|
Name |
Accession |
Description |
Interval |
E-value |
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
7-444 |
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: 561.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 7 LRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDLSnDAHAKDLEDLGISVVSGAHPLALLDEAPIIFKNPGIPYTVP 86
Cdd:COG0771 2 LKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAP-ELAAAELEAPGVEVVLGEHPEELLDGADLVVKSPGIPPDHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 87 IIQEAQKQGLKILTEVELSYLISEAPIIGITGTNGKTTVTSLIGDMFNKSRENGRLSGNIGFVASKVAQEVKTDEYLVTE 166
Cdd:COG0771 81 LLKAARAAGIPVIGEIELAYRLSPAPIIAITGTNGKTTTTTLIGHILKAAGLRVAVGGNIGTPLLDLLLEPEPPDVYVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 167 LSSFQLLGIEHYRPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFNDKQRHLID-TSKIRAKILYFSTQH 245
Cdd:COG0771 161 LSSFQLETTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANQTPDDYAVLNADDPLTRAlAEEAKARVVPFSLKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 246 RVD-GIYVEKEYIVYN--GVRLIHLDDIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYIGNNKTNK 322
Cdd:COG0771 241 PLEgGAGLEDGKLVDRasGEELLPVDDLRLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLEFVAEINGVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 323 YYNDSKATNTLATQFALSSFKQPVIWLCGGLDRGNGFDELIPYMN-NVRVMVTFGETQDKFVKLGESQGKYVIRAKDVTD 401
Cdd:COG0771 321 FINDSKATNPDATLAALESFDGPVVLIAGGLDKGADFSPLAPAVAeRVKAVVLIGEDAEKIAAALAGAGVPVVIVETMEE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 504427078 402 AVAKVQDVIEPNDVVLLSPACASWDQYDTFEQRGERFIEAFRA 444
Cdd:COG0771 401 AVAAAAELARPGDVVLLSPACASFDQFKNYEERGDVFKEAVRE 443
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
7-445 |
1.58e-142 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 415.14 E-value: 1.58e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 7 LRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDLSNDAHA-KDLEDLGISVVSGAHPLALLDEAPIIFKNPGIPYTV 85
Cdd:PRK14106 3 LKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEKEEDQLKEAlEELGELGIELVLGEYPEEFLEGVDLVVVSPGVPLDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 86 PIIQEAQKQGLKILTEVELSYLISEAPIIGITGTNGKTTVTSLIGDMFNKSRENGRLSGNIGFVASKVAQEVKTDEYLVT 165
Cdd:PRK14106 83 PPVVQAHKKGIEVIGEVELAYRFSKAPIVAITGTNGKTTTTTLLGEIFKNAGRKTLVAGNIGYPLIDAVEEYGEDDIIVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 166 ELSSFQLLGIEHYRPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN---DKQRHLIDtsKIRAKILYFS 242
Cdd:PRK14106 163 EVSSFQLETIKEFKPKVGCILNITPDHLDRHKTMENYIKAKARIFENQRPSDYTVLNyddPRTRSLAK--KAKARVIFFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 243 TQHRVD-GIYVEKEYIV--YNGVR--LIHLDDIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYIGN 317
Cdd:PRK14106 241 RKSLLEeGVFVKNGKIVisLGGKEeeVIDIDEIFIPGEHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFVAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 318 NKTNKYYNDSKATNTLATQFALSSFKQPVIWLCGGLDRGNGFDELIPYMN-NVRVMVTFGETQDKFVKLGESQG-KYVIR 395
Cdd:PRK14106 321 INGVKFINDSKGTNPDAAIKALEAYETPIVLIAGGYDKGSDFDEFAKAFKeKVKKLILLGETAQEIAEAARKYGfDNILF 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 504427078 396 AKDVTDAVAKVQDVIEPNDVVLLSPACASWDQYDTFEQRGERFIEAFRAH 445
Cdd:PRK14106 401 AETLEEAVKKAYEIAKPGDVVLLSPACASWDMFKNFEERGRLFKELVLEL 450
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
11-444 |
1.51e-134 |
|
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: 394.01 E-value: 1.51e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 11 KVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDLSNDAHAKDLEDLGISVVSGAHP-LALLDEAPIIFKNPGIPYTVPIIQ 89
Cdd:TIGR01087 1 KILILGLGKTGRAVARFLHKKGAEVTVTDLKPNEELEPSMGQLRLNEGSVLHTGLhLEDLNNADLVVKSPGIPPDHPLVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 90 EAQKQGLKILTEVELSYLISEAPIIGITGTNGKTTVTSLIGDMFNKSRENGRLSGNIGFVASKVAQEvKTDEYLVTELSS 169
Cdd:TIGR01087 81 AAAKRGIPVVGDIELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFLGGNIGTPALEVLDQ-EGAELYVLELSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 170 FQLLGIEHYRPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN-DKQRHLIDTSKIRAKILYFSTQHRVD 248
Cdd:TIGR01087 160 FQLETTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAVLNaDDPRFARLAQKSKAQVIWFSVEKDAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 249 -GIYVEKEYIVYNGVRLihldDIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYIGNNKTNKYYNDS 327
Cdd:TIGR01087 240 rGLCIRDGGLYLKPNDL----EGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQKNGVHFYNDS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 328 KATNTLATQFALSSFKQPVIWLCGGLDRGNGFDELIPYMNNVRVMV-TFGETQDKFVKLGESQGKYVIRAKDVTDAVAKV 406
Cdd:TIGR01087 316 KATNVHATLAALSAFDNPVILIVGGDDKGADFSPLAPAAAGKVKAVlAIGEDAAKIAPLLKEAGLSVYLVESLEEAVQAA 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 504427078 407 QDVIEPNDVVLLSPACASWDQYDTFEQRGERFIEAFRA 444
Cdd:TIGR01087 396 REVASPGDVVLLSPACASFDQFKSYEERGEKFKELVRA 433
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
116-288 |
2.32e-30 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 116.25 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 116 ITGTNGKTTVTSLIGDMFNKSrenGRLSGNIGFVASK--------------VAQEVKTD-EYLVTELSSFQLlgIEHY-- 178
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLA---GGVIGTIGTYIGKsgnttnnaiglpltLAEMVEAGaEYAVLEVSSHGL--GEGRls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 179 ---RPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN--DK--QRHLIDTSKIRAKILYFSTQHRVDgIY 251
Cdd:pfam08245 76 gllKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIAVINadDPygAFLIAKLKKAGVRVITYGIEGEAD-LR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504427078 252 VEKEYIVYNGVRL--------IHLDDIVLPGEHNLENILAAVMAA 288
Cdd:pfam08245 155 AANIELSSDGTSFdlftvpggELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| F430_CfbE |
NF033197 |
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ... |
112-419 |
2.48e-09 |
|
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: 58.88 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 112 PIIGITGTNGKTTVTSLIGDMFnkSRENGRLSGNIGFV--------------------ASKVAQEVKTDEY--LVTElSS 169
Cdd:NF033197 93 KFIEITGVKGKTTTAELLAHIL--SDEYVLLHTSRGTErypegelsnkgsitpasilnALELAEEIGIDDYgfLIFE-VS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 170 FQLLGIEHYrphiAIITNLysahldyhenLENYQ---------NAKKRIFEN-QTESDYLIFNDKQ---RHLIDTSKIRA 236
Cdd:NF033197 170 LGGTGAGDV----GIITNI----------LEDYPiaggkrsasAAKLQSLKNaKVGSINVADLGIYingKNKLVITVAGV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 237 KILYFSTQHRVDGIyvekeyivyNGVRLIHLddivLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQ--Y 314
Cdd:NF033197 236 EILSKYPLRFKYGN---------TEFEFNPL----LFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMAvkK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 315 IGNNKTNKyyNDSKATNTLATQFALSSFKQPVIWL-----------CGGLDrgngFDELIPYMNNVRvmVTFGETQDKFV 383
Cdd:NF033197 303 EGGVVIVD--NINPGLNVKAIEYALDDALELLGDGtlviggdfgvvCEEID----IDKLSEVLKKYR--PKIDILVGVGT 374
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 504427078 384 KLGESQGKYV-----IRAKDVTDAVAKVQDVIEPNDVVLLS 419
Cdd:NF033197 375 ELGKRLKKYLdklegYEAGTLEEGLDDARELTGEGNTLVIY 415
|
|
| NAD_bind_H4MPT_DH |
cd01078 |
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ... |
3-154 |
2.21e-05 |
|
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133446 [Multi-domain] Cd Length: 194 Bit Score: 45.08 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 3 HYTGLRGKKVLVIGMAKS-GYEAAKLLHRLGAEVTV--NDGNDLSNDA---HAKDLEDLG-ISVVSGAHPLALLDEAPII 75
Cdd:cd01078 22 MGKDLKGKTAVVLGGTGPvGQRAAVLLAREGARVVLvgRDLERAQKAAdslRARFGEGVGaVETSDDAARAAAIKGADVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 76 FKNPGIPYTVPIIQEAQKQGLKILTEVelsyliSEAPIIGITGTngkttvtsligDMFNKS--RENGRLSGNIGFVASKV 153
Cdd:cd01078 102 FAAGAAGVELLEKLAWAPKPLAVAADV------NAVPPVGIEGI-----------DVPDKGvdREGKVPYGAIGVGGLKM 164
|
.
gi 504427078 154 A 154
Cdd:cd01078 165 K 165
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
6-39 |
1.97e-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: 41.34 E-value: 1.97e-04
10 20 30
....*....|....*....|....*....|....
gi 504427078 6 GLRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVND 39
Cdd:smart01002 17 GVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLD 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
7-444 |
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: 561.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 7 LRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDLSnDAHAKDLEDLGISVVSGAHPLALLDEAPIIFKNPGIPYTVP 86
Cdd:COG0771 2 LKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAP-ELAAAELEAPGVEVVLGEHPEELLDGADLVVKSPGIPPDHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 87 IIQEAQKQGLKILTEVELSYLISEAPIIGITGTNGKTTVTSLIGDMFNKSRENGRLSGNIGFVASKVAQEVKTDEYLVTE 166
