|
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
|
|
|