|
Name |
Accession |
Description |
Interval |
E-value |
| AraD_Arch |
NF040866 |
arabinonate dehydratase; |
1-372 |
0e+00 |
|
arabinonate dehydratase;
Pssm-ID: 468803 [Multi-domain] Cd Length: 372 Bit Score: 708.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 1 MIKNIRTYKLCYEGINDEKDALAIKGLAEHPMEIVVTEIETSDGYVGYGESLAYGCSDVVQVMIEKVLKPLLLKEDEELI 80
Cdd:NF040866 1 MIKEIKTYKLCYEGINEERDALAVKGLAEHPMEIVVTEIETSDGEIGYGESLAYGCSDVVQVTIEKILKPLLLKEDEELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 81 EYLWDKMYKATLRFGRRGIAIAGISGVDTALWDIMGKKAKKPIYKLLGGSKTKVRAYITGGYYSEKKDLEKLKDEEAYYV 160
Cdd:NF040866 81 EGLWDKMYKATLRFGRRGIVIAGISGVDIALWDIMGKKTKKPIYKLLGGSKRKIRAYITGGYYSEKKDLEKLREEVAYYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 161 KMGFKGIKVKIGAKSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLA 240
Cdd:NF040866 161 KMGFKGVKIKIGGKSMEEDMERLKAIREVVGEDVKIAVDANNVYTFEEALKMGRELEKLGIWFFEEPIQTDLLDLSAELT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 241 EELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHVAAALN 320
Cdd:NF040866 241 EALEIPIAGYETAYTRWEFYEIMRKRSVDIVQTDAMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLVANLHVAAALG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1774062176 321 SPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTIREGVLEEYKCK 372
Cdd:NF040866 321 SPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTLREGVFEEYRCK 372
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-358 |
1.38e-138 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 398.52 E-value: 1.38e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 2 IKNIRTYKLCYEgindekdaLAIKGLAEHPMEIVVTEIETSDGYVGYGESLAYGCSDVVQVMIEKVLKPLLLKEDEELIE 81
Cdd:cd03316 2 ITDVETFVLRVP--------LPEPGGAVTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 82 YLWDKMYKATLRFGRRGIAIAGISGVDTALWDIMGKKAKKPIYKLLGG-SKTKVRAYITGGYYSEkkDLEKLKDEEAYYV 160
Cdd:cd03316 74 RLWEKLYRRLFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGkVRDRVRVYASGGGYDD--SPEELAEEAKRAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 161 KMGFKGIKVKIGA-----KSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDL 235
Cdd:cd03316 152 AEGFTAVKLKVGGpdsggEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 236 SARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHV 315
Cdd:cd03316 232 LARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1774062176 316 AAAL-NSPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLG 358
Cdd:cd03316 312 AAALpNFGILEYHLDDLPLREDLFKNPPEIEDGYVTVPDRPGLG 355
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-369 |
1.15e-110 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 327.55 E-value: 1.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 1 MIKNIRTYKLCYEgindEKDALAIKGLAEHPMEIVVTEIETSDGYVGYGESLAYGCS-DVVQVMIEKVLKPLLLKEDEEL 79
Cdd:COG4948 2 KITDIEVYPVRLP----LKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTGaEAVAAALEEALAPLLIGRDPLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 80 IEYLWDKMYKATlrfgrrGIAIAGISGVDTALWDIMGKKAKKPIYKLLGG-SKTKVRAYITGGYYSEKKDLEKLKDeeay 158
Cdd:COG4948 78 IEALWQRLYRAL------PGNPAAKAAVDMALWDLLGKALGVPVYQLLGGkVRDRVPVYATLGIDTPEEMAEEARE---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 159 YVKMGFKGIKVKIGAKSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSAR 238
Cdd:COG4948 148 AVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 239 LAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPH-YSAGGISLIGNLHVAA 317
Cdd:COG4948 228 LRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHcMLESGIGLAAALHLAA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1774062176 318 AL-NSPWIEMHLRKNDLRDkIFKESIEIDNGHLVVPDRPGLGYTIREGVLEEY 369
Cdd:COG4948 308 ALpNFDIVELDGPLLLADD-LVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
33-361 |
3.85e-89 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239443 [Multi-domain] Cd Length: 341 Bit Score: 271.90 E-value: 3.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 33 EIVVTEIETSDGYVGYGESLAygcSDVVQVMIEKVLKPLLLKEDEELIEYLWDKMYKATLRFGRRGIAIAGISGVDTALW 112
Cdd:cd03327 10 GWLFVEIETDDGTVGYANTTG---GPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAYGRKGIAMAAISAVDLALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 113 DIMGKKAKKPIYKLLGGS-KTKVRAYITGGYYSEKKDLEKLKDEeayYVKMGFKGIKVKI------GAKSMEEDIERLKV 185
Cdd:cd03327 87 DLLGKIRGEPVYKLLGGRtRDKIPAYASGLYPTDLDELPDEAKE---YLKEGYRGMKMRFgygpsdGHAGLRKNVELVRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 186 IREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRK 265
Cdd:cd03327 164 IREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 266 RAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHysAGGISligNLH-VAAALNSPWIE-----MHLRKNDLRDKIFK 339
Cdd:cd03327 244 RAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPH--ASQIY---NYHfIMSEPNSPFAEylpnsPDEVGNPLFYYIFL 318
|
330 340
....*....|....*....|..