Cdd:COG0771 81 LLKAARAAGIPVIGEIELAYRLSPAPIIAITGTNGKTTTTTLIGHILKAAGLRVAVGGNIGTPLLDLLLEPEPPDVYVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 167 LSSFQLLGIEHYRPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFNDKQRHLID-TSKIRAKILYFSTQH 245
Cdd:COG0771 161 LSSFQLETTPSLRPDVAVILNITPDHLDRHGSMEAYAAAKARIFANQTPDDYAVLNADDPLTRAlAEEAKARVVPFSLKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 246 RVD-GIYVEKEYIVYN--GVRLIHLDDIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYIGNNKTNK 322
Cdd:COG0771 241 PLEgGAGLEDGKLVDRasGEELLPVDDLRLPGRHNLENALAALAAARALGVPPEAIREALRSFKGLPHRLEFVAEINGVR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 323 YYNDSKATNTLATQFALSSFKQPVIWLCGGLDRGNGFDELIPYMN-NVRVMVTFGETQDKFVKLGESQGKYVIRAKDVTD 401
Cdd:COG0771 321 FINDSKATNPDATLAALESFDGPVVLIAGGLDKGADFSPLAPAVAeRVKAVVLIGEDAEKIAAALAGAGVPVVIVETMEE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 504427078 402 AVAKVQDVIEPNDVVLLSPACASWDQYDTFEQRGERFIEAFRA 444
Cdd:COG0771 401 AVAAAAELARPGDVVLLSPACASFDQFKNYEERGDVFKEAVRE 443
|
|
| murD |
PRK14106 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional |
7-445 |
1.58e-142 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Pssm-ID: 184511 [Multi-domain] Cd Length: 450 Bit Score: 415.14 E-value: 1.58e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 7 LRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDLSNDAHA-KDLEDLGISVVSGAHPLALLDEAPIIFKNPGIPYTV 85
Cdd:PRK14106 3 LKGKKVLVVGAGVSGLALAKFLKKLGAKVILTDEKEEDQLKEAlEELGELGIELVLGEYPEEFLEGVDLVVVSPGVPLDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 86 PIIQEAQKQGLKILTEVELSYLISEAPIIGITGTNGKTTVTSLIGDMFNKSRENGRLSGNIGFVASKVAQEVKTDEYLVT 165
Cdd:PRK14106 83 PPVVQAHKKGIEVIGEVELAYRFSKAPIVAITGTNGKTTTTTLLGEIFKNAGRKTLVAGNIGYPLIDAVEEYGEDDIIVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 166 ELSSFQLLGIEHYRPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN---DKQRHLIDtsKIRAKILYFS 242
Cdd:PRK14106 163 EVSSFQLETIKEFKPKVGCILNITPDHLDRHKTMENYIKAKARIFENQRPSDYTVLNyddPRTRSLAK--KAKARVIFFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 243 TQHRVD-GIYVEKEYIV--YNGVR--LIHLDDIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYIGN 317
Cdd:PRK14106 241 RKSLLEeGVFVKNGKIVisLGGKEeeVIDIDEIFIPGEHNLENALAATAAAYLLGISPDVIANTLKTFKGVEHRIEFVAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 318 NKTNKYYNDSKATNTLATQFALSSFKQPVIWLCGGLDRGNGFDELIPYMN-NVRVMVTFGETQDKFVKLGESQG-KYVIR 395
Cdd:PRK14106 321 INGVKFINDSKGTNPDAAIKALEAYETPIVLIAGGYDKGSDFDEFAKAFKeKVKKLILLGETAQEIAEAARKYGfDNILF 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 504427078 396 AKDVTDAVAKVQDVIEPNDVVLLSPACASWDQYDTFEQRGERFIEAFRAH 445
Cdd:PRK14106 401 AETLEEAVKKAYEIAKPGDVVLLSPACASWDMFKNFEERGRLFKELVLEL 450
|
|
| murD |
TIGR01087 |
UDP-N-acetylmuramoylalanine--D-glutamate ligase; [Cell envelope, Biosynthesis and degradation ... |
11-444 |
1.51e-134 |
|
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: 394.01 E-value: 1.51e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 11 KVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDLSNDAHAKDLEDLGISVVSGAHP-LALLDEAPIIFKNPGIPYTVPIIQ 89
Cdd:TIGR01087 1 KILILGLGKTGRAVARFLHKKGAEVTVTDLKPNEELEPSMGQLRLNEGSVLHTGLhLEDLNNADLVVKSPGIPPDHPLVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 90 EAQKQGLKILTEVELSYLISEAPIIGITGTNGKTTVTSLIGDMFNKSRENGRLSGNIGFVASKVAQEvKTDEYLVTELSS 169
Cdd:TIGR01087 81 AAAKRGIPVVGDIELFLRLVPLPVVAITGTNGKTTTTSLLYHLLKAAGLKAFLGGNIGTPALEVLDQ-EGAELYVLELSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 170 FQLLGIEHYRPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN-DKQRHLIDTSKIRAKILYFSTQHRVD 248
Cdd:TIGR01087 160 FQLETTESLRPEIALILNISEDHLDWHGSFEDYVAAKLKIFARQTEGDVAVLNaDDPRFARLAQKSKAQVIWFSVEKDAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 249 -GIYVEKEYIVYNGVRLihldDIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYIGNNKTNKYYNDS 327
Cdd:TIGR01087 240 rGLCIRDGGLYLKPNDL----EGSLLGLHNAENILAAIALAKSLGLNLEAILEALRSFKGLPHRLEYVGQKNGVHFYNDS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 328 KATNTLATQFALSSFKQPVIWLCGGLDRGNGFDELIPYMNNVRVMV-TFGETQDKFVKLGESQGKYVIRAKDVTDAVAKV 406
Cdd:TIGR01087 316 KATNVHATLAALSAFDNPVILIVGGDDKGADFSPLAPAAAGKVKAVlAIGEDAAKIAPLLKEAGLSVYLVESLEEAVQAA 395
|
410 420 430
....*....|....*....|....*....|....*...
