|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-382 |
0e+00 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 819.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 1 MKITKLTTFIVPPRWCFLKVETDQGVTGWGEPVVEGRAHTVAAAVEELSDYLIGKDPRNIEDIWTVLYRGGFYRGGAIHM 80
Cdd:PRK14017 1 MKITKLETFRVPPRWLFLKIETDEGIVGWGEPVVEGRARTVEAAVHELADYLIGKDPRRIEDHWQVMYRGGFYRGGPILM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 81 SALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMNGTEELQFLDSFEKV 160
Cdd:PRK14017 81 SAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVKMNGTEELQYIDSPRKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 161 DQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSR 240
Cdd:PRK14017 161 DAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 241 WDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPLGPIALAACLQLDAVCYNAFIQEQSLGIHYNES 320
Cdd:PRK14017 241 WDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDAVSPNAFIQEQSLGIHYNQG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489306207 321 NDLLDYVRDPGVFDYDQGFVKIPNGPGLGIEINEEYVIERAAIGHRWRNPIWRHADGSFAEW 382
Cdd:PRK14017 321 ADLLDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRERAKTGHDWRNPVWRHADGSVAEW 382
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-353 |
0e+00 |
|
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: 629.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 2 KITKLTTFIVPPRWCFLKVETDQGVTGWGEPVVEGRAHTVAAAVEELSDYLIGKDPRNIEDIWTVLYRGGFYRGGAIHMS 81
Cdd:cd03325 1 KITKIETFVVPPRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGGFYRGGPVLMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 82 ALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMNGTEELQFLDSFEKVD 161
Cdd:cd03325 81 AISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNATEELQWIDTSKKVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 162 QALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSRW 241
Cdd:cd03325 161 AAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 242 DFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPLGPIALAACLQLDAVCYNAFIQEQSLGIHYNESN 321
Cdd:cd03325 241 DFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDASTPNFLIQEQSLGIHYNEGD 320
|
330 340 350
....*....|....*....|....*....|..
gi 489306207 322 DLLDYVRDPGVFDYDQGFVKIPNGPGLGIEIN 353
Cdd:cd03325 321 DLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-357 |
1.34e-131 |
|
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: 381.09 E-value: 1.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 1 MKITKLTTFIVPP----------------RWCFLKVETDQGVTGWGEPVVEG-RAHTVAAAVEE-LSDYLIGKDPRNIED 62
Cdd:COG4948 1 MKITDIEVYPVRLplkrpftisrgtrterDVVLVRVETDDGITGWGEAVPGGtGAEAVAAALEEaLAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 63 IWTVLYRGGFyrggaIHMSALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTA 142
Cdd:COG4948 81 LWQRLYRALP-----GNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 143 VKMNGTeelqfldsFEKVDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKE 222
Cdd:COG4948 156 LKLKVG--------GPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 223 LAPLTSTPIALGERLFSRWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPL-GPIALAACLQLDA 301
Cdd:COG4948 228 LRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLeSGIGLAAALHLAA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489306207 302 VCYNAFIQEQSLGIHYNEsndllDYVRDPgvFDYDQGFVKIPNGPGLGIEINEEYV 357
Cdd:COG4948 308 ALPNFDIVELDGPLLLAD-----DLVEDP--LRIEDGYLTVPDGPGLGVELDEDAL 356
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
127-355 |
1.57e-82 |
|
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: 250.94 E-value: 1.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 127 DTARAAKEAV-ARGFTAVKMNGTEElqfldsfeKVDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKL 205
Cdd:pfam13378 1 ELAAEARRAVeARGFRAFKLKVGGP--------DPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 206 MFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALH 285
Cdd:pfam13378 73 LWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPH 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 286 CPLGPIALAACLQLDAVCYNAFIQEQSLGIHYnesndlLDYVRDPGVFDYDQGFVKIPNGPGLGIEINEE 355
Cdd:pfam13378 153 SGGGPIGLAASLHLAAAVPNLLIQEYFLDPLL------LEDDLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
17-275 |
1.53e-19 |
|
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: 88.36 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 17 FLKVETDQGVTGWGEPVVEGR----AHTVAAAVEELSDYLIGKDPRNIEDIWTVLyrgGFYRGGAIHMSALAGIDQALWD 92
Cdd:TIGR01928 25 IIELIDDKGNAGFGEVVAFQTpwytHETIATVKHIIEDFFEPNINKEFEHPSEAL---ELVRSLKGTPMAKAGLEMALWD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 93 IKGKALGVSVSDLLGGqVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMNGTEElqfldsfekVDQALanVAAVRD 172
Cdd:TIGR01928 102 MYHKLPSFSLAYGQGK-LRDKAPAGAVSGLANDEQMLKQIESLKATGYKRIKLKITPQ---------IMHQL--VKLRRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 173 AVgPNVGIGVDFHGRVHKPMAKVLmKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDFKRVLSEGYV 252
Cdd:TIGR01928 170 RF-PQIPLVIDANESYDLQDFPRL-KELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSLDDARNLIELGNV 247
|
250 260
....*....|....*....|...