gi 1774062176 340 ESIEIDNGHLVVPDRPGLGYTI 361
Cdd:cd03327 319 NEPVPVNGYFDLSDKPGFGLEL 340
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
156-363 |
5.81e-77 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 236.31 E-value: 5.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 156 EAYYVKMGFKGIKVKIGAKSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDL 235
Cdd:pfam13378 7 RRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 236 SARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHV 315
Cdd:pfam13378 87 LARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPIGLAASLHL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1774062176 316 AAAL-NSPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTIRE 363
Cdd:pfam13378 167 AAAVpNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDE 215
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
39-361 |
3.47e-62 |
|
D-galactonate dehydratase catalyses the dehydration of galactonate to 2-keto-3-deoxygalactonate (KDGal), as part of the D-galactonate nonphosphorolytic catabolic Entner-Doudoroff pathway. D-galactonate dehydratase belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239441 [Multi-domain] Cd Length: 352 Bit Score: 202.94 E-value: 3.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 39 IETSDGYVGYGESLAYGCSDVVQVMIEKvLKPLLLKEDEELIEYLWDKMYKAtlRFGRRG-IAIAGISGVDTALWDIMGK 117
Cdd:cd03325 19 IETDEGVVGWGEPTVEGKARTVEAAVQE-LEDYLIGKDPMNIEHHWQVMYRG--GFYRGGpVLMSAISGIDQALWDIKGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 118 KAKKPIYKLLGGS-KTKVRAY--ITGGYYSEKKDLEKLKDEEAY-YVKMGFKG-IKVKIGAKSMEEDIERLKVIREVVGE 192
Cdd:cd03325 96 VLGVPVHQLLGGQvRDRVRVYswIGGDRPSDVAEAARARREAGFtAVKMNATEeLQWIDTSKKVDAAVERVAALREAVGP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 193 EVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQ 272
Cdd:cd03325 176 DIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 273 TDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHVAAALNSPWI-EMHL-----RKNDLRDKIF-KESIEID 345
Cdd:cd03325 256 PDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDASTPNFLIqEQSLgihynEGDDLLDYLVdPEVFDME 335
|
330
....*....|....*.
gi 1774062176 346 NGHLVVPDRPGLGYTI 361
Cdd:cd03325 336 NGYVKLPTGPGLGIEI 351
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
39-368 |
3.59e-55 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 185.48 E-value: 3.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 39 IETSDGYVGYGESLAYGCSDVVQVMIEKvLKPLLLKEDEELIEYLWDKMYKATlrFGRRG-IAIAGISGVDTALWDIMGK 117
Cdd:PRK14017 20 IETDEGIVGWGEPVVEGRARTVEAAVHE-LADYLIGKDPRRIEDHWQVMYRGG--FYRGGpILMSAIAGIDQALWDIKGK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 118 KAKKPIYKLLGGS-KTKVRAY--ITGGYYSEKKDLEKLKdeeayyVKMGFKGIKVKiGAKSM---------EEDIERLKV 185
Cdd:PRK14017 97 ALGVPVHELLGGLvRDRIRVYswIGGDRPADVAEAARAR------VERGFTAVKMN-GTEELqyidsprkvDAAVARVAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 186 IREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRK 265
Cdd:PRK14017 170 VREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 266 RAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHVAAALNSPWI-EMHL-----RKNDLRDKIF- 338
Cdd:PRK14017 250 GGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDAVSPNAFIqEQSLgihynQGADLLDYVKn 329
|
330 340 350
....*....|....*....|....*....|
gi 1774062176 339 KESIEIDNGHLVVPDRPGLGYTIREGVLEE 368
Cdd:PRK14017 330 KEVFAYEDGFVAIPTGPGLGIEIDEAKVRE 359
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
38-368 |
4.40e-51 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239445 [Multi-domain] Cd Length: 368 Bit Score: 174.51 E-value: 4.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 38 EIETSDGYVGYgeslAYGCSDVVQ-VMIEKVLKPLLLKEDEELIEYLWDKMYKAtlrfgRRGIAIAGISGVDTALWDIMG 116
