|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-404 |
0e+00 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 908.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 1 MKIVGAEVFVTCPGRNFVTLKITTEDGITGLGDATLNGRELPVASYLTDHLCPQLIGRDARRIEDIWQFFYKGAYWRRGP 80
Cdd:PRK15072 1 MKIVDAEVIVTCPGRNFVTLKITTDDGVTGLGDATLNGRELAVASYLQDHVCPLLIGRDAHRIEDIWQYLYRGAYWRRGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 81 VTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHTIDDVLEDYARHKEQGFKAIRVQCGVPGMKTTYG 160
Cdd:PRK15072 81 VTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLELGYKAIRVQCGVPGLKTTYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 161 MAKGKGLAYEPATKGQWPEEQLWSTEKYLDFTPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDP 240
Cdd:PRK15072 161 VSKGKGLAYEPATKGLLPEEELWSTEKYLRFVPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWLEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 241 TPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSDLS 320
Cdd:PRK15072 241 TPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPTDLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 321 PVCMAAALHFDLWVPNFGVQEFMGYSEQMLEVFPHNWTFEGGYMHPGDKPGLGIEFDEKLAAKYPYDPAYLPVARLEDGT 400
Cdd:PRK15072 321 PVCMAAALHFDLWVPNFGIQEYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDFDEKLAAKYPYEPAYLPVARLEDGT 400
|
....
gi 446628923 401 LWNW 404
Cdd:PRK15072 401 MWNW 404
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-404 |
0e+00 |
|
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: 681.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 2 KIVGAEVFVTCPGRNFVTLKITTEDGITGLGDATLNGRELPVASYLTDHLCPQLIGRDARRIEDIWQFFYKGAYWRRGPV 81
Cdd:cd03322 1 KITAIEVIVTCPGRNFVTLKITTDQGVTGLGDATLNGRELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 82 TMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHTIDDVLEDYARHKEQGFKAIRVQCgvpgmkttygm 161
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRVQL----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 162 akgkglayepatkgqwpeeqlwstekyldftPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPT 241
Cdd:cd03322 150 -------------------------------PKLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 242 PAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSDLSP 321
Cdd:cd03322 199 PAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPTDLSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 322 VCMAAALHFDLWVPNFGVQEFMGYSEQMLEVFPHNWTFEGGYMHPGDKPGLGIEFDEKLAAKYPYDPAYLPVARLEDGTL 401
Cdd:cd03322 279 VGMAAALHLDLWVPNFGIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYLPVARLEDGTV 358
|
...
gi 446628923 402 WNW 404
Cdd:cd03322 359 HNW 361
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-375 |
5.07e-134 |
|
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: 388.12 E-value: 5.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 2 KIVGAEVFVTCP----------GRNFVTLKITTEDGITGLGDATLNGRELPVASYLTDHLCPQLIGRDARRIEDIWQFFY 71
Cdd:cd03316 1 KITDVETFVLRVplpepggavtWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 72 KGAYWR-RGPVTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHT--TGHTIDDVLEDYARHKEQGFKAIRV 148
Cdd:cd03316 81 RRLFWRgRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGggYDDSPEELAEEAKRAVAEGFTAVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 149 QCGVPGMKttygmakgkglayepatkgqwpeeqlwstEKYLDFTPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKS 228
Cdd:cd03316 161 KVGGPDSG-----------------------------GEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 229 IEDYRLFWMEDPTPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQ 308
Cdd:cd03316 212 LEEYDLFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHG 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446628923 309 VRTGSHGPsdLSPVCMAAALHFDLWVPNFGVQEFMGYSEQ-MLEVFPHNWTFEGGYMHPGDKPGLGIE 375