gi 489306207 253 DIIQPDASHAGGITETRKIANMA 275
Cdd:TIGR01928 248 KVINIKPGRLGGLTEVQKAIDTC 270
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
125-229 |
9.42e-19 |
|
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: 80.40 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 125 PADTARAAKEAV-ARGFTAVKMNGTEELqfldsfekvDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPY 203
Cdd:smart00922 1 PEELAEAARRAVaEAGFRAVKVKVGGGP---------LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDEL 71
|
90 100
....*....|....*....|....*.
gi 489306207 204 KLMFIEEPVLSENYEALKELAPLTST 229
Cdd:smart00922 72 GLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14017 |
PRK14017 |
galactonate dehydratase; Provisional |
1-382 |
0e+00 |
|
galactonate dehydratase; Provisional
Pssm-ID: 184455 [Multi-domain] Cd Length: 382 Bit Score: 819.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 1 MKITKLTTFIVPPRWCFLKVETDQGVTGWGEPVVEGRAHTVAAAVEELSDYLIGKDPRNIEDIWTVLYRGGFYRGGAIHM 80
Cdd:PRK14017 1 MKITKLETFRVPPRWLFLKIETDEGIVGWGEPVVEGRARTVEAAVHELADYLIGKDPRRIEDHWQVMYRGGFYRGGPILM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 81 SALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMNGTEELQFLDSFEKV 160
Cdd:PRK14017 81 SAIAGIDQALWDIKGKALGVPVHELLGGLVRDRIRVYSWIGGDRPADVAEAARARVERGFTAVKMNGTEELQYIDSPRKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 161 DQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSR 240
Cdd:PRK14017 161 DAAVARVAAVREAVGPEIGIGVDFHGRVHKPMAKVLAKELEPYRPMFIEEPVLPENAEALPEIAAQTSIPIATGERLFSR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 241 WDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPLGPIALAACLQLDAVCYNAFIQEQSLGIHYNES 320
Cdd:PRK14017 241 WDFKRVLEAGGVDIIQPDLSHAGGITECRKIAAMAEAYDVALAPHCPLGPIALAACLQVDAVSPNAFIQEQSLGIHYNQG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489306207 321 NDLLDYVRDPGVFDYDQGFVKIPNGPGLGIEINEEYVIERAAIGHRWRNPIWRHADGSFAEW 382
Cdd:PRK14017 321 ADLLDYVKNKEVFAYEDGFVAIPTGPGLGIEIDEAKVRERAKTGHDWRNPVWRHADGSVAEW 382
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
2-353 |
0e+00 |
|
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: 629.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 2 KITKLTTFIVPPRWCFLKVETDQGVTGWGEPVVEGRAHTVAAAVEELSDYLIGKDPRNIEDIWTVLYRGGFYRGGAIHMS 81
Cdd:cd03325 1 KITKIETFVVPPRWLFVKIETDEGVVGWGEPTVEGKARTVEAAVQELEDYLIGKDPMNIEHHWQVMYRGGFYRGGPVLMS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 82 ALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMNGTEELQFLDSFEKVD 161
Cdd:cd03325 81 AISGIDQALWDIKGKVLGVPVHQLLGGQVRDRVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNATEELQWIDTSKKVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 162 QALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSRW 241
Cdd:cd03325 161 AAVERVAALREAVGPDIDIGVDFHGRVSKPMAKDLAKELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 242 DFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPLGPIALAACLQLDAVCYNAFIQEQSLGIHYNESN 321
Cdd:cd03325 241 DFKELLEDGAVDIIQPDISHAGGITELKKIAAMAEAYDVALAPHCPLGPIALAASLHVDASTPNFLIQEQSLGIHYNEGD 320
|
330 340 350
....*....|....*....|....*....|..