gi 504427078 407 QDVIEPNDVVLLSPACASWDQYDTFEQRGERFIEAFRA 444
Cdd:TIGR01087 396 REVASPGDVVLLSPACASFDQFKSYEERGEKFKELVRA 433
|
|
| MurC |
COG0773 |
UDP-N-acetylmuramate-alanine ligase MurC and related ligases, MurC/Mpl family [Cell wall ... |
15-417 |
5.55e-38 |
|
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: 143.28 E-value: 5.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 15 IGMakSGyeAAKLLHRLGAEVTvndGNDLSNDAHAKDLEDLGISVVSGAHPlALLDEAPIIFKNPGIPYTVPIIQEAQKQ 94
Cdd:COG0773 15 IGM--SG--LAEILLALGYKVS---GSDLAESPMTERLEALGIPVFIGHDA-ENIDDADLVVVSSAIPRDNPELVAARER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 95 GLKILT--EVeLSYLISEAPIIGITGTNGKTTVTSLIGDMFNKSRE---------------NGRLSGNIGFVAskvaqEV 157
Cdd:COG0773 87 GIPVLSraEM-LAELMRGKRSIAVAGTHGKTTTTSMLAHILEEAGLdptfliggilnnfgtNARLGDGDYFVA-----EA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 158 ktDEYLvtelSSFqllgiEHYRPHIAIITNLYSAHLDYHENLENYQNAKKRiFENQTESDYLIF---NDKQ-RHLIDtsK 233
Cdd:COG0773 161 --DESD----GSF-----LHYSPDIAVVTNIEADHLDIYGDLEAIKEAFHE-FARNVPFYGLLVlcaDDPGlRELLP--R 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 234 IRAKILYFSTQH----RVDGIYVEKEY----IVYNGVRLIHLDdIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTF 305
Cdd:COG0773 227 CGRPVITYGFSEdadyRAENIRIDGGGstfdVLRRGEELGEVE-LNLPGRHNVLNALAAIAVALELGVDPEAIAEALASF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 306 SGIAHRLQYIGNNKTNKYYND----------------SKA----------------TNTLATQFAlSSFKQpviwlcggl 353
Cdd:COG0773 306 KGVKRRFELKGEVGGVTVIDDyahhpteiaatlaaarEKYpdrrlvavfqphrysrTRDFLDEFA-EALSL--------- 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427078 354 drgngFDELI---PYmnNVRVMVTFGETQDKFVKLGESQGKYVIRAKDVTDAVAKVQDVIEPNDVVL 417
Cdd:COG0773 376 -----ADEVIlldIY--AAREKPIPGVSSEDLAEAIRKRGKDVVYVPDLDELVEALAEIARPGDVVL 435
|
|
| MurE |
COG0769 |
UDP-N-acetylmuramyl tripeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
113-319 |
7.85e-31 |
|
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: 123.65 E-value: 7.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 113 IIGITGTNGKTTVTSLIGDMFnksRENGRLSGNIGFVASKVAQEVKTD----------------------EYLVTELSSf 170
Cdd:COG0769 82 LIGVTGTNGKTTTTYLLAQIL---RALGKKTGLIGTVGNGIGGELIPSslttpealdlqrllaemvdagvTHVVMEVSS- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 171 qlLGIEHYR-----PHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN--DKQ-RHLIDtsKIRAKILYFS 242
Cdd:COG0769 158 --HALDQGRvdgvrFDVAVFTNLTRDHLDYHGTMEAYFAAKARLFDQLGPGGAAVINadDPYgRRLAA--AAPARVITYG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 243 TQHRVDgIYVEKeyIVY--NGVR--LIHLDDIV-----LPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQ 313
Cdd:COG0769 234 LKADAD-LRATD--IELsaDGTRftLVTPGGEVevrlpLIGRFNVYNALAAIAAALALGIDLEEILAALEKLKGVPGRME 310
|
....*.
gi 504427078 314 YIGNNK 319
Cdd:COG0769 311 RVDGGQ 316
|
|
| murC |
TIGR01082 |
UDP-N-acetylmuramate--L-alanine ligase; This model describes the MurC protein in bacterial ... |
2-335 |
8.38e-31 |
|
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: 123.19 E-value: 8.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 2 IHYTGLRGkkvlvIGMakSGYeaAKLLHRLGAEVTvndGNDLSNDAHAKDLEDLGISVVSGaHPLALLDEAPIIFKNPGI 81
Cdd:TIGR01082 2 IHFVGIGG-----IGM--SGI--AEILLNRGYQVS---GSDIAENATTKRLEALGIPIYIG-HSAENLDDADVVVVSAAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 82 PYTVPIIQEAQKQGLKILTEVE-LSYLISEAPIIGITGTNGKTTVTSLIGDMFNksreNGRLSGNIgFVASKVAQ----- 155
Cdd:TIGR01082 69 KDDNPEIVEAKERGIPVIRRAEmLAELMRFRHSIAVAGTHGKTTTTAMIAVILK----EAGLDPTV-VVGGLVKEagtna 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 156 EVKTDEYLVTEL----SSFQllgieHYRPHIAIITNLYSAHLDYHEN-LENYQNAKKRIFENQTESDYLIFNDKQ---RH 227
Cdd:TIGR01082 144 RLGSGEYLVAEAdesdASFL-----HLQPNVAIVTNIEPDHLDTYGSsFERLKAAFEKFIHNLPFYGLAVICADDpvlRE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 228 LIDTSKIRAKILYFS--------TQHRVDGIYVEKEYIVYNGVRL-IHLddiVLPGEHNLENILAAVMAAILAGVSISAI 298
Cdd:TIGR01082 219 LVPKATEQVITYGGSgedadyraENIQQSGAEGKFSVRGKGKLYLeFTL---NLPGRHNVLNALAAIAVALELGIDFEAI 295
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 504427078 299 VQSLSTFSGIAHRLQYIGNNKTNKYYND-----SKATNTLAT 335
Cdd:TIGR01082 296 LRALANFQGVKRRFEILGEFGGVLLIDDyahhpTEIKATLKA 337
|
|
| Mur_ligase_M |
pfam08245 |
Mur ligase middle domain; |
116-288 |
2.32e-30 |
|
Mur ligase middle domain;
Pssm-ID: 462409 [Multi-domain] Cd Length: 199 Bit Score: 116.25 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 116 ITGTNGKTTVTSLIGDMFNKSrenGRLSGNIGFVASK--------------VAQEVKTD-EYLVTELSSFQLlgIEHY-- 178
Cdd:pfam08245 1 VTGTNGKTTTTELIAAILSLA---GGVIGTIGTYIGKsgnttnnaiglpltLAEMVEAGaEYAVLEVSSHGL--GEGRls 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 179 ---RPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN--DK--QRHLIDTSKIRAKILYFSTQHRVDgIY 251
