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Conserved domains on  [gi|1655159775|ref|WP_137643686|]
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UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase [Lactiplantibacillus modestisalitolerans]

Protein Classification

Mur ligase family protein( domain architecture ID 11433699)

Mur ligase family protein similar to UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase (MurD) and UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase (MurD2), which catalyze the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
6-452 0e+00

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: 545.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   6 QYRNQKVLVLGLAKSGVNAARLLHKLGAFVTVNDKKDFDQNPdAQELLSDGIKVITGGHPLSLLDeDFKVVVKNPGIPYS 85
Cdd:COG0771     1 DLKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELA-AAELEAPGVEVVLGEHPEELLD-GADLVVKSPGIPPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  86 NPIVSGAIQKHIPVITEVELAAQILE-------------------GELIGvtgtngktttttlitmmlnqrsQAG-KAYV 145
Cdd:COG0771    79 HPLLKAARAAGIPVIGEIELAYRLSPapiiaitgtngktttttliGHILK----------------------AAGlRVAV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 146 AGNIGVPASAVAQKAGANDTMVTELSSFMLCGIDQLHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVIN 225
Cdd:COG0771   137 GGNIGTPLLDLLLEPEPPDVYVLELSSFQLETTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANQTPDDYAVLN 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 226 WDSQEWRDLSQQSRAQVVPFSRQGNSTDGAYERDGQLYFR--DEYIMDAKEIKIPGEHNVENALAAIAVAKLQGVPTNGI 303
Cdd:COG0771   217 ADDPLTRALAEEAKARVVPFSLKEPLEGGAGLEDGKLVDRasGEELLPVDDLRLPGRHNLENALAALAAARALGVPPEAI 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 304 VEVLKSFSGVRHRTQYVETYEGRQFYNDSKATNIVSTEMALRGFDHPVVLLAGGLDRGNTFEKLAPALKKHVKTLIVFGE 383
Cdd:COG0771   297 REALRSFKGLPHRLEFVAEINGVRFINDSKATNPDATLAALESFDGPVVLIAGGLDKGADFSPLAPAVAERVKAVVLIGE 376
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655159775 384 TAQKLADAGKLAGIEdIEFTKNCETAVPLAWKQSAAGDIIMLSPACASWDQYPNFEVRGDRYIKAVEQL 452
Cdd:COG0771   377 DAEKIAAALAGAGVP-VVIVETMEEAVAAAAELARPGDVVLLSPACASFDQFKNYEERGDVFKEAVREL 444
 
Name Accession Description Interval E-value
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
6-452 0e+00

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: 545.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   6 QYRNQKVLVLGLAKSGVNAARLLHKLGAFVTVNDKKDFDQNPdAQELLSDGIKVITGGHPLSLLDeDFKVVVKNPGIPYS 85
Cdd:COG0771     1 DLKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELA-AAELEAPGVEVVLGEHPEELLD-GADLVVKSPGIPPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  86 NPIVSGAIQKHIPVITEVELAAQILE-------------------GELIGvtgtngktttttlitmmlnqrsQAG-KAYV 145
Cdd:COG0771    79 HPLLKAARAAGIPVIGEIELAYRLSPapiiaitgtngktttttliGHILK----------------------AAGlRVAV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 146 AGNIGVPASAVAQKAGANDTMVTELSSFMLCGIDQLHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVIN 225
Cdd:COG0771   137 GGNIGTPLLDLLLEPEPPDVYVLELSSFQLETTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANQTPDDYAVLN 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 226 WDSQEWRDLSQQSRAQVVPFSRQGNSTDGAYERDGQLYFR--DEYIMDAKEIKIPGEHNVENALAAIAVAKLQGVPTNGI 303
Cdd:COG0771   217 ADDPLTRALAEEAKARVVPFSLKEPLEGGAGLEDGKLVDRasGEELLPVDDLRLPGRHNLENALAALAAARALGVPPEAI 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 304 VEVLKSFSGVRHRTQYVETYEGRQFYNDSKATNIVSTEMALRGFDHPVVLLAGGLDRGNTFEKLAPALKKHVKTLIVFGE 383
Cdd:COG0771   297 REALRSFKGLPHRLEFVAEINGVRFINDSKATNPDATLAALESFDGPVVLIAGGLDKGADFSPLAPAVAERVKAVVLIGE 376
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655159775 384 TAQKLADAGKLAGIEdIEFTKNCETAVPLAWKQSAAGDIIMLSPACASWDQYPNFEVRGDRYIKAVEQL 452
Cdd:COG0771   377 DAEKIAAALAGAGVP-VVIVETMEEAVAAAAELARPGDVVLLSPACASFDQFKNYEERGDVFKEAVREL 444
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
6-452 2.18e-142

