVKMVR 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 182 PDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPL---LKPHVKEVENAKCISIGV--ATDNALVCC 256
Cdd:PRK14093 184 PHVAIITTVEPVHLEFFSGIEAIADAKAEIFTGLEPGGAAVLNRDNPQfdrLAASARAAGIARIVSFGAdeKADARLLDV 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 257 VDDRDTTGISFTINNKE-HYDLPILGKHNMKNATIAIA----VGHELGLTYNTIYQnLKNVSLTGMRmeqHTLE---NDI 328
Cdd:PRK14093 264 ALHADCSAVHADILGHDvTYKLGMPGRHIAMNSLAVLAaaelAGADLALAALALSQ-VQPAAGRGVR---HTLEvggGEA 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 329 TVINDAYNASPTSMRAAIDTLSTLT----GRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLYTFGNEAKYIYD--- 401
Cdd:PRK14093 340 TLIDESYNANPASMAAALGVLGRAPvgpqGRRIAVLGDMLELGPRGPELHRGLAEAIRANAIDLVFCCGPLMRNLWDals 419
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446534110 402 SGQQ--HVEKAQHFNSKddmigvLTSDLKAHDRVLVKGSRGMKLEEVVNAL 450
Cdd:PRK14093 420 SGKRggYAEDAAALESQ------VVAAIRAGDVIMVKGSLGSRMKTIVTAL 464
PRK11930 PRK11930
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ...
2-450 8.47e-60

putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional


Pssm-ID: 237026 [Multi-domain]  Cd Length: 822  Bit Score: 209.43  E-value: 8.47e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   2 INVTLKQIQSWIPCEIEDQFlNQEINGVTIDSRAIS--KNMLFIPFEGENVDGHRFVSKALQDGAgAAFYQKGTPIDENV 79
Cdd:PRK11930   1 MSYTLESISGILGAEGLGDK-DAIIDQILTDSRSLSfpENTLFFALKGERNDGHRYIQELYEKGV-RNFVVSEEKHPEES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  80 SGPIIW--VEDTLTALQQLAQAYLRHVNPKVIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNNEIGLPLTILELDND 157
Cdd:PRK11930  79 YPDANFlkVKDPLKALQELAAYHRSQFDIPVIGITGSNGKTIVKEWLYQLLSPDYNIVRSPRSYNSQIGVPLSVWQLNEE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 158 TEISILEMGMSGFHEIEFLSNLAQPDIAVITNIGESHMQDLGSREGIAKAKSEItigLKDNGTFIYDGD-EPLLKPHVKE 236
Cdd:PRK11930 159 HELGIFEAGISQPGEMEALQKIIKPTIGILTNIGGAHQENFRSIKQKIMEKLKL---FKDCDVIIYNGDnELISSCITKS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 237 VENAKCISIGVATDNA--LVCCVD-DRDTTGISFTINNKE-HYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNV 312
Cdd:PRK11930 236 NLTLKLISWSRKDPEAplYIPFVEkKEDHTVISYTYKGEDfHFEIPFIDDASIENLIHCIAVLLYLGYSADQIQERMARL 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 313 SLTGMRMEQHTLENDITVINDAYNASPTSMRAAIDTLS--TLTGRRILILGDVLELGENSKEMHIGVGNYLEEKHIDVLY 390
Cdd:PRK11930 316 EPVAMRLEVKEGINNCTLINDSYNSDLQSLDIALDFLNrrSQSKKKTLILSDILQSGQSPEELYRKVAQLISKRGIDRLI 395
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446534110 391 TFGNE---AKYIYDSGqqhveKAQHFNSKDDMIGVLTSDLKAHDRVLVKGSRGMKLEEVVNAL 450
Cdd:PRK11930 396 GIGEEissEASKFEGT-----EKEFFKTTEAFLKSFAFLKFRNELILVKGARKFEFEQITELL 453
Mur_ligase_M pfam08245
Mur ligase middle domain;
111-295 8.81e-45