gi 489306207 322 DLLDYVRDPGVFDYDQGFVKIPNGPGLGIEIN 353
Cdd:cd03325 321 DLLDYLVDPEVFDMENGYVKLPTGPGLGIEID 352
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-357 |
1.34e-131 |
|
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: 381.09 E-value: 1.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 1 MKITKLTTFIVPP----------------RWCFLKVETDQGVTGWGEPVVEG-RAHTVAAAVEE-LSDYLIGKDPRNIED 62
Cdd:COG4948 1 MKITDIEVYPVRLplkrpftisrgtrterDVVLVRVETDDGITGWGEAVPGGtGAEAVAAALEEaLAPLLIGRDPLDIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 63 IWTVLYRGGFyrggaIHMSALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTA 142
Cdd:COG4948 81 LWQRLYRALP-----GNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDRVPVYATLGIDTPEEMAEEAREAVARGFRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 143 VKMNGTeelqfldsFEKVDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKE 222
Cdd:COG4948 156 LKLKVG--------GPDPEEDVERVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLPAEDLEGLAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 223 LAPLTSTPIALGERLFSRWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPL-GPIALAACLQLDA 301
Cdd:COG4948 228 LRRATPVPIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLeSGIGLAAALHLAA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489306207 302 VCYNAFIQEQSLGIHYNEsndllDYVRDPgvFDYDQGFVKIPNGPGLGIEINEEYV 357
Cdd:COG4948 308 ALPNFDIVELDGPLLLAD-----DLVEDP--LRIEDGYLTVPDGPGLGVELDEDAL 356
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
2-351 |
1.17e-128 |
|
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: 373.49 E-value: 1.17e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 2 KITKLTTFIVPP------------RWCFLKVETDQGVTGWGEPVVEGRAHTVAAAVEE-LSDYLIGKDPRNIEDIWTVLY 68
Cdd:cd03316 1 KITDVETFVLRVplpepggavtwrNLVLVRVTTDDGITGWGEAYPGGRPSAVAAAIEDlLAPLLIGRDPLDIERLWEKLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 69 RGGFYRG-GAIHMSALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGG--DRPADTARAAKEAVARGFTAVKM 145
Cdd:cd03316 81 RRLFWRGrGGVAMAAISAVDIALWDIKGKAAGVPVYKLLGGKVRDRVRVYASGGGydDSPEELAEEAKRAVAEGFTAVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 146 NGTeelQFLDSFEKVDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAP 225
Cdd:cd03316 161 KVG---GPDSGGEDLREDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVPPDDLEGLARLRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 226 LTSTPIALGERLFSRWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPLGPIALAACLQLDAVCYN 305
Cdd:cd03316 238 ATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVAPHGAGGPIGLAASLHLAAALPN 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489306207 306 AFIQEqslgihYNESNDLLDYVRDPGVFDYDQGFVKIPNGPGLGIE 351
Cdd:cd03316 318 FGILE------YHLDDLPLREDLFKNPPEIEDGYVTVPDRPGLGVE 357
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
127-355 |
1.57e-82 |
|
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: 250.94 E-value: 1.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 127 DTARAAKEAV-ARGFTAVKMNGTEElqfldsfeKVDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKL 205
Cdd:pfam13378 1 ELAAEARRAVeARGFRAFKLKVGGP--------DPEEDVERVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 206 MFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALH 285
Cdd:pfam13378 73 LWIEEPVPPDDLEGLARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPH 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 286 CPLGPIALAACLQLDAVCYNAFIQEQSLGIHYnesndlLDYVRDPGVFDYDQGFVKIPNGPGLGIEINEE 355
Cdd:pfam13378 153 SGGGPIGLAASLHLAAAVPNLLIQEYFLDPLL------LEDDLLTEPLEVEDGRVAVPDGPGLGVELDED 216
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
2-382 |
1.59e-80 |
|
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: 250.82 E-value: 1.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 2 KITKLTTFIVPPRWCF--LKVETDQGVTGWGEPVVEGRAHTVAAAVEE-LSDYLIGKDPRNIEDIWTVLYRGGFYRGGAI 78