Cdd:cd03316 292 VRVAPHGA--GGPIGLAASLHLAAALPNFGILEYHLDDLPlREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-384 |
8.50e-119 |
|
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: 349.51 E-value: 8.50e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 1 MKIVGAEVFV--------------TCPGRNFVTLKITTEDGITGLGDATLNGRELP-VASYLTDHLCPQLIGRDARRIED 65
Cdd:COG4948 1 MKITDIEVYPvrlplkrpftisrgTRTERDVVLVRVETDDGITGWGEAVPGGTGAEaVAAALEEALAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 66 IWQFFYkgaywRRGPVTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHTIDDVLEDYARHKEQGFKA 145
Cdd:COG4948 81 LWQRLY-----RALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 146 IRVQCGVPGmkttygmakgkglayepatkgqwpeeqlwstekyLDFTPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARF 225
Cdd:COG4948 156 LKLKVGGPD----------------------------------PEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 226 GKSIEDYRLFWMEDPTPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFAS 305
Cdd:COG4948 202 LRALEDLGLEWIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAE 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446628923 306 LYQVRTGSHGPSDlSPVCMAAALHFDLWVPNFGVQEFMGYSEQMLEVFPHNWTFEGGYMHPGDKPGLGIEFDEKLAAKY 384
Cdd:COG4948 282 AHGVPVMPHCMLE-SGIGLAAALHLAAALPNFDIVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-377 |
1.29e-94 |
|
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: 287.69 E-value: 1.29e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 2 KIVGAEVFVtCPgRNFVTLKITTEDGITGLGDATLNGRELPVASYLTDhLCPQLIGRDARRIEDIWQFFYKGAYWRRGPV 81
Cdd:cd03325 1 KITKIETFV-VP-PRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQE-LEDYLIGKDPMNIEHHWQVMYRGGFYRGGPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 82 TMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHTIDDVLEDYARHKEQGFKAIRVQCGvpgmkttygm 161
Cdd:cd03325 78 LMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNAT---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 162 akgkglayepatkgqwPEEQLWSTEKYLDFTPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPT 241
Cdd:cd03325 148 ----------------EELQWIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 242 PAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPsdLSP 321
Cdd:cd03325 212 LPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCP--LGP 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446628923 322 VCMAAALHFDLWVPNFGVQEFMG-----YSEQMLEVFPHNWTF--EGGYMHPGDKPGLGIEFD 377
Cdd:cd03325 290 IALAASLHVDASTPNFLIQEQSLgihynEGDDLLDYLVDPEVFdmENGYVKLPTGPGLGIEID 352
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-404 |
3.34e-84 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 261.75 E-value: 3.34e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 1 MKIVGAEVFVTCPGRNFvtLKITTEDGITGLGDATLNGRELPVASYLTDhLCPQLIGRDARRIEDIWQFFYKGAYWRRGP 80
Cdd:PRK14017 1 MKITKLETFRVPPRWLF--LKIETDEGIVGWGEPVVEGRARTVEAAVHE-LADYLIGKDPRRIEDHWQVMYRGGFYRGGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 81 VTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHTIDDVLEDYARHKEQGFKAIRvqcgvpgMKTTyg 160
Cdd:PRK14017 78 ILMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVK-------MNGT-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 161 makgkglayepatkgqwPEEQLWSTEKYLDFTPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDP 240
Cdd:PRK14017 149 -----------------EELQYIDSPRKVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 241 TPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPsdLS 320
Cdd:PRK14017 212 VLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCP--LG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 321 PVCMAAALHFDLWVPNFGVQEF-MG--YSE--QMLEVF--PHNWTFEGGYMHPGDKPGLGIEFDEKL---AAKYPYDpAY 390
Cdd:PRK14017 290 PIALAACLQVDAVSPNAFIQEQsLGihYNQgaDLLDYVknKEVFAYEDGFVAIPTGPGLGIEIDEAKvreRAKTGHD-WR 368
|
410
....*....|....