Cdd:cd03329 38 TIETDEGAKGH----AFGGRPVTDpALVDRFLKKVLIGQDPLDRERLWQDLWRL-----QRGLTDRGLGLVDIALWDLAG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 117 KKAKKPIYKLLGGSKTKVRAYITGGYYSekkDLEKLKDEEAY------YVKMGFKGIKVKI-GAKSMEEDIERLKVIREV 189
Cdd:cd03329 109 KYLGLPVHRLLGGYREKIPAYASTMVGD---DLEGLESPEAYadfaeeCKALGYRAIKLHPwGPGVVRRDLKACLAVREA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 190 VGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIqtDYLDLSA--RLAEELEVPIAGYETAYTRWEFY-EIMRKR 266
Cdd:cd03329 186 VGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPL--REASISSyrWLAEKLDIPILGTEHSRGALESRaDWVLAG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 267 AVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHysAGGISligNLHVAAAL-NSPWIEMHL----RKNDLRDKIFKE- 340
Cdd:cd03329 264 ATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELH--GNGAA---NLHVIAAIrNTRYYERGLlhpsQKYDVYAGYLSVl 338
|
330 340
....*....|....*....|....*....
gi 1774062176 341 SIEIDNGHLV-VPDRPGLGYTIREGVLEE 368
Cdd:cd03329 339 DDPVDSDGFVhVPKGPGLGVEIDFDYIER 367
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
35-369 |
1.49e-49 |
|
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose putative targets are homoserine lactone (HSL)-derivative. They are part of the mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subfamily share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and catalytic residues, a partially conserved Lys-X-Lys motif and a conserved histidine-aspartate dyad.
Pssm-ID: 239438 [Multi-domain] Cd Length: 361 Bit Score: 170.31 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 35 VVTEIETSDGYVGYGESLAYGCSDVVQVMIEKVLKPLLLKEDEELIEYLWDKMYKATlrFGRRG-IAIAGISGVDTALWD 113
Cdd:cd03322 17 VTLKITTDQGVTGLGDATLNGRELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGA--YWRRGpVTMNAIAAVDMALWD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 114 IMGKKAKKPIYKLLGG-SKTKVRAYitggYYSEKKDLEKLKDEEAYYVKMGFKGIKVKIgaksmeedIERLKVIREVVGE 192
Cdd:cd03322 95 IKGKAAGMPLYQLLGGkSRDGIMVY----SHASGRDIPELLEAVERHLAQGYRAIRVQL--------PKLFEAVREKFGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 193 EVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQ 272
Cdd:cd03322 163 EFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 273 TDVMWTGGISEMMKIGNMAKVMGYPLIPHySAGGISLIG---NLHVAAALNSPWIEMHLRKNDLRDKIFKESIEIDNGHL 349
Cdd:cd03322 243 TTVSHAGGITPARKIADLASLYGVRTGWH-GPTDLSPVGmaaALHLDLWVPNFGIQEYMRHAEETLEVFPHSVRFEDGYL 321
|
330 340
....*....|....*....|
gi 1774062176 350 VVPDRPGLGYTIREGVLEEY 369
Cdd:cd03322 322 HPGEEPGLGVEIDEKAAAKF 341
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
35-358 |
3.04e-45 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 159.89 E-value: 3.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 35 VVTEIETSDGYVGY-----GESLAYgcsdvvqvMIEKVLKPLLLKEDEELIEYLWDKMYKATLRFGRRGIAIAGISGVDT 109
Cdd:PRK15440 59 LVVEVEAENGQVGFavstaGEMGAF--------IVEKHLNRFIEGKCVSDIELIWDQMLNATLYYGRKGLVMNTISCVDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 110 ALWDIMGKKAKKPIYKLLGGsktKVRA----YITGGyyseKKDLEKlkdeeayyvKMGFKGIKVKI------GAKSMEED 179
Cdd:PRK15440 131 ALWDLLGKVRGLPVYKLLGG---AVRDelqfYATGA----RPDLAK---------EMGFIGGKMPLhhgpadGDAGLRKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 180 IERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTD----YLDLSARLAEELEVPIAGYETayT 255
Cdd:PRK15440 195 AAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDdywgYRELKRNAPAGMMVTSGEHEA--T 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 256 RWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHysagGISLIGNLHVAAALNSPWIE---MHLRKND 332
Cdd:PRK15440 273 LQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH----GSSVYSHHFVITRTNSPFSEflmMSPDADT 348
|
330 340 350
....*....|....*....|....*....|..
