|
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 1618847557 1 MKIIAADVFVTCPGRNFVTLKITTESGLCGLGDATLNGRELSVASYLKDHLCPQLIGRDASRIEDIWQFFYKGAYWRRGP 80
Cdd:PRK15072 1 MKIVDAEVIVTCPGRNFVTLKITTDDGVTGLGDATLNGRELAVASYLQDHVCPLLIGRDAHRIEDIWQYLYRGAYWRRGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 81 VTMSAISAIDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGRTIDEVLEDYAKHQQMGFKAIRVQCGVPGMQTTYG 160
Cdd:PRK15072 81 VTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLELGYKAIRVQCGVPGLKTTYG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 161 LAKGKGLAYEPATKGLWPEEQLWSSEKYLDFTPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDP 240
Cdd:PRK15072 161 VSKGKGLAYEPATKGLLPEEELWSTEKYLRFVPKLFEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRLFWLEDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 241 TPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPSDLS 320
Cdd:PRK15072 241 TPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSHGPTDLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 321 PVCHAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHSWRFEEGYMHPGDEPGLGISFDEKLAAKYPYDPAYLPVARLEDGT 400
Cdd:PRK15072 321 PVCMAAALHFDLWVPNFGIQEYMGHSEETLEVFPHSYTFEDGYLHPGDAPGLGVDFDEKLAAKYPYEPAYLPVARLEDGT 400
|
....
gi 1618847557 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: 703.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 2 KIIAADVFVTCPGRNFVTLKITTESGLCGLGDATLNGRELSVASYLKDHLCPQLIGRDASRIEDIWQFFYKGAYWRRGPV 81
Cdd:cd03322 1 KITAIEVIVTCPGRNFVTLKITTDQGVTGLGDATLNGRELAVKAYLREHLKPLLIGRDANRIEDIWQYLYRGAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 82 TMSAISAIDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGRTIDEVLEDYAKHQQMGFKAIRVQCgvpgmqttygl 161
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRVQL----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 162 akgkglayepatkglwpeeqlwssekyldftPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPT 241
Cdd:cd03322 150 -------------------------------PKLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 242 PAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPSDLSP 321
Cdd:cd03322 199 PAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPTDLSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 322 VCHAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHSWRFEEGYMHPGDEPGLGISFDEKLAAKYPYDPAYLPVARLEDGTL 401
Cdd:cd03322 279 VGMAAALHLDLWVPNFGIQEYMRHAEETLEVFPHSVRFEDGYLHPGEEPGLGVEIDEKAAAKFPYVPRYLPVARLEDGTV 358
|
...
gi 1618847557 402 WNW 404
Cdd:cd03322 359 HNW 361
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-374 |
2.96e-133 |
|
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: 386.20 E-value: 2.96e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 2 KIIAADVFVTCP----------GRNFVTLKITTESGLCGLGDATLNGRELSVASYLKDHLCPQLIGRDASRIEDIWQFFY 71
Cdd:cd03316 1 KITDVETFVLRVplpepggavtWRNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDLLAPLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 72 KGAYWR-RGPVTMSAISAIDMALWDIKAKAANMPLYQLLGGASREGVMVYCHT--TGRTIDEVLEDYAKHQQMGFKAIRV 148
Cdd:cd03316 81 RRLFWRgRGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGggYDDSPEELAEEAKRAVAEGFTAVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 149 QCGVPGMQttyglakgkglayepatkglwpeeqlwssEKYLDFTPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKS 228
Cdd:cd03316 161 KVGGPDSG-----------------------------GEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 229 IEDYRLFWMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQ 308
Cdd:cd03316 212 LEEYDLFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHG 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1618847557 309 VRTGSHGPsdLSPVCHAAALHFDLWVPNFGVQEYMGYSEQ-MLEVFPHSWRFEEGYMHPGDEPGLGI 374
Cdd:cd03316 292 VRVAPHGA--GGPIGLAASLHLAAALPNFGILEYHLDDLPlREDLFKNPPEIEDGYVTVPDRPGLGV 356