gi 446628923 391 LPVARLEDGTLWNW 404
Cdd:PRK14017 369 NPVWRHADGSVAEW 382
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
2-377 |
9.01e-56 |
|
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: 187.15 E-value: 9.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 2 KIVGAEVFVtcpgrNFVTLKITTEDGITGLGDATLNgrelPVASYLTD-HLCPQLIGRDARRIEDIWQFFYKGA-YWRRG 79
Cdd:cd03327 1 KIKSVRTRV-----GWLFVEIETDDGTVGYANTTGG----PVACWIVDqHLARFLIGKDPSDIEKLWDQMYRATlAYGRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 80 PVTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHTIDDVLEDYARH-KEQGFKAIRvqcgvpgMKTT 158
Cdd:cd03327 72 GIAMAAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYASGLYPTDLDELPDEAKEyLKEGYRGMK-------MRFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 159 YGMAKG-KGLayepatkgqwpeeqlwstEKYLDFTPKLFDAVrntfGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWM 237
Cdd:cd03327 145 YGPSDGhAGL------------------RKNVELVRAIREAV----GYDVDLMLDCYMSWNLNYAIKMARALEKYELRWI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 238 EDPTPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPS 317
Cdd:cd03327 203 EEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQ 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446628923 318 dlspvcmAAALHFDLWVPNFGVQEFMGYS--EQMLEVFPHNWTFE----GGYMHPGDKPGLGIEFD 377
Cdd:cd03327 283 -------IYNYHFIMSEPNSPFAEYLPNSpdEVGNPLFYYIFLNEpvpvNGYFDLSDKPGFGLELN 341
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
11-342 |
1.12e-55 |
|
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: 183.30 E-value: 1.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 11 TCPGRNFVTLKITTEDGITGLGDAtlngrelpvasyltdhlcpqligrdarriediwqffykgaywrrgpvtmsaISAVD 90
Cdd:cd00308 20 TADTNDTVLVKLTTDSGVVGWGEV---------------------------------------------------ISGID 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 91 MALWDIKAKAANMPLYQLLGGASREGVMVYCHttghtiddvledyarhkeqgfkairvqcgvpgmkttygmakgkglaye 170
Cdd:cd00308 49 MALWDLAAKALGVPLAELLGGGSRDRVPAYGS------------------------------------------------ 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 171 patkgqwpeeqlwstekyldftPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQACFR 250
Cdd:cd00308 81 ----------------------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYA 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 251 LIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSDlSPVCMAAALHF 330
Cdd:cd00308 139 ALRRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE-SSIGTAAALHL 217
|
330
....*....|..
gi 446628923 331 DLWVPNFGVQEF 342
Cdd:cd00308 218 AAALPNDRAIET 229
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
198-378 |
7.98e-49 |
|
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: 165.05 E-value: 7.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 198 AVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIE 277
Cdd:pfam13378 36 AVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 278 EQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSdlSPVCMAAALHFDLWVPNFGVQEFMGYSEQMLE-VFPHN 356
Cdd:pfam13378 116 AGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGG--GPIGLAASLHLAAAVPNLLIQEYFLDPLLLEDdLLTEP 193
|
170 180
....*....|....*....|..