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 154.77  E-value: 8.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  111 VTGSNGKTTTKDMIESVLHTEFKVKKTQG--------NYNNEIGLPLTILEL-DNDTEISILEMGMSGFHEiEFLSNLAQ 181
Cdd:pfam08245   1 VTGTNGKTTTTELIAAILSLAGGVIGTIGtyigksgnTTNNAIGLPLTLAEMvEAGAEYAVLEVSSHGLGE-GRLSGLLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  182 PDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVENAKC--ISIGVATDNALVCC--- 256
Cdd:pfam08245  80 PDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIAVINADDPYGAFLIAKLKKAGVrvITYGIEGEADLRAAnie 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 446534110  257 VDDRDTTGISFTINNKEH-YDLPILGKHNMKNATIAIAVG 295
Cdd:pfam08245 160 LSSDGTSFDLFTVPGGELeIEIPLLGRHNVYNALAAIAAA 199
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
28-361 2.53e-34

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: 133.28  E-value: 2.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  28 GVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQK-GTPIDENVsgPIIWVEDTLTALQQLAQAYLRHvnP 106
Cdd:COG0769    1 GITYDSRKVKPGDLFVALPGARVDGHDFIAQAIARGAVAVVTEApGALLAAGV--PVIVVPDPRAALALLAAAFYGH--P 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 107 ----KVIAVTGSNGKTTTKDMIESVLhtefkvkkTQGNYN------NEIGLPLTILELDNDT------------------ 158
Cdd:COG0769   77 sqklKLIGVTGTNGKTTTTYLLAQIL--------RALGKKtgligtVGNGIGGELIPSSLTTpealdlqrllaemvdagv 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 159 -----EIS--ILEMGMsgFHEIEFlsnlaqpDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLK 231
Cdd:COG0769  149 thvvmEVSshALDQGR--VDGVRF-------DVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQLGPGGAAVINADDPYGR 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 232 PHVKEVeNAKCISIGVATDNALVCCVDDRDTTGISFTINNKE---HYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQN 308
Cdd:COG0769  220 RLAAAA-PARVITYGLKADADLRATDIELSADGTRFTLVTPGgevEVRLPLIGRFNVYNALAAIAAALALGIDLEEILAA 298
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446534110 309 LKNVS-LTGmRMEQHTLENDITVINDaYNASPTSMRAAIDTLSTLTGRR-ILILG 361
Cdd:COG0769  299 LEKLKgVPG-RMERVDGGQGPTVIVD-YAHTPDALENVLEALRPHTKGRlIVVFG 351
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
102-361 7.21e-33

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: 129.05  E-value: 7.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 102 RHVNPKVIAVTGSNGKTTTKDMIESVLHTEFkvKKTQ--GNynneIGLP-LTILELDNDTEISILEmgMSGFhEIEFLSN 178
Cdd:COG0771  101 RLSPAPIIAITGTNGKTTTTTLIGHILKAAG--LRVAvgGN----IGTPlLDLLLEPEPPDVYVLE--LSSF-QLETTPS 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 179 LAqPDIAVITNIGESHMqDL-GSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEVeNAKCISIGVATDNALVCCV 257
Cdd:COG0771  172 LR-PDVAVILNITPDHL-DRhGSMEAYAAAKARIFANQTPDDYAVLNADDPLTRALAEEA-KARVVPFSLKEPLEGGAGL 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 258 DDRDttgISFTINNKEHY---DLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKnvSLTGM--RMEQHTLENDITVIN 332
Cdd:COG0771  249 EDGK---LVDRASGEELLpvdDLRLPGRHNLENALAALAAARALGVPPEAIREALR--SFKGLphRLEFVAEINGVRFIN 323
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446534110 333 D--AYNasPTSMRAAidtLSTLTGRRILILG 361
Cdd:COG0771  324 DskATN--PDATLAA---LESFDGPVVLIAG 349
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
26-360 1.98e-28