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-384 |
9.45e-117 |
|
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: 344.11 E-value: 9.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 1 MKIIAADVFV--------------TCPGRNFVTLKITTESGLCGLGDATLNGREL-SVASYLKDHLCPQLIGRDASRIED 65
Cdd:COG4948 1 MKITDIEVYPvrlplkrpftisrgTRTERDVVLVRVETDDGITGWGEAVPGGTGAeAVAAALEEALAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 66 IWQFFYkgaywRRGPVTMSAISAIDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGRTIDEVLEDYAKHQQMGFKA 145
Cdd:COG4948 81 LWQRLY-----RALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 146 IRVQCGVPGmqttyglakgkglayepatkglwpeeqlwssekyLDFTPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARF 225
Cdd:COG4948 156 LKLKVGGPD----------------------------------PEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 226 GKSIEDYRLFWMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFAS 305
Cdd:COG4948 202 LRALEDLGLEWIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAE 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1618847557 306 LYQVRTGSHGPSDlSPVCHAAALHFDLWVPNFGVQEYMGYSEQMLEVFPHSWRFEEGYMHPGDEPGLGISFDEKLAAKY 384
Cdd:COG4948 282 AHGVPVMPHCMLE-SGIGLAAALHLAAALPNFDIVELDGPLLLADDLVEDPLRIEDGYLTVPDGPGLGVELDEDALARY 359
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-377 |
9.91e-92 |
|
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: 279.98 E-value: 9.91e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 2 KIIAADVFVtCPgRNFVTLKITTESGLCGLGDATLNGRELSVASYLKDhLCPQLIGRDASRIEDIWQFFYKGAYWRRGPV 81
Cdd:cd03325 1 KITKIETFV-VP-PRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQE-LEDYLIGKDPMNIEHHWQVMYRGGFYRGGPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 82 TMSAISAIDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGRTIDEVLEDYAKHQQMGFKAIRVQCGvpgmqttygl 161
Cdd:cd03325 78 LMSAISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNAT---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 162 akgkglayepatkglwPEEQLWSSEKYLDFTPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPT 241
Cdd:cd03325 148 ----------------EELQWIDTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 242 PAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPsdLSP 321
Cdd:cd03325 212 LPENVEALAEIAARTTIPIATGERLFSRWDFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCP--LGP 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1618847557 322 VCHAAALHFDLWVPNFGVQEYMG-----YSEQMLEVF--PHSWRFEEGYMHPGDEPGLGISFD 377
Cdd:cd03325 290 IALAASLHVDASTPNFLIQEQSLgihynEGDDLLDYLvdPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-404 |
1.89e-79 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 249.43 E-value: 1.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 1 MKIIAADVFVTCPGRNFvtLKITTESGLCGLGDATLNGRELSVASYLKDhLCPQLIGRDASRIEDIWQFFYKGAYWRRGP 80
Cdd:PRK14017 1 MKITKLETFRVPPRWLF--LKIETDEGIVGWGEPVVEGRARTVEAAVHE-LADYLIGKDPRRIEDHWQVMYRGGFYRGGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 81 VTMSAISAIDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGRTIDEVLEDYAKHQQMGFKAIRvqcgvpgMQTTyg 160
Cdd:PRK14017 78 ILMSAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVK-------MNGT-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 161 lakgkglayepatkglwPEEQLWSSEKYLDFTPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDP 240
Cdd:PRK14017 149 -----------------EELQYIDSPRKVDAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 241 TPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPsdLS 320
Cdd:PRK14017 212 VLPENAEALPEIAAQTSIPIATGERLFSRWDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCP--LG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 321 PVCHAAALHFDLWVPNFGVQEY-MG--YSE--QMLEVF--PHSWRFEEGYMHPGDEPGLGISFDEKL---AAKYPYDpAY 390
Cdd:PRK14017 290 PIALAACLQVDAVSPNAFIQEQsLGihYNQgaDLLDYVknKEVFAYEDGFVAIPTGPGLGIEIDEAKvreRAKTGHD-WR 368
|
410
....*....|....
