|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
2-386 |
0e+00 |
|
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: 729.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 2 KIVEIREHTVPISSPIRNAYIDFSKMTLSLVAVITDVMRDGKPVVGYGFNSNGRYGQGTLMRERFIPRILEADPASLVND 81
Cdd:cd03326 1 RIVAIREKAIPLSSPIANAYVDFSGLTTSLVAVVTDVVRDGRPVVGYGFDSIGRYAQGGLLRERFIPRLLAAAPDSLLDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 82 AGDNLDPHKIWATMFTNEKPGGHGERSVAIGTIDMAVWDAAAKIEGKPLFQLLAERYGQGQPNRSIFVYAAGGYYYPGQN 161
Cdd:cd03326 81 AGGNLDPARAWAAMMRNEKPGGHGERAVAVGALDMAVWDAVAKIAGLPLYRLLARRYGRGQADPRVPVYAAGGYYYPGDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 162 HDKLKDEMRSYIDRGYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAG 241
Cdd:cd03326 161 LGRLRDEMRRYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 242 DPLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYGGMRADRDWLQFDCALSYGLVEYLRTLDMLHQHGWSPSRCIPH 321
Cdd:cd03326 241 DPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGMRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWSRRRFFPH 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1423780213 322 GGHQMSLNIAAGLGLGGNESYPDLFQPYGGFPDGVKVDNGYITLPELPGIGFEGKADLFAEMRKL 386
Cdd:cd03326 321 GGHLMSLHIAAGLGLGGNESYPDVFQPFGGFADGCKVENGYVRLPDAPGIGFEGKAELAAEMREL 385
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-382 |
6.02e-65 |
|
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: 210.83 E-value: 6.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 1 MKI--VEIREHTVPISSPIRNAYIDFSKMTLSLVAVITDvmrDGkpVVGYGFNSNGRYGQGTLM---RERFIPRILEADP 75
Cdd:COG4948 1 MKItdIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETD---DG--ITGWGEAVPGGTGAEAVAaalEEALAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 76 aslvndagdnLDPHKIWATMFTNEKPGGHgersvAIGTIDMAVWDAAAKIEGKPLFQLLAerygqGQPNRSIFVYAAGGY 155
Cdd:COG4948 76 ----------LDIEALWQRLYRALPGNPA-----AKAAVDMALWDLLGKALGVPVYQLLG-----GKVRDRVPVYATLGI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 156 YYPgqnhDKLKDEMRSYIDRGYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLF 235
Cdd:COG4948 136 DTP----EEMAEEAREAVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 236 WYEEAGDPLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDMLHQHGwsp 315
Cdd:COG4948 212 WIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAV----DIVNIKLSKVGGLTEALRIAALAEAHG--- 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423780213 316 srcIPHGGHQM---SLNIAAGLGLG---GNESYPDLFQPYGG----FPDGVKVDNGYITLPELPGIGFEGKADLFAE 382
Cdd:COG4948 285 ---VPVMPHCMlesGIGLAAALHLAaalPNFDIVELDGPLLLaddlVEDPLRIEDGYLTVPDGPGLGVELDEDALAR 358
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
164-374 |
1.41e-47 |
|
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: 161.19 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 164 KLKDEMRSYIDR-GYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGD 242
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 243 PLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDMLHQHGWspsRCIPHG 322
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAV----DIVQPDVTRVGGITEALKIAALAEAFGV---PVAPHS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 323 GHqMSLNIAAGLGLG---GNESYPDLF-----QPYGGFPDGVKVDNGYITLPELPGIGFE 374
Cdd:pfam13378 154 GG-GPIGLAASLHLAaavPNLLIQEYFldpllLEDDLLTEPLEVEDGRVAVPDGPGLGVE 212
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
163-253 |
7.31e-20 |
|
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: 83.48 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 163 DKLKDEMRSYI-DRGYTVVKKKIGGAsLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAG 241
Cdd:smart00922 2 EELAEAARRAVaEAGFRAVKVKVGGG-PLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
90
....*....|..
