|
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: 720.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 1 MIKDIRTYKLCYEGINDERDALAIKGLAEHPMEIVVTEIETSDGYVGYGESLAYGCSDAVQVTIEKILKPLLLKEDEELI 80
Cdd:NF040866 1 MIKEIKTYKLCYEGINEERDALAVKGLAEHPMEIVVTEIETSDGEIGYGESLAYGCSDVVQVTIEKILKPLLLKEDEELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 81 EYLWDKMYKATLRFGRRGIAIAGISGVDTGLWDIMGKKAKKPIYKLLGGSKRKVRAYITGGYYSEKKDLEKLRDEEAYYV 160
Cdd:NF040866 81 EGLWDKMYKATLRFGRRGIVIAGISGVDIALWDIMGKKTKKPIYKLLGGSKRKIRAYITGGYYSEKKDLEKLREEVAYYV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 161 KMGFKGIKVKIGAKSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLA 240
Cdd:NF040866 161 KMGFKGVKIKIGGKSMEEDMERLKAIREVVGEDVKIAVDANNVYTFEEALKMGRELEKLGIWFFEEPIQTDLLDLSAELT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 241 EELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHVAAALN 320
Cdd:NF040866 241 EALEIPIAGYETAYTRWEFYEIMRKRSVDIVQTDAMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLVANLHVAAALG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502139558 321 SPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTIRDGVFEEYECK 372
Cdd:NF040866 321 SPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTLREGVFEEYRCK 372
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-358 |
8.28e-139 |
|
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: 398.91 E-value: 8.28e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 2 IKDIRTYKLCYEginderdaLAIKGLAEHPMEIVVTEIETSDGYVGYGESLAYGCSDAVQVTIEKILKPLLLKEDEELIE 81
Cdd:cd03316 2 ITDVETFVLRVP--------LPEPGGAVTWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 82 YLWDKMYKATLRFGRRGIAIAGISGVDTGLWDIMGKKAKKPIYKLLGGSKR-KVRAYITGGYYSEkkDLEKLRDEEAYYV 160
Cdd:cd03316 74 RLWEKLYRRLFWRGRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRdRVRVYASGGGYDD--SPEELAEEAKRAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 161 KMGFKGIKVKIGA-----KSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDL 235
Cdd:cd03316 152 AEGFTAVKLKVGGpdsggEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 236 SARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHV 315
Cdd:cd03316 232 LARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 502139558 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 |
2.39e-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: 326.78 E-value: 2.39e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 1 MIKDIRTYKLCYEgindERDALAIKGLAEHPMEIVVTEIETSDGYVGYGESLAYGCS-DAVQVTIEKILKPLLLKEDEEL 79
Cdd:COG4948 2 KITDIEVYPVRLP----LKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTGaEAVAAALEEALAPLLIGRDPLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 80 IEYLWDKMYKATlrfgrrGIAIAGISGVDTGLWDIMGKKAKKPIYKLLGGSKR-KVRAYITGGYysekKDLEKLRDEEAY 158
Cdd:COG4948 78 IEALWQRLYRAL------PGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRdRVPVYATLGI----DTPEEMAEEARE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 159 YVKMGFKGIKVKIGAKSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSAR 238
Cdd:COG4948 148 AVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 239 LAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPH-YSAGGISLIGNLHVAA 317
Cdd:COG4948 228 LRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHcMLESGIGLAAALHLAA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 502139558 318 AL-NSPWIEMHLRKNDLRDkIFKESIEIDNGHLVVPDRPGLGYTIRDGVFEEY 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 |
2.72e-87 |
|
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: 267.28 E-value: 2.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 33 EIVVTEIETSDGYVGYGESLAygcSDAVQVTIEKILKPLLLKEDEELIEYLWDKMYKATLRFGRRGIAIAGISGVDTGLW 112
Cdd:cd03327 10 GWLFVEIETDDGTVGYANTTG---GPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATLAYGRKGIAMAAISAVDLALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 113 DIMGKKAKKPIYKLLGGSKR-KVRAYITGGYYSekkDLEKLRDEEAYYVKMGFKGIKVKI------GAKSMEEDIERLKA 185
Cdd:cd03327 87 DLLGKIRGEPVYKLLGGRTRdKIPAYASGLYPT---DLDELPDEAKEYLKEGYRGMKMRFgygpsdGHAGLRKNVELVRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 186 IREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRK 265
Cdd:cd03327 164 IREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 266 RAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHysAGGISligNLH-VAAALNSPWIE-----MHLRKNDLRDKIFK 339
Cdd:cd03327 244 RAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPH--ASQIY---NYHfIMSEPNSPFAEylpnsPDEVGNPLFYYIFL 318
|
330 340
....*....|....*....|..