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


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 415.14  E-value: 2.18e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   6 QYRNQKVLVLGLAKSGVNAARLLHKLGAFVTVNDKKDFDQNPDAQELLSD-GIKVITGGHPLSLLDeDFKVVVKNPGIPY 84
Cdd:PRK14106    2 ELKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEKEEDQLKEALEELGElGIELVLGEYPEEFLE-GVDLVVVSPGVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  85 SNPIVSGAIQKHIPVITEVELA-----AQI--------------LEGELIgvtgtngktttttlitmmlnqRSQAGKAYV 145
Cdd:PRK14106   81 DSPPVVQAHKKGIEVIGEVELAyrfskAPIvaitgtngktttttLLGEIF---------------------KNAGRKTLV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 146 AGNIGVPASAVAQKAGANDTMVTELSSFMLCGIDQLHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVIN 225
Cdd:PRK14106  140 AGNIGYPLIDAVEEYGEDDIIVAEVSSFQLETIKEFKPKVGCILNITPDHLDRHKTMENYIKAKARIFENQRPSDYTVLN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 226 WDSQEWRDLSQQSRAQVVPFSRQGNSTDGAYERDGQLYFR----DEYIMDAKEIKIPGEHNVENALAAIAVAKLQGVPTN 301
Cdd:PRK14106  220 YDDPRTRSLAKKAKARVIFFSRKSLLEEGVFVKNGKIVISlggkEEEVIDIDEIFIPGEHNLENALAATAAAYLLGISPD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 302 GIVEVLKSFSGVRHRTQYVETYEGRQFYNDSKATNIVSTEMALRGFDHPVVLLAGGLDRGNTFEKLAPALKKHVKTLIVF 381
Cdd:PRK14106  300 VIANTLKTFKGVEHRIEFVAEINGVKFINDSKGTNPDAAIKALEAYETPIVLIAGGYDKGSDFDEFAKAFKEKVKKLILL 379
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655159775 382 GETAQKLADAGKLAGIEDIEFTKNCETAVPLAWKQSAAGDIIMLSPACASWDQYPNFEVRGDRYIKAVEQL 452
Cdd:PRK14106  380 GETAQEIAEAARKYGFDNILFAETLEEAVKKAYEIAKPGDVVLLSPACASWDMFKNFEERGRLFKELVLEL 450
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
11-451 1.18e-135

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: 397.48  E-value: 1.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  11 KVLVLGLAKSGVNAARLLHKLGAFVTVNDKKDFDQNPDAQELLSDGIKVITGGHPLSLLDEDFKVVVKNPGIPYSNPIVS 90
Cdd:TIGR01087   1 KILILGLGKTGRAVARFLHKKGAEVTVTDLKPNEELEPSMGQLRLNEGSVLHTGLHLEDLNNADLVVKSPGIPPDHPLVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  91 GAIQKHIPVITEVELAAQILEGELIGVTGTNGKTTTTTLITMMLNQRSQagKAYVAGNIGVPASAVAQKAGAnDTMVTEL 170
Cdd:TIGR01087  81 AAAKRGIPVVGDIELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGL--KAFLGGNIGTPALEVLDQEGA-ELYVLEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 171 SSFMLCGIDQLHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVINWDSQEWRDLSQQSRAQVVPFSRQGN 250
Cdd:TIGR01087 158 SSFQLETTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAVLNADDPRFARLAQKSKAQVIWFSVEKD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 251 STDGAYERDGQLYFRDeyimDAKEIKIPGEHNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQYVETYEGRQFYN 330
Cdd:TIGR01087 238 AERGLCIRDGGLYLKP----NDLEGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQKNGVHFYN 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 331 DSKATNIVSTEMALRGFDHPVVLLAGGLDRGNTFEKLAPALKKHVKTLIVFGETAQKLADAGKLAGIEDIEFtKNCETAV 410
Cdd:TIGR01087 314 DSKATNVHATLAALSAFDNPVILIVGGDDKGADFSPLAPAAAGKVKAVLAIGEDAAKIAPLLKEAGLSVYLV-ESLEEAV 392
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1655159775 411 PLAWKQSAAGDIIMLSPACASWDQYPNFEVRGDRYIKAVEQ 451
Cdd:TIGR01087 393 QAAREVASPGDVVLLSPACASFDQFKSYEERGEKFKELVRA 433
Mur_ligase_M pfam08245
Mur ligase middle domain;
149-293 4.23e-27

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 107.39  E-value: 4.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 149 IGVPAS-AVAQKAGAnDTMVTELSSFmlcGIDQ------LHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDY 221
Cdd:pfam08245  43 IGLPLTlAEMVEAGA-EYAVLEVSSH---GLGEgrlsglLKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 222 FVINWD---SQEWRDLSQQSRAQVVPFSRQGNSTDGA----YERDGQLYFRDEYIMDAKEIKIP--GEHNVENALAAIAV 292
Cdd:pfam08245 119 AVINADdpyGAFLIAKLKKAGVRVITYGIEGEADLRAanieLSSDGTSFDLFTVPGGELEIEIPllGRHNVYNALAAIAA 198

                  .
gi 1655159775 293 A 293
Cdd:pfam08245 199 A 199
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
11-115 1.17e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 42.11  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   11 KVLVLGLAKSGVNAARLLHKLGAFVTVndkkdFDQNPDAQELLSD--GIKVIT---GGHPLSLLDEDFKVVVKNPGIPYs 85
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTV-----LDVRPARLRQLESllGARFTTlysQAELLEEAVKEADLVIGAVLIPG- 95
                           90       100       110
                   ....*....|....*....|....*....|
gi 1655159775   86 npivsgaiqKHIPVITEVELAAQILEGELI 115
Cdd:smart01002  96 ---------AKAPKLVTREMVKSMKPGSVI 116
F430_CfbE NF033197
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ...
123-370 4.28e-03

