|
Name |
Accession |
Description |
Interval |
E-value |
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
8-325 |
3.51e-59 |
|
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: 191.70 E-value: 3.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 8 RRALRFNFPARTSRGALTEHVAHYLLLSDSgaPERAGWGEAAPLAglspdygpdfeatlegfvhefnrrqlrellpheaa 87
Cdd:cd03320 5 PYSLPLSRPLGTSRGRLTRRRGLLLRLEDL--TGPVGWGEIAPLP----------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 88 dlvgpewpaLRFALETAALDYQHGARRqlydnaFSRGEAGLPINGLVWMGDAAFMREqIEAKLAAGFDCLKLKIGSLDFA 167
Cdd:cd03320 48 ---------LAFGIESALANLEALLVG------FTRPRNRIPVNALLPAGDAAALGE-AKAAYGGGYRTVKLKVGATSFE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 168 TELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAAGQWAALAEvcRHSPVPVALDEELIGL 247
Cdd:cd03320 112 EDLARLRALREALPAD-AKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRR--LAAGVPIALDESLRRL 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518791782 248 TNPagwPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLASTVARPGFPQGLGT 325
Cdd:cd03320 189 DDP---LALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPLPAACGLGT 263
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
10-356 |
8.97e-51 |
|
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: 173.08 E-value: 8.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 10 ALRFNFPARTSRGALTEHVAHYL-LLSDSGAperAGWGEAAPlaglspdyGPDFEATLEGFVHEFNRRQLRELLPHEAAD 88
Cdd:COG4948 12 RLPLKRPFTISRGTRTERDVVLVrVETDDGI---TGWGEAVP--------GGTGAEAVAAALEEALAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 89 LV------GPEWPALRFALETAALD----------YQH--GARRQlydnafsrgeaGLPINGLVWMGDAAFMREQIEAKL 150
Cdd:COG4948 81 LWqrlyraLPGNPAAKAAVDMALWDllgkalgvpvYQLlgGKVRD-----------RVPVYATLGIDTPEEMAEEAREAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 151 AAGFDCLKLKIGSLDFATELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAAGQWAALAEV 230
Cdd:COG4948 150 ARGFRALKLKVGGPDPEEDVERVRAVREAVGPD-ARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 231 CRHSPVPVALDEeliGLTNPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQL 310
Cdd:COG4948 229 RRATPVPIAADE---SLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 518791782 311 ASTVARPGFPQGLGTGQLYHNNLAAPLSIAAGQLHyhpagPWEAPG 356
Cdd:COG4948 306 AAALPNFDIVELDGPLLLADDLVEDPLRIEDGYLT-----VPDGPG 346
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
142-351 |
8.52e-27 |
|
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: 105.72 E-value: 8.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 142 MREQIEAKLAA-GFDCLKLKIGSLDFATELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIA 220
Cdd:pfam13378 2 LAAEARRAVEArGFRAFKLKVGGPDPEEDVERVRAVREAVGPG-VDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 221 AGQWAALAEVCRHSPVPVALDEeliGLTNPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALES 300
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGE---SLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518791782 301 nVGLNAISQLASTVARPGFP-QGLGTGQLYHNNLAAPLSIAAGQLHYhPAGP 351
Cdd:pfam13378 158 -IGLAASLHLAAAVPNLLIQeYFLDPLLLEDDLLTEPLEVEDGRVAV-PDGP 207