gi 502139558 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 ... |
151-363 |
6.71e-78 |
|
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: 238.62 E-value: 6.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 151 KLRDE-EAYYVKMGFKGIKVKIGAKSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQ 229
Cdd:pfam13378 1 ELAAEaRRAVEARGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 230 TDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISL 309
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGPIGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502139558 310 IGNLHVAAAL-NSPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTIRD 363
Cdd:pfam13378 161 AASLHLAAAVpNLLIQEYFLDPLLLEDDLLTEPLEVEDGRVAVPDGPGLGVELDE 215
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
39-361 |
1.68e-64 |
|
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: 209.10 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 39 IETSDGYVGYGESLAYGCSDAVQVTIEKiLKPLLLKEDEELIEYLWDKMYKAtlRFGRRG-IAIAGISGVDTGLWDIMGK 117
Cdd:cd03325 19 IETDEGVVGWGEPTVEGKARTVEAAVQE-LEDYLIGKDPMNIEHHWQVMYRG--GFYRGGpVLMSAISGIDQALWDIKGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 118 KAKKPIYKLLGGSKR-KVRAY--ITGGYYSEKKDLEKLRDEEAY-YVKMGFKG-IKVKIGAKSMEEDIERLKAIREVVGE 192
Cdd:cd03325 96 VLGVPVHQLLGGQVRdRVRVYswIGGDRPSDVAEAARARREAGFtAVKMNATEeLQWIDTSKKVDAAVERVAALREAVGP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 193 DIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQ 272
Cdd:cd03325 176 DIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 273 TDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHVAAALNSPWI-EMHL-----RKNDLRDKIF-KESIEID 345
Cdd:cd03325 256 PDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDASTPNFLIqEQSLgihynEGDDLLDYLVdPEVFDME 335
|
330
....*....|....*.
gi 502139558 346 NGHLVVPDRPGLGYTI 361
Cdd:cd03325 336 NGYVKLPTGPGLGIEI 351
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
39-361 |
9.64e-56 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 187.03 E-value: 9.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 39 IETSDGYVGYGESLAYGCSDAVQVTIEKiLKPLLLKEDEELIEYLWDKMYKATlrFGRRG-IAIAGISGVDTGLWDIMGK 117
Cdd:PRK14017 20 IETDEGIVGWGEPVVEGRARTVEAAVHE-LADYLIGKDPRRIEDHWQVMYRGG--FYRGGpILMSAIAGIDQALWDIKGK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 118 KAKKPIYKLLGGSKR-KVRAY--ITGGYYSEKKDLEKLRdeeayyVKMGFKGIKVKiGAKSM---------EEDIERLKA 185
Cdd:PRK14017 97 ALGVPVHELLGGLVRdRIRVYswIGGDRPADVAEAARAR------VERGFTAVKMN-GTEELqyidsprkvDAAVARVAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 186 IREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRK 265
Cdd:PRK14017 170 VREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 266 RAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAGGISLIGNLHVAAALNSPWI-EMHL-----RKNDLRDKIF- 338
Cdd:PRK14017 250 GGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDAVSPNAFIqEQSLgihynQGADLLDYVKn 329
|
330 340
....*....|....*....|...