gi 1618847557 391 LPVARLEDGTLWNW 404
Cdd:PRK14017 369 NPVWRHADGSVAEW 382
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
11-342 |
1.04e-58 |
|
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: 191.00 E-value: 1.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 11 TCPGRNFVTLKITTESGLCGLGDAtlngrelsvasylkdhlcpqligrdasriediwqffykgaywrrgpvtmsaISAID 90
Cdd:cd00308 20 TADTNDTVLVKLTTDSGVVGWGEV---------------------------------------------------ISGID 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 91 MALWDIKAKAANMPLYQLLGGASREGVMVYCHttgrtidevledyakhqqmgfkairvqcgvpgmqttyglakgkglaye 170
Cdd:cd00308 49 MALWDLAAKALGVPLAELLGGGSRDRVPAYGS------------------------------------------------ 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 171 patkglwpeeqlwssekyldftPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQECFR 250
Cdd:cd00308 81 ----------------------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYA 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 251 LIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPSDlSPVCHAAALHF 330
Cdd:cd00308 139 ALRRRTGIPIAADESVTTVDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLE-SSIGTAAALHL 217
|
330
....*....|..
gi 1618847557 331 DLWVPNFGVQEY 342
Cdd:cd00308 218 AAALPNDRAIET 229
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
18-377 |
1.26e-51 |
|
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: 175.98 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 18 VTLKITTESGLCGLGDATLNgrELSVASYLKdHLCPQLIGRDASRIEDIWQFFYKGA-YWRRGPVTMSAISAIDMALWDI 96
Cdd:cd03327 12 LFVEIETDDGTVGYANTTGG--PVACWIVDQ-HLARFLIGKDPSDIEKLWDQMYRATlAYGRKGIAMAAISAVDLALWDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 97 KAKAANMPLYQLLGGASREGVMVYCHTTGRTIDEVLEDYAKH-QQMGFKAIRvqcgvpgMQTTYGLAKGKglayepatKG 175
Cdd:cd03327 89 LGKIRGEPVYKLLGGRTRDKIPAYASGLYPTDLDELPDEAKEyLKEGYRGMK-------MRFGYGPSDGH--------AG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 176 LwpeeqlwssEKYLDftpkLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQECFRLIRQH 255
Cdd:cd03327 154 L---------RKNVE----LVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 256 TVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPSdlspvchAAALHFDLWVP 335
Cdd:cd03327 221 TGIPISTGEHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHASQ-------IYNYHFIMSEP 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1618847557 336 NFGVQEYMGYS------EQMLEVFPHSWRFEEGYMHPGDEPGLGISFD 377
Cdd:cd03327 294 NSPFAEYLPNSpdevgnPLFYYIFLNEPVPVNGYFDLSDKPGFGLELN 341
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
197-378 |
4.99e-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: 165.43 E-value: 4.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 197 EAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLI 276
Cdd:pfam13378 35 RAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 277 EEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGPSdlSPVCHAAALHFDLWVPNFGVQEYMGYSEQMLE-VFPH 355
Cdd:pfam13378 115 EAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGG--GPIGLAASLHLAAAVPNLLIQEYFLDPLLLEDdLLTE 192
|
170 180
....*....|....*....|...