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: 118.65  E-value: 1.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  26 INGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFY-QKGTPIDENVSGPIIWVEDTLTALQQLAQAYLRHV 104
Cdd:PRK11929  29 TADLRLDSREVQPGDLFVACRGAASDGRAFIDQALARGAAAVLVeAEGEDQVAAADALVLPVADLRKALGELAARWYGRP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 105 NPK--VIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNYNN-----EIGLPLTILE-----------LDNDTEISILEMG 166
Cdd:PRK11929 109 SEQlsLVAVTGTNGKTSCAQLLAQLLTRLGKPCGSIGTLGArldgrLIPGSLTTPDaiilhrilarmRAAGADAVAMEAS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 167 MSGFhEIEFLSNLAQpDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLkPHVKEVENaKCISIG 246
Cdd:PRK11929 189 SHGL-EQGRLDGLRI-AVAGFTNLTRDHLDYHGTMQDYEEAKAALFSKLPGLGAAVINADDPAA-ARLLAALP-RGLKVG 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 247 VATDN--ALVCCVDDRDT-TGISFTI-NNKEHY--DLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRME 320
Cdd:PRK11929 265 YSPQNagADVQARDLRATaHGQVFTLaTPDGSYqlVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSPVPGRME 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 446534110 321 ---QHTLENDITVINDaYNASPTSMRAAIDTLSTLT---GRRILIL 360
Cdd:PRK11929 345 rvgPTAGAQGPLVVVD-YAHTPDALAKALTALRPVAqarNGRLVCV 389
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
19-361 1.84e-27

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 114.07  E-value: 1.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  19 DQFLNQEINGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGTPIDENVsgPIIWVEDTLTALQQLAQ 98
Cdd:PRK00139   8 DLLAPVEITGLTYDSRKVKPGDLFVALPGHKVDGRDFIAQAIANGAAAVVAEADGEAGTGV--PVIIVPDLRKALALLAA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  99 AYLRHvnP----KVIAVTGSNGKTTTKDMIESVLH-----------TEFKVkktqGNYNNEIGL----PLTILELDNDte 159
Cdd:PRK00139  86 AFYGH--PsdklKLIGVTGTNGKTTTAYLLAQILRllgektaligtLGNGI----GGELIPSGLttpdALDLQRLLAE-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 160 isILEMGMSGF--------------HEIEFlsnlaqpDIAVITNIGESHMQDLGSREGIAKAKSEItigLKDNGTF-IYD 224
Cdd:PRK00139 158 --LVDAGVTYAamevsshaldqgrvDGLKF-------DVAVFTNLSRDHLDYHGTMEDYLAAKARL---FSELGLAaVIN 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 225 GDEPllkphVKEVENAKCISIGVATDNALVCCVDDR-DTTGISFTINNkeHYDLPILGKHNMKNATIAIAVGHELGLTYN 303
Cdd:PRK00139 226 ADDE-----VGRRLLALPDAYAVSMAGADLRATDVEyTDSGQTFTLVT--EVESPLIGRFNVSNLLAALAALLALGVPLE 298
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446534110 304 TIYQNLKNvsLTGM--RMEQHTLENDITVIND-AYNasPTSMRAAIDTLSTLT-GRRILILG 361
Cdd:PRK00139 299 DALAALAK--LQGVpgRMERVDAGQGPLVIVDyAHT--PDALEKVLEALRPHAkGRLICVFG 356
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
107-435 1.06e-24

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: 105.92  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 107 KVIAVTGSNGKTTTKDMIESVLHtefkvkktqgnynnEIGLPLTIL---ELDN--------DTEISIlemgmsgfheIE- 174
Cdd:COG0773  105 RSIAVAGTHGKTTTTSMLAHILE--------------EAGLDPTFLiggILNNfgtnarlgDGDYFV----------AEa 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 175 ------FLsNLaQPDIAVITNIGESHMqDL-GSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKpHVKEVENAKCISIGV 247
Cdd:COG0773  161 desdgsFL-HY-SPDIAVVTNIEADHL-DIyGDLEAIKEAFHEFARNVPFYGLLVLCADDPGLR-ELLPRCGRPVITYGF 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 248 AtDNALVCCVDDR-DTTGISFTI--NNKE--HYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRMEQH 322
Cdd:COG0773  237 S-EDADYRAENIRiDGGGSTFDVlrRGEElgEVELNLPGRHNVLNALAAIAVALELGVDPEAIAEALASFKGVKRRFELK 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 323 TLENDITVINDaYNASPTSMRAAIDTL-STLTGRRILIlgdVLELGENS--KEMhigvgnyLEE-----KHIDVLYTFgn 394
Cdd:COG0773  316 GEVGGVTVIDD-YAHHPTEIAATLAAArEKYPDRRLVA---VFQPHRYSrtRDF-------LDEfaealSLADEVILL-- 382
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446534110 395 eakYIYDSG----------------QQHVEKAQHFNSKDDMIGVLTSDLKAHDRVLV 435
Cdd:COG0773  383 ---DIYAARekpipgvssedlaeaiRKRGKDVVYVPDLDELVEALAEIARPGDVVLT 436
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
23-360 2.00e-23