gi 1774062176 333 LRDK----IFKESIEIdNGHLVVP--DRPGLG 358
Cdd:PRK15440 349 VVPQfdpiLLDEPVPV-NGRIHKSvlDKPGFG 379
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
27-364 |
1.38e-44 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239444 [Multi-domain] Cd Length: 352 Bit Score: 157.19 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 27 LAEHPMEIVVTEIETSdGYVGYGeslaYGCSDV-VQVMIEKVLKPLLLKEDEELIEYLWDKMYKATLRFGRRGIAIAGIS 105
Cdd:cd03328 23 LAWDATTLVLVEVRAG-GRTGLG----YTYADAaAAALVDGLLAPVVEGRDALDPPAAWEAMQRAVRNAGRPGVAAMAIS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 106 GVDTALWDIMGKKAKKPIYKLLGGSKTKVRAYITGGYYSekKDLEKLKDEEAYYVKMGFKGIKVKIGAkSMEEDIERLKV 185
Cdd:cd03328 98 AVDIALWDLKARLLGLPLARLLGRAHDSVPVYGSGGFTS--YDDDRLREQLSGWVAQGIPRVKMKIGR-DPRRDPDRVAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 186 IREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLD----LSARLAEELEvpIAGYETAYTRWEFYE 261
Cdd:cd03328 175 ARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAglrlVRERGPAGMD--IAAGEYAYTLAYFRR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 262 IMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHySAGGISlignLHVAAALNS----PWIEMHLRKNDLrdkI 337
Cdd:cd03328 253 LLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH-CAPALH----AHVACAVPRlrhlEWFHDHVRIERM---L 324
|
330 340
....*....|....*....|....*...
gi 1774062176 338 FKESIEIDNGHLVV-PDRPGLGYTIREG 364
Cdd:cd03328 325 FDGAPDPSGGALRPdLSRPGLGLELRAR 352
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
29-363 |
1.64e-44 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 157.09 E-value: 1.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 29 EHPMEIVVTEIETSDGYVGYGES-----LAYG--CSDVVQVMIEKVLKPLLLKEDEELIEYLWDKMYKATlrfgrRGIAI 101
Cdd:cd03318 25 MHTQSLVLVRLTTSDGVVGIGEAttpggPAWGgeSPETIKAIIDRYLAPLLIGRDATNIGAAMALLDRAV-----AGNLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 102 AGiSGVDTALWDIMGKKAKKPIYKLLGGsktKVRAYI-------TGGYYSEKKDLEKLKDEEAYYVkmgfkgIKVKIGAK 174
Cdd:cd03318 100 AK-AAIEMALLDAQGRRLGLPVSELLGG---RVRDSLpvawtlaSGDTERDIAEAEEMLEAGRHRR------FKLKMGAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 175 SMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAY 254
Cdd:cd03318 170 PPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 255 TRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGyplIPHYSA----GGISLIGNLHVAAALNS-PW----IE 325
Cdd:cd03318 250 GPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAG---IALYGGtmleSSIGTAASAHLFATLPSlPFgcelFG 326
|
330 340 350
....*....|....*....|....*....|....*...