Cdd:pfam08245 76 gllKPDIAVFTNISPDHLDFHGTMENYAKAKAELFEGLPEDGIAVINadDPygAFLIAKLKKAGVRVITYGIEGEAD-LR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504427078 252 VEKEYIVYNGVRL--------IHLDDIVLPGEHNLENILAAVMAA 288
Cdd:pfam08245 155 AANIELSSDGTSFdlftvpggELEIEIPLLGRHNVYNALAAIAAA 199
|
|
| MurF |
COG0770 |
UDP-N-acetylmuramyl pentapeptide synthase [Cell wall/membrane/envelope biogenesis]; ... |
109-418 |
1.02e-25 |
|
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: 108.65 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 109 SEAPIIGITGTNGKTTVTSLIGDMFnksRENGRL---SGN----IGfvaskvaqeV--------KTDEYLVTELssfqll 173
Cdd:COG0770 98 FNIPVIAITGSNGKTTTKEMLAAVL---STKGKVlatPGNfnneIG---------VpltllrlpEDHEFAVLEM------ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 174 GIEHY----------RPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN---DKQRHLIDtsKIRAKILY 240
Cdd:COG0770 160 GMNHPgeiaylariaRPDIAVITNIGPAHLEGFGSLEGIARAKGEIFEGLPPGGVAVLNaddPLLAALAE--RAKARVLT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 241 FSTQHRVDgIYVEKEYIVYNGVRL-IHLDD------IVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQ 313
Cdd:COG0770 238 FGLSEDAD-VRAEDIELDEDGTRFtLHTPGgelevtLPLPGRHNVSNALAAAAVALALGLDLEEIAAGLAAFQPVKGRLE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 314 YI--GNNKT--NKYYN---DS-KAT-NTLATQfalsSFKQPVIWLCG-----GLDRGNGFDELIPY--MNNVRVMVTFGE 377
Cdd:COG0770 317 VIegAGGVTliDDSYNanpDSmKAAlDVLAQL----PGGGRRIAVLGdmlelGEESEELHREVGELaaELGIDRLFTVGE 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 504427078 378 ----TQDKFvklGESQGKYViraKDVTDAVAKVQDVIEPNDVVLL 418
Cdd:COG0770 393 laraIAEAA---GGERAEHF---EDKEELLAALKALLRPGDVVLV 431
|
|
| murE |
PRK00139 |
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional |
113-318 |
1.43e-24 |
|
UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional
Pssm-ID: 234660 [Multi-domain] Cd Length: 460 Bit Score: 105.60 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 113 IIGITGTNGKTTVTSLIGDMFNKSrenGRLSGNIGFVASKVA-QEVKTD---------------------EYLVTELSSF 170
Cdd:PRK00139 97 LIGVTGTNGKTTTAYLLAQILRLL---GEKTALIGTLGNGIGgELIPSGlttpdaldlqrllaelvdagvTYAAMEVSSH 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 171 qllGIEHYRPH-----IAIITNLYSAHLDYHENLENYQNAKKRIFENQTESdYLIFND----------KQRHLIDTSK-- 233
Cdd:PRK00139 174 ---ALDQGRVDglkfdVAVFTNLSRDHLDYHGTMEDYLAAKARLFSELGLA-AVINADdevgrrllalPDAYAVSMAGad 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 234 IRAKILYFSTqhrvDGIYVEKEYIVyngvrlihldDIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQ 313
Cdd:PRK00139 250 LRATDVEYTD----SGQTFTLVTEV----------ESPLIGRFNVSNLLAALAALLALGVPLEDALAALAKLQGVPGRME 315
|
....*
gi 504427078 314 YIGNN 318
Cdd:PRK00139 316 RVDAG 320
|
|
| murF |
TIGR01143 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; This family consists of the ... |
111-418 |
1.95e-21 |
|
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: 95.80 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 111 APIIGITGTNGKTTVTSLIGDMFNKSRE----NGRLSGNIGfVASKVAQEVKTDEYLVTElssfqlLGIEHY-------- 178
Cdd:TIGR01143 74 GKVIGITGSSGKTTTKEMLAAILSHKYKvfatPGNFNNEIG-LPLTLLRAPGDHDYAVLE------MGASHPgeiaylae 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 179 --RPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFNDKQRHLIDTSKI--RAKILYFSTQHR-VDGIYVE 253
Cdd:TIGR01143 147 iaKPDIAVITNIGPAHLEGFGSLEGIAEAKGEILQGLKENGIAVINADDPAFADLAKRlpNRNILSFGFEGGdFVAKDIS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 254 KEYIVYNGVRLIHLD---DIVLP--GEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYI-GNNKT--NKYYN 325
Cdd:TIGR01143 227 YSALGSTSFTLVAPGgefEVSLPllGRHNVMNALAAAALALELGIPLEEIAEGLAELKLVKGRFEVQtKNGLTliDDTYN 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 326 DSKATNTLATQfALSSFKQPVIWLCG-----GLDRGNGFDELIPYMN--NVRVMVTFGEtqdKFVKLGESQGKYVIRAKD 398
Cdd:TIGR01143 307 ANPDSMRAALD-ALARFPGKKILVLGdmaelGEYSEELHAEVGRYANslGIDLVFLVGE---EAAVIYDSFGKQGKHFAD 382
|
330 340
....*....|....*....|
gi 504427078 399 VTDAVAKVQDVIEPNDVVLL 418
Cdd:TIGR01143 383 KDELLAFLKTLVRKGDVVLV 402
|
|
| murE |
TIGR01085 |
UDP-N-acetylmuramyl-tripeptide synthetase; Most members of this family are EC 6.3.2.13, ... |
39-315 |
1.89e-20 |
|
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: 93.53 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 39 DGNDLSNDAHAKdledlgisvvsGAhpLALLDEAPIIFKNPGIPYtvpIIQEAQKQGLKILTEVELSYLISEAPIIGITG 118
Cdd:TIGR01085 29 DGHDFIHDAIAN-----------GA--VAVVVERDVDFYVAPVPV---IIVPDLRHALSSLAAAFYGHPSKKLKVIGVTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 119 TNGKTTVTSLIGDMFNKSRENGRLSGNIGF-------VASKVAQ------EVKTD---------EYLVTELSSFqllGIE 176