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: 39.23  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 123 KTTTTTLITMMLNQRSQAgkayvAGNIgVPASAVAQKAGAN--DTMVTElSSFMLCGI-DqlhphIAVITNI---YSThl 196
Cdd:NF033197  125 RGTERYPEGELSNKGSIT-----PASI-LNALELAEEIGIDdyGFLIFE-VSLGGTGAgD-----VGIITNIledYPI-- 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 197 dwHGNRENYVKAKMRITMNQTADDYFVINWDSQEWRDLSQQSRaqvvpfsrqGNSTDGAYERDGQLYFRDEYImdakEIK 276
Cdd:NF033197  191 --AGGKRSASAAKLQSLKNAKVGSINVADLGIYINGKNKLVIT---------VAGVEILSKYPLRFKYGNTEF----EFN 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 277 --IPGEHNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQyVETYEGRQFYNDSK-ATNIVSTEMAL---RGFDHP 350
Cdd:NF033197  256 plLFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMA-VKKEGGVVIVDNINpGLNVKAIEYALddaLELLGD 334
                         250       260
                  ....*....|....*....|
gi 1655159775 351 VVLLAGGlDRGNTFEKLAPA 370
Cdd:NF033197  335 GTLVIGG-DFGVVCEEIDID 353
 
Name Accession Description Interval E-value
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
6-452 0e+00

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: 545.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   6 QYRNQKVLVLGLAKSGVNAARLLHKLGAFVTVNDKKDFDQNPdAQELLSDGIKVITGGHPLSLLDeDFKVVVKNPGIPYS 85
Cdd:COG0771     1 DLKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELA-AAELEAPGVEVVLGEHPEELLD-GADLVVKSPGIPPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  86 NPIVSGAIQKHIPVITEVELAAQILE-------------------GELIGvtgtngktttttlitmmlnqrsQAG-KAYV 145
Cdd:COG0771    79 HPLLKAARAAGIPVIGEIELAYRLSPapiiaitgtngktttttliGHILK----------------------AAGlRVAV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 146 AGNIGVPASAVAQKAGANDTMVTELSSFMLCGIDQLHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVIN 225
Cdd:COG0771   137 GGNIGTPLLDLLLEPEPPDVYVLELSSFQLETTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANQTPDDYAVLN 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 226 WDSQEWRDLSQQSRAQVVPFSRQGNSTDGAYERDGQLYFR--DEYIMDAKEIKIPGEHNVENALAAIAVAKLQGVPTNGI 303
Cdd:COG0771   217 ADDPLTRALAEEAKARVVPFSLKEPLEGGAGLEDGKLVDRasGEELLPVDDLRLPGRHNLENALAALAAARALGVPPEAI 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 304 VEVLKSFSGVRHRTQYVETYEGRQFYNDSKATNIVSTEMALRGFDHPVVLLAGGLDRGNTFEKLAPALKKHVKTLIVFGE 383
Cdd:COG0771   297 REALRSFKGLPHRLEFVAEINGVRFINDSKATNPDATLAALESFDGPVVLIAGGLDKGADFSPLAPAVAERVKAVVLIGE 376
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655159775 384 TAQKLADAGKLAGIEdIEFTKNCETAVPLAWKQSAAGDIIMLSPACASWDQYPNFEVRGDRYIKAVEQL 452
Cdd:COG0771   377 DAEKIAAALAGAGVP-VVIVETMEEAVAAAAELARPGDVVLLSPACASFDQFKNYEERGDVFKEAVREL 444
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
6-452 2.18e-142

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


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 415.14  E-value: 2.18e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   6 QYRNQKVLVLGLAKSGVNAARLLHKLGAFVTVNDKKDFDQNPDAQELLSD-GIKVITGGHPLSLLDeDFKVVVKNPGIPY 84
Cdd:PRK14106    2 ELKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEKEEDQLKEALEELGElGIELVLGEYPEEFLE-GVDLVVVSPGVPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  85 SNPIVSGAIQKHIPVITEVELA-----AQI--------------LEGELIgvtgtngktttttlitmmlnqRSQAGKAYV 145
Cdd:PRK14106   81 DSPPVVQAHKKGIEVIGEVELAyrfskAPIvaitgtngktttttLLGEIF---------------------KNAGRKTLV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 146 AGNIGVPASAVAQKAGANDTMVTELSSFMLCGIDQLHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVIN 225
Cdd:PRK14106  140 AGNIGYPLIDAVEEYGEDDIIVAEVSSFQLETIKEFKPKVGCILNITPDHLDRHKTMENYIKAKARIFENQRPSDYTVLN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 226 WDSQEWRDLSQQSRAQVVPFSRQGNSTDGAYERDGQLYFR----DEYIMDAKEIKIPGEHNVENALAAIAVAKLQGVPTN 301
Cdd:PRK14106  220 YDDPRTRSLAKKAKARVIFFSRKSLLEEGVFVKNGKIVISlggkEEEVIDIDEIFIPGEHNLENALAATAAAYLLGISPD 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 302 GIVEVLKSFSGVRHRTQYVETYEGRQFYNDSKATNIVSTEMALRGFDHPVVLLAGGLDRGNTFEKLAPALKKHVKTLIVF 381
Cdd:PRK14106  300 VIANTLKTFKGVEHRIEFVAEINGVKFINDSKGTNPDAAIKALEAYETPIVLIAGGYDKGSDFDEFAKAFKEKVKKLILL 379
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655159775 382 GETAQKLADAGKLAGIEDIEFTKNCETAVPLAWKQSAAGDIIMLSPACASWDQYPNFEVRGDRYIKAVEQL 452
Cdd:PRK14106  380 GETAQEIAEAARKYGFDNILFAETLEEAVKKAYEIAKPGDVVLLSPACASWDMFKNFEERGRLFKELVLEL 450
murD TIGR01087
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ...
11-451 1.18e-135