gi 1774062176 326 MHLrkndLRDKIFKESIEIDNGHLVVPDRPGLGYTIRE 363
Cdd:cd03318 327 PLL----LAEDLLEEPLAYRDGELHVPTGPGLGVRLDE 360
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
27-369 |
8.37e-44 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 154.95 E-value: 8.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 27 LAEHPMeiVVTEIETSDGYVGYGESLAYgcsdvvqvmIEKVLKPLL--------LKEDEELIEYLWDKMYKATLRF-GRR 97
Cdd:cd03321 26 VATAPL--VLIDLATDEGVTGHSYLFTY---------TPAALKSLKqllddmaaLLVGEPLAPAELERALAKRFRLlGYT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 98 GIAIAGISGVDTALWDIMGKKAKKPIYKLLGGSKTKVRAYITGGYysekkDLEKLKDEEAY-YVKMGFKGIKVKIGAKSM 176
Cdd:cd03321 95 GLVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGL-----DGAKLATERAVtAAEEGFHAVKTKIGYPTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 177 EEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTR 256
Cdd:cd03321 170 DEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 257 WEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYP----LIPHYSAGGISLIGNLHvaaalnspWIEmhlrKND 332
Cdd:cd03321 250 EEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPmsshLFQEISAHLLAVTPTAH--------WLE----YVD 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1774062176 333 LRDKIFKESIEIDNGHLVVPDRPGLGYTIREGVLEEY 369
Cdd:cd03321 318 WAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
95-370 |
1.18e-42 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239442 [Multi-domain] Cd Length: 385 Bit Score: 152.93 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 95 GRRGIAIAGIsgvDTALWDIMGKKAKKPIYKLL------GGSKTKVRAYITGGYYSEKKDLEKLKDEEAYYVKMGFKGIK 168
Cdd:cd03326 104 GERAVAVGAL---DMAVWDAVAKIAGLPLYRLLarrygrGQADPRVPVYAAGGYYYPGDDLGRLRDEMRRYLDRGYTVVK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 169 VKIGAKSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPiqTDYLD--LSARLAEELEVP 246
Cdd:cd03326 181 IKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEP--GDPLDyaLQAELADHYDGP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 247 IAGYETAYTRWEFYEIMR----KRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYP---LIPHysaGGISLigNLHVAAAL 319
Cdd:cd03326 259 IATGENLFSLQDARNLLRyggmRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWSrrrFFPH---GGHLM--SLHIAAGL 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1774062176 320 nspwiemHLRKNDLRDKIFK------ESIEIDNGHLVVPDRPGLGYTIREGVLEEYK 370
Cdd:cd03326 334 -------GLGGNESYPDVFQpfggfaDGCKVENGYVRLPDAPGIGFEGKAELAAEMR 383
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
95-324 |
4.37e-42 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 146.70 E-value: 4.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 95 GRRGIAIAgISGVDTALWDIMGKKAKKPIY-KLLGGSKTKVRAYITggyysekkdleklkdeeayyvkmgfkgikvkiga 173
Cdd:cd00308 36 GVVGWGEV-ISGIDMALWDLAAKALGVPLAeLLGGGSRDRVPAYGS---------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 174 ksmeedIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETA 253
Cdd:cd00308 81 ------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774062176 254 YTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGG-ISLIGNLHVAAALNSPWI 324
Cdd:cd00308 155 TTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESsIGTAAALHLAAALPNDRA 226
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
95-322 |
5.96e-40 |
|
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions.
Pssm-ID: 239431 [Multi-domain] Cd Length: 265 Bit Score: 142.48 E-value: 5.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 95 GRRGIAIAGISGVDTALWDIMGKKAKKPIYKLLGGSKTKVR-AYITGGyysekKDLEKLKDEEAYYVKMGFKGIKVKIGa 173
Cdd:cd03315 36 GLVGWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRvAHMLGL-----GEPAEVAEEARRALEAGFRTFKLKVG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 174 KSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETA 253
Cdd:cd03315 110 RDPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESA 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 254 YTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSA-GGISLIGNLHVAAALNSP 322
Cdd:cd03315 190 FTPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIeSGLGTLANAHLAAALRAV 259
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
39-358 |
3.54e-37 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239440 [Multi-domain] Cd Length: 415 Bit Score: 138.63 E-value: 3.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 39 IET-SDGYVGYGESLAYGCSDVVQVMIEKVLKPLLLKEDEELIEYLWDKMYK-----ATLRF-----GRRGIAIAGISgv 107
Cdd:cd03324 38 LRTdAAGLKGHGLTFTIGRGNEIVCAAIEALAHLVVGRDLESIVADMGKFWRrltsdSQLRWigpekGVIHLATAAVV-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 108 dTALWDIMGKKAKKPIYKLL----------------------------------GGSKTKVRAYITGGY----------- 142
Cdd:cd03324 116 -NAVWDLWAKAEGKPLWKLLvdmtpeelvscidfryitdaltpeealeilrrgqPGKAAREADLLAEGYpayttsagwlg 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 143 YSEkkdlEKLKDEEAYYVKMGFKGIKVKIGAkSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIW 222