gi 1423780213 242 DPLDYELQATLR 253
Cdd:smart00922 81 PPDDLEGLAELR 92
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
110-374 |
1.09e-14 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 74.95 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 110 AIGTIDMAVWDAAAKIEGKPLFQLL--AERYGqgqpnrsIFVYAAGGyyypGQNHDKLKDEMRSYIDRGYTVVKKKIG-- 185
Cdd:PRK15072 85 AIAAVDMALWDIKAKAAGMPLYQLLggASREG-------VMVYGHAN----GRDIDELLDDVARHLELGYKAIRVQCGvp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 186 ---------------------GASLDED-------LRRIDSIL----SVLGDGQKLAVDANGRFDLDTAIRYAKALSQYD 233
Cdd:PRK15072 154 glkttygvskgkglayepatkGLLPEEElwstekyLRFVPKLFeavrNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 234 LFWYEeagDPLDYELQATL---RNYYDKPMATGENLFSMQDARNLIRyggmraDRdwlqfdcalsygLVEYLRTlDMLHQ 310
Cdd:PRK15072 234 LFWLE---DPTPAENQEAFrliRQHTTTPLAVGEVFNSIWDCKQLIE------EQ------------LIDYIRT-TVTHA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 311 HGWSPSRCI------------PHGGHQMS-LNIAAGLGLGgnESYPDL-FQPYGG--------FPDGVKVDNGYITLPEL 368
Cdd:PRK15072 292 GGITHLRRIadfaalyqvrtgSHGPTDLSpVCMAAALHFD--LWVPNFgIQEYMGhseetlevFPHSYTFEDGYLHPGDA 369
|
....*.
gi 1423780213 369 PGIGFE 374
Cdd:PRK15072 370 PGLGVD 375
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
174-229 |
9.70e-05 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 44.03 E-value: 9.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1423780213 174 DRGYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKAL 229
Cdd:TIGR01927 122 AEGFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKAL 177
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
2-386 |
0e+00 |
|
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: 729.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 2 KIVEIREHTVPISSPIRNAYIDFSKMTLSLVAVITDVMRDGKPVVGYGFNSNGRYGQGTLMRERFIPRILEADPASLVND 81
Cdd:cd03326 1 RIVAIREKAIPLSSPIANAYVDFSGLTTSLVAVVTDVVRDGRPVVGYGFDSIGRYAQGGLLRERFIPRLLAAAPDSLLDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 82 AGDNLDPHKIWATMFTNEKPGGHGERSVAIGTIDMAVWDAAAKIEGKPLFQLLAERYGQGQPNRSIFVYAAGGYYYPGQN 161
Cdd:cd03326 81 AGGNLDPARAWAAMMRNEKPGGHGERAVAVGALDMAVWDAVAKIAGLPLYRLLARRYGRGQADPRVPVYAAGGYYYPGDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 162 HDKLKDEMRSYIDRGYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAG 241
Cdd:cd03326 161 LGRLRDEMRRYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 242 DPLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYGGMRADRDWLQFDCALSYGLVEYLRTLDMLHQHGWSPSRCIPH 321
Cdd:cd03326 241 DPLDYALQAELADHYDGPIATGENLFSLQDARNLLRYGGMRPDRDVLQFDPGLSYGLPEYLRMLDVLEAHGWSRRRFFPH 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1423780213 322 GGHQMSLNIAAGLGLGGNESYPDLFQPYGGFPDGVKVDNGYITLPELPGIGFEGKADLFAEMRKL 386
Cdd:cd03326 321 GGHLMSLHIAAGLGLGGNESYPDVFQPFGGFADGCKVENGYVRLPDAPGIGFEGKAELAAEMREL 385
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-374 |
6.38e-86 |
|
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: 264.86 E-value: 6.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 2 KIVEIRehTVPISSPIRNAYIDFSKMTLSLVAVITDvmrDGkpVVGYGFNSNGRYGQGT--LMRERFIPRILEADPaslv 79
Cdd:cd03316 1 KITDVE--TFVLRVPLPEPGGAVTWRNLVLVRVTTD---DG--ITGWGEAYPGGRPSAVaaAIEDLLAPLLIGRDP---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 80 ndagdnLDPHKIWATMFTNEKPGG-HGERSVAIGTIDMAVWDAAAKIEGKPLFQLLAerygqGQPNRSIFVYAAGGYYYP 158
Cdd:cd03316 70 ------LDIERLWEKLYRRLFWRGrGGVAMAAISAVDIALWDIKGKAAGVPVYKLLG-----GKVRDRVRVYASGGGYDD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 159 GqnHDKLKDEMRSYIDRGYTVVKKKIGGAS-----LDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYD 233
Cdd:cd03316 139 S--PEELAEEAKRAVAEGFTAVKLKVGGPDsggedLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 234 LFWYEEAGDPLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDMLHQHGw 313
Cdd:cd03316 217 LFWFEEPVPPDDLEGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAV----DIIQPDVTKVGGITEAKKIAALAEAHG- 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423780213 314 spSRCIPHG-----GHQMSLNIAAGLGLGG-NESYPDLFQPYGG-FPDGVKVDNGYITLPELPGIGFE 374