gi 1618847557 356 SWRFEEGYMHPGDEPGLGISFDE 378
Cdd:pfam13378 193 PLEVEDGRVAVPDGPGLGVELDE 215
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
5-110 |
1.96e-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: 139.53 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 5 AADVFVTCPGRN---------------FVTLKITTESGLCGLGDATLNG-RELSVASYLKDHLCPQLIGRDASRIEDIWQ 68
Cdd:pfam02746 1 AIEVFVVDVGWPlrpiqmafgtvqqqsLVIVRIETSEGVVGIGEATSYGgRAETIKAILDDHLAPLLIGRDAANISDLWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1618847557 69 FFYKGAYWrrgpvTMSAISAIDMALWDIKAKAANMPLYQLLG 110
Cdd:pfam02746 81 LMYRAALG-----NMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
20-377 |
2.41e-28 |
|
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: 114.42 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 20 LKITTESGLCGlgdATLNGRELSVASYLKDHLCPQLIGRDASRIEDIWQffyKGAYWRRGpVTMSAISAIDMALWDIKAK 99
Cdd:cd03329 37 LTIETDEGAKG---HAFGGRPVTDPALVDRFLKKVLIGQDPLDRERLWQ---DLWRLQRG-LTDRGLGLVDIALWDLAGK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 100 AANMPLYQLLGGAsREGVMVYCHTTGRTIDEVL---EDYA----KHQQMGFKAIRVQCGVPGMqttyglakgkglayepa 172
Cdd:cd03329 110 YLGLPVHRLLGGY-REKIPAYASTMVGDDLEGLespEAYAdfaeECKALGYRAIKLHPWGPGV----------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 173 tkglwpeeqlwssekyLDFTPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQECFRLI 252
Cdd:cd03329 172 ----------------VRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 253 RQHTVTPIAVGE-VFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGpsdlspvCHAAALH-- 329
Cdd:cd03329 236 AEKLDIPILGTEhSRGALESRADWVLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHG-------NGAANLHvi 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1618847557 330 --------FDLWV--PNFGVQEYMGY-SEQMLEVfphswrFEEGYMHPGDEPGLGISFD 377
Cdd:cd03329 309 aairntryYERGLlhPSQKYDVYAGYlSVLDDPV------DSDGFVHVPKGPGLGVEID 361
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
78-384 |
5.30e-25 |
|
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: 104.87 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 78 RGPVTMsAISAIDMALWDIKAKAANMPLYQLLGGASREgVMVYcHTTGRTIDEVLEDYAKH-QQMGFKAIRVQCGVPGMq 156
Cdd:cd03321 94 TGLVRM-AAAGIDMAAWDALAKVHGLPLAKLLGGNPRP-VQAY-DSHGLDGAKLATERAVTaAEEGFHAVKTKIGYPTA- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 157 ttyglakgkglayepatkglwpEEQLwssekyldftpKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFW 236
Cdd:cd03321 170 ----------------------DEDL-----------AVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTW 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 237 MEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRTGSHGP 316
Cdd:cd03321 217 IEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGIPMSSHLF 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1618847557 317 SDLS-------PVCHaaalhfdlWVpnfgvqEYMGYSEQMLEvfpHSWRFEEGYMHPGDEPGLGISFDEKLAAKY 384
Cdd:cd03321 297 QEISahllavtPTAH--------WL------EYVDWAGAILE---PPLKFEDGNAVIPDEPGNGIIWREKAVRKY 354
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
18-378 |
1.24e-24 |
|
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: 103.94 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 18 VTLKITTESGLCGLGDATLNGREL-------SVASYLKDHLCPQLIGRDASRIEDIWQffykgAYWRRGPVTMSAISAID 90
Cdd:cd03318 31 VLVRLTTSDGVVGIGEATTPGGPAwggespeTIKAIIDRYLAPLLIGRDATNIGAAMA-----LLDRAVAGNLFAKAAIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 91 MALWDIKAKAANMPLYQLLGGASREGVMVYCH----TTGRTIDEVLE--DYAKHQ----QMGFKAIRVQcgvpgmqttyg 160
Cdd:cd03318 106 MALLDAQGRRLGLPVSELLGGRVRDSLPVAWTlasgDTERDIAEAEEmlEAGRHRrfklKMGARPPADD----------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 161 LAKgkglayepatkglwpeeqlwssekyldftpklFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDP 240
Cdd:cd03318 175 LAH--------------------------------VEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 241 TPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVrtGSHGPSDL- 319
Cdd:cd03318 223 VPRENLDGLARLRSRNRVPIMADESVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGI--ALYGGTMLe 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1618847557 320 SPVCHAAALHFDLWVPN--FGVqEYMG---YSEQMLEVfphSWRFEEGYMHPGDEPGLGISFDE 378
Cdd:cd03318 301 SSIGTAASAHLFATLPSlpFGC-ELFGpllLAEDLLEE---PLAYRDGELHVPTGPGLGVRLDE 360
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
50-387 |