Cdd:cd03324 195 YSD----EKLRRLCKEALAQGFTHFKLKVGA-DLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPW 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 223 FFEEPIQTDYLDLSARLAEELE---VPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLI 299
Cdd:cd03324 270 WIEEPTSPDDILGHAAIRKALAplpIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVC 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 300 PHysAGGI---------SLIGNLHVAAALNSPWIEM--HLRKNdlrdkiFKESIEIDNGHLVVPDRPGLG 358
Cdd:cd03324 350 PH--AGGVglcelvqhlSMIDYICVSGSKEGRVIEYvdHLHEH------FVYPVVIQNGAYMPPTDPGYS 411
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
35-369 |
2.52e-35 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 133.50 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 35 VVTEIETSDGYVGYGESLAYGCSDVVQVMIEKVLKPLLLKEDEELIEYLWDKMYKATlrFGRRG-IAIAGISGVDTALWD 113
Cdd:PRK15072 18 VTLKITTDDGVTGLGDATLNGRELAVASYLQDHVCPLLIGRDAHRIEDIWQYLYRGA--YWRRGpVTMSAIAAVDMALWD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 114 IMGKKAKKPIYKLLGG-SKTKVRAYitgGYYSeKKDLEKLKDEEAYYVKMGFKGIKVKIG------------AKSM---- 176
Cdd:PRK15072 96 IKAKAAGMPLYQLLGGaSREGVMVY---GHAN-GRDIDELLDDVARHLELGYKAIRVQCGvpglkttygvskGKGLayep 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 177 --------EED----------IERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDlSAR 238
Cdd:PRK15072 172 atkgllpeEELwstekylrfvPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWLEDPTPAENQE-AFR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 239 LAEELEV-PIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHySAGGISLIG---NLH 314
Cdd:PRK15072 251 LIRQHTTtPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSH-GPTDLSPVCmaaALH 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1774062176 315 VAAALNSPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTIREGVLEEY 369
Cdd:PRK15072 330 FDLWVPNFGIQEYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDFDEKLAAKY 384
|
|
| L-Ala-DL-Glu_epimerase |
cd03319 |
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ... |
32-298 |
3.53e-34 |
|
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239435 [Multi-domain] Cd Length: 316 Bit Score: 128.46 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 32 MEIVVTEIETsDGYVGYGE--SLAYGCSDVVQVMIEKV--LKPLLLKED---EELIEYLWDKMYKATlrfgrrgiaiAGI 104
Cdd:cd03319 25 AENVIVEIEL-DGITGYGEaaPTPRVTGETVESVLAALksVRPALIGGDprlEKLLEALQELLPGNG----------AAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 105 SGVDTALWDIMGKKAKKPIYKL-LGGSKTKVRAYITGGYYSEKKDLEKLKDeeayYVKMGFKGIKVKIGaKSMEEDIERL 183
Cdd:cd03319 94 AAVDIALWDLEAKLLGLPLYQLwGGGAPRPLETDYTISIDTPEAMAAAAKK----AAKRGFPLLKIKLG-GDLEDDIERI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 184 KVIREVVGEeVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIM 263
Cdd:cd03319 169 RAIREAAPD-ARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSAADAARLA 247
|
250 260 270
....*....|....*....|....*....|....*
gi 1774062176 264 RKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPL 298
Cdd:cd03319 248 GGGAYDGINIKLMKTGGLTEALRIADLARAAGLKV 282
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
33-368 |
1.38e-30 |
|
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239433 [Multi-domain] Cd Length: 354 Bit Score: 119.65 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 33 EIVVTEIETSDGYVGYGESLA-----YGCSDVVQ--VMIEKVLKPLLLKED----EELIEYLW----DKMYKAtlrfgrr 97
Cdd:cd03317 25 EFLIVELTDEEGITGYGEVVAfegpfYTEETNATawHILKDYLLPLLLGREfshpEEVSERLApikgNNMAKA------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 98 giaiagisGVDTALWDIMGKKAKKPIYKLLGGSKTKVRAYITGGYyseKKDLEKLKDEEAYYVKMGFKGIKVKIGAksmE 177
Cdd:cd03317 98 --------GLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGI---QDDVEQLLKQIERYLEEGYKRIKLKIKP---G 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 178 EDIERLKVIREVVGeEVKIAVDANNVYTFEEALEMgRKLEKLGIWFFEEPIQTDYLDLSARLAEELEVP------IAGYE 251
Cdd:cd03317 164 WDVEPLKAVRERFP-DIPLMADANSAYTLADIPLL-KRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPicldesIQSAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 252 TAytRWEFyEIMRKRAVDIVQTDVmwtGGISEMMKIGNMAKVMGyplIPHYSAG----GISLIGNLHVAAALN------- 320
Cdd:cd03317 242 DA--RKAI-ELGACKIINIKPGRV---GGLTEALKIHDLCQEHG---IPVWCGGmlesGIGRAHNVALASLPNftypgdi 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1774062176 321 SP----WIEmhlrkndlrdKIFKESIEIDNGHLVVPDRPGLGYTIREGVLEE 368
Cdd:cd03317 313 SAssryFEE----------DIITPPFELENGIISVPTGPGIGVTVDREALKK 354
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
149-245 |
4.18e-24 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 95.04 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 149 LEKLKDE-EAYYVKMGFKGIKVKIGAKSmEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEP 227
Cdd:smart00922 1 PEELAEAaRRAVAEAGFRAVKVKVGGGP-LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEP 79
|
90
....*....|....*...