Cdd:cd03322 1 KITAIEVIVTCPGRNFvtLKITTDQGVTGLGDATLNGRELAVKAYLREhLKPLLIGRDANRIEDIWQYLYRGAYWRRGPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 79 HMSALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMngteelqfldsfe 158
Cdd:cd03322 81 TMNAIAAVDMALWDIKGKAAGMPLYQLLGGKSRDGIMVYSHASGRDIPELLEAVERHLAQGYRAIRV------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 159 kvdQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLF 238
Cdd:cd03322 148 ---QLPKLFEAVREKFGFEFHLLHDVHHRLTPNQAARFGKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 239 SRWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCP--LGPIALAACLQLDAVCYNAFIQEqslgih 316
Cdd:cd03322 225 SIWDWQNLIQERLIDYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPtdLSPVGMAAALHLDLWVPNFGIQE------ 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489306207 317 YNESNDLLDYVRdPGVFDYDQGFVKIPNGPGLGIEINEEyVIERAAIGHRWRnPIWRHADGSFAEW 382
Cdd:cd03322 299 YMRHAEETLEVF-PHSVRFEDGYLHPGEEPGLGVEIDEK-AAAKFPYVPRYL-PVARLEDGTVHNW 361
|
|
| PRK15072 |
PRK15072 |
D-galactonate dehydratase family protein; |
1-382 |
1.46e-75 |
|
D-galactonate dehydratase family protein;
Pssm-ID: 237901 [Multi-domain] Cd Length: 404 Bit Score: 239.43 E-value: 1.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 1 MKITKLTTFIVPPRWCF--LKVETDQGVTGWGEPVVEGRAHTVAAAVEE-LSDYLIGKDPRNIEDIWTVLYRGGFYRGGA 77
Cdd:PRK15072 1 MKIVDAEVIVTCPGRNFvtLKITTDDGVTGLGDATLNGRELAVASYLQDhVCPLLIGRDAHRIEDIWQYLYRGAYWRRGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 78 IHMSALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVK-------MNGT-- 148
Cdd:PRK15072 81 VTMSAIAAVDMALWDIKAKAAGMPLYQLLGGASREGVMVYGHANGRDIDELLDDVARHLELGYKAIRvqcgvpgLKTTyg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 149 -------------------EEL----QFLDSFEKVdqalanVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKL 205
Cdd:PRK15072 161 vskgkglayepatkgllpeEELwsteKYLRFVPKL------FEAVRNKFGFDLHLLHDVHHRLTPIEAARLGKSLEPYRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 206 MFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALH 285
Cdd:PRK15072 235 FWLEDPTPAENQEAFRLIRQHTTTPLAVGEVFNSIWDCKQLIEEQLIDYIRTTVTHAGGITHLRRIADFAALYQVRTGSH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 286 CP--LGPIALAACLQLDAVCYNAFIQEqslgihYNESNDLLDYVRdPGVFDYDQGFVKIPNGPGLGIEINEE----YVIE 359
Cdd:PRK15072 315 GPtdLSPVCMAAALHFDLWVPNFGIQE------YMGHSEETLEVF-PHSYTFEDGYLHPGDAPGLGVDFDEKlaakYPYE 387
|
410 420
....*....|....*....|...
gi 489306207 360 RAAIghrwrnPIWRHADGSFAEW 382
Cdd:PRK15072 388 PAYL------PVARLEDGTMWNW 404
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
2-353 |
2.05e-68 |
|
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: 219.13 E-value: 2.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 2 KITKLTTFIvppRWCFLKVETDQGVTGWGEPVveGRAHTVAAAVEELSDYLIGKDPRNIEDIWTVLYRGG-FYRGGAIHM 80
Cdd:cd03327 1 KIKSVRTRV---GWLFVEIETDDGTVGYANTT--GGPVACWIVDQHLARFLIGKDPSDIEKLWDQMYRATlAYGRKGIAM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 81 SALAGIDQALWDIKGKALGVSVSDLLGGQVRDKIRVY-SWIGGDRPADTARAAKEAVARGFTAVKMngteelqFL----- 154
Cdd:cd03327 76 AAISAVDLALWDLLGKIRGEPVYKLLGGRTRDKIPAYaSGLYPTDLDELPDEAKEYLKEGYRGMKM-------RFgygps 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 155 DSFEKVDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALG 234
Cdd:cd03327 149 DGHAGLRKNVELVRAIREAVGYDVDLMLDCYMSWNLNYAIKMARALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 235 ERLFSRWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCplgpiALAACLQLDAVCYNAFIQEQSLG 314
Cdd:cd03327 229 EHEYTVYGFKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPVVPHA-----SQIYNYHFIMSEPNSPFAEYLPN 303
|
330 340 350
....*....|....*....|....*....|....*....