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
13-318 |
3.58e-24 |
|
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 low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 101.07 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 13 FNFPARTSRGALTEHVAHYL-LLSDSGAperAGWGEAAplAGLSPDYGPDFEATLEGFVHEFNRRQLRELLPH--EAADL 89
Cdd:TIGR01928 7 FKSPFKTSKGTLNHRDCLIIeLIDDKGN---AGFGEVV--AFQTPWYTHETIATVKHIIEDFFEPNINKEFEHpsEALEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 90 V-GPE-WPALRFALETAALDYQHGARRQLYDNAFSRGEAGLPINGLVWMGDAAFMREQIEAKLAAGFDCLKLKIgSLDFA 167
Cdd:TIGR01928 82 VrSLKgTPMAKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSGLANDEQMLKQIESLKATGYKRIKLKI-TPQIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 168 TELRILadiRAQAGPErLTLRVDANGAFAPAEaLGKLEQLARFDLHSIEQPIAAGQWAALAEVCRHSPVPVALDEELIGL 247
Cdd:TIGR01928 161 HQLVKL---RRLRFPQ-IPLVIDANESYDLQD-FPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518791782 248 TNPAgwpELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLAS--TVARPG 318
Cdd:TIGR01928 236 DDAR---NLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGISRAFNVALASlgGNDYPG 305
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
12-331 |
3.89e-23 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 98.16 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 12 RFNFPARTSRGALTEHVAHYLLLSDSGApeRAGWGEAAPLaglsPDYGPDfeaTLE---GFVhefnrRQLRELLPHEAAD 88
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDETG--KIGWGEIAPL----PWFGSE---TLEealAFC-----QQLPGEITPEQIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 89 LVGPEWPALRFALETAALDYQHGARrqlydnafSRGEAGLPINGLVWMGDAAFmrEQIEAKLAAGFDCLKLKIGSLDFAT 168
Cdd:PRK02714 79 SIPDALPACQFGFESALENESGSRS--------NVTLNPLSYSALLPAGEAAL--QQWQTLWQQGYRTFKWKIGVDPLEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 169 ELRILADIrAQAGPERLTLRVDANGAFAPAEA---LGKLEQLARFDLHSIEQPIAAGQWAALAEVCRHSPVPVALDEELI 245
Cdd:PRK02714 149 ELKIFEQL-LERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 246 GLTNPA-----GWPELlervrpayLVLKPTLLGGLAASQSWaalADAHGIGWWLTSALESNVGLNAISQLASTVARPGFP 320
Cdd:PRK02714 228 NLAQLQqcyqqGWRGI--------FVIKPAIAGSPSRLRQF---CQQHPLDAVFSSVFETAIGRKAALALAAELSRPDRA 296
|
330
....*....|.
gi 518791782 321 QGLGTGQLYHN 331
Cdd:PRK02714 297 LGFGVTHWFSD 307
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
142-236 |
8.58e-18 |
|
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: 77.71 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 142 MREQIEAKLAA-GFDCLKLKIGSLDFAtELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIA 220
Cdd:smart00922 4 LAEAARRAVAEaGFRAVKVKVGGGPLE-DLARVAAVREAVGPD-ADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81
|
90
....*....|....*.
gi 518791782 221 AGQWAALAEVCRHSPV 236
Cdd:smart00922 82 PDDLEGLAELRRATPI 97
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
8-325 |
3.51e-59 |
|
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: 191.70 E-value: 3.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 8 RRALRFNFPARTSRGALTEHVAHYLLLSDSgaPERAGWGEAAPLAglspdygpdfeatlegfvhefnrrqlrellpheaa 87