1.43e-24 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 104.04 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 50 HLCPQLIGRDASRIEDIW-QFFYKGAYWRRGPVTMSAISAIDMALWDIKAKAANMPLYQLLGGASREGVMVYChTTGRTi 128
Cdd:PRK15440 88 HLNRFIEGKCVSDIELIWdQMLNATLYYGRKGLVMNTISCVDLALWDLLGKVRGLPVYKLLGGAVRDELQFYA-TGARP- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 129 devleDYAKhqQMGFkairvqcgVPG-MQTTYGLAKGkglayepatkglwpEEQLwssEKYLDftpkLFEAVRNKFGFNE 207
Cdd:PRK15440 166 -----DLAK--EMGF--------IGGkMPLHHGPADG--------------DAGL---RKNAA----MVADMREKVGDDF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 208 HLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQECFRLIRQHTVTPIAV--GEVFNSIWDCKQLIEEQLIDYIR 285
Cdd:PRK15440 210 WLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMMVtsGEHEATLQGFRTLLEMGCIDIIQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 286 TTITHAGGITGMRRIADFASLYQVRTGSHGPSDLSpvchaaaLHFDLWVPNFGVQEYMGYSEQMLEVFP--HSWRFEE-- 361
Cdd:PRK15440 290 PDVGWCGGLTELVKIAALAKARGQLVVPHGSSVYS-------HHFVITRTNSPFSEFLMMSPDADTVVPqfDPILLDEpv 362
|
330 340 350
....*....|....*....|....*....|.
gi 1618847557 362 ---GYMH--PGDEPGLGISFDEKLAAKYPYD 387
Cdd:PRK15440 363 pvnGRIHksVLDKPGFGVELNRDCNLKRPYS 393
|
|
| 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 |
5.34e-21 |
|
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: 92.64 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 16 NFVTLKITTEsGLCGLGDATLNGREL-----SVASYLKdHLCPQLIGRDAsRIEDIWQffykgAYWRRGPVTMSAISAID 90
Cdd:cd03319 26 ENVIVEIELD-GITGYGEAAPTPRVTgetveSVLAALK-SVRPALIGGDP-RLEKLLE-----ALQELLPGNGAARAAVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 91 MALWDIKAKAANMPLYQLLGGASREGVmvychTTGRTI-----DEVLEDYAKHQQMGFKAIRVQCGvpgmqttyglakgk 165
Cdd:cd03319 98 IALWDLEAKLLGLPLYQLWGGGAPRPL-----ETDYTIsidtpEAMAAAAKKAAKRGFPLLKIKLG-------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 166 glayepatkglwpeeqlwsSEKYLDftPKLFEAVRNKFGfNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAEN 245
Cdd:cd03319 159 -------------------GDLEDD--IERIRAIREAAP-DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 246 QECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVRT--GSHGPSDLS--P 321
Cdd:cd03319 217 DDGLAYLRDKSPLPIMADESCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVmvGCMVESSLSiaA 296
|
330
....*....|....*..
gi 1618847557 322 VCHAAALHF---DLWVP 335
Cdd:cd03319 297 AAHLAAAKAdfvDLDGP 313
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
87-304 |
2.15e-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: 87.01 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 87 SAIDMALWDIKAKAANMPLYQLLGGAsREGVMVyCHTTG-RTIDEVLEDYAKHQQMGFKAIRVQCGVPGMQTTyglakgk 165
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGGY-RDRVRV-AHMLGlGEPAEVAEEARRALEAGFRTFKLKVGRDPARDV------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 166 glayepatkglwpeeqlwssekyldftpKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAEN 245
Cdd:cd03315 117 ----------------------------AVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1618847557 246 QECFRLIRQHTVTPIAVGEvfnSIW---DCKQLIEEQLIDYIRTTITHAGGITGMRRIADFA 304
Cdd:cd03315 169 LEGRAALARATDTPIMADE---SAFtphDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVA 227
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
41-378 |
1.22e-18 |
|
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: 86.31 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 41 LSVASYLKDHLCPQLIGRDASRIEDIWQffykgAYWR------RGPVTMSAISAIDMALWDIKAKAANMPLYQLLgGASR 114
Cdd:cd03328 50 AAAAALVDGLLAPVVEGRDALDPPAAWE-----AMQRavrnagRPGVAAMAISAVDIALWDLKARLLGLPLARLL-GRAH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 115 EGVMVYcHTTGRTI--DEVLEDyakhQQMGFKAIRVqcgvpgmqttyglakgkglayePATK---GLWPEEQlwssekyl 189
Cdd:cd03328 124 DSVPVY-GSGGFTSydDDRLRE----QLSGWVAQGI----------------------PRVKmkiGRDPRRD-------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 190 dftPKLFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQECFRLIRQHTVT--PIAVGEVFN 267
Cdd:cd03328 169 ---PDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVRERGPAgmDIAAGEYAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 268 SIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQVrtgshgpsDLSPVChAAALHFDLW--VPNFGVQEYMG- 344
Cdd:cd03328 246 TLAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHV--------DLSAHC-APALHAHVAcaVPRLRHLEWFHd 316
|
330 340 350
....*....|....*....|....*....|....*..