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: 102.39  E-value: 2.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   23 NQEINGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQkgTPIDENVSG-PIIWVEDTLTALQQLAQAYL 101
Cdd:TIGR01085   1 DLEVTGLTLDSREVKPGDLFVAIKGTHVDGHDFIHDAIANGAVAVVVE--RDVDFYVAPvPVIIVPDLRHALSSLAAAFY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  102 RHV--NPKVIAVTGSNGKTTTKDMIESVLhtEFKVKKTQ--GNYNNEIGLPLTILELDNDTEISILEMgMSGFHE----- 172
Cdd:TIGR01085  79 GHPskKLKVIGVTGTNGKTTTTSLIAQLL--RLLGKKTGliGTIGYRLGGNDLIKNPAALTTPEALTL-QSTLAEmveag 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  173 -----IEFLSN-LAQP-------DIAVITNIGESHMQDLGSREGIAKAKSEI--TIGLKDNGTFIYD---GDEpLLK--P 232
Cdd:TIGR01085 156 aqyavMEVSSHaLAQGrvrgvrfDAAVFTNLSRDHLDFHGTMENYFAAKASLftELGLKRFAVINLDdeyGAQ-FVKrlP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  233 HVKEVENAKCISIGVATDNALVccVDDRDTTGISFTI---NNKEHYDLPILGKHNMKNATIAIAVGHELG-LTYNTIYQN 308
Cdd:TIGR01085 235 KDITVSAITQPADGRAQDIKIT--DSGYSFEGQQFTFetpAGEGHLHTPLIGRFNVYNLLAALATLLHLGgIDLEDIVAA 312
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446534110  309 LKNVSLTGMRMEQHTLENDITVINDaYNASPTSMRAAIDTLSTLTGRRILIL 360
Cdd:TIGR01085 313 LEKFRGVPGRMELVDGGQKFLVIVD-YAHTPDALEKALRTLRKHKDGRLIVV 363
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
101-434 3.62e-23

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: 101.26  E-value: 3.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  101 LRHVNPKVIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNynneIGLPLTILELDNDTEISILEmgMSGFhEIEFLSNLA 180
Cdd:TIGR01087  97 LRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFLGGN----IGTPALEVLDQEGAELYVLE--LSSF-QLETTESLR 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  181 qPDIAVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHvKEVENAKCISIGV--ATDNALVccvd 258
Cdd:TIGR01087 170 -PEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAVLNADDPRFARL-AQKSKAQVIWFSVekDAERGLC---- 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  259 dRDTTGISFTINNKEhydLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKnvSLTGM--RMEQHTLENDITVINDAYN 336
Cdd:TIGR01087 244 -IRDGGLYLKPNDLE---GSLLGLHNAENILAAIALAKSLGLNLEAILEALR--SFKGLphRLEYVGQKNGVHFYNDSKA 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  337 ASPTSMRAAidtLSTLTGRRILILGdvlelGENSKEMHIGVGNYLEEKHIDVlYTFGNEAKYIYDSGQQHVEKAQHFNSK 416
Cdd:TIGR01087 318 TNVHATLAA---LSAFDNPVILIVG-----GDDKGADFSPLAPAAAGKVKAV-LAIGEDAAKIAPLLKEAGLSVYLVESL 388
                         330
                  ....*....|....*...
gi 446534110  417 DDMIGVLTSDLKAHDRVL 434
Cdd:TIGR01087 389 EEAVQAAREVASPGDVVL 406
FolC COG0285
Folylpolyglutamate synthase/Dihydropteroate synthase [Coenzyme transport and metabolism]; ...
103-361 6.21e-15