Cdd:TIGR01085 93 TNGKTTTTSLIAQLLRLLGKKTGLIGTIGYrlggndlIKNPAALttpealTLQSTlaemveagaQYAVMEVSSH---ALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 177 HYRPH-----IAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLI----------FNDKQRHLIDTSKIRAKILYF 241
Cdd:TIGR01085 170 QGRVRgvrfdAAVFTNLSRDHLDFHGTMENYFAAKASLFTELGLKRFAVinlddeygaqFVKRLPKDITVSAITQPADGR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 242 STQHRVDGIYVEKEYIVY-----NGVRLIHlddIVLPGEHNLENILAAVMAAI-LAGVSISAIVQSLSTFSGIAHRLQYI 315
Cdd:TIGR01085 250 AQDIKITDSGYSFEGQQFtfetpAGEGHLH---TPLIGRFNVYNLLAALATLLhLGGIDLEDIVAALEKFRGVPGRMELV 326
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
113-316 |
2.22e-20 |
|
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: 94.39 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 113 IIGITGTNGKTTVTSLIGDMFNKsreNGRLSGNIGFVASKV-AQEVKTD---------------------EYLVTELSSF 170
Cdd:PRK11929 114 LVAVTGTNGKTSCAQLLAQLLTR---LGKPCGSIGTLGARLdGRLIPGSlttpdaiilhrilarmraagaDAVAMEASSH 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 171 QL-LG-IEHYRPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN--DKQ-RHLIDTSKIRAKILYFSTQH 245
Cdd:PRK11929 191 GLeQGrLDGLRIAVAGFTNLTRDHLDYHGTMQDYEEAKAALFSKLPGLGAAVINadDPAaARLLAALPRGLKVGYSPQNA 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427078 246 RVDgIYVEKEYIVYNG--VRLIHLD-----DIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYIG 316
Cdd:PRK11929 271 GAD-VQARDLRATAHGqvFTLATPDgsyqlVTRLLGRFNVSNLLLVAAALKKLGLPLAQIARALAAVSPVPGRMERVG 347
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
112-305 |
5.93e-18 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 86.36 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 112 PIIGITGTNGKTTVTSLIGDMFNKSRE------------NGRL--SG-NIGFVASKVAQEVKTDEYLVTELSSFQLL--G 174
Cdd:PRK14016 481 PIVAVTGTNGKTTTTRLIAHILKLSGKrvgmtttdgvyiDGRLidKGdCTGPKSARRVLMNPDVEAAVLETARGGILreG 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 175 IEHYRPHIAIITNLYSAHL--DYHENLENYQNAKKRIFENQTESDYLIFN--DKQ-RHLIDtsKIRAKILYFST------ 243
Cdd:PRK14016 561 LAYDRCDVGVVTNIGEDHLglGGINTLEDLAKVKRVVVEAVKPDGYAVLNadDPMvAAMAE--RCKGKVIFFSMdpdnpv 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427078 244 --QHRVDG---IYVEKEYIV-YNG---VRLIHLDDIVLPGE----HNLENILAAVMAAILAGVSISAIVQSLSTF 305
Cdd:PRK14016 639 iaEHRAQGgraVYVEGDYIVlAEGgweIRIISLADIPLTLGgkagFNIENALAAIAAAWALGIDIELIRAGLRTF 713
|
|
| PRK11929 |
PRK11929 |
bifunctional UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE ... |
112-342 |
4.73e-17 |
|
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: 83.99 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 112 PIIGITGTNGKTTVTSLIGDMFNK-SRENGRL--SGN----IGfVASKVAQEVKTDEYLVTELssfqllGIEH------- 177
Cdd:PRK11929 604 PVVAITGSNGKTTTKEMIAAILAAwQGEDRVLatEGNfnneIG-VPLTLLRLRAQHRAAVFEL------GMNHpgeiayl 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 178 ---YRPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFNDKQRHLIDTSKI--RAKILYFSTQHRVDGiYV 252
Cdd:PRK11929 677 aaiAAPTVALVTNAQREHQEFMHSVEAVARAKGEIIAALPEDGVAVVNGDDPYTAIWAKLagARRVLRFGLQPGADV-YA 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 253 EKE-------------YIVYNGVRLIHLDdIVLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQYIGNNK 319
Cdd:PRK11929 756 EKIakdisvgeaggtrCQVVTPAGSAEVY-LPLIGEHNLRNALAAIACALAAGASLKQIRAGLERFQPVAGRMQRRRLSC 834
|
250 260
....*....|....*....|...
gi 504427078 320 TNKYYNDSKATNTLATQFALSSF 342
Cdd:PRK11929 835 GTRIIDDTYNANPDSMRAAIDVL 857
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
3-313 |
1.17e-16 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 82.56 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 3 HYTGLRGkkvlvIGMAKSgyeAAKLLHRlGAEVTvndGNDLSNDAHAKDLEDLGISVVSGAHPLALLDEAPIIFKNpGIP 82
Cdd:PRK14573 8 HFIGIGG-----IGMSAL---AHILLDR-GYSVS---GSDLSEGKTVEKLKAKGARFFLGHQEEHVPEDAVVVYSS-SIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 83 YTVPIIQEAQKQGLKILTEVEL-SYLISEAPIIGITGTNGKTTVTSLIGDMFNKSRENGrlSGNIGFVASK-VAQEVKTD 160
Cdd:PRK14573 75 KDNVEYLSAKSRGNRLVHRAELlAELMQEQISILVSGSHGKTTVSSLITAIFQEAKKDP--SYAIGGLNQEgLNGYSGSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 161 EYLVTELSSFQLlGIEHYRPHIAIITNLYSAHLDyhenleNYQNAKKRI------FENQTESDYLIFNDKqrhliDTSKI 234
Cdd:PRK14573 153 EYFVAEADESDG-SLKHYTPEFSVITNIDNEHLS------NFEGDRELLlasiqdFARKVQQINKCFYNG-----DCPRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 235 RAKI------------LYFSTqHRVDG-------IYVEKEYivyngvrlihLD-DIVLPGEHNLENILAAVMAAILAGVS 294
Cdd:PRK14573 221 KGCLqghsygfssscdLHILS-YYQEGwrsyfsaKFLGVVY----------QDiELNLVGMHNVANAAAAMGIALTLGID 289
|
330
....*....|....*....