gi 1618847557 345 --YSEQMLevFPHSWRFEEGYMHPGD-EPGLGISFDE 378
Cdd:cd03328 317 hvRIERML--FDGAPDPSGGALRPDLsRPGLGLELRA 351
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
15-309 |
2.42e-15 |
|
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: 76.50 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 15 RNFVTLKITTESGLCGLGDATL------NGRELSVASY-LKDHLCPQLIGRDASRIEDIWQFF--YKGAywrrgpvTMsA 85
Cdd:cd03317 24 REFLIVELTDEEGITGYGEVVAfegpfyTEETNATAWHiLKDYLLPLLLGREFSHPEEVSERLapIKGN-------NM-A 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 86 ISAIDMALWDIKAKAANMPLYQLLGGASRE---GVMVychttGR--TIDEVLEDYAKHQQMGFKAIRVQcgvpgmqttyg 160
Cdd:cd03317 96 KAGLEMAVWDLYAKAQGQSLAQYLGGTRDSipvGVSI-----GIqdDVEQLLKQIERYLEEGYKRIKLK----------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 161 LAKGKGLAyepatkglwpeeqlwssekyldftpkLFEAVRNKFGfNEHLLHDMHHRLTPIEAARFgKSIEDYRLFWMEDP 240
Cdd:cd03317 160 IKPGWDVE--------------------------PLKAVRERFP-DIPLMADANSAYTLADIPLL-KRLDEYGLLMIEQP 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1618847557 241 TPAENqecfrlIRQHTV------TPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGITGMRRIADFASLYQV 309
Cdd:cd03317 212 LAADD------LIDHAElqkllkTPICLDESIQSAEDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGI 280
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
129-258 |
1.28e-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: 69.23 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 129 DEVLEDYAKH-QQMGFKAIRVQCGVPGmqttyglakgkglayepatkglwpeeqlwssekylDFTPKLFEAVRNKFGFNE 207
Cdd:smart00922 2 EELAEAARRAvAEAGFRAVKVKVGGGP-----------------------------------LEDLARVAAVREAVGPDA 46
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1618847557 208 HLLHDMHHRLTPIEAARFGKSIEDYRLFWMEDPTPAENQECFRLIRQHTVT 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 |
1.35e-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: 62.34 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 15 RNFVTlkITTESGLCGLGDATlnGRELSVASYLKDhlCPQLIGRDAS-----RIEDIWQFFYKGAYWRRGPVTMS----- 84
Cdd:cd03323 30 RNIVE--LTDDNGNTGVGESP--GGAEALEALLEA--ARSLVGGDVFgaylaVLESVRVAFADRDAGGRGLQTFDlrttv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 85 -AISAIDMALWDIKAKAANMPLYQLLGGASREGV--MVYC------HTTG-------------RTIDEVLEDY-AKHQQM 141
Cdd:cd03323 104 hVVTAFEVALLDLLGQALGVPVADLLGGGQRDSVpfLAYLfykgdrHKTDlpypwfrdrwgeaLTPEGVVRLArAAIDRY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 142 GFKAIRVQCGVpgmqttyglakgkglayepatkgLWPEEQLwssekyldftpklfEAVRN-KFGFNEHLLhdmhhRLTP- 219
Cdd:cd03323 184 GFKSFKLKGGV-----------------------LPGEEEI--------------EAVKAlAEAFPGARL-----RLDPn 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 220 -----IEAARFGKSIEDyRLFWMEDPTPAenQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTITHAGGI 294
Cdd:cd03323 222 gawslETAIRLAKELEG-VLAYLEDPCGG--REGMAEFRRATGLPLATNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 295 TGMRRIADFASLYQVRTGSHGPS----DLSPVCHAAALhfdlwVPNFGV---QEYMGYSEQMLEVFPhsWRFEEGYMHPG 367
Cdd:cd03323 299 RGSVRVAQVCETWGLGWGMHSNNhlgiSLAMMTHVAAA-----APGLITacdTHWIWQDGQVITGEP--LRIKDGKVAVP 371
|
410
....*....|....*..