Cdd:cd03320 5 PYSLPLSRPLGTSRGRLTRRRGLLLRLEDL--TGPVGWGEIAPLP----------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 88 dlvgpewpaLRFALETAALDYQHGARRqlydnaFSRGEAGLPINGLVWMGDAAFMREqIEAKLAAGFDCLKLKIGSLDFA 167
Cdd:cd03320 48 ---------LAFGIESALANLEALLVG------FTRPRNRIPVNALLPAGDAAALGE-AKAAYGGGYRTVKLKVGATSFE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 168 TELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAAGQWAALAEvcRHSPVPVALDEELIGL 247
Cdd:cd03320 112 EDLARLRALREALPAD-AKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRR--LAAGVPIALDESLRRL 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518791782 248 TNPagwPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLASTVARPGFPQGLGT 325
Cdd:cd03320 189 DDP---LALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAALPPLPAACGLGT 263
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
10-356 |
8.97e-51 |
|
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: 173.08 E-value: 8.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 10 ALRFNFPARTSRGALTEHVAHYL-LLSDSGAperAGWGEAAPlaglspdyGPDFEATLEGFVHEFNRRQLRELLPHEAAD 88
Cdd:COG4948 12 RLPLKRPFTISRGTRTERDVVLVrVETDDGI---TGWGEAVP--------GGTGAEAVAAALEEALAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 89 LV------GPEWPALRFALETAALD----------YQH--GARRQlydnafsrgeaGLPINGLVWMGDAAFMREQIEAKL 150
Cdd:COG4948 81 LWqrlyraLPGNPAAKAAVDMALWDllgkalgvpvYQLlgGKVRD-----------RVPVYATLGIDTPEEMAEEAREAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 151 AAGFDCLKLKIGSLDFATELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAAGQWAALAEV 230
Cdd:COG4948 150 ARGFRALKLKVGGPDPEEDVERVRAVREAVGPD-ARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 231 CRHSPVPVALDEeliGLTNPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQL 310
Cdd:COG4948 229 RRATPVPIAADE---SLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHL 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 518791782 311 ASTVARPGFPQGLGTGQLYHNNLAAPLSIAAGQLHyhpagPWEAPG 356
Cdd:COG4948 306 AAALPNFDIVELDGPLLLADDLVEDPLRIEDGYLT-----VPDGPG 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 ... |
2-316 |
3.71e-30 |
|
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: 117.29 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 2 LQLRSARRALRFNFpaRTSRGALTE----HVAhyllLSDSGAperAGWGEAAPLAglsPDYGPDFEATLE---------- 67
Cdd:cd03319 2 ISLRPERLPLKRPF--TIARGSRTEaenvIVE----IELDGI---TGYGEAAPTP---RVTGETVESVLAalksvrpali 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 68 --GFVHEFNRRQLRELLPHEaadlvgpewPALRFALETAALDY--QHgARRQLYDNAFSRGEAGLPINGLVWMGDAAFMR 143
Cdd:cd03319 70 ggDPRLEKLLEALQELLPGN---------GAARAAVDIALWDLeaKL-LGLPLYQLWGGGAPRPLETDYTISIDTPEAMA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 144 EQIEAKLAAGFDCLKLKIGSlDFATELRILADIRAQAGpeRLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAAGQ 223
Cdd:cd03319 140 AAAKKAAKRGFPLLKIKLGG-DLEDDIERIRAIREAAP--DARLRVDANQGWTPEEAVELLRELAELGVELIEQPVPAGD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 224 WAALAEVCRHSPVPVALDEeliGLTNPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVG 303
Cdd:cd03319 217 DDGLAYLRDKSPLPIMADE---SCFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLS 293
|
330
....*....|...