gi 502139558 339 KESIEIDNGHLVVPDRPGLGYTI 361
Cdd:PRK14017 330 KEVFAYEDGFVAIPTGPGLGIEI 352
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
2-368 |
1.89e-49 |
|
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: 170.27 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 2 IKDIRTYKLCYEGINDERDALAIKGLAEHPMEIVVTEIETSDGYVGYgeslAYGCSDAVQ-VTIEKILKPLLLKEDEELI 80
Cdd:cd03329 2 ITDVEVTVFEYPTQPVSFDGGHHHPGPAGTRKLALLTIETDEGAKGH----AFGGRPVTDpALVDRFLKKVLIGQDPLDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 81 EYLWDKMYKAtlrfgRRGIAIAGISGVDTGLWDIMGKKAKKPIYKLLGGSKRKVRAYITGGYYSekkDLEKLRDEEAY-- 158
Cdd:cd03329 78 ERLWQDLWRL-----QRGLTDRGLGLVDIALWDLAGKYLGLPVHRLLGGYREKIPAYASTMVGD---DLEGLESPEAYad 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 159 ----YVKMGFKGIKVKI-GAKSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIqtDYL 233
Cdd:cd03329 150 faeeCKALGYRAIKLHPwGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPL--REA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 234 DLSA--RLAEELEVPIAGYETAYTRWEFY-EIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHysAGGISli 310
Cdd:cd03329 228 SISSyrWLAEKLDIPILGTEHSRGALESRaDWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELH--GNGAA-- 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502139558 311 gNLHVAAAL-NSPWIEMHL----RKNDLRDKIFKE-SIEIDNGHLV-VPDRPGLGYTIRDGVFEE 368
Cdd:cd03329 304 -NLHVIAAIrNTRYYERGLlhpsQKYDVYAGYLSVlDDPVDSDGFVhVPKGPGLGVEIDFDYIER 367
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
35-369 |
8.17e-48 |
|
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: 165.69 E-value: 8.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 35 VVTEIETSDGYVGYGESLAYGCSDAVQVTIEKILKPLLLKEDEELIEYLWDKMYKATlrFGRRG-IAIAGISGVDTGLWD 113
Cdd:cd03322 17 VTLKITTDQGVTGLGDATLNGRELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGA--YWRRGpVTMNAIAAVDMALWD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 114 IMGKKAKKPIYKLLGGSKRK-VRAYitggYYSEKKDLEKLRDEEAYYVKMGFKGIKVKIgaksmeedIERLKAIREVVGE 192
Cdd:cd03322 95 IKGKAAGMPLYQLLGGKSRDgIMVY----SHASGRDIPELLEAVERHLAQGYRAIRVQL--------PKLFEAVREKFGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 193 DIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQ 272
Cdd:cd03322 163 EFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 273 TDVMWTGGISEMMKIGNMAKVMGYPLIPHySAGGISLIG---NLHVAAALNSPWIEMHLRKNDLRDKIFKESIEIDNGHL 349
Cdd:cd03322 243 TTVSHAGGITPARKIADLASLYGVRTGWH-GPTDLSPVGmaaALHLDLWVPNFGIQEYMRHAEETLEVFPHSVRFEDGYL 321
|
330 340
....*....|....*....|
gi 502139558 350 VVPDRPGLGYTIRDGVFEEY 369
Cdd:cd03322 322 HPGEEPGLGVEIDEKAAAKF 341
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
35-358 |
4.86e-45 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 159.12 E-value: 4.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 35 VVTEIETSDGYVGY-----GESLAYgcsdavqvTIEKILKPLLLKEDEELIEYLWDKMYKATLRFGRRGIAIAGISGVDT 109
Cdd:PRK15440 59 LVVEVEAENGQVGFavstaGEMGAF--------IVEKHLNRFIEGKCVSDIELIWDQMLNATLYYGRKGLVMNTISCVDL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 110 GLWDIMGKKAKKPIYKLLGGSKR-KVRAYITGGyyseKKDLEKlrdeeayyvKMGFKGIKVKI------GAKSMEEDIER 182
Cdd:PRK15440 131 ALWDLLGKVRGLPVYKLLGGAVRdELQFYATGA----RPDLAK---------EMGFIGGKMPLhhgpadGDAGLRKNAAM 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 183 LKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTD----YLDLSARLAEELEVPIAGYETayTRWE 258
Cdd:PRK15440 198 VADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDdywgYRELKRNAPAGMMVTSGEHEA--TLQG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 259 FYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHysagGISLIGNLHVAAALNSPWIE---MHLRKNDLRD 335
Cdd:PRK15440 276 FRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPH----GSSVYSHHFVITRTNSPFSEflmMSPDADTVVP 351
|
330 340
....*....|....*....|....*....