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: 397.48  E-value: 1.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  11 KVLVLGLAKSGVNAARLLHKLGAFVTVNDKKDFDQNPDAQELLSDGIKVITGGHPLSLLDEDFKVVVKNPGIPYSNPIVS 90
Cdd:TIGR01087   1 KILILGLGKTGRAVARFLHKKGAEVTVTDLKPNEELEPSMGQLRLNEGSVLHTGLHLEDLNNADLVVKSPGIPPDHPLVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  91 GAIQKHIPVITEVELAAQILEGELIGVTGTNGKTTTTTLITMMLNQRSQagKAYVAGNIGVPASAVAQKAGAnDTMVTEL 170
Cdd:TIGR01087  81 AAAKRGIPVVGDIELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGL--KAFLGGNIGTPALEVLDQEGA-ELYVLEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 171 SSFMLCGIDQLHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVINWDSQEWRDLSQQSRAQVVPFSRQGN 250
Cdd:TIGR01087 158 SSFQLETTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAVLNADDPRFARLAQKSKAQVIWFSVEKD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 251 STDGAYERDGQLYFRDeyimDAKEIKIPGEHNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQYVETYEGRQFYN 330
Cdd:TIGR01087 238 AERGLCIRDGGLYLKP----NDLEGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQKNGVHFYN 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 331 DSKATNIVSTEMALRGFDHPVVLLAGGLDRGNTFEKLAPALKKHVKTLIVFGETAQKLADAGKLAGIEDIEFtKNCETAV 410
Cdd:TIGR01087 314 DSKATNVHATLAALSAFDNPVILIVGGDDKGADFSPLAPAAAGKVKAVLAIGEDAAKIAPLLKEAGLSVYLV-ESLEEAV 392
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1655159775 411 PLAWKQSAAGDIIMLSPACASWDQYPNFEVRGDRYIKAVEQ 451
Cdd:TIGR01087 393 QAAREVASPGDVVLLSPACASFDQFKSYEERGEKFKELVRA 433
MurF COG0770
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
175-425 3.40e-29

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: 119.05  E-value: 3.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 175 LCGIdqLHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVINWDSQEWRDLSQQSRAQVVPFSRQGNST-- 252
Cdd:COG0770   170 LARI--ARPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGLPPGGVAVLNADDPLLAALAERAKARVLTFGLSEDADvr 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 253 -DGAYERDGQLYFRDEYIMDAKEIKIP--GEHNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQYVETYEGRQFY 329
Cdd:COG0770   248 aEDIELDEDGTRFTLHTPGGELEVTLPlpGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLEVIEGAGGVTLI 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 330 NDS-KAtNIVSTEMALRGF-----DHPVVLLAG-----GLDRGNTFEKLA-PALKKHVKTLIVFGETAQKLADAgklAGI 397
Cdd:COG0770   328 DDSyNA-NPDSMKAALDVLaqlpgGGRRIAVLGdmlelGEESEELHREVGeLAAELGIDRLFTVGELARAIAEA---AGG 403
                         250       260
                  ....*....|....*....|....*...
gi 1655159775 398 EDIEFTKNCETAVPLAWKQSAAGDIIML 425
Cdd:COG0770   404 ERAEHFEDKEELLAALKALLRPGDVVLV 431
MurC COG0773
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ...
25-331 4.32e-29

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: 118.63  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  25 ARLLHKLGAFVTVNDKKDfdqNPDAQELLSDGIKVITGGHPLSLLDEDfkVVVKNPGIPYSNPIVSGAIQKHIPVITeve 104
Cdd:COG0773    21 AEILLALGYKVSGSDLAE---SPMTERLEALGIPVFIGHDAENIDDAD--LVVVSSAIPRDNPELVAARERGIPVLS--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 105 lAAQILeGELIGvtgtngktttttlitmmlNQRS---------------------QAGKA--YVAG----NIGVPAsava 157
Cdd:COG0773    93 -RAEML-AELMR------------------GKRSiavagthgkttttsmlahileEAGLDptFLIGgilnNFGTNA---- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 158 qKAGANDTMVTE----LSSFMlcgidQLHPHIAVITNIYSTHLDWHGNRENYVKAkMRITMNQTADDYFVI-NWDSQEWR 232
Cdd:COG0773   149 -RLGDGDYFVAEadesDGSFL-----HYSPDIAVVTNIEADHLDIYGDLEAIKEA-FHEFARNVPFYGLLVlCADDPGLR 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 233 DLSQQSRAQVVPFSRQGNS----TDGAYERDGQ---LYFRDEYIMDAkEIKIPGEHNVENALAAIAVAKLQGVPTNGIVE 305
Cdd:COG0773   222 ELLPRCGRPVITYGFSEDAdyraENIRIDGGGStfdVLRRGEELGEV-ELNLPGRHNVLNALAAIAVALELGVDPEAIAE 300
                         330       340
                  ....*....|....*....|....*.
gi 1655159775 306 VLKSFSGVRHRTQYVETYEGRQFYND 331
Cdd:COG0773   301 ALASFKGVKRRFELKGEVGGVTVIDD 326
Mur_ligase_M pfam08245
Mur ligase middle domain;
149-293 4.23e-27