gi 504427078 295 ISAIVQSLSTFSGIAHRLQ 313
Cdd:PRK14573 290 EGAIRNALKGFSGVQRRLE 308
|
|
| F430_CfbE |
NF033197 |
coenzyme F430 synthase; Members of this family are coenzyme F430 synthase, involving in ... |
112-419 |
2.48e-09 |
|
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: 58.88 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 112 PIIGITGTNGKTTVTSLIGDMFnkSRENGRLSGNIGFV--------------------ASKVAQEVKTDEY--LVTElSS 169
Cdd:NF033197 93 KFIEITGVKGKTTTAELLAHIL--SDEYVLLHTSRGTErypegelsnkgsitpasilnALELAEEIGIDDYgfLIFE-VS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 170 FQLLGIEHYrphiAIITNLysahldyhenLENYQ---------NAKKRIFEN-QTESDYLIFNDKQ---RHLIDTSKIRA 236
Cdd:NF033197 170 LGGTGAGDV----GIITNI----------LEDYPiaggkrsasAAKLQSLKNaKVGSINVADLGIYingKNKLVITVAGV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 237 KILYFSTQHRVDGIyvekeyivyNGVRLIHLddivLPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRLQ--Y 314
Cdd:NF033197 236 EILSKYPLRFKYGN---------TEFEFNPL----LFGPHYRENSLFAIEAALNLGVDPEDIISALKGFKGLPGRMAvkK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 315 IGNNKTNKyyNDSKATNTLATQFALSSFKQPVIWL-----------CGGLDrgngFDELIPYMNNVRvmVTFGETQDKFV 383
Cdd:NF033197 303 EGGVVIVD--NINPGLNVKAIEYALDDALELLGDGtlviggdfgvvCEEID----IDKLSEVLKKYR--PKIDILVGVGT 374
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 504427078 384 KLGESQGKYV-----IRAKDVTDAVAKVQDVIEPNDVVLLS 419
Cdd:NF033197 375 ELGKRLKKYLdklegYEAGTLEEGLDDARELTGEGNTLVIY 415
|
|
| PRK14022 |
PRK14022 |
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase; |
113-300 |
5.70e-09 |
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
Pssm-ID: 237588 [Multi-domain] Cd Length: 481 Bit Score: 58.12 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 113 IIGITGTNGKTTVTSLIGDMFNKSRENGRLSGNIGFVASK------------------VAQEVKTD-EYLVTELSSFQLL 173
Cdd:PRK14022 112 LLAFTGTKGKTTAAYFAYHILKQLHKPAMLSTMNTTLDGEtffksalttpesldlfkmMAEAVDNGmTHLIMEVSSQAYL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 174 -----GIEHyrpHIAIITNLYSAHLDY--HENLENYQNAKKRIFENqteSDYLIFNDKQRHLidtSKIRAKILYFstQHR 246
Cdd:PRK14022 192 vgrvyGLTF---DVGVFLNITPDHIGPieHPTFEDYFYHKRLLMEN---SKAVVVNSDMDHF---SELLEQVTPQ--EHD 260
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 247 VDGIYVEKEYIVYNGV------RLIHLDDIVLPGEHNLENILAAVMAAILAGVSISAIVQ 300
Cdd:PRK14022 261 FYGIDSENQIMASNAFsfeatgKLAGTYDIQLIGKFNQENAMAAGLACLRLGASLEDIQK 320
|
|
| murF |
PRK10773 |
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed |
109-312 |
1.37e-07 |
|
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase; Reviewed
Pssm-ID: 182718 [Multi-domain] Cd Length: 453 Bit Score: 53.50 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 109 SEAPIIGITGTNGKTTV----TSLIGDMFNKSRENGRLSGNIGfVASKVAQEVKTDEYLVTELSSFQLLGI----EHYRP 180
Cdd:PRK10773 98 VPARVVALTGSSGKTSVkemtAAILRQCGNTLYTAGNLNNDIG-VPLTLLRLTPEHDYAVIELGANHQGEIaytvSLTRP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 181 HIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFN-DKQRHLIDTSKIRAKILY-FSTQhRVDGI--YVEKEY 256
Cdd:PRK10773 177 EAALVNNLAAAHLEGFGSLAGVAKAKGEIFSGLPENGIAIMNaDSNDWLNWQSVIGSKTVWrFSPN-AANSVdfTATNIH 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427078 257 IVYNGVRL-IH--LDDIV----LPGEHNLENILAAVMAAILAGVSISAIVQSLSTFSGIAHRL 312
Cdd:PRK10773 256 VTSHGTEFtLHtpTGSVDvllpLPGRHNIANALAAAALAMSVGATLDAVKAGLANLKAVPGRL 318
|
|
| Mur_ligase_C |
pfam02875 |
Mur ligase family, glutamate ligase domain; This family contains a number of related ligase ... |
308-369 |
2.78e-07 |
|
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: 48.11 E-value: 2.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427078 308 IAHRLQYIGNNKTNKYYNDsKATNTLATQFALSSFKQ----PVIWLCGG-LDRGNGFDELIPYMNNV 369
Cdd:pfam02875 1 VPGRLEVVGENNGVLVIDD-YAHNPDAMEAALRALRNlfpgRLILVFGGmGDRDAEFHALLGRLAAA 66
|
|
| NAD_bind_H4MPT_DH |
cd01078 |
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ... |
3-154 |
2.21e-05 |
|
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133446 [Multi-domain] Cd Length: 194 Bit Score: 45.08 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 3 HYTGLRGKKVLVIGMAKS-GYEAAKLLHRLGAEVTV--NDGNDLSNDA---HAKDLEDLG-ISVVSGAHPLALLDEAPII 75
Cdd:cd01078 22 MGKDLKGKTAVVLGGTGPvGQRAAVLLAREGARVVLvgRDLERAQKAAdslRARFGEGVGaVETSDDAARAAAIKGADVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 76 FKNPGIPYTVPIIQEAQKQGLKILTEVelsyliSEAPIIGITGTngkttvtsligDMFNKS--RENGRLSGNIGFVASKV 153
Cdd:cd01078 102 FAAGAAGVELLEKLAWAPKPLAVAADV------NAVPPVGIEGI-----------DVPDKGvdREGKVPYGAIGVGGLKM 164
|
.