gi 502139558 336 K----IFKESIEIdNGHLVVP--DRPGLG 358
Cdd:PRK15440 352 QfdpiLLDEPVPV-NGRIHKSvlDKPGFG 379
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
29-361 |
9.32e-45 |
|
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: 157.86 E-value: 9.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 29 EHPMEIVVTEIETSDGYVGYGES-----LAYG--CSDAVQVTIEKILKPLLLKEDEELIEYLWDKMYKATlrfgrRGIAI 101
Cdd:cd03318 25 MHTQSLVLVRLTTSDGVVGIGEAttpggPAWGgeSPETIKAIIDRYLAPLLIGRDATNIGAAMALLDRAV-----AGNLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 102 AGiSGVDTGLWDIMGKKAKKPIYKLLGGSKRK---VRAYITGGYYSEKKDL-EKLRDEEAYYVkmgfkgIKVKIGAKSME 177
Cdd:cd03318 100 AK-AAIEMALLDAQGRRLGLPVSELLGGRVRDslpVAWTLASGDTERDIAEaEEMLEAGRHRR------FKLKMGARPPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 178 EDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRW 257
Cdd:cd03318 173 DDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 258 EFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGyplIPHYSA----GGISLIGNLHVAAALNS-PW----IEMHL 328
Cdd:cd03318 253 DAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAG---IALYGGtmleSSIGTAASAHLFATLPSlPFgcelFGPLL 329
|
330 340 350
....*....|....*....|....*....|...
gi 502139558 329 rkndLRDKIFKESIEIDNGHLVVPDRPGLGYTI 361
Cdd:cd03318 330 ----LAEDLLEEPLAYRDGELHVPTGPGLGVRL 358
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
27-362 |
4.76e-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: 155.65 E-value: 4.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 27 LAEHPMEIVVTEIETSdGYVGYGESlaYGCSDAVQVtIEKILKPLLLKEDEELIEYLWDKMYKATLRFGRRGIAIAGISG 106
Cdd:cd03328 23 LAWDATTLVLVEVRAG-GRTGLGYT--YADAAAAAL-VDGLLAPVVEGRDALDPPAAWEAMQRAVRNAGRPGVAAMAISA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 107 VDTGLWDIMGKKAKKPIYKLLGGSKRKVRAYITGGYYSekKDLEKLRDEEAYYVKMGFKGIKVKIGAkSMEEDIERLKAI 186
Cdd:cd03328 99 VDIALWDLKARLLGLPLARLLGRAHDSVPVYGSGGFTS--YDDDRLREQLSGWVAQGIPRVKMKIGR-DPRRDPDRVAAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 187 REVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLD----LSARLAEELEvpIAGYETAYTRWEFYEI 262
Cdd:cd03328 176 RRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAglrlVRERGPAGMD--IAAGEYAYTLAYFRRL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 263 MRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHySAGGISlignLHVAAALNS----PWIEMHLRKNDLrdkIF 338
Cdd:cd03328 254 LEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAH-CAPALH----AHVACAVPRlrhlEWFHDHVRIERM---LF 325
|
330 340
....*....|....*....|....*
gi 502139558 339 KESIEIDNGHLVV-PDRPGLGYTIR 362
Cdd:cd03328 326 DGAPDPSGGALRPdLSRPGLGLELR 350
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
27-369 |
1.05e-43 |
|
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: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 27 LAEHPMeiVVTEIETSDGYVGYGESLAYgcsdavqvtIEKILKPLL--------LKEDEELIEYLWDKMYKATLRF-GRR 97
Cdd:cd03321 26 VATAPL--VLIDLATDEGVTGHSYLFTY---------TPAALKSLKqllddmaaLLVGEPLAPAELERALAKRFRLlGYT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 98 GIAIAGISGVDTGLWDIMGKKAKKPIYKLLGGSKRKVRAYITGGYysekkDLEKLRDEEAY-YVKMGFKGIKVKIGAKSM 176
Cdd:cd03321 95 GLVRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGL-----DGAKLATERAVtAAEEGFHAVKTKIGYPTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 177 EEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTR 256
Cdd:cd03321 170 DEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 257 WEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYP----LIPHYSAGGISLIGNLHvaaalnspWIEmhlrKND 332
Cdd:cd03321 250 EEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPmsshLFQEISAHLLAVTPTAH--------WLE----YVD 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 502139558 333 LRDKIFKESIEIDNGHLVVPDRPGLGYTIRDGVFEEY 369
Cdd:cd03321 318 WAGAILEPPLKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
95-368 |
4.82e-43 |
|