gi 1774062176 228 IQTDYLDLSARLAEELEV 245
Cdd:smart00922 80 VPPDDLEGLAELRRATPI 97
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
35-369 |
3.32e-23 |
|
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239439 [Multi-domain] Cd Length: 395 Bit Score: 99.70 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 35 VVTEIETSDGYVGYGESlaYGCSD----VVQVMIEKVLKPLLLKEDEELieylwDKMYKATLRFGRRG---------IAI 101
Cdd:cd03323 31 NIVELTDDNGNTGVGES--PGGAEaleaLLEAARSLVGGDVFGAYLAVL-----ESVRVAFADRDAGGrglqtfdlrTTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 102 AGISGVDTALWDIMGKKAKKPIYKLLGGsktKVR------AY--------ITGGYYSEKKDL--EKLKDE------EAYY 159
Cdd:cd03323 104 HVVTAFEVALLDLLGQALGVPVADLLGG---GQRdsvpflAYlfykgdrhKTDLPYPWFRDRwgEALTPEgvvrlaRAAI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 160 VKMGFKGIKVKIGAKSMEEDIERLKVIREVVgEEVKIAVDANNVYTFEEALEMGRKLEKLgIWFFEEPiqTDYLDLSARL 239
Cdd:cd03323 181 DRYGFKSFKLKGGVLPGEEEIEAVKALAEAF-PGARLRLDPNGAWSLETAIRLAKELEGV-LAYLEDP--CGGREGMAEF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 240 AEELEVPIAGyETAYTRW-EFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAG-GISLIGNLHVAA 317
Cdd:cd03323 257 RRATGLPLAT-NMIVTDFrQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNNHlGISLAMMTHVAA 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1774062176 318 AL-------NSPWIEMHlrkndlRDKIFKESIEIDNGHLVVPDRPGLGYTIREGVLEEY 369
Cdd:cd03323 336 AApglitacDTHWIWQD------GQVITGEPLRIKDGKVAVPDKPGLGVELDRDKLAKA 388
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
30-128 |
1.97e-17 |
|
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold similarity with enolase N-terminal domain.
Pssm-ID: 397046 [Multi-domain] Cd Length: 117 Bit Score: 77.51 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 30 HPMEIVVTEIETSDGYVGYGESLAYG-CSDVVQVMIEKVLKPLLLKEDEELIEYLWDKMYKATLrfgrrGIAIAgISGVD 108
Cdd:pfam02746 24 QQQSLVIVRIETSEGVVGIGEATSYGgRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAAL-----GNMSA-KAAID 97
|
90 100
....*....|....*....|
gi 1774062176 109 TALWDIMGKKAKKPIYKLLG 128
Cdd:pfam02746 98 MALWDLKAKVLNLPLADLLG 117
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
159-319 |
3.35e-17 |
|
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239436 [Multi-domain] Cd Length: 263 Bit Score: 80.38 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 159 YVKMGFKGIKVKIGAKSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQTDylDLSAR 238
Cdd:cd03320 93 AYGGGYRTVKLKVGATSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPD--DLAEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 239 LAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIphYSA---GGISLIGNLHV 315
Cdd:cd03320 171 RRLAAGVPIALDESLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAV--VSSaleSSIGLGALAHL 248
|
....
gi 1774062176 316 AAAL 319
Cdd:cd03320 249 AAAL 252
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
160-252 |
1.54e-10 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 62.95 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 160 VKMGFKGIKVKIGAK-SMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLGIWFFEEPIQtDYLDLsAR 238
Cdd:PLN02980 1102 VEEGFSAIKLKVGRRvSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQ-DEDDL-IK 1179
|
90
....*....|....