gi 446628923 357 WTFEGGYMHPGDKPGLGIEFDE 378
Cdd:pfam13378 194 LEVEDGRVAVPDGPGLGVELDE 215
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
6-110 |
3.53e-40 |
|
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: 138.76 E-value: 3.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 6 AEVFVTCPGRN---------------FVTLKITTEDGITGLGDATLNG-RELPVASYLTDHLCPQLIGRDARRIEDIWQF 69
Cdd:pfam02746 2 IEVFVVDVGWPlrpiqmafgtvqqqsLVIVRIETSEGVVGIGEATSYGgRAETIKAILDDHLAPLLIGRDAANISDLWQL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446628923 70 FYKGAYWrrgpvTMSAISAVDMALWDIKAKAANMPLYQLLG 110
Cdd:pfam02746 82 MYRAALG-----NMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
20-377 |
9.56e-32 |
|
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: 123.66 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 20 LKITTEDGITGlgdATLNGRELPVASYLTDHLCPQLIGRDARRIEDIWQffyKGAYWRRGpVTMSAISAVDMALWDIKAK 99
Cdd:cd03329 37 LTIETDEGAKG---HAFGGRPVTDPALVDRFLKKVLIGQDPLDRERLWQ---DLWRLQRG-LTDRGLGLVDIALWDLAGK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 100 AANMPLYQLLGGAsREGVMVYCHTTGHTIDDVL---EDYARHKEQ----GFKAIRVQCGVPGMkttygmakgkglayepa 172
Cdd:cd03329 110 YLGLPVHRLLGGY-REKIPAYASTMVGDDLEGLespEAYADFAEEckalGYRAIKLHPWGPGV----------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 173 tkgqwpeeqlwstekyLDFTPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQACFRLI 252
Cdd:cd03329 172 ----------------VRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 253 RQHTVTPIAVGE-VFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSdlspvcmAAALHFD 331
Cdd:cd03329 236 AEKLDIPILGTEhSRGALESRADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGNG-------AANLHVI 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446628923 332 LWVPNfgvQEFmgYSEQMLEVFPHNWTFEGGY------------MHPGDKPGLGIEFD 377
Cdd:cd03329 309 AAIRN---TRY--YERGLLHPSQKYDVYAGYLsvlddpvdsdgfVHVPKGPGLGVEID 361
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
78-384 |
1.98e-23 |
|
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: 100.25 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 78 RGPVTMsAISAVDMALWDIKAKAANMPLYQLLGGASREgVMVYchtTGHTIDDVLEDYARHKE---QGFKAIRVQCGVPG 154
Cdd:cd03321 94 TGLVRM-AAAGIDMAAWDALAKVHGLPLAKLLGGNPRP-VQAY---DSHGLDGAKLATERAVTaaeEGFHAVKTKIGYPT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 155 MKttygmakgkglayepatkgqwpeEQLwstekyldftpKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRL 234
Cdd:cd03321 169 AD-----------------------EDL-----------AVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 235 FWMEDPTPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSH 314
Cdd:cd03321 215 TWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSH 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446628923 315 GPSDLSP--VCMAAALHfdlWVpnfgvqEFMGYSEQMLEvfpHNWTFEGGYMHPGDKPGLGIEFDEKLAAKY 384
Cdd:cd03321 295 LFQEISAhlLAVTPTAH---WL------EYVDWAGAILE---PPLKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
18-387 |
2.15e-23 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 100.57 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 18 VTLKITTEDGITGLGDATlnGRElPVASYLTDHLCPQLIGRDARRIEDIW-QFFYKGAYWRRGPVTMSAISAVDMALWDI 96
Cdd:PRK15440 59 LVVEVEAENGQVGFAVST--AGE-MGAFIVEKHLNRFIEGKCVSDIELIWdQMLNATLYYGRKGLVMNTISCVDLALWDL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 97 KAKAANMPLYQLLGGASREGVMVYchTTGHTiddvlEDYArhKEQGFkairvqcgVPG-MKTTYGMAKGkglayepatkg 175