gi 489306207 315 IHYNESNDLLDYVRDPGVFDYDqGFVKIPNGPGLGIEIN 353
Cdd:cd03327 304 SPDEVGNPLFYYIFLNEPVPVN-GYFDLSDKPGFGLELN 341
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
17-310 |
1.14e-47 |
|
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: 161.73 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 17 FLKVETDQGVTGWGEPVvegrahtvaaaveelsdyligkdprniediwtvlyrggfyrggaihmsalAGIDQALWDIKGK 96
Cdd:cd00308 28 LVKLTTDSGVVGWGEVI--------------------------------------------------SGIDMALWDLAAK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 97 ALGVSVSDLLGGQVRDKIRVYSWIggdrpadtaraakeavargftavkmngteelqfldsfekvdqalANVAAVRDAVGP 176
Cdd:cd00308 58 ALGVPLAELLGGGSRDRVPAYGSI--------------------------------------------ERVRAVREAFGP 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 177 NVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDFKRVLSEGYVDIIQ 256
Cdd:cd00308 94 DARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTTVDDALEALELGAVDILQ 173
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489306207 257 PDASHAGGITETRKIANMAEAYDVALALHCPLG-PIALAACLQLDAVCYNAFIQE 310
Cdd:cd00308 174 IKPTRVGGLTESRRAADLAEAFGIRVMVHGTLEsSIGTAAALHLAAALPNDRAIE 228
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
18-357 |
4.07e-42 |
|
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: 151.01 E-value: 4.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 18 LKVETDQGVTGWGepvVEGRAHTVAAAVEE-LSDYLIGKDPRNIEDIWTVLYRggfyRGGAIHMSALAGIDQALWDIKGK 96
Cdd:cd03329 37 LTIETDEGAKGHA---FGGRPVTDPALVDRfLKKVLIGQDPLDRERLWQDLWR----LQRGLTDRGLGLVDIALWDLAGK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 97 ALGVSVSDLLGGqVRDKIRVY--SWIGGDR-----PADTARAAKEAVARGFTAVKMNGteelqFLDSFEKVDqaLANVAA 169
Cdd:cd03329 110 YLGLPVHRLLGG-YREKIPAYasTMVGDDLeglesPEAYADFAEECKALGYRAIKLHP-----WGPGVVRRD--LKACLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 170 VRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGE----RLFSRWDFkr 245
Cdd:cd03329 182 VREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEhsrgALESRADW-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 246 vLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPlgpiaLAACLQLDAVCYNAFIQEQSL---GIHYNESND 322
Cdd:cd03329 260 -VLAGATDFLRADVNLVGGITGAMKTAHLAEAFGLDVELHGN-----GAANLHVIAAIRNTRYYERGLlhpSQKYDVYAG 333
|
330 340 350
....*....|....*....|....*....|....*
gi 489306207 323 LLDYVRDPgvFDyDQGFVKIPNGPGLGIEINEEYV 357
Cdd:cd03329 334 YLSVLDDP--VD-SDGFVHVPKGPGLGVEIDFDYI 365
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
16-357 |
2.39e-41 |
|
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: 149.00 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 16 CFLKVETDQGVTGWGEPV-VEGRAH------TVAAAVEE-LSDYLIGKDPRNIEDIWTVLYRGGFYrggaiHMSALAGID 87
Cdd:cd03318 31 VLVRLTTSDGVVGIGEATtPGGPAWggespeTIKAIIDRyLAPLLIGRDATNIGAAMALLDRAVAG-----NLFAKAAIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 88 QALWDIKGKALGVSVSDLLGGQVRDKIRVySWI--GGDRPADTARAAKEAVARGFTA--VKMngteelqfldSFEKVDQA 163
Cdd:cd03318 106 MALLDAQGRRLGLPVSELLGGRVRDSLPV-AWTlaSGDTERDIAEAEEMLEAGRHRRfkLKM----------GARPPADD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 164 LANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDF 243
Cdd:cd03318 175 LAHVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESVSGPADA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 244 KRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPL-GPIALAACLQLDAVcynafIQEQSLGIHYNESND 322
Cdd:cd03318 255 FELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLeSSIGTAASAHLFAT-----LPSLPFGCELFGPLL 329
|
330 340 350
....*....|....*....|....*....|....*
gi 489306207 323 LLDYVRDPGVFdYDQGFVKIPNGPGLGIEINEEYV 357
Cdd:cd03318 330 LAEDLLEEPLA-YRDGELHVPTGPGLGVRLDEDKV 363
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
18-357 |
1.76e-36 |
|
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: 135.69 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 18 LKVETDQGVTG--WGEPVVEGRAHTVAAAVEELSDYLIGKD--PRNIEDIWTVLYRGGFYRGgaIHMSALAGIDQALWDI 93
Cdd:cd03321 34 IDLATDEGVTGhsYLFTYTPAALKSLKQLLDDMAALLVGEPlaPAELERALAKRFRLLGYTG--LVRMAAAGIDMAAWDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 94 KGKALGVSVSDLLGGQVRdKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMNgteelqflDSFEKVDQALANVAAVRDA 173
Cdd:cd03321 112 LAKVHGLPLAKLLGGNPR-PVQAYDSHGLDGAKLATERAVTAAEEGFHAVKTK--------IGYPTADEDLAVVRSIRQA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 174 VGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDFKRVLSEGYVD 253
Cdd:cd03321 183 VGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENWLGPEEMFKALSAGACD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 254 IIQPDASHAGGITETRKIANMAEAYDVALALHcpLGPIALAACLQLDAVCynafiqeqslgiHYNESNDLLDYVRDPgVF 333
Cdd:cd03321 263 LVMPDLMKIGGVTGWLRASALAEQAGIPMSSH--LFQEISAHLLAVTPTA------------HWLEYVDWAGAILEP-PL 327
|
330 340
....*....|....*....|....