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: 153.70 E-value: 4.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 95 GRRGIAIAGIsgvDTGLWDIMGKKAKKPIYKLL------GGSKRKVRAYITGGYYSEKKDLEKLRDEEAYYVKMGFKGIK 168
Cdd:cd03326 104 GERAVAVGAL---DMAVWDAVAKIAGLPLYRLLarrygrGQADPRVPVYAAGGYYYPGDDLGRLRDEMRRYLDRGYTVVK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 169 VKIGAKSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPiqTDYLD--LSARLAEELEVP 246
Cdd:cd03326 181 IKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEP--GDPLDyaLQAELADHYDGP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 247 IAGYETAYTRWEFYEIMR----KRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYP---LIPHysaGGISLigNLHVAAAL 319
Cdd:cd03326 259 IATGENLFSLQDARNLLRyggmRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWSrrrFFPH---GGHLM--SLHIAAGL 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 502139558 320 nspwiemHLRKNDLRDKIFK------ESIEIDNGHLVVPDRPGLGYTIRDGVFEE 368
Cdd:cd03326 334 -------GLGGNESYPDVFQpfggfaDGCKVENGYVRLPDAPGIGFEGKAELAAE 381
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
95-324 |
3.58e-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: 147.09 E-value: 3.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 95 GRRGIAIAgISGVDTGLWDIMGKKAKKPIY-KLLGGSKRKVRAYITggyysekkdleklrdeeayyvkmgfkgikvkiga 173
Cdd:cd00308 36 GVVGWGEV-ISGIDMALWDLAAKALGVPLAeLLGGGSRDRVPAYGS---------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 174 ksmeedIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETA 253
Cdd:cd00308 81 ------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502139558 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 |
5.90e-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: 5.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 95 GRRGIAIAGISGVDTGLWDIMGKKAKKPIYKLLGGSKRKVRAYITGGYYSEKKDLEKLRdeeaYYVKMGFKGIKVKIGaK 174
Cdd:cd03315 36 GLVGWAEATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGLGEPAEVAEEAR----RALEAGFRTFKLKVG-R 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 175 SMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAY 254
Cdd:cd03315 111 DPARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAF 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502139558 255 TRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSA-GGISLIGNLHVAAALNSP 322
Cdd:cd03315 191 TPHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIeSGLGTLANAHLAAALRAV 259
|
|
| 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 |
5.56e-36 |
|
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: 133.08 E-value: 5.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 32 MEIVVTEIETsDGYVGYGESLA----YGCS-DAVQVTIEKILKPLL--LKEDEELIEYLWDKMYKATlrfgrrgiaiAGI 104
Cdd:cd03319 25 AENVIVEIEL-DGITGYGEAAPtprvTGETvESVLAALKSVRPALIggDPRLEKLLEALQELLPGNG----------AAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 105 SGVDTGLWDIMGKKAKKPIYKL-LGGSKRKVRAYITGGYYSEKKDLEKLRDeeayYVKMGFKGIKVKIGaKSMEEDIERL 183
Cdd:cd03319 94 AAVDIALWDLEAKLLGLPLYQLwGGGAPRPLETDYTISIDTPEAMAAAAKK----AAKRGFPLLKIKLG-GDLEDDIERI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 184 KAIREVVGeDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVPIAGYETAYTRWEFYEIM 263
Cdd:cd03319 169 RAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSAADAARLA 247
|
250 260 270
....*....|....*....|....*....|....*
gi 502139558 264 RKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPL 298
Cdd:cd03319 248 GGGAYDGINIKLMKTGGLTEALRIADLARAAGLKV 282
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
39-358 |
3.01e-35 |
|
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: 133.62 E-value: 3.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 39 IET-SDGYVGYGESLAYGCSDAVQVTIEKILKPLLLKEDEELIEYLWDKMYK-----ATLRF-----GRRGIAIAGISgv 107
Cdd:cd03324 38 LRTdAAGLKGHGLTFTIGRGNEIVCAAIEALAHLVVGRDLESIVADMGKFWRrltsdSQLRWigpekGVIHLATAAVV-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 108 dTGLWDIMGKKAKKPIYKLL----------------------------------GGSKRKVRAYITGGY----------- 142