Cdd:cd03316 292 --VRVAPHGaggpiGLAASLHLAAALPNFGiLEYHLDDLPLREDlFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-382 |
6.02e-65 |
|
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: 210.83 E-value: 6.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 1 MKI--VEIREHTVPISSPIRNAYIDFSKMTLSLVAVITDvmrDGkpVVGYGFNSNGRYGQGTLM---RERFIPRILEADP 75
Cdd:COG4948 1 MKItdIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETD---DG--ITGWGEAVPGGTGAEAVAaalEEALAPLLIGRDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 76 aslvndagdnLDPHKIWATMFTNEKPGGHgersvAIGTIDMAVWDAAAKIEGKPLFQLLAerygqGQPNRSIFVYAAGGY 155
Cdd:COG4948 76 ----------LDIEALWQRLYRALPGNPA-----AKAAVDMALWDLLGKALGVPVYQLLG-----GKVRDRVPVYATLGI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 156 YYPgqnhDKLKDEMRSYIDRGYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLF 235
Cdd:COG4948 136 DTP----EEMAEEAREAVARGFRALKLKVGGPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 236 WYEEAGDPLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDMLHQHGwsp 315
Cdd:COG4948 212 WIEQPLPAEDLEGLAELRRATPVPIAADESLTSRADFRRLIEAGAV----DIVNIKLSKVGGLTEALRIAALAEAHG--- 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423780213 316 srcIPHGGHQM---SLNIAAGLGLG---GNESYPDLFQPYGG----FPDGVKVDNGYITLPELPGIGFEGKADLFAE 382
Cdd:COG4948 285 ---VPVMPHCMlesGIGLAAALHLAaalPNFDIVELDGPLLLaddlVEDPLRIEDGYLTVPDGPGLGVELDEDALAR 358
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
164-374 |
1.41e-47 |
|
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: 161.19 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 164 KLKDEMRSYIDR-GYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGD 242
Cdd:pfam13378 1 ELAAEARRAVEArGFRAFKLKVGGPDPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 243 PLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDMLHQHGWspsRCIPHG 322
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAV----DIVQPDVTRVGGITEALKIAALAEAFGV---PVAPHS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 323 GHqMSLNIAAGLGLG---GNESYPDLF-----QPYGGFPDGVKVDNGYITLPELPGIGFE 374
Cdd:pfam13378 154 GG-GPIGLAASLHLAaavPNLLIQEYFldpllLEDDLLTEPLEVEDGRVAVPDGPGLGVE 212
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
103-335 |
4.93e-37 |
|
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: 133.99 E-value: 4.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 103 GHGErsvAIGTIDMAVWDAAAKIEGKPLFQLLAerygqGQPNRSIFVYAAggyyypgqnhdklkdemrsyidrgytvvkk 182
Cdd:cd00308 39 GWGE---VISGIDMALWDLAAKALGVPLAELLG-----GGSRDRVPAYGS------------------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 183 kiggasldedLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGDPLDYELQATLRNYYDKPMAT 262
Cdd:cd00308 81 ----------IERVRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1423780213 263 GENLFSMQDARNLIRYGGmradRDWLQFDCALSYGLVEYLRTLDMLHQHGWspsRCIPHG------GHQMSLNIAAGLG 335
Cdd:cd00308 151 DESVTTVDDALEALELGA----VDILQIKPTRVGGLTESRRAADLAEAFGI---RVMVHGtlessiGTAAALHLAAALP 222
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
84-374 |
4.84e-28 |
|
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: 112.43 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 84 DNLDPHKIWATMFTNEKP-GGHGERSVAIGTIDMAVWDAAAKIEGKPLFQLLAerygqGQPNRSIFVYAAGGYYypgQNH 162
Cdd:cd03327 50 DPSDIEKLWDQMYRATLAyGRKGIAMAAISAVDLALWDLLGKIRGEPVYKLLG-----GRTRDKIPAYASGLYP---TDL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 163 DKLKDEMRSYIDRGYTVVKKKI------GGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFW 236
Cdd:cd03327 122 DELPDEAKEYLKEGYRGMKMRFgygpsdGHAGLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 237 YEEAGDPLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDMLHQHGwspS 316
Cdd:cd03327 202 IEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYGFKRLLEGRAV----DILQPDVNWVGGITELKKIAALAEAYG---V 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423780213 317 RCIPHGGHQMSLN---------IAAGLGLGGNESYPDLFqpYGGFPDGVKVDNGYITLPELPGIGFE 374
Cdd:cd03327 275 PVVPHASQIYNYHfimsepnspFAEYLPNSPDEVGNPLF--YYIFLNEPVPVNGYFDLSDKPGFGLE 339
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
110-376 |