gi 489306207 334 DYDQGFVKIPNGPGLGIEINEEYV 357
Cdd:cd03321 328 KFEDGNAVIPDEPGNGIIWREKAV 351
|
|
| PRK15440 |
PRK15440 |
L-rhamnonate dehydratase; Provisional |
25-285 |
3.15e-35 |
|
L-rhamnonate dehydratase; Provisional
Pssm-ID: 185337 [Multi-domain] Cd Length: 394 Bit Score: 133.32 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 25 GVTGWGEPVvegrahtvAAAVEE-LSDYLIGKDPRNIEDIWTVLYRGGFYRG-GAIHMSALAGIDQALWDIKGKALGVSV 102
Cdd:PRK15440 73 AVSTAGEMG--------AFIVEKhLNRFIEGKCVSDIELIWDQMLNATLYYGrKGLVMNTISCVDLALWDLLGKVRGLPV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 103 SDLLGGQVRDKIRVYSwiGGDRPadtaRAAKEAvarGFTAVKMngteELQF--LDSFEKVDQALANVAAVRDAVGPNVGI 180
Cdd:PRK15440 145 YKLLGGAVRDELQFYA--TGARP----DLAKEM---GFIGGKM----PLHHgpADGDAGLRKNAAMVADMREKVGDDFWL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 181 GVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKEL---APlTSTPIALGERLFSRWDFKRVLSEGYVDIIQP 257
Cdd:PRK15440 212 MLDCWMSLDVNYATKLAHACAPYGLKWIEECLPPDDYWGYRELkrnAP-AGMMVTSGEHEATLQGFRTLLEMGCIDIIQP 290
|
250 260
....*....|....*....|....*...
gi 489306207 258 DASHAGGITETRKIANMAEAYDVALALH 285
Cdd:PRK15440 291 DVGWCGGLTELVKIAALAKARGQLVVPH 318
|
|
| 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 ... |
19-299 |
8.58e-31 |
|
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: 119.60 E-value: 8.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 19 KVETDqGVTGWGE----PVVEG-RAHTVAAAVEELSDYLIGKDPR---NIEDIWTVLYRGGfyrggaihmSALAGIDQAL 90
Cdd:cd03319 31 EIELD-GITGYGEaaptPRVTGeTVESVLAALKSVRPALIGGDPRlekLLEALQELLPGNG---------AARAAVDIAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 91 WDIKGKALGVSVSDLLGGQVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMngteelqfldsfeKVDQALAN---- 166
Cdd:cd03319 101 WDLEAKLLGLPLYQLWGGGAPRPLETDYTISIDTPEAMAAAAKKAAKRGFPLLKI-------------KLGGDLEDdier 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 167 VAAVRDAVgPNVGIGVD------FHGrvhkpmAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSR 240
Cdd:cd03319 168 IRAIREAA-PDARLRVDanqgwtPEE------AVELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADESCFSA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 241 WDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCPLG-PIALAACLQL 299
Cdd:cd03319 241 ADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVEsSLSIAAAAHL 300
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
18-357 |
3.81e-29 |
|
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: 115.79 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 18 LKVETDQGVTGWGEPVVEG----RAHTVAAAVEELSDYLI----GKDPRNIEDIWTVLyrgGFYRGgaiHMSALAGIDQA 89
Cdd:cd03317 29 VELTDEEGITGYGEVVAFEgpfyTEETNATAWHILKDYLLplllGREFSHPEEVSERL---APIKG---NNMAKAGLEMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 90 LWDIKGKALGVSVSDLLGGqVRDKIRVYSWIG-GDRPADTARAAKEAVARGFTAVKMngteelqfldsfeKVD--QALAN 166
Cdd:cd03317 103 VWDLYAKAQGQSLAQYLGG-TRDSIPVGVSIGiQDDVEQLLKQIERYLEEGYKRIKL-------------KIKpgWDVEP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 167 VAAVRDAVgPNVGIGVDFHGRVHKPMAKVLmKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDFKRV 246
Cdd:cd03317 169 LKAVRERF-PDIPLMADANSAYTLADIPLL-KRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSAEDARKA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 247 LSEGYVDIIQPDASHAGGITETRKIANMAEAYDVAL----ALHCPLGPIALAACLQLDAVCYNAFIQEQSlgiHYNESnd 322
Cdd:cd03317 247 IELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVwcggMLESGIGRAHNVALASLPNFTYPGDISASS---RYFEE-- 321