gi 518791782 304 LNAISQLASTVAR 316
Cdd:cd03319 294 IAAAAHLAAAKAD 306
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
142-351 |
8.52e-27 |
|
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: 105.72 E-value: 8.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 142 MREQIEAKLAA-GFDCLKLKIGSLDFATELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIA 220
Cdd:pfam13378 2 LAAEARRAVEArGFRAFKLKVGGPDPEEDVERVRAVREAVGPG-VDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 221 AGQWAALAEVCRHSPVPVALDEeliGLTNPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALES 300
Cdd:pfam13378 81 PDDLEGLARLRRATPVPIATGE---SLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSGGGP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518791782 301 nVGLNAISQLASTVARPGFP-QGLGTGQLYHNNLAAPLSIAAGQLHYhPAGP 351
Cdd:pfam13378 158 -IGLAASLHLAAAVPNLLIQeYFLDPLLLEDDLLTEPLEVEDGRVAV-PDGP 207
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
137-351 |
1.20e-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: 103.17 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 137 GDAAFMREQIEAKLAAGFdclKLKIGSLDFATELRILADIrAQAGPERLTLRVDANGAFAPAEALGKLEQLARFDLHSIE 216
Cdd:cd03318 145 RDIAEAEEMLEAGRHRRF---KLKMGARPPADDLAHVEAI-AKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 217 QPIAAGQWAALAEVCRHSPVPVALDEeliGLTNPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTS 296
Cdd:cd03318 221 QPVPRENLDGLARLRSRNRVPIMADE---SVSGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGT 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518791782 297 ALESNVGLNAISQLASTVarPGFPQG---LGTGQLYHNNLAAPLSIAAGQLHYhPAGP 351
Cdd:cd03318 298 MLESSIGTAASAHLFATL--PSLPFGcelFGPLLLAEDLLEEPLAYRDGELHV-PTGP 352
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
13-318 |
3.58e-24 |
|
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 low GC gram positive bacteria and archaea. Also included in the seed and in the model are enzymes with the com-name of N-acylamino acid racemase (or the more general term, racemase / racemase family), which refers to the enzyme's industrial application as racemases, and not to its biological function as o-succinylbenzoic acid synthetase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 213667 [Multi-domain] Cd Length: 324 Bit Score: 101.07 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 13 FNFPARTSRGALTEHVAHYL-LLSDSGAperAGWGEAAplAGLSPDYGPDFEATLEGFVHEFNRRQLRELLPH--EAADL 89
Cdd:TIGR01928 7 FKSPFKTSKGTLNHRDCLIIeLIDDKGN---AGFGEVV--AFQTPWYTHETIATVKHIIEDFFEPNINKEFEHpsEALEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 90 V-GPE-WPALRFALETAALDYQHGARRQLYDNAFSRGEAGLPINGLVWMGDAAFMREQIEAKLAAGFDCLKLKIgSLDFA 167
Cdd:TIGR01928 82 VrSLKgTPMAKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSGLANDEQMLKQIESLKATGYKRIKLKI-TPQIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 168 TELRILadiRAQAGPErLTLRVDANGAFAPAEaLGKLEQLARFDLHSIEQPIAAGQWAALAEVCRHSPVPVALDEELIGL 247
Cdd:TIGR01928 161 HQLVKL---RRLRFPQ-IPLVIDANESYDLQD-FPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518791782 248 TNPAgwpELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLAS--TVARPG 318
Cdd:TIGR01928 236 DDAR---NLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGISRAFNVALASlgGNDYPG 305
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
8-335 |
1.20e-23 |
|
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: 99.11 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 8 RRALRFNFPARTSRGALTEHVAHYLLLSDSGapeRAGWGEAAPLAGLSPDygpDFEATLEGFvhefnrRQLRELLPHEAA 87
Cdd:TIGR01927 2 RYQMPFDAPVVTRHGLLARREGLIVRLTDEG---RTGWGEIAPLPGFGTE---TLAEALDFC------RALIEEITRGDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 88 DLVGPEWPALRFALETAALDYQHGAR----RQLYDNAFSRGEAGLPINGLVWMgdaafmreqieaklaAGFDCLKLKIGS 163
Cdd:TIGR01927 70 EAIDDQLPSVAFGFESALIELESGDElppaSNYYVALLPAGDPALLLLRSAKA---------------EGFRTFKWKVGV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 164 LDFATELRILaDIRAQAGPERLTLRVDANGAFAPAEALGKLEQLARfDLHS----IEQPIAAGqwAALAEVCRHSPVPVA 239
Cdd:TIGR01927 135 GELAREGMLV-NLLLEALPDKAELRLDANGGLSPDEAQQFLKALDP-NLRGriafLEEPLPDA--DEMSAFSEATGTAIA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 240 LDEELIGLTNPAGwpELLERVRPAYlVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLASTVARPGF 319
Cdd:TIGR01927 211 LDESLWELPQLAD--EYGPGWRGAL-VIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAAKLSPDPA 287
|
330
....*....|....*.