1.01e-23 |
|
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: 101.65 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 110 AIGTIDMAVWDAAAKIEGKPLFQLLAE------------RY--------------GQGQPNRSIFVYAAGGYYYP----- 158
Cdd:cd03324 110 ATAAVVNAVWDLWAKAEGKPLWKLLVDmtpeelvscidfRYitdaltpeealeilRRGQPGKAAREADLLAEGYPaytts 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 159 ----GQNHDKLKDEMRSYIDRGYTVVKKKIGgASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDL 234
Cdd:cd03324 190 agwlGYSDEKLRRLCKEALAQGFTHFKLKVG-ADLEDDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKP 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 235 FWYEEAGDPLDYELQATLRN---YYDKPMATGEnlfsMQDARNLIRYGGMRADRDWLQFDCALSYGLVEYLRTLDMLHQH 311
Cdd:cd03324 269 WWIEEPTSPDDILGHAAIRKalaPLPIGVATGE----HCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 312 GwspSRCIPHGGhqmslniaaGLGL----------------GGNES----YPDLFQPYggFPDGVKVDNGYITLPELPGI 371
Cdd:cd03324 345 G---VPVCPHAG---------GVGLcelvqhlsmidyicvsGSKEGrvieYVDHLHEH--FVYPVVIQNGAYMPPTDPGY 410
|
....*
gi 1423780213 372 GFEGK 376
Cdd:cd03324 411 SIEMK 415
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
4-303 |
8.39e-22 |
|
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: 95.17 E-value: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 4 VEIREHTVPISSPIRNAYIDFSKMTLSLVAVitdvmrDGKPVVGYGFNsngrYGQGTlmrerfIPRILEADPASLVNDAg 83
Cdd:cd03328 5 VEARAYTVPTDAPEADGTLAWDATTLVLVEV------RAGGRTGLGYT----YADAA------AAALVDGLLAPVVEGR- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 84 DNLDPHKIWATMFTN-EKPGGHGERSVAIGTIDMAVWDAAAKIEGKPLFQLLaerygqGQPNRSIFVYAAGGYY-YPgqn 161
Cdd:cd03328 68 DALDPPAAWEAMQRAvRNAGRPGVAAMAISAVDIALWDLKARLLGLPLARLL------GRAHDSVPVYGSGGFTsYD--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 162 HDKLKDEMRSYIDRGYTVVKKKIGgASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAG 241
Cdd:cd03328 139 DDRLREQLSGWVAQGIPRVKMKIG-RDPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPV 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1423780213 242 DPLDYELQATLRNYYDKPM--ATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLR 303
Cdd:cd03328 218 SSDDLAGLRLVRERGPAGMdiAAGEYAYTLAYFRRLLEAHAV----DVLQADVTRCGGVTGFLQ 277
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
110-374 |
1.00e-21 |
|
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: 95.09 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 110 AIGTIDMAVWDAAAKIEGKPLFQLLAerygqGQPNRSIFVYAAGGyyypGQNHDKLKDEMRSYIDRGYTVVKKKI----- 184
Cdd:cd03325 81 AISGIDQALWDIKGKVLGVPVHQLLG-----GQVRDRVRVYSWIG----GDRPSDVAEAARARREAGFTAVKMNAteelq 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 185 ---GGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGDPLDYELQATLRNYYDKPMA 261
Cdd:cd03325 152 widTSKKVDAAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 262 TGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDM----------------------LHQHGWSPSRCI 319
Cdd:cd03325 232 TGERLFSRWDFKELLEDGAV----DIIQPDISHAGGITELKKIAAMaeaydvalaphcplgpialaasLHVDASTPNFLI 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1423780213 320 phggHQMSLNIAAGLglgGNESYPDLFQpyggfPDGVKVDNGYITLPELPGIGFE 374
Cdd:cd03325 308 ----QEQSLGIHYNE---GDDLLDYLVD-----PEVFDMENGYVKLPTGPGLGIE 350
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
102-374 |
1.33e-21 |
|
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: 94.86 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 102 GGHGERSVAIGTIDMAVWDAAAKIEGKPLFQLLAerygqGQPnRSIFVYAAGGYyypgqnhDKLK---DEMRSYIDRGYT 178
Cdd:cd03321 92 GYTGLVRMAAAGIDMAAWDALAKVHGLPLAKLLG-----GNP-RPVQAYDSHGL-------DGAKlatERAVTAAEEGFH 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 179 VVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGDPLDYELQATLRNYYDK 258
Cdd:cd03321 159 AVKTKIGYPTADEDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 259 PMATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDMLHQHGwspsrcIPHGGH---QMSLNIAAGLG 335
Cdd:cd03321 239 PVQMGENWLGPEEMFKALSAGAC----DLVMPDLMKIGGVTGWLRASALAEQAG------IPMSSHlfqEISAHLLAVTP 308
|
250 260 270
....*....|....*....|....*....|....*....