Cdd:PRK15440 136 LGKVRGLPVYKLLGGAVRDELQFY--ATGAR-----PDLA--KEMGF--------IGGkMPLHHGPADG----------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 176 qwpEEQLwstEKYLDftpkLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQACFRLIRQH 255
Cdd:PRK15440 188 ---DAGL---RKNAA----MVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 256 TVTPIAV--GEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSHGPSDLSpvcmaaaLHFDLW 333
Cdd:PRK15440 258 APAGMMVtsGEHEATLQGFRTLLEMGCIDIIQPDVGWCGGLTELVKIAALAKARGQLVVPHGSSVYS-------HHFVIT 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446628923 334 VPNFGVQEFMGYSEQMLEVFPhnwTF----------EGGYMH--PGDKPGLGIEFDEKLAAKYPYD 387
Cdd:PRK15440 331 RTNSPFSEFLMMSPDADTVVP---QFdpilldepvpVNGRIHksVLDKPGFGVELNRDCNLKRPYS 393
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
18-378 |
6.18e-23 |
|
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: 98.93 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 18 VTLKITTEDGITGLGDATLNGR-----ELPVASYLT--DHLCPQLIGRDARRIEDIWQffykgAYWRRGPVTMSAISAVD 90
Cdd:cd03318 31 VLVRLTTSDGVVGIGEATTPGGpawggESPETIKAIidRYLAPLLIGRDATNIGAAMA-----LLDRAVAGNLFAKAAIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 91 MALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHTIDDVLEDYARHKEQG-FKAIRVQCGVpgmkttygmakgkglay 169
Cdd:cd03318 106 MALLDAQGRRLGLPVSELLGGRVRDSLPVAWTLASGDTERDIAEAEEMLEAGrHRRFKLKMGA----------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 170 EPatkgqwPEEQLWSTEkyldftpklfdAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQACF 249
Cdd:cd03318 169 RP------PADDLAHVE-----------AIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 250 RLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVrtGSHGPSDL-SPVCMAAAL 328
Cdd:cd03318 232 ARLRSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGI--ALYGGTMLeSSIGTAASA 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446628923 329 HFDLWVPN--FGVqEFMG---YSEQMLEVFPhnwTFEGGYMHPGDKPGLGIEFDE 378
Cdd:cd03318 310 HLFATLPSlpFGC-ELFGpllLAEDLLEEPL---AYRDGELHVPTGPGLGVRLDE 360
|
|
| 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 ... |
16-335 |
1.66e-22 |
|
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: 96.87 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 16 NFVTLKITTeDGITGLGDATLNGRE----LPVASYLTDHLCPQLIGRDARrIEDIWQffykgAYWRRGPVTMSAISAVDM 91
Cdd:cd03319 26 ENVIVEIEL-DGITGYGEAAPTPRVtgetVESVLAALKSVRPALIGGDPR-LEKLLE-----ALQELLPGNGAARAAVDI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 92 ALWDIKAKAANMPLYQLLGGASREGVmvychTTGHTI-----DDVLEDYARHKEQGFKAIRVQCGvpgmkttygmakgkg 166
Cdd:cd03319 99 ALWDLEAKLLGLPLYQLWGGGAPRPL-----ETDYTIsidtpEAMAAAAKKAAKRGFPLLKIKLG--------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 167 layepatkgqwpeeqlwsTEKYLDftPKLFDAVRNTFGfNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQ 246
Cdd:cd03319 159 ------------------GDLEDD--IERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGDD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 247 ACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRT--GSHGPSDLSpvcM 324
Cdd:cd03319 218 DGLAYLRDKSPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVmvGCMVESSLS---I 294
|
330
....*....|....*....