Mur ligase middle domain;


Pssm-ID: 462409 [Multi-domain]  Cd Length: 199  Bit Score: 107.39  E-value: 4.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 149 IGVPAS-AVAQKAGAnDTMVTELSSFmlcGIDQ------LHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDY 221
Cdd:pfam08245  43 IGLPLTlAEMVEAGA-EYAVLEVSSH---GLGEgrlsglLKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 222 FVINWD---SQEWRDLSQQSRAQVVPFSRQGNSTDGA----YERDGQLYFRDEYIMDAKEIKIP--GEHNVENALAAIAV 292
Cdd:pfam08245 119 AVINADdpyGAFLIAKLKKAGVRVITYGIEGEADLRAanieLSSDGTSFDLFTVPGGELEIEIPllGRHNVYNALAAIAA 198

                  .
gi 1655159775 293 A 293
Cdd:pfam08245 199 A 199
murC TIGR01082
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ...
16-347 3.86e-24

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: 104.31  E-value: 3.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  16 GLAKSGVnaARLLHKLGAFVTVNDKKDfdqNPDAQELLSDGIKVITGGHPLSLldEDFKVVVKNPGIPYSNPIVSGAIQK 95
Cdd:TIGR01082   9 GIGMSGI--AEILLNRGYQVSGSDIAE---NATTKRLEALGIPIYIGHSAENL--DDADVVVVSAAIKDDNPEIVEAKER 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  96 HIPVITEVELAAQILEGEligvtgtngktttttlitmmlnqRSQA-----GK-------AYVAGNIGVPASAVA------ 157
Cdd:TIGR01082  82 GIPVIRRAEMLAELMRFR-----------------------HSIAvagthGKttttamiAVILKEAGLDPTVVVgglvke 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 158 ----QKAGANDTMVTEL----SSFMlcgidQLHPHIAVITNIYSTHLDWHGNR-ENYVKAKMRITMNQTADDYFVINWDS 228
Cdd:TIGR01082 139 agtnARLGSGEYLVAEAdesdASFL-----HLQPNVAIVTNIEPDHLDTYGSSfERLKAAFEKFIHNLPFYGLAVICADD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 229 QEWRDLSQqsRAQVVPFSRQGNSTDGAY------ERDGQLYF----RDEYIMDAKeIKIPGEHNVENALAAIAVAKLQGV 298
Cdd:TIGR01082 214 PVLRELVP--KATEQVITYGGSGEDADYraeniqQSGAEGKFsvrgKGKLYLEFT-LNLPGRHNVLNALAAIAVALELGI 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1655159775 299 PTNGIVEVLKSFSGVRHRTQYVETYEGRQFYND--SKATNIVSTEMALRGF 347
Cdd:TIGR01082 291 DFEAILRALANFQGVKRRFEILGEFGGVLLIDDyaHHPTEIKATLKAARQG 341
MurE COG0769
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ...
155-331 1.03e-22

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: 100.15  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 155 AVAQKAGAnDTMVTELSSFmlcGIDQ-----LHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVINWDSQ 229
Cdd:COG0769   141 AEMVDAGV-THVVMEVSSH---ALDQgrvdgVRFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQLGPGGAAVINADDP 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 230 EWRDLSQQSRAQVVPFSRQGNS----TDGAYERDGQlyfrdEYIMDAK------EIKIPGEHNVENALAAIAVAKLQGVP 299
Cdd:COG0769   217 YGRRLAAAAPARVITYGLKADAdlraTDIELSADGT-----RFTLVTPggevevRLPLIGRFNVYNALAAIAAALALGID 291
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1655159775 300 TNGIVEVLKSFSGVRHRTQYVETYEGRQFYND 331
Cdd:COG0769   292 LEEILAALEKLKGVPGRMERVDGGQGPTVIVD 323
murF TIGR01143
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ...
148-344 4.09e-18