gi 518791782 320 PQGLGTGQLYHNNLAA 335
Cdd:TIGR01927 288 AVGFTTALLRAQDLEA 303
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
12-331 |
3.89e-23 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 98.16 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 12 RFNFPARTSRGALTEHVAHYLLLSDSGApeRAGWGEAAPLaglsPDYGPDfeaTLE---GFVhefnrRQLRELLPHEAAD 88
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDETG--KIGWGEIAPL----PWFGSE---TLEealAFC-----QQLPGEITPEQIF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 89 LVGPEWPALRFALETAALDYQHGARrqlydnafSRGEAGLPINGLVWMGDAAFmrEQIEAKLAAGFDCLKLKIGSLDFAT 168
Cdd:PRK02714 79 SIPDALPACQFGFESALENESGSRS--------NVTLNPLSYSALLPAGEAAL--QQWQTLWQQGYRTFKWKIGVDPLEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 169 ELRILADIrAQAGPERLTLRVDANGAFAPAEA---LGKLEQLARFDLHSIEQPIAAGQWAALAEVCRHSPVPVALDEELI 245
Cdd:PRK02714 149 ELKIFEQL-LERLPAGAKLRLDANGGLSLEEAkrwLQLCDRRLSGKIEFIEQPLPPDQFDEMLQLSQDYQTPIALDESVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 246 GLTNPA-----GWPELlervrpayLVLKPTLLGGLAASQSWaalADAHGIGWWLTSALESNVGLNAISQLASTVARPGFP 320
Cdd:PRK02714 228 NLAQLQqcyqqGWRGI--------FVIKPAIAGSPSRLRQF---CQQHPLDAVFSSVFETAIGRKAALALAAELSRPDRA 296
|
330
....*....|.
gi 518791782 321 QGLGTGQLYHN 331
Cdd:PRK02714 297 LGFGVTHWFSD 307
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
4-319 |
1.74e-21 |
|
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: 93.84 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 4 LRSARRALRFNFpaRTSRGALTEHvaHYLLLSDSGAPERAGWGEAapLAGLSPDYGPDFEATlegfvhefNRRQLRELL- 82
Cdd:cd03317 3 LFHVRMPLKFPF--ETSFGTLNER--EFLIVELTDEEGITGYGEV--VAFEGPFYTEETNAT--------AWHILKDYLl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 83 ----------PHEAADLVGPeWPALRFA---LETAALDYQhgARRQ---LYDNAF-SRG--EAGLPInGLvwMGDAAFMR 143
Cdd:cd03317 69 plllgrefshPEEVSERLAP-IKGNNMAkagLEMAVWDLY--AKAQgqsLAQYLGgTRDsiPVGVSI-GI--QDDVEQLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 144 EQIEAKLAAGFDCLKLKIG-SLDFAtelrILADIRaQAGPErLTLRVDANGAFAPAEAlGKLEQLARFDLHSIEQPIAAG 222
Cdd:cd03317 143 KQIERYLEEGYKRIKLKIKpGWDVE----PLKAVR-ERFPD-IPLMADANSAYTLADI-PLLKRLDEYGLLMIEQPLAAD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 223 QWAALAEVCRHSPVPVALDEELIGLtnpagwpellERVRPAY-------LVLKPTLLGGLAASQSWAALADAHGIGWWLT 295
Cdd:cd03317 216 DLIDHAELQKLLKTPICLDESIQSA----------EDARKAIelgackiINIKPGRVGGLTEALKIHDLCQEHGIPVWCG 285
|
330 340
....*....|....*....|....