|
330 340 350
....*....|....*....|....*....|....*
gi 489306207 323 llDYVRDPgvFDYDQGFVKIPNGPGLGIEINEEYV 357
Cdd:cd03317 322 --DIITPP--FELENGIISVPTGPGIGVTVDREAL 352
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
84-280 |
5.05e-29 |
|
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: 113.59 E-value: 5.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 84 AGIDQALWDIKGKALGVSVSDLLGGQvRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMngteelqfldsfeKV--- 160
Cdd:cd03315 46 AAVDMALWDLWGKRLGVPVYLLLGGY-RDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKL-------------KVgrd 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 161 -DQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFS 239
Cdd:cd03315 112 pARDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489306207 240 RWDFKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDV 280
Cdd:cd03315 192 PHDAFRELALGAADAVNIKTAKTGGLTKAQRVLAVAEALGL 232
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
5-107 |
1.79e-27 |
|
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: 104.86 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 5 KLTTFIVPPRW-----------------CFLKVETDQGVTGWGEPVVEG-RAHTVAAAVEE-LSDYLIGKDPRNIEDIWT 65
Cdd:pfam02746 1 AIEVFVVDVGWplrpiqmafgtvqqqslVIVRIETSEGVVGIGEATSYGgRAETIKAILDDhLAPLLIGRDAANISDLWQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489306207 66 VLYRGGFYrggaiHMSALAGIDQALWDIKGKALGVSVSDLLG 107
Cdd:pfam02746 81 LMYRAALG-----NMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
25-296 |
1.83e-27 |
|
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: 110.96 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 25 GVTGWGepVVEGRAHTVAAAVEELSDYLIGKDPRNIEDIWTVLYRG--GFYRGGAIHMsALAGIDQALWDIKGKALGVSV 102
Cdd:cd03328 39 GRTGLG--YTYADAAAAALVDGLLAPVVEGRDALDPPAAWEAMQRAvrNAGRPGVAAM-AISAVDIALWDLKARLLGLPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 103 SDLLGgQVRDKIRVYSWIGGDRPADTARAAKEA--VARGFTAVKMNGTEELQfldsfekvdQALANVAAVRDAVGPNVGI 180
Cdd:cd03328 116 ARLLG-RAHDSVPVYGSGGFTSYDDDRLREQLSgwVAQGIPRVKMKIGRDPR---------RDPDRVAAARRAIGPDAEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 181 GVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKEL---APlTSTPIALGERLFSRWDFKRVLSEGYVDIIQP 257
Cdd:cd03328 186 FVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDLAGLRLVrerGP-AGMDIAAGEYAYTLAYFRRLLEAHAVDVLQA 264
|
250 260 270
....*....|....*....|....*....|....*....
gi 489306207 258 DASHAGGITETRKIANMAEAYDVALALHCPLGPIALAAC 296
Cdd:cd03328 265 DVTRCGGVTGFLQAAALAAAHHVDLSAHCAPALHAHVAC 303
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
17-275 |
1.53e-19 |
|
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: 88.36 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 17 FLKVETDQGVTGWGEPVVEGR----AHTVAAAVEELSDYLIGKDPRNIEDIWTVLyrgGFYRGGAIHMSALAGIDQALWD 92
Cdd:TIGR01928 25 IIELIDDKGNAGFGEVVAFQTpwytHETIATVKHIIEDFFEPNINKEFEHPSEAL---ELVRSLKGTPMAKAGLEMALWD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 93 IKGKALGVSVSDLLGGqVRDKIRVYSWIGGDRPADTARAAKEAVARGFTAVKMNGTEElqfldsfekVDQALanVAAVRD 172
Cdd:TIGR01928 102 MYHKLPSFSLAYGQGK-LRDKAPAGAVSGLANDEQMLKQIESLKATGYKRIKLKITPQ---------IMHQL--VKLRRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 173 AVgPNVGIGVDFHGRVHKPMAKVLmKELDPYKLMFIEEPVLSENYEALKELAPLTSTPIALGERLFSRWDFKRVLSEGYV 252
Cdd:TIGR01928 170 RF-PQIPLVIDANESYDLQDFPRL-KELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSLDDARNLIELGNV 247
|
250 260
....*....|....*....|...