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: 86.17  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 148 NIGVPASaVAQKAGANDTMVTELSsfM--------LCGIDQlhPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTAD 219
Cdd:TIGR01143 112 EIGLPLT-LLRAPGDHDYAVLEMG--AshpgeiayLAEIAK--PDIAVITNIGPAHLEGFGSLEGIAEAKGEILQGLKEN 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 220 DYFVINWDS---QEWRdlSQQSRAQVVPFSRQGNSTDGA---YERDGQLYFRDEYIMDAKEIKIP--GEHNVENALAAIA 291
Cdd:TIGR01143 187 GIAVINADDpafADLA--KRLPNRNILSFGFEGGDFVAKdisYSALGSTSFTLVAPGGEFEVSLPllGRHNVMNALAAAA 264
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1655159775 292 VAKLQGVPTNGIVEVLKSFSGVRHRTQYVETyEGRQFYNDSKATNIVSTEMAL 344
Cdd:TIGR01143 265 LALELGIPLEEIAEGLAELKLVKGRFEVQTK-NGLTLIDDTYNANPDSMRAAL 316
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
139-424 2.05e-16

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: 82.06  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 139 QAGKAYVAGN----IGVPASAVAQKAGaNDTMVTELSSFMLCGIDQL----HPHIAVITNIYSTHLDWHGNRENYVKAKM 210
Cdd:PRK11929  631 EDRVLATEGNfnneIGVPLTLLRLRAQ-HRAAVFELGMNHPGEIAYLaaiaAPTVALVTNAQREHQEFMHSVEAVARAKG 709
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 211 RITMNQTADDYFVINWD---SQEWRDLSQQSRAQVVPFSRQGNS------TDGAYERDGQLYFRDEYIMDAKEIKIP--G 279
Cdd:PRK11929  710 EIIAALPEDGVAVVNGDdpyTAIWAKLAGARRVLRFGLQPGADVyaekiaKDISVGEAGGTRCQVVTPAGSAEVYLPliG 789
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 280 EHNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQYVETYEGRQFYNDSKATNIVSTEMALRGFDH----PVVLLA 355
Cdd:PRK11929  790 EHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSCGTRIIDDTYNANPDSMRAAIDVLAElpngPRALVL 869
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 356 GG-LDRGNTFEKL-----APALKKHVKTLIVFGETAQKLADA------GKLAGIEDIeftkncetavpLAWKQS--AAGD 421
Cdd:PRK11929  870 GDmLELGDNGPAMhrevgKYARQLGIDALITLGEAARDAAAAfgagarGVCASVDEI-----------IAALRGalPEGD 938

                  ...
gi 1655159775 422 IIM 424
Cdd:PRK11929  939 SVL 941
PRK14573 PRK14573
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
42-331 7.04e-15

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


Pssm-ID: 184752 [Multi-domain]  Cd Length: 809  Bit Score: 77.16  E-value: 7.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775  42 DFDQNPDAQELLSDGIKVITGgHPLSLLDEDfKVVVKNPGIPYSNPIVSGAIQKHIPVITEVELAAQILEGELIGVTGTN 121
Cdd:PRK14573   35 DLSEGKTVEKLKAKGARFFLG-HQEEHVPED-AVVVYSSSISKDNVEYLSAKSRGNRLVHRAELLAELMQEQISILVSGS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 122 GKTTTTTLITMMLNQRSQAGKAYVAGniGVPASAVAQKAGANDTMVTELSSfMLCGIDQLHPHIAVITNIYSTHL-DWHG 200
Cdd:PRK14573  113 HGKTTVSSLITAIFQEAKKDPSYAIG--GLNQEGLNGYSGSSEYFVAEADE-SDGSLKHYTPEFSVITNIDNEHLsNFEG 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 201 NRENYVKAKMRITMNQTADDYFVINWDSQEWRD--------LSQQSRAQVVPFSRQGNSTDGAYERDGQLYfrdeyiMDA 272
Cdd:PRK14573  190 DRELLLASIQDFARKVQQINKCFYNGDCPRLKGclqghsygFSSSCDLHILSYYQEGWRSYFSAKFLGVVY------QDI 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1655159775 273 kEIKIPGEHNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQYVETYEGRQFYND 331
Cdd:PRK14573  264 -ELNLVGMHNVANAAAAMGIALTLGIDEGAIRNALKGFSGVQRRLERKNSSETFLFLED 321
murE PRK00139
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
155-320 1.61e-14

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


Pssm-ID: 234660 [Multi-domain]  Cd Length: 460  Bit Score: 75.17  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 155 AVAQKAGAnDTMVTELSSFmlcGIDQ-----LHPHIAVITNIYSTHLDWHGNRENYVKAKMRITmnQTADDYFVINWDSQ 229
Cdd:PRK00139  156 AELVDAGV-TYAAMEVSSH---ALDQgrvdgLKFDVAVFTNLSRDHLDYHGTMEDYLAAKARLF--SELGLAAVINADDE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 230 EWRDLSQqsRAQVVPFSRQGNS---TDGAYERDGQ-LYFRDEYimdakEIKIPGEHNVENALAAIAVAKLQGVPTNGIVE 305
Cdd:PRK00139  230 VGRRLLA--LPDAYAVSMAGADlraTDVEYTDSGQtFTLVTEV-----ESPLIGRFNVSNLLAALAALLALGVPLEDALA 302
                         170
                  ....*....|....*
gi 1655159775 306 VLKSFSGVRHRTQYV 320
Cdd:PRK00139  303 ALAKLQGVPGRMERV 317
PRK11929 PRK11929
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ...
159-327 2.30e-12