gi 1423780213 336 LGGNESYPDLFQPYGGFPdgVKVDNGYITLPELPGIGFE 374
Cdd:cd03321 309 TAHWLEYVDWAGAILEPP--LKFEDGNAVIPDEPGNGII 345
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
163-253 |
7.31e-20 |
|
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: 83.48 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 163 DKLKDEMRSYI-DRGYTVVKKKIGGAsLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAG 241
Cdd:smart00922 2 EELAEAARRAVaEAGFRAVKVKVGGG-PLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPV 80
|
90
....*....|..
gi 1423780213 242 DPLDYELQATLR 253
Cdd:smart00922 81 PPDDLEGLAELR 92
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
112-312 |
4.09e-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: 86.24 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 112 GTIDMAVWDAAAKIEGKPLFQLLaerygqGQPNRSIFVyaagGYYYPGQNHDKLKDEMRSYIDRGYTVVKKKIGGaSLDE 191
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLL------GGYRDRVRV----AHMLGLGEPAEVAEEARRALEAGFRTFKLKVGR-DPAR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 192 DLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGDPLDYELQATLRNYYDKPMATGENLFSMQD 271
Cdd:cd03315 115 DVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHD 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1423780213 272 ARNLIRYGGMRAdrdwLQFDCALSYGLVEYLRTLDMLHQHG 312
Cdd:cd03315 195 AFRELALGAADA----VNIKTAKTGGLTKAQRVLAVAEALG 231
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
110-374 |
3.67e-18 |
|
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: 84.80 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 110 AIGTIDMAVWDAAAKIEGKPLFQLLAerygqGQPNRSIFVYAaggyYYPGQNHDKLKDEMRSYIDRGYTVVKKKIggasl 189
Cdd:cd03322 84 AIAAVDMALWDIKGKAAGMPLYQLLG-----GKSRDGIMVYS----HASGRDIPELLEAVERHLAQGYRAIRVQL----- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 190 dedLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGDPLDYELQATLRNYYDKPMATGENLFSM 269
Cdd:cd03322 150 ---PKLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSI 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 270 QDARNLIryggmradrdwlqfdcalSYGLVEYLRTlDMLHQHGWSPSRCIP------------HGGHQMSlNIAAGLGLG 337
Cdd:cd03322 227 WDWQNLI------------------QERLIDYIRT-TVSHAGGITPARKIAdlaslygvrtgwHGPTDLS-PVGMAAALH 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1423780213 338 GNESYPDL----FQPYGG-----FPDGVKVDNGYITLPELPGIGFE 374
Cdd:cd03322 287 LDLWVPNFgiqeYMRHAEetlevFPHSVRFEDGYLHPGEEPGLGVE 332
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
2-279 |
8.01e-15 |
|
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: 75.05 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 2 KIVEIREHTV--PISSPIRNAYIDFSKMTLSLVAVITDvmrDGkpVVGYG-FNSNGRYGQGTLMRERfIPRILEA--DPA 76
Cdd:cd03318 1 KIEAIETTIVdlPTRRPHQFAGTTMHTQSLVLVRLTTS---DG--VVGIGeATTPGGPAWGGESPET-IKAIIDRylAPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 77 SLVNDAGDnldPHKIWATMftnekpgghgERSV-----AIGTIDMAVWDAAAKIEGKPLFQLLAERYGQGQPNRsiFVYA 151
Cdd:cd03318 75 LIGRDATN---IGAAMALL----------DRAVagnlfAKAAIEMALLDAQGRRLGLPVSELLGGRVRDSLPVA--WTLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 152 AGGYyypgqnhDKLKDEMRSYIDRG-YTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALS 230