gi 518791782 296 SALESNVGLNAISQLAStvaRPGF 319
Cdd:cd03317 286 GMLESGIGRAHNVALAS---LPNF 306
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
96-323 |
2.52e-21 |
|
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: 92.02 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 96 ALRFALETAALDYQHGARRQLYDNAFSRGEAGLPINGLVWMGDAAFMREQIEAKLAAGFDCLKLKIGsLDFATELRILAD 175
Cdd:cd03315 43 ATKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVG-RDPARDVAVVAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 176 IRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAAGQWAALAEVCRHSPVPVALDEELIgltNPAGWPE 255
Cdd:cd03315 122 LREAVGDD-AELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAF---TPHDAFR 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518791782 256 LLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLASTVARPGFPQGL 323
Cdd:cd03315 198 ELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALRAVTLPGEL 265
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
142-236 |
8.58e-18 |
|
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: 77.71 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 142 MREQIEAKLAA-GFDCLKLKIGSLDFAtELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIA 220
Cdd:smart00922 4 LAEAARRAVAEaGFRAVKVKVGGGPLE-DLARVAAVREAVGPD-ADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVP 81
|
90
....*....|....*.
gi 518791782 221 AGQWAALAEVCRHSPV 236
Cdd:smart00922 82 PDDLEGLAELRRATPI 97
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
43-345 |
1.85e-16 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 79.24 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 43 AGWGEAAPLaglsPDYGPDfeatlegfvhefnrrqlrellphEAAdlvgpewPALRFALETAALDYQHGARRqlydnafs 122
Cdd:PRK02901 40 AGWGEFSPF----LEYDPA-----------------------EAA-------AWLASAIEAAYGGPPPPVRD-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 123 rgeaGLPINGLVWMGDAAFMREQIEAklAAGFDCLKLKIGS--LDFATELRILADIRAQAGPERlTLRVDANGAFAPAEA 200
Cdd:PRK02901 78 ----RVPVNATVPAVDAAQVPEVLAR--FPGCRTAKVKVAEpgQTLADDVARVNAVRDALGPDG-RVRVDANGGWSVDEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 201 LGKLEQL-ARFDLHSIEQPIAAgqWAALAEVCRHSPVPVALDEELIGLTNPAgwpelleRVRPA----YLVLKPTLLGGL 275
Cdd:PRK02901 151 VAAARALdADGPLEYVEQPCAT--VEELAELRRRVGVPIAADESIRRAEDPL-------RVARAgaadVAVLKVAPLGGV 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 276 AASqswAALADAHGIGWWLTSALESNVGLNAISQLASTVARPGFPQGLGTGQLYHNNLAAPLSIAAGQLH 345
Cdd:PRK02901 222 RAA---LDIAEQIGLPVVVSSALDTSVGIAAGLALAAALPELDHACGLATGGLFEEDVADPLLPVDGFLP 288
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
170-321 |
2.33e-15 |
|
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: 74.29 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 170 LRILADIRAQAGPERLtLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAAGQWAALAEVCRHSPVPVALDEELigltn 249
Cdd:cd00308 81 IERVRAVREAFGPDAR-LAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESV----- 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518791782 250 pAGWPELLERVRPA---YLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLASTVARPGFPQ 321
Cdd:cd00308 155 -TTVDDALEALELGavdILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLAAALPNDRAIE 228
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
40-328 |
2.67e-15 |
|
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441050 [Multi-domain] Cd Length: 325 Bit Score: 75.69 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 40 PERAGWGEAAPLAGLSpdygpdfEATLEGFVHEFnRRQLRELLPHEAADLVgPEWPALRFALETAALDYQHgarrQLYDn 119
Cdd:COG1441 37 GGREGWGEIAPLPGFS-------QETLEQAEQQA-LAWLQRWLAGDLLDEK-SLLPSVAFGLSCALAELEG----ELPE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 120 afsrgEAGLPINGLVWmGDaafmREQIEAKLAA--GFDCLKLKIGSLDFATELRIlADIRAQAGPErLTLRVDANGAFAP 197