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: 69.35  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 159 KAGAnDTMVTELSSFmlcGIDQ-----LHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVINWDSQEWRD 233
Cdd:PRK11929  177 AAGA-DAVAMEASSH---GLEQgrldgLRIAVAGFTNLTRDHLDYHGTMQDYEEAKAALFSKLPGLGAAVINADDPAAAR 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 234 L-SQQSRAQVVPFSRQGNSTDgAYERD------GQL----YFRDEYIMDakeIKIPGEHNVENALAAIAVAKLQGVPTNG 302
Cdd:PRK11929  253 LlAALPRGLKVGYSPQNAGAD-VQARDlratahGQVftlaTPDGSYQLV---TRLLGRFNVSNLLLVAAALKKLGLPLAQ 328
                         170       180
                  ....*....|....*....|....*
gi 1655159775 303 IVEVLKSFSGVRHRTQYVETYEGRQ 327
Cdd:PRK11929  329 IARALAAVSPVPGRMERVGPTAGAQ 353
Mur_ligase_C pfam02875
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ...
313-381 2.16e-08

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: 51.19  E-value: 2.16e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655159775 313 VRHRTQYVETYEGRQFYNDsKATNIVSTEMALRG----FDHPVVLLAGG-LDRGNTFEKLAPALKKHVKTLIVF 381
Cdd:pfam02875   1 VPGRLEVVGENNGVLVIDD-YAHNPDAMEAALRAlrnlFPGRLILVFGGmGDRDAEFHALLGRLAAALADVVIL 73
PRK14016 PRK14016
cyanophycin synthetase; Provisional
184-310 6.52e-07

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 51.70  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 184 HIAVITNIYSTHLDWHG--NRENYVKAKMRITMNQTADDYFVINWDSQEWRDLSQQSRAQVVPFSRQGNS-------TDG 254
Cdd:PRK14016  567 DVGVVTNIGEDHLGLGGinTLEDLAKVKRVVVEAVKPDGYAVLNADDPMVAAMAERCKGKVIFFSMDPDNpviaehrAQG 646
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655159775 255 ---AYERDGQLYFRD----EYIMDAKEIKIPGE----HNVENALAAIAVAKLQGVPTNGIVEVLKSF 310
Cdd:PRK14016  647 graVYVEGDYIVLAEggweIRIISLADIPLTLGgkagFNIENALAAIAAAWALGIDIELIRAGLRTF 713
murF PRK10773
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
138-339 6.54e-07

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


Pssm-ID: 182718 [Multi-domain]  Cd Length: 453  Bit Score: 51.57  E-value: 6.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 138 SQAGKA-YVAGN----IGVPASAVAQKAgANDTMVTELSSFMLCGI----DQLHPHIAVITNIYSTHLDWHGNRENYVKA 208
Cdd:PRK10773  123 RQCGNTlYTAGNlnndIGVPLTLLRLTP-EHDYAVIELGANHQGEIaytvSLTRPEAALVNNLAAAHLEGFGSLAGVAKA 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 209 KMRITMNQTADDYFVINWDSQEWRDLSQQSRAQVV-PFSRQGNSTDGAYERDGQL-----YFRDEYIMDAKEIKIP--GE 280
Cdd:PRK10773  202 KGEIFSGLPENGIAIMNADSNDWLNWQSVIGSKTVwRFSPNAANSVDFTATNIHVtshgtEFTLHTPTGSVDVLLPlpGR 281
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1655159775 281 HNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQYVETYEGRQFYNDSKATNIVS 339
Cdd:PRK10773  282 HNIANALAAAALAMSVGATLDAVKAGLANLKAVPGRLFPIQLAEGQLLLDDSYNANVGS 340
murE TIGR01085
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ...
121-320 1.55e-05

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: 47.31  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 121 NGKTTTTTLITMMLnqRSQAGKAYVAGNIG----------------VPASAVAQKAGAN------DTMVTELSSFmlcGI 178
Cdd:TIGR01085  94 NGKTTTTSLIAQLL--RLLGKKTGLIGTIGyrlggndliknpaaltTPEALTLQSTLAEmveagaQYAVMEVSSH---AL 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 179 DQ-----LHPHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVINWD---SQEWRDLSQQS-----RAQVVPF 245
Cdd:TIGR01085 169 AQgrvrgVRFDAAVFTNLSRDHLDFHGTMENYFAAKASLFTELGLKRFAVINLDdeyGAQFVKRLPKDitvsaITQPADG 248
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655159775 246 SRQGNS-TDGAYERDGQLyFRDEYIMDAKEIKIP--GEHNVENALAAIAVAKLQG-VPTNGIVEVLKSFSGVRHRTQYV 320
Cdd:TIGR01085 249 RAQDIKiTDSGYSFEGQQ-FTFETPAGEGHLHTPliGRFNVYNLLAALATLLHLGgIDLEDIVAALEKFRGVPGRMELV 326
PRK11930 PRK11930
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ...
183-459 2.02e-05