Cdd:cd03318 140 SGDT-------ERDIAEAEEMLEAGrHRRFKLKMGARPPADDLAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLE 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1423780213 231 QYDLFWYEEAGDPLDYELQATLRNYYDKPMATGENLFSMQDARNLIRYG 279
Cdd:cd03318 213 AAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGPADAFELARRG 261
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
110-374 |
1.09e-14 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 74.95 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 110 AIGTIDMAVWDAAAKIEGKPLFQLL--AERYGqgqpnrsIFVYAAGGyyypGQNHDKLKDEMRSYIDRGYTVVKKKIG-- 185
Cdd:PRK15072 85 AIAAVDMALWDIKAKAAGMPLYQLLggASREG-------VMVYGHAN----GRDIDELLDDVARHLELGYKAIRVQCGvp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 186 ---------------------GASLDED-------LRRIDSIL----SVLGDGQKLAVDANGRFDLDTAIRYAKALSQYD 233
Cdd:PRK15072 154 glkttygvskgkglayepatkGLLPEEElwstekyLRFVPKLFeavrNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 234 LFWYEeagDPLDYELQATL---RNYYDKPMATGENLFSMQDARNLIRyggmraDRdwlqfdcalsygLVEYLRTlDMLHQ 310
Cdd:PRK15072 234 LFWLE---DPTPAENQEAFrliRQHTTTPLAVGEVFNSIWDCKQLIE------EQ------------LIDYIRT-TVTHA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 311 HGWSPSRCI------------PHGGHQMS-LNIAAGLGLGgnESYPDL-FQPYGG--------FPDGVKVDNGYITLPEL 368
Cdd:PRK15072 292 GGITHLRRIadfaalyqvrtgSHGPTDLSpVCMAAALHFD--LWVPNFgIQEYMGhseetlevFPHSYTFEDGYLHPGDA 369
|
....*.
gi 1423780213 369 PGIGFE 374
Cdd:PRK15072 370 PGLGVD 375
|
|
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
110-374 |
1.59e-14 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 74.16 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 110 AIGTIDMAVWDAAAKIEGKPLFQLLaerygqGQPNR-SIFVYAAGGyyypGQNHDKLKDEMRSYIDRGYTVVkkKIGGas 188
Cdd:PRK14017 82 AIAGIDQALWDIKGKALGVPVHELL------GGLVRdRIRVYSWIG----GDRPADVAEAARARVERGFTAV--KMNG-- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 189 lDEDLRRIDS-------------ILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGDPLDYELQATLRNY 255
Cdd:PRK14017 148 -TEELQYIDSprkvdaavarvaaVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 256 YDKPMATGENLFSMQDARNLIRYGGMradrDWLQFDCALSYGLVEYLRTLDM-------LHQHgwspsrCiPHGGHQM-- 326
Cdd:PRK14017 227 TSIPIATGERLFSRWDFKRVLEAGGV----DIIQPDLSHAGGITECRKIAAMaeaydvaLAPH------C-PLGPIALaa 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1423780213 327 SLNIAAG----------LGLGGNESYPDLfqPYGGFPDGVKVDNGYITLPELPGIGFE 374
Cdd:PRK14017 296 CLQVDAVspnafiqeqsLGIHYNQGADLL--DYVKNKEVFAYEDGFVAIPTGPGLGIE 351
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
166-289 |
3.33e-14 |
|
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: 71.91 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 166 KDEMRSYIDRGYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGDPLD 245
Cdd:cd03320 87 LGEAKAAYGGGYRTVKLKVGATSFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDD 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1423780213 246 YELQATLRnyYDKPMATGENLFSMQDARNLIR-------------YGGMRADRDWLQ 289
Cdd:cd03320 167 LAELRRLA--AGVPIALDESLRRLDDPLALAAagalgalvlkpalLGGPRALLELAE 221
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
61-374 |
4.11e-13 |
|
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: 69.96 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 61 LMRERFIPRILEADPASlvndagdnldPHKIwATMFTNEKpgGHgerSVAIGTIDMAVWDAAAKIEGKPLFQLLaerygq 140