Cdd:cd03324 116 -NAVWDLWAKAEGKPLWKLLvdmtpeelvscidfryitdaltpeealeilrrgqPGKAAREADLLAEGYpayttsagwlg 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 143 YSEkkdlEKLRDEEAYYVKMGFKGIKVKIGAkSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIW 222
Cdd:cd03324 195 YSD----EKLRRLCKEALAQGFTHFKLKVGA-DLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPW 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 223 FFEEPIQTDYLDLSARLAEELE---VPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLI 299
Cdd:cd03324 270 WIEEPTSPDDILGHAAIRKALAplpIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKFGVPVC 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 300 PHysAGGI---------SLIGNLHVAAALNSPWIEM--HLRKNdlrdkiFKESIEIDNGHLVVPDRPGLG 358
Cdd:cd03324 350 PH--AGGVglcelvqhlSMIDYICVSGSKEGRVIEYvdHLHEH------FVYPVVIQNGAYMPPTDPGYS 411
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
35-361 |
9.99e-35 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 131.95 E-value: 9.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 35 VVTEIETSDGYVGYGESLAYGCSDAVQVTIEKILKPLLLKEDEELIEYLWDKMYKATlrFGRRG-IAIAGISGVDTGLWD 113
Cdd:PRK15072 18 VTLKITTDDGVTGLGDATLNGRELAVASYLQDHVCPLLIGRDAHRIEDIWQYLYRGA--YWRRGpVTMSAIAAVDMALWD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 114 IMGKKAKKPIYKLLGG-SKRKVRAYitgGYYSeKKDLEKLRDEEAYYVKMGFKGIKVKIGAKSM---------------- 176
Cdd:PRK15072 96 IKAKAAGMPLYQLLGGaSREGVMVY---GHAN-GRDIDELLDDVARHLELGYKAIRVQCGVPGLkttygvskgkglayep 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 177 --------EED----------IERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQTDYLDlSAR 238
Cdd:PRK15072 172 atkgllpeEELwstekylrfvPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWLEDPTPAENQE-AFR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 239 LAEELEV-PIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHySAGGISLIG---NLH 314
Cdd:PRK15072 251 LIRQHTTtPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSH-GPTDLSPVCmaaALH 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502139558 315 VAAALNSPWIEMHLRKNDLRDKIFKESIEIDNGHLVVPDRPGLGYTI 361
Cdd:PRK15072 330 FDLWVPNFGIQEYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDF 376
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
33-361 |
9.48e-31 |
|
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: 120.03 E-value: 9.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 33 EIVVTEIETSDGYVGYGESLA-----YgcSDAVQVTIEKILK----PLLLKED----EELIEYLW----DKMYKAtlrfg 95
Cdd:cd03317 25 EFLIVELTDEEGITGYGEVVAfegpfY--TEETNATAWHILKdyllPLLLGREfshpEEVSERLApikgNNMAKA----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 96 rrgiaiagisGVDTGLWDIMGKKAKKPIYKLLGGSKRKVRAYITGGYyseKKDLEKLRDEEAYYVKMGFKGIKVKIGAks 175
Cdd:cd03317 98 ----------GLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGI---QDDVEQLLKQIERYLEEGYKRIKLKIKP-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 176 mEEDIERLKAIREVVGeDIKIAVDANNVYTFEEALEMgRRLEKLGIWFFEEPIQTDYLDLSARLAEELEVP------IAG 249
Cdd:cd03317 163 -GWDVEPLKAVRERFP-DIPLMADANSAYTLADIPLL-KRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPicldesIQS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 250 YETAytRWEFyEIMRKRAVDIVQTDVmwtGGISEMMKIGNMAKVMGyplIPHYSAG----GISLIGNLHVAAALN----- 320
Cdd:cd03317 240 AEDA--RKAI-ELGACKIINIKPGRV---GGLTEALKIHDLCQEHG---IPVWCGGmlesGIGRAHNVALASLPNftypg 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 502139558 321 --SP----WIEmhlrkndlrdKIFKESIEIDNGHLVVPDRPGLGYTI 361
Cdd:cd03317 311 diSAssryFEE----------DIITPPFELENGIISVPTGPGIGVTV 347
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
149-245 |
7.57e-26 |
|
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: 99.66 E-value: 7.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 149 LEKLRDE-EAYYVKMGFKGIKVKIGAKSmEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEP 227
Cdd:smart00922 1 PEELAEAaRRAVAEAGFRAVKVKVGGGP-LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEP 79
|
90
....*....|....*...