gi 446628923 325 AAALHF--------DLWVP 335
Cdd:cd03319 295 AAAAHLaaakadfvDLDGP 313
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
27-378 |
1.73e-20 |
|
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: 91.70 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 27 GITGLG----DATlngrelpVASYLTDHLCPQLIGRDARRIEDIWQffykgAYWR------RGPVTMSAISAVDMALWDI 96
Cdd:cd03328 39 GRTGLGytyaDAA-------AAALVDGLLAPVVEGRDALDPPAAWE-----AMQRavrnagRPGVAAMAISAVDIALWDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 97 KAKAANMPLYQLLgGASREGVMVYCHT--TGHTIDDVLEDYARHKEQGFKAIRvqcgvpgMKTtygmakgkglayepatk 174
Cdd:cd03328 107 KARLLGLPLARLL-GRAHDSVPVYGSGgfTSYDDDRLREQLSGWVAQGIPRVK-------MKI----------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 175 GQWPEEQlwstekyldftPKLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQACFRLIRQ 254
Cdd:cd03328 162 GRDPRRD-----------PDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 255 HTVT--PIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQVRTGSH-GPSDLSPVCMAA--ALH 329
Cdd:cd03328 231 RGPAgmDIAAGEYAYTLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDLSAHcAPALHAHVACAVprLRH 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446628923 330 FDLWVPNFGVqefmgysEQMLevFPHNWTFEGGYMHPGD-KPGLGIEFDE 378
Cdd:cd03328 311 LEWFHDHVRI-------ERML--FDGAPDPSGGALRPDLsRPGLGLELRA 351
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
87-304 |
3.60e-19 |
|
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: 86.63 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 87 SAVDMALWDIKAKAANMPLYQLLGGAsREGVMVychttGHTI-----DDVLEDYARHKEQGFKAIRVQCGVPgmkttygm 161
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGGY-RDRVRV-----AHMLglgepAEVAEEARRALEAGFRTFKLKVGRD-------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 162 akgkglayePATKGQwpeeqlwstekyldftpkLFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPT 241
Cdd:cd03315 112 ---------PARDVA------------------VVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446628923 242 PAENQACFRLIRQHTVTPIAVGEvfnSIW---DCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFA 304
Cdd:cd03315 165 PADDLEGRAALARATDTPIMADE---SAFtphDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVA 227
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
15-309 |
1.75e-14 |
|
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: 74.19 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 15 RNFVTLKITTEDGITGLGDATL------NGRELPVASY-LTDHLCPQLIGRDARRIEDIWQFF--YKGAywrrgpvTMsA 85
Cdd:cd03317 24 REFLIVELTDEEGITGYGEVVAfegpfyTEETNATAWHiLKDYLLPLLLGREFSHPEEVSERLapIKGN-------NM-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 86 ISAVDMALWDIKAKAANMPLYQLLGGASRE---GVMVychttG--HTIDDVLEDYARHKEQGFKAIRVQcgvpgmkttyg 160
Cdd:cd03317 96 KAGLEMAVWDLYAKAQGQSLAQYLGGTRDSipvGVSI-----GiqDDVEQLLKQIERYLEEGYKRIKLK----------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 161 MAKGKGLAYEPATKGQWPEEQLwstekyldftpkLFDAvrNTfgfnehllhdmhhRLTPIEAARFgKSIEDYRLFWMEDP 240
Cdd:cd03317 160 IKPGWDVEPLKAVRERFPDIPL------------MADA--NS-------------AYTLADIPLL-KRLDEYGLLMIEQP 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446628923 241 TPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQV 309
Cdd:cd03317 212 LAADDLIDHAELQKLLKTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGI 280
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
129-258 |
3.85e-14 |
|
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: 67.69 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 129 DDVLEDYARH-KEQGFKAIRVQCGVPGmkttygmakgkglayepatkgqwpeeqlwstekylDFTPKLFDAVRNTFGFNE 207
Cdd:smart00922 2 EELAEAARRAvAEAGFRAVKVKVGGGP-----------------------------------LEDLARVAAVREAVGPDA 46
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446628923 208 HLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQACFRLIRQHTVT 258
Cdd:smart00922 47 DLMVDANGAWTAEEAIRALEALDELGLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
15-384 |
1.23e-10 |
|
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: 62.73 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 15 RNFVTlkITTEDGITGLGDATLNGRELPvasyLTDHLCPQLIGRDA-----RRIEDIWQFFYKGAYWRRGPVTMS----- 84
Cdd:cd03323 30 RNIVE--LTDDNGNTGVGESPGGAEALE----ALLEAARSLVGGDVfgaylAVLESVRVAFADRDAGGRGLQTFDlrttv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 85 -AISAVDMALWDIKAKAANMPLYQLLGGASREGV--MVYC------HTTGH-------------TIDDVLEDYARHKEQ- 141
Cdd:cd03323 104 hVVTAFEVALLDLLGQALGVPVADLLGGGQRDSVpfLAYLfykgdrHKTDLpypwfrdrwgealTPEGVVRLARAAIDRy 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 142 GFKAIRVQCGV-PGmktTYGMAKGKGLAYEpatkgqWPEEQL-------WSTEkyldftpklfdavrntfgfnehllhdm 213
Cdd:cd03323 184 GFKSFKLKGGVlPG---EEEIEAVKALAEA------FPGARLrldpngaWSLE--------------------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 214 hhrltpiEAARFGKSIEDyRLFWMEDPTPAENQacFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGG 293
Cdd:cd03323 228 -------TAIRLAKELEG-VLAYLEDPCGGREG--MAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 294 ITGMRRIADFASLYQVRTGSHGPSDLSpVCMAAALHFDLWVPNFGVQEFMGYSEQMLEVFPHN-WTFEGGYMHPGDKPGL 372
Cdd:cd03323 298 MRGSVRVAQVCETWGLGWGMHSNNHLG-ISLAMMTHVAAAAPGLITACDTHWIWQDGQVITGEpLRIKDGKVAVPDKPGL 376
|
410
....*....|..