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: 76.30  E-value: 6.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 103 HVNPKVIAVTGSNGKTTTKDMIESVL-------------H--------------------TEF--KVKKtqgnYNNEIGL 147
Cdd:COG0285   37 QRKLPVIHVAGTNGKGSTAAMLESILraagyrvglytspHlvrfneriringepisdeelVEAleEVEP----AVEEVDA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 148 -PLTILEL----------DNDTEISILEMGMSGfheiEFLS-NLAQPDIAVITNIGESHMQDLGS-REGIAKAKSEItig 214
Cdd:COG0285  113 gPPTFFEVttaaaflyfaEAPVDVAVLEVGLGG----RLDAtNVIDPLVSVITSIGLDHTDFLGDtLEEIAREKAGI--- 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 215 LKDNGT-FIYDGDEPLLKP---HVKEVeNAKCISIGVAtdnalvCCVDDRDTTGISFTINNKEHYDLPI--LGKHNMKNA 288
Cdd:COG0285  186 IKPGVPvVTGDQQPEALEVieeRAAEL-GAPLYRAGRD------FSVEEREGAVFSYQGPGGEYEDLPLplLGAHQAENA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 289 TIAIAV-----GHELGLTYNTIYQNLKNVSLTGmRMEQhtLENDITVIND-AYNasPTSMRAAIDTLSTL--TGRRILIL 360
Cdd:COG0285  259 ALALAAlealrELGLPISEEAIREGLANARWPG-RLEV--LSRGPLVILDgAHN--PAGARALAETLKELfpFRKLHLVF 333

                 .
gi 446534110 361 G 361
Cdd:COG0285  334 G 334
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
107-361 1.15e-14

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


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 75.78  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 107 KVIAVTGSNGKTTTKDMIESVLHTEFKVKKTQGNynneIGLPL--TILELDNDTEISIlemGMSGFhEIEFLSNLAqPDI 184
Cdd:PRK14106 109 PIVAITGTNGKTTTTTLLGEIFKNAGRKTLVAGN----IGYPLidAVEEYGEDDIIVA---EVSSF-QLETIKEFK-PKV 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 185 AVITNIGESHMQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPL---LKPHVKE----------------VENAKcISI 245
Cdd:PRK14106 180 GCILNITPDHLDRHKTMENYIKAKARIFENQRPSDYTVLNYDDPRtrsLAKKAKArviffsrkslleegvfVKNGK-IVI 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 246 GVATDNALVCCVDdrdttgisftinnkehyDLPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRMEQHTLE 325
Cdd:PRK14106 259 SLGGKEEEVIDID-----------------EIFIPGEHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFVAEI 321
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446534110 326 NDITVINDAYNASPTsmrAAIDTLSTLTGRRILILG 361
Cdd:PRK14106 322 NGVKFINDSKGTNPD---AAIKALEAYETPIVLIAG 354
Mur_ligase pfam01225
Mur ligase family, catalytic domain; This family contains a number of related ligase enzymes ...
25-100 1.27e-13

Mur ligase family, catalytic 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: 460121 [Multi-domain]  Cd Length: 84  Bit Score: 66.10  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110   25 EINGVTIDSRAISKNMLFIPFEGENVDGHRFVSKALQDGAGAAFYQKGT-------PIDENVSGPIIWVEDTLTALQQLA 97
Cdd:pfam01225   1 EIHFVGIDGRGMSPGALFLALKGYRVDGSDFIESLIALGAAAVVGHDAAnnispdnPELEAAKVPGIPVIDRREALAELA 80

                  ...
gi 446534110   98 QAY 100
Cdd:pfam01225  81 AAF 83
PRK14573 PRK14573
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
93-358 7.00e-13

bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;


Pssm-ID: 184752 [Multi-domain]  Cd Length: 809  Bit Score: 70.62  E-value: 7.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  93 LQQLAQAYLRhvnpkvIAVTGSNGKTTTKDMIESVLHTEFKvkktqgNYNNEIGlPLTILELDndteisilemGMSGFHE 172
Cdd:PRK14573  97 LAELMQEQIS------ILVSGSHGKTTVSSLITAIFQEAKK------DPSYAIG-GLNQEGLN----------GYSGSSE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 173 IeFLSNLAQ---------PDIAVITNIGESHMQDL-GSREGIAKAKSEITIGLKDNGTFIYDGDEPLLKPHVKEvenakc 242
Cdd:PRK14573 154 Y-FVAEADEsdgslkhytPEFSVITNIDNEHLSNFeGDRELLLASIQDFARKVQQINKCFYNGDCPRLKGCLQG------ 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 243 ISIGVATDNALVCCVDDRD--TTGISFTINNKEHYD--LPILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMR 318
Cdd:PRK14573 227 HSYGFSSSCDLHILSYYQEgwRSYFSAKFLGVVYQDieLNLVGMHNVANAAAAMGIALTLGIDEGAIRNALKGFSGVQRR 306
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446534110 319 MEQHTLENDITVINDaYNASPTSMRAAIDTLSTLTG-RRIL 358
Cdd:PRK14573 307 LERKNSSETFLFLED-YAHHPSEISCTLRAVRDAVGlRRII 346
folC TIGR01499
folylpolyglutamate synthase/dihydrofolate synthase; This model represents the FolC family of ...
103-360 5.23e-12