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


Pssm-ID: 237026 [Multi-domain]  Cd Length: 822  Bit Score: 47.26  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 183 PHIAVITNIYSTHLDWHGNRENYVKAKMRITmnqTADDYFVINWDSQE----------------WrDLSQQSRAQVVPFS 246
Cdd:PRK11930  183 PTIGILTNIGGAHQENFRSIKQKIMEKLKLF---KDCDVIIYNGDNELisscitksnltlklisW-SRKDPEAPLYIPFV 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 247 RQGNStdgayERDGQLYFRDEYImdakEIKIP--GEHNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQYVETYE 324
Cdd:PRK11930  259 EKKED-----HTVISYTYKGEDF----HFEIPfiDDASIENLIHCIAVLLYLGYSADQIQERMARLEPVAMRLEVKEGIN 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 325 GRQFYNDSKATNIVSTEMALRGFDH------PVVLLAGGLDRGNT----FEKLAPAL-KKHVKTLIVFGETAQKLADagK 393
Cdd:PRK11930  330 NCTLINDSYNSDLQSLDIALDFLNRrsqskkKTLILSDILQSGQSpeelYRKVAQLIsKRGIDRLIGIGEEISSEAS--K 407
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655159775 394 LAGIEdIEFTKNCETAVPLAWKQSAAGDIIMlspacaswdqypnfeVRGDRYI---KAVEQLTGKAEEN 459
Cdd:PRK11930  408 FEGTE-KEFFKTTEAFLKSFAFLKFRNELIL---------------VKGARKFefeQITELLEQKVHET 460
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
11-115 1.17e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 42.11  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   11 KVLVLGLAKSGVNAARLLHKLGAFVTVndkkdFDQNPDAQELLSD--GIKVIT---GGHPLSLLDEDFKVVVKNPGIPYs 85
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTV-----LDVRPARLRQLESllGARFTTlysQAELLEEAVKEADLVIGAVLIPG- 95
                           90       100       110
                   ....*....|....*....|....*....|
gi 1655159775   86 npivsgaiqKHIPVITEVELAAQILEGELI 115
Cdd:smart01002  96 ---------AKAPKLVTREMVKSMKPGSVI 116
PRK14093 PRK14093
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ...
183-297 1.67e-03

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


Pssm-ID: 184501 [Multi-domain]  Cd Length: 479  Bit Score: 40.53  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 183 PHIAVITNIYSTHLDWHGNRENYVKAKMRITMNQTADDYFVINWDSQEWRDLSQQSRA----QVVPFSRQGNS----TDG 254
Cdd:PRK14093  184 PHVAIITTVEPVHLEFFSGIEAIADAKAEIFTGLEPGGAAVLNRDNPQFDRLAASARAagiaRIVSFGADEKAdarlLDV 263
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1655159775 255 AYERDGQLYFRDeyIMDAK---EIKIPGEHNVENALAAIAVAKLQG 297
Cdd:PRK14093  264 ALHADCSAVHAD--ILGHDvtyKLGMPGRHIAMNSLAVLAAAELAG 307
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-79 3.92e-03

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 39.33  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   5 EQYRNQKVLVLGLAKSGVNAARLLHKLGAFVT-VNDKKDFDQNPDAQELL--SDGIKVITGGHPLSLLDEDF--KVVVKN 79
Cdd:COG0492   137 FFFRGKDVVVVGGGDSALEEALYLTKFASKVTlIHRRDELRASKILVERLraNPKIEVLWNTEVTEIEGDGRveGVTLKN 216
F430_CfbE NF033197
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ...
123-370 4.28e-03

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: 39.23  E-value: 4.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 123 KTTTTTLITMMLNQRSQAgkayvAGNIgVPASAVAQKAGAN--DTMVTElSSFMLCGI-DqlhphIAVITNI---YSThl 196
Cdd:NF033197  125 RGTERYPEGELSNKGSIT-----PASI-LNALELAEEIGIDdyGFLIFE-VSLGGTGAgD-----VGIITNIledYPI-- 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 197 dwHGNRENYVKAKMRITMNQTADDYFVINWDSQEWRDLSQQSRaqvvpfsrqGNSTDGAYERDGQLYFRDEYImdakEIK 276
Cdd:NF033197  191 --AGGKRSASAAKLQSLKNAKVGSINVADLGIYINGKNKLVIT---------VAGVEILSKYPLRFKYGNTEF----EFN 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775 277 --IPGEHNVENALAAIAVAKLQGVPTNGIVEVLKSFSGVRHRTQyVETYEGRQFYNDSK-ATNIVSTEMAL---RGFDHP 350
Cdd:NF033197  256 plLFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMA-VKKEGGVVIVDNINpGLNVKAIEYALddaLELLGD 334
                         250       260
                  ....*....|....*....|
gi 1655159775 351 VVLLAGGlDRGNTFEKLAPA 370
Cdd:NF033197  335 GTLVIGG-DFGVVCEEIDID 353
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
9-95 6.32e-03

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 38.34  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159775   9 NQKVLVLGLAKSGV--NAARLLHKLGAFVTVNDKKDFDQNPDAQELLSDGIKVItgGHPLSLLDED-------------- 72
Cdd:PRK13394    6 NGKTAVVTGAASGIgkEIALELARAGAAVAIADLNQDGANAVADEINKAGGKAI--GVAMDVTNEDavnagidkvaerfg 83
                          90       100
                  ....*....|....*....|....
gi 1655159775  73 -FKVVVKNPGIPYSNPIVSGAIQK 95
Cdd:PRK13394   84 sVDILVSNAGIQIVNPIENYSFAD 107
 
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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