gi 446628923 373 GIEFDEKLAAKY 384
Cdd:cd03323 377 GVELDRDKLAKA 388
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
17-294 |
3.50e-10 |
|
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: 61.20 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 17 FVTLKiTTEDGITGLGDATLNGRELPVASYLTDHLCPQLIGRDARRIEDIWqffykGAYWRR----------GP---VTM 83
Cdd:cd03324 35 YVVLR-TDAAGLKGHGLTFTIGRGNEIVCAAIEALAHLVVGRDLESIVADM-----GKFWRRltsdsqlrwiGPekgVIH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 84 SAISAVDMALWDIKAKAANMPLYQLLGGASREgVMVYCHTTGHTIDDVLEDYA---RHKEQGFKAIRVQC----GVPGMK 156
Cdd:cd03324 109 LATAAVVNAVWDLWAKAEGKPLWKLLVDMTPE-ELVSCIDFRYITDALTPEEAleiLRRGQPGKAAREADllaeGYPAYT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 157 TT-----YGMAKGKGLAYEPATKGqwpeeqlWSTEKyLDFTPKLFDAV------RNTFGFNEHLLHDMHHRLTPIEAARF 225
Cdd:cd03324 188 TSagwlgYSDEKLRRLCKEALAQG-------FTHFK-LKVGADLEDDIrrcrlaREVIGPDNKLMIDANQRWDVPEAIEW 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446628923 226 GKSIEDYRLFWMEDPTPAENQACFRLIRQHTVT---PIAVGE------VFnsiwdcKQLIEEQLIDYIRTTLTHAGGI 294
Cdd:cd03324 260 VKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPlpiGVATGEhcqnrvVF------KQLLQAGAIDVVQIDSCRLGGV 331
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
85-382 |
3.79e-10 |
|
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: 60.87 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 85 AISAVDMALWDIKAKAANMPLYQLLG-----GASREGVMVYC----HTTGHTIDDVLEDYARHKEQGFKAIRVQCGvpgm 155
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLArrygrGQADPRVPVYAaggyYYPGDDLGRLRDEMRRYLDRGYTVVKIKIG---- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 156 kttygmakGKGLAYEPATkgqwpeeqlwstekyldftpklFDAVRNTFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLF 235
Cdd:cd03326 185 --------GAPLDEDLRR----------------------IEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446628923 236 WMEDPTPAENQACFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLI----DYIRTTLTHAGGITGMRRIadfasLYQVRT 311
Cdd:cd03326 235 WYEEPGDPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRM-----LDVLEA 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446628923 312 GSHGPSDLSP-------VCMAAALHfdlwvpnFGVQEFMGYSEQMLEVFPHNWTFEGGYMHPGDKPGLGIEFDEKLAA 382
Cdd:cd03326 310 HGWSRRRFFPhgghlmsLHIAAGLG-------LGGNESYPDVFQPFGGFADGCKVENGYVRLPDAPGIGFEGKAELAA 380
|
|
| |