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: 67.31  E-value: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  103 HVNPKVIAVTGSNGKTTTKDMIESVL---------------------------------------HTEFKVKKTQGNYN- 142
Cdd:TIGR01499  15 QDLYPVIHVAGTNGKGSTCAFLESILraagykvglftsphlvsfneriringepisdeelaqafeQVRPILESLSQQPTy 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  143 NEIglpLTILEL----DNDTEISILEMGMSGfheiEFLS-NLAQPDIAVITNIGESHMQDLG-SREGIAKAKSEItigLK 216
Cdd:TIGR01499  95 FEL---LTLLAFlyfaQAQVDVAVLEVGLGG----RLDAtNVIEPLVSVITSIGLDHTEILGdTLEEIAWEKAGI---IK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  217 DnGTFIYDGDEPllkPHVKEVENAKCISIGV---ATDNALVCCVDDRDTTGISFTINNKEHYDLPILGKHNMKNATIAIA 293
Cdd:TIGR01499 165 E-GVPIVTGEQE---PEALNVLKKKAQEKGAplfVVGRDFNYSETDENYLSFSGANLFLEPLALSLLGDHQQENAALALA 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446534110  294 -----VGHELGLTYNTIYQNLKNVSLTGmRMEQHTLENDITVINDAYNasPTSMRAAIDTLSTLTGRRILIL 360
Cdd:TIGR01499 241 alevlGKQNPKLSEEAIRQGLANTIWPG-RLEILSEDNPNILLDGAHN--PHSAEALAEWFKKRFNGRPITL 309
PRK14022 PRK14022
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
23-373 3.62e-11

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


Pssm-ID: 237588 [Multi-domain]  Cd Length: 481  Bit Score: 65.06  E-value: 3.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  23 NQEINGVTIDSRAISKNMLFIPfEGENVDgHRFVSKALQDGAGaaFYQkgTPIDENVSGPIIWVEDTLTALQQLAQAYlr 102
Cdd:PRK14022  31 GVQFDDISYDSRTADEGTLFFA-KGAYFK-HKFLQNAITQGLK--LYV--SEKDYEVGIPQVIVPDIKKAMSLIAMEF-- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 103 HVNP----KVIAVTGSNGKTTTKDMIESVLHTEFK---VKKTQGNYNNE------------IGLPLTILE-LDNDTEISI 162
Cdd:PRK14022 103 YDNPqhklKLLAFTGTKGKTTAAYFAYHILKQLHKpamLSTMNTTLDGEtffksalttpesLDLFKMMAEaVDNGMTHLI 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 163 LEMGMSGF-----HEIEFlsnlaqpDIAVITNIGESH--------MQDLGSREGIAKAKSEITIGLKDNGTFiydgdePL 229
Cdd:PRK14022 183 MEVSSQAYlvgrvYGLTF-------DVGVFLNITPDHigpiehptFEDYFYHKRLLMENSKAVVVNSDMDHF------SE 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 230 LKphvKEVENAKCISIGVATDNALvccvddRDTTGISFTINNK--EHYDLPILGKHNMKNATIAIAVGHELGLTYNTIYQ 307
Cdd:PRK14022 250 LL---EQVTPQEHDFYGIDSENQI------MASNAFSFEATGKlaGTYDIQLIGKFNQENAMAAGLACLRLGASLEDIQK 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446534110 308 NLKNVSLTGmRMEQHTLENDITVINDaYNASPTSMRAAIDTLST-LTGRRILILGDVLELGEN-SKEM 373
Cdd:PRK14022 321 GIAQTPVPG-RMEVLTQSNGAKVFID-YAHNGDSLNKLIDVVEEhQKGKLILLLGAAGNKGESrRPDF 386
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
315-395 1.41e-09