gi 502139558 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 ... |
35-370 |
1.28e-24 |
|
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: 103.56 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 35 VVTEIETSDGYVGYGESlaYGCSDAVQVTIE-----KILKPLLlkEDEELIEylwdkmyKATLRFGRRGIAIAG------ 103
Cdd:cd03323 31 NIVELTDDNGNTGVGES--PGGAEALEALLEaarslVGGDVFG--AYLAVLE-------SVRVAFADRDAGGRGlqtfdl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 104 ------ISGVDTGLWDIMGKKAKKPIYKLLGGSKRK---VRAY--------ITGGYYSEKKDLEK--------LRDEEAY 158
Cdd:cd03323 100 rttvhvVTAFEVALLDLLGQALGVPVADLLGGGQRDsvpFLAYlfykgdrhKTDLPYPWFRDRWGealtpegvVRLARAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 159 YVKMGFKGIKVKIGAKSMEEDIERLKAIREVVGEDiKIAVDANNVYTFEEALEMGRRLEKLgIWFFEEPiqTDYLDLSAR 238
Cdd:cd03323 180 IDRYGFKSFKLKGGVLPGEEEIEAVKALAEAFPGA-RLRLDPNGAWSLETAIRLAKELEGV-LAYLEDP--CGGREGMAE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 239 LAEELEVPIAGyETAYTRW-EFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIPHYSAG-GISLIGNLHVA 316
Cdd:cd03323 256 FRRATGLPLAT-NMIVTDFrQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNNHlGISLAMMTHVA 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502139558 317 AAL-------NSPWIEMHlrkndlRDKIFKESIEIDNGHLVVPDRPGLGYTI-RDGVFEEYE 370
Cdd:cd03323 335 AAApglitacDTHWIWQD------GQVITGEPLRIKDGKVAVPDKPGLGVELdRDKLAKAHE 390
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
147-319 |
1.62e-19 |
|
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: 86.93 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 147 KDLEKLRDEEAYyvKMGFKGIKVKIGAKSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEE 226
Cdd:cd03320 83 DAAALGEAKAAY--GGGYRTVKLKVGATSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 227 PIQTDylDLSARLAEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIphYSA-- 304
Cdd:cd03320 161 PLPPD--DLAELRRLAAGVPIALDESLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAV--VSSal 236
|
170
....*....|....*.
gi 502139558 305 -GGISLIGNLHVAAAL 319
Cdd:cd03320 237 eSSIGLGALAHLAAAL 252
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
30-128 |
1.03e-16 |
|
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: 75.59 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 30 HPMEIVVTEIETSDGYVGYGESLAYG-CSDAVQVTIEKILKPLLLKEDEELIEYLWDKMYKATLrfgrrGIAIAgISGVD 108
Cdd:pfam02746 24 QQQSLVIVRIETSEGVVGIGEATSYGgRAETIKAILDDHLAPLLIGRDAANISDLWQLMYRAAL-----GNMSA-KAAID 97
|
90 100
....*....|....*....|
gi 502139558 109 TGLWDIMGKKAKKPIYKLLG 128
Cdd:pfam02746 98 MALWDLKAKVLNLPLADLLG 117
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
160-252 |
2.03e-11 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 65.65 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 160 VKMGFKGIKVKIGAK-SMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLGIWFFEEPIQtDYLDLsAR 238
Cdd:PLN02980 1102 VEEGFSAIKLKVGRRvSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQ-DEDDL-IK 1179
|
90
....*....|....
gi 502139558 239 LAEELEVPIAGYET 252
Cdd:PLN02980 1180 FCEETGLPVALDET 1193
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
163-248 |
5.60e-08 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 53.86 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 163 GFKGIKVKIGAKSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEA---LEMGRRLEKLGIWFFEEPIQTDYLDLSARL 239
Cdd:PRK02714 133 GYRTFKWKIGVDPLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQL 212
|
....*....