Cdd:cd03317 62 ILKDYLLPLLLGREFSH----------PEEV-SERLAPIK--GN---NMAKAGLEMAVWDLYAKAQGQSLAQYL------ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 141 GQPNRSIFVYAAGGYyypGQNHDKLKDEMRSYIDRGYTVVKKKIgGASLDEDLrrIDSILSVLGDgQKLAVDANGRFDLD 220
Cdd:cd03317 120 GGTRDSIPVGVSIGI---QDDVEQLLKQIERYLEEGYKRIKLKI-KPGWDVEP--LKAVRERFPD-IPLMADANSAYTLA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 221 TAIRYaKALSQYDLFWYEE---AGDPLDY-ELQATLRnyydKPMATGENLFSMQDARNLIRYGGMRAdrdwLQFDCALSY 296
Cdd:cd03317 193 DIPLL-KRLDEYGLLMIEQplaADDLIDHaELQKLLK----TPICLDESIQSAEDARKAIELGACKI----INIKPGRVG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 297 GLVEYLRTLDMLHQHGwspsrcIP--HGGhqM-------SLNIA-AGLglgGNESYP------------DLFQPyggfpd 354
Cdd:cd03317 264 GLTEALKIHDLCQEHG------IPvwCGG--MlesgigrAHNVAlASL---PNFTYPgdisassryfeeDIITP------ 326
|
330 340
....*....|....*....|
gi 1423780213 355 GVKVDNGYITLPELPGIGFE 374
Cdd:cd03317 327 PFELENGIISVPTGPGIGVT 346
|
|
| 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 ... |
4-284 |
1.22e-12 |
|
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: 67.98 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 4 VEIREHTVPISSPIRNAYIDFSKMTLSLVAVITDvmrdGkpVVGYGFNS-NGR-YGQGTLMRERFIPRILEADpaslvnd 81
Cdd:cd03319 2 ISLRPERLPLKRPFTIARGSRTEAENVIVEIELD----G--ITGYGEAApTPRvTGETVESVLAALKSVRPAL------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 82 AGDNLDPHKIWATMFTNEKPGGhgersVAIGTIDMAVWDAAAKIEGKPLFQLLaeryGQGQPNR-------SIfvyaagg 154
Cdd:cd03319 69 IGGDPRLEKLLEALQELLPGNG-----AARAAVDIALWDLEAKLLGLPLYQLW----GGGAPRPletdytiSI------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 155 yyypgQNHDKLKDEMRSYIDRGYTVVKKKIGGaSLDEDLRRIDSILSVLGDgQKLAVDANGRFDLDTAIRYAKALSQYDL 234
Cdd:cd03319 133 -----DTPEAMAAAAKKAAKRGFPLLKIKLGG-DLEDDIERIRAIREAAPD-ARLRVDANQGWTPEEAVELLRELAELGV 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1423780213 235 FWYEE---AGDPLDYelqATLRNYYDKPMATGENLFSMQDARNLIryGGMRAD 284
Cdd:cd03319 206 ELIEQpvpAGDDDGL---AYLRDKSPLPIMADESCFSAADAARLA--GGGAYD 253
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
46-322 |
1.86e-11 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 65.13 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 46 VGYGFNSNGRygQGTLMRERFIPRILEADPASlvndagdnlDPHKIWATMFTNEKPggHGERSVAIGTI---DMAVWDAA 122
Cdd:PRK15440 70 VGFAVSTAGE--MGAFIVEKHLNRFIEGKCVS---------DIELIWDQMLNATLY--YGRKGLVMNTIscvDLALWDLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 123 AKIEGKPLFQLLaerygqGQPNR-SIFVYAAGGyyypgqnHDKLKDEMrsyidrGYtvvkkkIGG------------ASL 189
Cdd:PRK15440 137 GKVRGLPVYKLL------GGAVRdELQFYATGA-------RPDLAKEM------GF------IGGkmplhhgpadgdAGL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 190 DEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDLFWYEEAGDPLDYELQATLRNYYDKPM--ATGENLF 267
Cdd:PRK15440 192 RKNAAMVADMREKVGDDFWLMLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELKRNAPAGMmvTSGEHEA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1423780213 268 SMQDARNLIRYGgmraDRDWLQFDCALSYGLVEYLRTLDMLHQHGwspSRCIPHG 322
Cdd:PRK15440 272 TLQGFRTLLEMG----CIDIIQPDVGWCGGLTELVKIAALAKARG---QLVVPHG 319
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