gi 1774062176 239 LAEELEVPIAGYET 252
Cdd:PLN02980 1180 FCEETGLPVALDET 1193
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
163-319 |
8.39e-07 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 50.35 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 163 GFKGIKVKIGAK--SMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKL-EKLGIWFFEEPIQTdyldlSARL 239
Cdd:PRK02901 102 GCRTAKVKVAEPgqTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALdADGPLEYVEQPCAT-----VEEL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 240 AE---ELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIgnmAKVMGYPLIPHY---SAGGISLigNL 313
Cdd:PRK02901 177 AElrrRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAALDI---AEQIGLPVVVSSaldTSVGIAA--GL 251
|
....*.
gi 1774062176 314 HVAAAL 319
Cdd:PRK02901 252 ALAAAL 257
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
163-248 |
1.11e-06 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 49.63 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 163 GFKGIKVKIGAKSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEA---LEMGRKLEKLGIWFFEEPIQTDYLDLSARL 239
Cdd:PRK02714 133 GYRTFKWKIGVDPLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQL 212
|
....*....
gi 1774062176 240 AEELEVPIA 248
Cdd:PRK02714 213 SQDYQTPIA 221
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
163-322 |
1.03e-05 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 46.72 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 163 GFKGIKVKIGAKSMEEDIERLKVIREVVGEEVKIAVDANNVYTFEEALEMGRKLEKLG---IWFFEEPIQTDylDLSARL 239
Cdd:TIGR01927 124 GFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDPNLrgrIAFLEEPLPDA--DEMSAF 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 240 AEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIphYSA---GGISLIGNLHVA 316
Cdd:TIGR01927 202 SEATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAV--FSSvfeSSIALGQLARLA 279
|
....*.
gi 1774062176 317 AALNSP 322
Cdd:TIGR01927 280 AKLSPD 285
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
186-283 |
1.19e-05 |
|
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];
Pssm-ID: 441506 [Multi-domain] Cd Length: 365 Bit Score: 46.70 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 186 IREVVGEEVKIAV------DANNVYTFEEALEMGRKLEKLGIwffeepiqtDYLDLSARLAEELEVPIAGYETAYTRWeF 259
Cdd:COG1902 209 VRAAVGPDFPVGVrlsptdFVEGGLTLEESVELAKALEEAGV---------DYLHVSSGGYEPDAMIPTIVPEGYQLP-F 278
|
90 100
....*....|....*....|....
gi 1774062176 260 YEIMRKrAVDIVqtdVMWTGGISE 283
Cdd:COG1902 279 AARIRK-AVGIP---VIAVGGITT 298
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
180-281 |
4.64e-04 |
|
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 41.79 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 180 IERLKVIREVVGEE----VKIAVDANNVY--TFEEALEMGRKLEKLGIwffeepiqtDYLDLSARLAEELEVPIAGYETA 253
Cdd:cd02803 195 LEIVAAVREAVGPDfpvgVRLSADDFVPGglTLEEAIEIAKALEEAGV---------DALHVSGGSYESPPPIIPPPYVP 265
|
90 100
....*....|....*....|....*...
gi 1774062176 254 YTRWEFYEIMRKRAVDIvqtDVMWTGGI 281
Cdd:cd02803 266 EGYFLELAEKIKKAVKI---PVIAVGGI 290
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
34-299 |
2.09e-03 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 39.73 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 34 IVVTEIEtSDG---------YVGYGESLAygcSDVVQVMiekvlkplllkedeELIEYLWDKMYKATLRfgRRGIAIAGI 104
Cdd:PRK15129 29 VVVVELE-EEGikgtgectpYPRYGESDA---SVMAQIM--------------SVVPQLEKGLTREALQ--KLLPAGAAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 105 SGVDTALWDIMGKKAKKPIYKLLGgskTKVRAYITGGYYSEKKDLEKLKDEEAYYVKMGFKGIKVKIGAKSMEediERLK 184
Cdd:PRK15129 89 NAVDCALWDLAARQQQQSLAQLIG---ITLPETVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHLIS---ERMV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774062176 185 VIREVVGEEVKIaVDANNVYTFEEALEMGRKLEKLGIWFFEEPiqtdyldLSARLAEELE-----VPIAGYETAYTRwEF 259
Cdd:PRK15129 163 AIRSAVPDATLI-VDANESWRAEGLAARCQLLADLGVAMLEQP-------LPAQDDAALEnfihpLPICADESCHTR-SS 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1774062176 260 YEIMRKRaVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLI 299
Cdd:PRK15129 234 LKALKGR-YEMVNIKLDKTGGLTEALALATEARAQGFALM 272
|
|
| |