gi 502139558 240 AEELEVPIA 248
Cdd:PRK02714 213 SQDYQTPIA 221
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
163-319 |
6.18e-08 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 53.82 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 163 GFKGIKVKIGAK--SMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRL-EKLGIWFFEEPIQTdyldlSARL 239
Cdd:PRK02901 102 GCRTAKVKVAEPgqTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALdADGPLEYVEQPCAT-----VEEL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 240 AE---ELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIgnmAKVMGYPLIPHY---SAGGISLigNL 313
Cdd:PRK02901 177 AElrrRVGVPIAADESIRRAEDPLRVARAGAADVAVLKVAPLGGVRAALDI---AEQIGLPVVVSSaldTSVGIAA--GL 251
|
....*.
gi 502139558 314 HVAAAL 319
Cdd:PRK02901 252 ALAAAL 257
|
|
| FadH |
COG1902 |
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ... |
183-283 |
1.43e-07 |
|
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: 52.86 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 183 LKAIREVVGEDIKIAV------DANNVYTFEEALEMGRRLEKLGIwffeepiqtDYLDLSARLAEELEVPIAGYETAYTR 256
Cdd:COG1902 206 VEAVRAAVGPDFPVGVrlsptdFVEGGLTLEESVELAKALEEAGV---------DYLHVSSGGYEPDAMIPTIVPEGYQL 276
|
90 100
....*....|....*....|....*..
gi 502139558 257 WeFYEIMRKrAVDIVqtdVMWTGGISE 283
Cdd:COG1902 277 P-FAARIRK-AVGIP---VIAVGGITT 298
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
163-322 |
4.81e-06 |
|
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: 47.88 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 163 GFKGIKVKIGAKSMEEDIERLKAIREVVGEDIKIAVDANNVYTFEEALEMGRRLEKLG---IWFFEEPIQTDylDLSARL 239
Cdd:TIGR01927 124 GFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDPNLrgrIAFLEEPLPDA--DEMSAF 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 240 AEELEVPIAGYETAYTRWEFYEIMRKRAVDIVQTDVMWTGGISEMMKIGNMAKVMGYPLIphYSA---GGISLIGNLHVA 316
Cdd:TIGR01927 202 SEATGTAIALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAV--FSSvfeSSIALGQLARLA 279
|
....*.
gi 502139558 317 AALNSP 322
Cdd:TIGR01927 280 AKLSPD 285
|
|
| OYE_like_FMN_family |
cd02803 |
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ... |
180-281 |
6.47e-06 |
|
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: 47.57 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 180 IERLKAIREVVGED----IKIAVDANNVY--TFEEALEMGRRLEKLGIwffeepiqtDYLDLSARLAEELEVPIAGYETA 253
Cdd:cd02803 195 LEIVAAVREAVGPDfpvgVRLSADDFVPGglTLEEAIEIAKALEEAGV---------DALHVSGGSYESPPPIIPPPYVP 265
|
90 100
....*....|....*....|....*...
gi 502139558 254 YTRWEFYEIMRKRAVDIvqtDVMWTGGI 281
Cdd:cd02803 266 EGYFLELAEKIKKAVKI---PVIAVGGI 290
|
|
| OYE_like_2_FMN |
cd04733 |
Old yellow enzyme (OYE)-related FMN binding domain, group 2. Each monomer of OYE contains FMN ... |
180-281 |
1.86e-03 |
|
Old yellow enzyme (OYE)-related FMN binding domain, group 2. 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. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 240084 [Multi-domain] Cd Length: 338 Bit Score: 39.88 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502139558 180 IERLKAIREVVGEDIKIAVDANNV------YTFEEALEMGRRLEKLGIwffeepiqtDYLDLSARLAEELevPIAGYETA 253
Cdd:cd04733 203 LEIYDAIRAAVGPGFPVGIKLNSAdfqrggFTEEDALEVVEALEEAGV---------DLVELSGGTYESP--AMAGAKKE 271
|
90 100 110
....*....|....*....|....*....|....
gi 502139558 254 YTR------WEFYEIMRKravdIVQTDVMWTGGI 281
Cdd:cd04733 272 STIareayfLEFAEKIRK----VTKTPLMVTGGF 301
|
|
| |