Cdd:COG1441 103 -----AANYRAAPLCS-GD----PDELIARLNQmpGEKVAKVKVGLYEAVRDGMV-VNLLLEAIPD-LRLRLDANRSWTL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 198 AEALGKLEQLARFDLHSI---EQPIAAGQwaALAEVCRHSPVPVALDEELigltnpagW-PELLERVRP--AYLVLKPTL 271
Cdd:COG1441 171 DKAVQFAKYVNPEHRSRIaflEEPCKTPE--ESREFARETGIAIAWDESV--------RePDFRVEAEPgvAAIVIKPTL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 518791782 272 LGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLASTVArPGFPQGLGTGQL 328
Cdd:COG1441 241 VGSLQRCRQLIEQAHQLGLQAVISSSIESSLGLTQLARLAAWLT-PDTAPGLDTLDL 296
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
144-318 |
1.48e-13 |
|
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: 70.72 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 144 EQIEAKLAAGFDCLKLKIGSLDFATE-----LRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQP 218
Cdd:cd03316 145 EEAKRAVAEGFTAVKLKVGGPDSGGEdlredLARVRAVREAVGPD-VDLMVDANGRWDLAEAIRLARALEEYDLFWFEEP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 219 IAAGQWAALAEVCRHSPVPVALDEEligLTNPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGIgWWLTSAL 298
Cdd:cd03316 224 VPPDDLEGLARLRQATSVPIAAGEN---LYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGV-RVAPHGA 299
|
170 180
....*....|....*....|
gi 518791782 299 ESNVGLNAISQLASTVARPG 318
Cdd:cd03316 300 GGPIGLAASLHLAAALPNFG 319
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
44-344 |
2.64e-11 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 65.26 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 44 GWGEAAPLAGLSPDYgPDFEATLEGFVHEFNRRQLRELLPHEAADLVGPEW-----------PALRFALETA---ALDYQ 109
Cdd:PLN02980 976 GFGEVAPLEIHEEDL-LDVEEQLRFLLHVIKGAKISFMLPLLKGSFSSWIWselgippssifPSVRCGLEMAilnAIAVR 1054
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 110 HG-------ARRQLYDNAFSRgEAGLPINGLVWMGDAAFMREQIEAKLAA-GFDCLKLKIGS-LDFATELRILADIRAQA 180
Cdd:PLN02980 1055 HGssllnilDPYQKDENGSEQ-SHSVQICALLDSNGSPLEVAYVARKLVEeGFSAIKLKVGRrVSPIQDAAVIQEVRKAV 1133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 181 GPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAAGQwaALAEVCRHSPVPVALDEELIGLT-NPAgwPELLER 259
Cdd:PLN02980 1134 GYQ-IELRADANRNWTYEEAIEFGSLVKSCNLKYIEEPVQDED--DLIKFCEETGLPVALDETIDKFEeCPL--RMLTKY 1208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 260 VRPAY--LVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLASTVAR--------------PGFPQGL 323
Cdd:PLN02980 1209 THPGIvaVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYIQFASYLEMqnakasremnkgtcPSVAHGL 1288
|
330 340
....*....|....*....|..
gi 518791782 324 GTGQ-LYHNNLAAPLSIAAGQL 344
Cdd:PLN02980 1289 GTYRwLKEDVTMNPLGIFRSPY 1310
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
185-311 |
1.10e-09 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 59.08 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 185 LTLRVDANGAFAPAEALGKLEQLARFDLHSIEqpiaagqwaALAEVCRH----------SPVPVALDEELigltNPAGW- 253
Cdd:PRK05105 158 LKLRLDANRGWTLEKAQQFAKYVPPDYRHRIA---------FLEEPCKTpddsrafaraTGIAIAWDESL----REPDFq 224
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 518791782 254 PELLERVRPayLVLKPTLLGGLAASQSWAALADAHGIGWWLTSALESNVGLNAISQLA 311
Cdd:PRK05105 225 FEAEPGVRA--IVIKPTLTGSLEKCQELIEQAHALGLRAVISSSIESSLGLTQLARLA 280
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
135-242 |
1.53e-08 |
|
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: 55.81 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 135 WMG--DAAFMREQIEAkLAAGFDCLKLKIGSlDFATELRILADIRAQAGPERlTLRVDANGAFAPAEALGKLEQLARFDL 212
Cdd:cd03324 192 WLGysDEKLRRLCKEA-LAQGFTHFKLKVGA-DLEDDIRRCRLAREVIGPDN-KLMIDANQRWDVPEAIEWVKQLAEFKP 268
|
90 100 110
....*....|....*....|....*....|....