gi 504427078 154 A 154
Cdd:cd01078 165 K 165
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
45-222 |
5.74e-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: 45.72 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 45 NDAHA--KDLEDLGIS---VVSGAHPLALLDEAP-IIFKNPgipytvpiiqeaqkqgLKILTEVELSY-LISEAPIIGIT 117
Cdd:PRK11930 50 NDGHRyiQELYEKGVRnfvVSEEKHPEESYPDANfLKVKDP----------------LKALQELAAYHrSQFDIPVIGIT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 118 GTNGKTTVTS----LIGDMFNKSRENGRLSGNIGfVASKVAQEVKTDEYLVTElssfqlLGIEH----------YRPHIA 183
Cdd:PRK11930 114 GSNGKTIVKEwlyqLLSPDYNIVRSPRSYNSQIG-VPLSVWQLNEEHELGIFE------AGISQpgemealqkiIKPTIG 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 504427078 184 IITNLYSAHLDYHENLENYQNAKKRIFenqTESDYLIFN 222
Cdd:PRK11930 187 ILTNIGGAHQENFRSIKQKIMEKLKLF---KDCDVIIYN 222
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
5-73 |
6.16e-05 |
|
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.
Pssm-ID: 240621 [Multi-domain] Cd Length: 317 Bit Score: 44.71 E-value: 6.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427078 5 TGLRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDLSndahAKDLEDLGISVVSGAHPLALLDEAP 73
Cdd:cd01620 158 GGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEK----LKGVETLGGSRLRYSQKEELEKELK 222
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
21-75 |
9.76e-05 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 44.47 E-value: 9.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 21 GYEAAKLLHRLGAEVTV---NDGNDLSNDA--HAKDLEDLGISVVSGAHPLALLDEAPII 75
Cdd:COG0062 63 GLVAARLLAEAGYNVTVfllGDPEKLSGDAaaNLERLKAAGIPILELDDELPELAEADLI 122
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
6-39 |
1.97e-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: 41.34 E-value: 1.97e-04
10 20 30
....*....|....*....|....*....|....
gi 504427078 6 GLRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVND 39
Cdd:smart01002 17 GVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLD 50
|
|
| PRK14093 |
PRK14093 |
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; ... |
179-330 |
2.42e-04 |
|
UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate--D-alanyl-D-alanine ligase; Provisional
Pssm-ID: 184501 [Multi-domain] Cd Length: 479 Bit Score: 43.22 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 179 RPHIAIITNLYSAHLDYHENLENYQNAKKRIFENQTESDYLIFNDKQRH---LIDTSKIR--AKILYFSTQHRVDgiyve 253
Cdd:PRK14093 183 RPHVAIITTVEPVHLEFFSGIEAIADAKAEIFTGLEPGGAAVLNRDNPQfdrLAASARAAgiARIVSFGADEKAD----- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 254 keyivyngVRLIhldDIVL----------------------PGEHNLENILAAVMAAILAGVSISAIVQSLSTFS----- 306
Cdd:PRK14093 258 --------ARLL---DVALhadcsavhadilghdvtyklgmPGRHIAMNSLAVLAAAELAGADLALAALALSQVQpaagr 326
|
170 180
....*....|....*....|....*.
gi 504427078 307 GIAHRLQYIGNNKT--NKYYNDSKAT 330
Cdd:PRK14093 327 GVRHTLEVGGGEATliDESYNANPAS 352
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
3-108 |
4.96e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 41.83 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 3 HYTGLRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDLSNDAHAkdleDLGISVvsgahplalldeapiifknpgIP 82
Cdd:pfam13738 149 DFHPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDS----DPSYSL---------------------SP 203
|
90 100 110
....*....|....*....|....*....|....*
gi 504427078 83 YTVPIIQEAQKQG---------LKILTEVELSYLI 108
Cdd:pfam13738 204 DTLNRLEELVKNGkikahfnaeVKEITEVDVSYKV 238
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
11-68 |
4.41e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 36.03 E-value: 4.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427078 11 KVLVIGMAKSGYEAAKLLHRLGAEVTVNDGNDL---SNDAHA-----KDLEDLGISVVSGAHPLAL 68
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRllpGFDPEIakilqEKLEKNGIEFLLNTTVEAI 66
|
|
| NAD_bind_Leu_Phe_Val_DH |
cd01075 |
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ... |
7-39 |
4.92e-03 |
|
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133444 Cd Length: 200 Bit Score: 37.96 E-value: 4.92e-03
10 20 30
....*....|....*....|....*....|...
gi 504427078 7 LRGKKVLVIGMAKSGYEAAKLLHRLGAEVTVND 39
Cdd:cd01075 26 LEGKTVAVQGLGKVGYKLAEHLLEEGAKLIVAD 58
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|
| PRK12429 |
PRK12429 |
3-hydroxybutyrate dehydrogenase; Provisional |
7-85 |
4.98e-03 |
|
3-hydroxybutyrate dehydrogenase; Provisional
Pssm-ID: 237100 [Multi-domain] Cd Length: 258 Bit Score: 38.71 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 7 LRGKKVLVIGMAKS-GYEAAKLLHRLGAEVTVNDGNDLSNDAHAKDLEDLGISVVsgAHPLALLDEAPIifkNPGIPYTV 85
Cdd:PRK12429 2 LKGKVALVTGAASGiGLEIALALAKEGAKVVIADLNDEAAAAAAEALQKAGGKAI--GVAMDVTDEEAI---NAGIDYAV 76
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
6-94 |
5.10e-03 |
|
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 38.79 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427078 6 GLRGKKVLVIGMAKSGYEAAKLLHRLG-AEVTV-NdgndlSNDAHAKDL-EDLGISVVSGAHPLALLDEAPIIFKNPGIP 82
Cdd:cd05213 175 NLKGKKVLVIGAGEMGELAAKHLAAKGvAEITIaN-----RTYERAEELaKELGGNAVPLDELLELLNEADVVISATGAP 249
|
90
....*....|..
gi 504427078 83 YTVPIIQEAQKQ 94
Cdd:cd05213 250 HYAKIVERAMKK 261
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