4-374 |
5.25e-11 |
|
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: 63.57 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 4 VEIREHTVPISSPIRNAYIDF----SKMTLSLVAVITDvmrDGkpVVGYGFNsnGRYGQGTLMRERFI-PRILEADPasl 78
Cdd:cd03329 5 VEVTVFEYPTQPVSFDGGHHHpgpaGTRKLALLTIETD---EG--AKGHAFG--GRPVTDPALVDRFLkKVLIGQDP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 79 vndagdnLDPHKIWATMFTNEKpgghGERSVAIGTIDMAVWDAAAKIEGKPLFQLLaerygqGQPNRSIFVYA--AGGYY 156
Cdd:cd03329 75 -------LDRERLWQDLWRLQR----GLTDRGLGLVDIALWDLAGKYLGLPVHRLL------GGYREKIPAYAstMVGDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 157 YPGQNH-DKLKDEMRSYIDRGYTVVK-KKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYDL 234
Cdd:cd03329 138 LEGLESpEAYADFAEECKALGYRAIKlHPWGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 235 FWYEeagDPLDYELQAT---LRNYYDKPMATGENLFSMQDAR-NLIRYGGMradrDWLQFDCALSYGLVEYLRTLDMLHQ 310
Cdd:cd03329 218 FWYE---DPLREASISSyrwLAEKLDIPILGTEHSRGALESRaDWVLAGAT----DFLRADVNLVGGITGAMKTAHLAEA 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1423780213 311 HGWspsRCIPHGGHQMSLNIAAGLglgGNESY-----PDLFQPYGGFPDGVKV------DNGYITLPELPGIGFE 374
Cdd:cd03329 291 FGL---DVELHGNGAANLHVIAAI---RNTRYyerglLHPSQKYDVYAGYLSVlddpvdSDGFVHVPKGPGLGVE 359
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
176-264 |
1.11e-06 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 49.97 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 176 GYTVVKKKIG--GASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSqydlfwyeeAGDPLDY------- 246
Cdd:PRK02901 102 GCRTAKVKVAepGQTLADDVARVNAVRDALGPDGRVRVDANGGWSVDEAVAAARALD---------ADGPLEYveqpcat 172
|
90 100
....*....|....*....|
gi 1423780213 247 --ELqATLRNYYDKPMATGE 264
Cdd:PRK02901 173 veEL-AELRRRVGVPIAADE 191
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
174-229 |
9.70e-05 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 44.03 E-value: 9.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1423780213 174 DRGYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKAL 229
Cdd:TIGR01927 122 AEGFRTFKWKVGVGELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKAL 177
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
10-134 |
1.46e-04 |
|
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: 40.92 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 10 TVPISSPIRNAYIDFSKMTLSLVAVITDVMRDGKPVVGYGFnSNGRygqgtlmRERFIPRILEADPASLVNdagdNLDPH 89
Cdd:pfam02746 6 VVDVGWPLRPIQMAFGTVQQQSLVIVRIETSEGVVGIGEAT-SYGG-------RAETIKAILDDHLAPLLI----GRDAA 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1423780213 90 KIWATMFTNEKpGGHGERSvAIGTIDMAVWDAAAKIEGKPLFQLL 134
Cdd:pfam02746 74 NISDLWQLMYR-AALGNMS-AKAAIDMALWDLKAKVLNLPLADLL 116
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
167-271 |
1.52e-04 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 43.46 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423780213 167 DEMRSYIDRGYTVVKKKIGGASLDEDLRRIDSILSVLGDGQKLAVDANGRFDLDTAIRYAKALSQYD---LFWYEEAGDP 243
Cdd:PRK02714 124 QQWQTLWQQGYRTFKWKIGVDPLEQELKIFEQLLERLPAGAKLRLDANGGLSLEEAKRWLQLCDRRLsgkIEFIEQPLPP 203
|
90 100 110
....*....|....*....|....*....|.
gi 1423780213 244 LDYELQATLRNYYDKPMATGE---NLFSMQD 271
Cdd:PRK02714 204 DQFDEMLQLSQDYQTPIALDEsvaNLAQLQQ 234
|
|
| |