gi 518791782 213 HSIEQPIA----AGQwAALAEVCRHSPVPVALDE 242
Cdd:cd03324 269 WWIEEPTSpddiLGH-AAIRKALAPLPIGVATGE 301
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
142-290 |
4.77e-08 |
|
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: 53.96 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 142 MREQIEAKLAAGFDCLKLKIGSlDFATELRILADIRAQAGPErLTLRVDANGAFAPAEALGKLEQLARFDLHSIEQPIAA 221
Cdd:cd03328 142 LREQLSGWVAQGIPRVKMKIGR-DPRRDPDRVAAARRAIGPD-AELFVDANGAYSRKQALALARAFADEGVTWFEEPVSS 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518791782 222 GQWAALAEVCRHSPVPVALDEELIGLTnPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGI 290
Cdd:cd03328 220 DDLAGLRLVRERGPAGMDIAAGEYAYT-LAYFRRLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHV 287
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
130-291 |
1.61e-06 |
|
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: 49.25 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 130 INGLVWMG--DAAFMREQIEAKLAAGFDCLKLKIGSLDFATE--------LRILADIRAQAGPErLTLRVDANGAFAPAE 199
Cdd:cd03325 113 VRVYSWIGgdRPSDVAEAARARREAGFTAVKMNATEELQWIDtskkvdaaVERVAALREAVGPD-IDIGVDFHGRVSKPM 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 200 ALGKLEQLARFDLHSIEQPIAAGQWAALAEVCRHSPVPVALDEELIGltnPAGWPELLErvRPAYLVLKPTL--LGGLAA 277
Cdd:cd03325 192 AKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFS---RWDFKELLE--DGAVDIIQPDIshAGGITE 266
|
170
....*....|....
gi 518791782 278 SQSWAALADAHGIG 291
Cdd:cd03325 267 LKKIAAMAEAYDVA 280
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
136-290 |
4.05e-06 |
|
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: 48.25 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 136 MGDAAFMREQIEAKLAAGFDCLKLKIGSLDFATELRILADIRaQAGPERLTLRVDANGAFAPAEALGKLEQLARFDLHSI 215
Cdd:cd03321 139 LDGAKLATERAVTAAEEGFHAVKTKIGYPTADEDLAVVRSIR-QAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWI 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518791782 216 EQPIAAGQWAALAEVCRHSPVPVALDEELIGltnPAGWPELLERVRPAYLVLKPTLLGGLAASQSWAALADAHGI 290
Cdd:cd03321 218 EEPTLQHDYEGHARIASALRTPVQMGENWLG---PEEMFKALSAGACDLVMPDLMKIGGVTGWLRASALAEQAGI 289
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
137-247 |
5.64e-06 |
|
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: 47.77 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518791782 137 GDAAFMREQIEAKLAAGFDCLKLKIGSLDFATELRILADIRAQAGPERlTLRVDANGAFAPAEALGKLEQLARFDLHSIE 216
Cdd:cd03326 159 DDLGRLRDEMRRYLDRGYTVVKIKIGGAPLDEDLRRIEAALDVLGDGA-RLAVDANGRFDLETAIAYAKALAPYGLRWYE 237
|
90 100 110
....*....|....*....|....*....|.
gi 518791782 217 QPIAAGQWAALAEVCRHSPVPVALDEELIGL 247
Cdd:cd03326 238 EPGDPLDYALQAELADHYDGPIATGENLFSL 268
|
|
| |