gi 1618847557 368 DEPGLGISFDEKLAAKY 384
Cdd:cd03323 372 DKPGLGVELDRDKLAKA 388
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
17-294 |
1.42e-09 |
|
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: 59.28 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 17 FVTLKiTTESGLCGLGDATLNGR--ELSVASYlkDHLCPQLIGRDASRIEDIWqffykGAYWRR----------GP---V 81
Cdd:cd03324 35 YVVLR-TDAAGLKGHGLTFTIGRgnEIVCAAI--EALAHLVVGRDLESIVADM-----GKFWRRltsdsqlrwiGPekgV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 82 TMSAISAIDMALWDIKAKAANMPLYQLLGGASREgVMVYCH-----TTGRTIDEVLEDYAKHQQmgFKAIRVQC----GV 152
Cdd:cd03324 107 IHLATAAVVNAVWDLWAKAEGKPLWKLLVDMTPE-ELVSCIdfryiTDALTPEEALEILRRGQP--GKAAREADllaeGY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 153 PGMQTT-----YGLAKGKGLAYEPATKGlwpeeqlWSSEKY-----LDFTPKLFEAVRNKFGFNEHLLHDMHHRLTPIEA 222
Cdd:cd03324 184 PAYTTSagwlgYSDEKLRRLCKEALAQG-------FTHFKLkvgadLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 223 ARFGKSIEDYRLFWMEDPTPAENQECFRLIRQHTVT---PIAVGE------VFnsiwdcKQLIEEQLIDYIRTTITHAGG 293
Cdd:cd03324 257 IEWVKQLAEFKPWWIEEPTSPDDILGHAAIRKALAPlpiGVATGEhcqnrvVF------KQLLQAGAIDVVQIDSCRLGG 330
|
.
gi 1618847557 294 I 294
Cdd:cd03324 331 V 331
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
85-382 |
4.48e-09 |
|
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: 57.79 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 85 AISAIDMALWDIKAKAANMPLYQLLG-----GASREGVMVYC----HTTGRTIDEVLEDYAKHQQMGFKAIRVQCGvpgm 155
Cdd:cd03326 109 AVGALDMAVWDAVAKIAGLPLYRLLArrygrGQADPRVPVYAaggyYYPGDDLGRLRDEMRRYLDRGYTVVKIKIG---- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 156 qttyglakGKGLAYEPATkglwpeeqlwssekyldftpklFEAVRNKFGFNEHLLHDMHHRLTPIEAARFGKSIEDYRLF 235
Cdd:cd03326 185 --------GAPLDEDLRR----------------------IEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 236 WMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLI----DYIRTTITHAGGITGMRRIadfasLYQVRT 311
Cdd:cd03326 235 WYEEPGDPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRM-----LDVLEA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618847557 312 GSHGPSDLSPvcH---------AAALHFDlwvpnfGVQEYMGYSeQMLEVFPHSWRFEEGYMHPGDEPGLGISFDEKLAA 382
Cdd:cd03326 310 HGWSRRRFFP--HgghlmslhiAAGLGLG------GNESYPDVF-QPFGGFADGCKVENGYVRLPDAPGIGFEGKAELAA 380
|
|
| |