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: 54.66  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110  315 TGMRMEQHTLENDITVINDaYNASPTSMRAAIDTLSTLT-GRRILILGDvleLGENSKEMHIGVGnYLEEKHIDVLYTFG 393
Cdd:pfam02875   1 VPGRLEVVGENNGVLVIDD-YAHNPDAMEAALRALRNLFpGRLILVFGG---MGDRDAEFHALLG-RLAAALADVVILTG 75

                  ..
gi 446534110  394 NE 395
Cdd:pfam02875  76 DY 77
PRK14016 PRK14016
cyanophycin synthetase; Provisional
108-310 4.22e-07

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 52.47  E-value: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 108 VIAVTGSNGKTTTKDMIESVLHTEFKV---KKTQGNY-NNEI-------GlPL---TILeLDNDTEISILEMGMSGFHEi 173
Cdd:PRK14016 482 IVAVTGTNGKTTTTRLIAHILKLSGKRvgmTTTDGVYiDGRLidkgdctG-PKsarRVL-MNPDVEAAVLETARGGILR- 558
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 174 eflSNLA--QPDIAVITNIGESH--MQDLGSREGIAKAKSEITIGLKDNGTFIYDGDEPLLK---PHVKevenAKCISIG 246
Cdd:PRK14016 559 ---EGLAydRCDVGVVTNIGEDHlgLGGINTLEDLAKVKRVVVEAVKPDGYAVLNADDPMVAamaERCK----GKVIFFS 631
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 247 VATDNALVC---------CVDDRDTtgISFTINNKEHY-----DLPIL--GK--HNMKNATIAIAVGHELGLTYNTIYQN 308
Cdd:PRK14016 632 MDPDNPVIAehraqggraVYVEGDY--IVLAEGGWEIRiislaDIPLTlgGKagFNIENALAAIAAAWALGIDIELIRAG 709

                 ..
gi 446534110 309 LK 310
Cdd:PRK14016 710 LR 711
F430_CfbE NF033197
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ...
107-361 8.41e-05

coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in synthesizing coenzyme F430, which is used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) MurD, an enzyme of bacterial cell wall biosynthesis.


Pssm-ID: 467992 [Multi-domain]  Cd Length: 419  Bit Score: 44.62  E-value: 8.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 107 KVIAVTGSNGKTTTKDMIESVLHTEFKVKKT-QGNYNNEIGL--------PLTILE-LDNDTEISILEMGMSGFhEIEfL 176
Cdd:NF033197  93 KFIEITGVKGKTTTAELLAHILSDEYVLLHTsRGTERYPEGElsnkgsitPASILNaLELAEEIGIDDYGFLIF-EVS-L 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 177 SNLAQPDIAVITNIGESHmqdlgsreGIAK-------AKSEIT-------IGLKDNGTFIYDGDEPLLKPHVKEVENAKC 242
Cdd:NF033197 171 GGTGAGDVGIITNILEDY--------PIAGgkrsasaAKLQSLknakvgsINVADLGIYINGKNKLVITVAGVEILSKYP 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446534110 243 IsigvatdnalvccVDDRDTTGISFtiNNKehydlpILGKHNMKNATIAIAVGHELGLTYNTIYQNLKNVSLTGMRMEQH 322
Cdd:NF033197 243 L-------------RFKYGNTEFEF--NPL------LFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMAVK 301
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446534110 323 TLENdITVINdayNASP-TSMRA---AIDTLSTLTGRRILILG 361
Cdd:NF033197 302 KEGG-VVIVD---NINPgLNVKAieyALDDALELLGDGTLVIG 340
PLN02913 PLN02913
dihydrofolate synthetase
159-211 4.98e-03

dihydrofolate synthetase


Pssm-ID: 178501 [Multi-domain]  Cd Length: 510  Bit Score: 39.03  E-value: 4.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446534110 159 EISILEMGMSGFHE---IEFLSNLAQpdiAVITNIGESHMQDL-GSREGIAKAKSEI 211
Cdd:PLN02913 175 DIAVIEAGLGGARDatnVIDSSGLAA---SVITTIGEEHLAALgGSLESIALAKSGI 228
 
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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