gi 489306207 253 DIIQPDASHAGGITETRKIANMA 275
Cdd:TIGR01928 248 KVINIKPGRLGGLTEVQKAIDTC 270
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
16-366 |
1.75e-19 |
|
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239439 [Multi-domain] Cd Length: 395 Bit Score: 88.92 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 16 CFLKVETDQGVTGWGEpvVEGRAHTVAAAVEELSDYLIGK----DPRNIEDIW-TVLYRGGFYRGGAIH-----MSALAG 85
Cdd:cd03323 31 NIVELTDDNGNTGVGE--SPGGAEALEALLEAARSLVGGDvfgaYLAVLESVRvAFADRDAGGRGLQTFdlrttVHVVTA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 86 IDQALWDIKGKALGVSVSDLLGGQVRDKIRV--YSWIGGDR-------------------PADTARAAKEAVAR-GFTAV 143
Cdd:cd03323 109 FEVALLDLLGQALGVPVADLLGGGQRDSVPFlaYLFYKGDRhktdlpypwfrdrwgealtPEGVVRLARAAIDRyGFKSF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 144 KMNGteelqflDSFEKvDQALANVAAVRDA-------VGPNVGIGVDFHGRVHKPMAKVLmkeldPYklmfIEEPVLSEn 216
Cdd:cd03323 189 KLKG-------GVLPG-EEEIEAVKALAEAfpgarlrLDPNGAWSLETAIRLAKELEGVL-----AY----LEDPCGGR- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 217 yEALKELAPLTSTPIALgERLFSRWD-FKRVLSEGYVDIIQPDASHAGGITETRKIANMAEAYDVALALHCP--LGpIAL 293
Cdd:cd03323 251 -EGMAEFRRATGLPLAT-NMIVTDFRqLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNnhLG-ISL 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489306207 294 AACLQLDAVCYNafiQEQSLGIHY-NESNDLLdyvrDPGVFDYDQGFVKIPNGPGLGIEINEEYVIERAAIGHR 366
Cdd:cd03323 328 AMMTHVAAAAPG---LITACDTHWiWQDGQVI----TGEPLRIKDGKVAVPDKPGLGVELDRDKLAKAHELYQR 394
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
125-229 |
9.42e-19 |
|
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: 80.40 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 125 PADTARAAKEAV-ARGFTAVKMNGTEELqfldsfekvDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPY 203
Cdd:smart00922 1 PEELAEAARRAVaEAGFRAVKVKVGGGP---------LEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDEL 71
|
90 100
....*....|....*....|....*.
gi 489306207 204 KLMFIEEPVLSENYEALKELAPLTST 229
Cdd:smart00922 72 GLEWIEEPVPPDDLEGLAELRRATPI 97
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
17-287 |
1.07e-18 |
|
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: 87.01 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 17 FLKVETD-QGVTGWGEPVVEGRAH-TVAAAVEELSDYLIGKDPRNIEDIWtvlyrGGFYR--------------GGAIHM 80
Cdd:cd03324 35 YVVLRTDaAGLKGHGLTFTIGRGNeIVCAAIEALAHLVVGRDLESIVADM-----GKFWRrltsdsqlrwigpeKGVIHL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 81 sALAGIDQALWDIKGKALG---------------VSVSD----------------LLGGQVRDKIRVYSWIGGDRPADT- 128
Cdd:cd03324 110 -ATAAVVNAVWDLWAKAEGkplwkllvdmtpeelVSCIDfryitdaltpeealeiLRRGQPGKAAREADLLAEGYPAYTt 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 129 ------------ARAAKEAVARGFTAVKMngteelqfldsfeKVDQALAN----VAAVRDAVGPNVGIGVDFHGRVHKPM 192
Cdd:cd03324 189 sagwlgysdeklRRLCKEALAQGFTHFKL-------------KVGADLEDdirrCRLAREVIGPDNKLMIDANQRWDVPE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 193 AKVLMKELDPYKLMFIEEPVLSENYEA----LKELAPLtSTPIALGERLFSRWDFKRVLSEGYVDIIQPDASHAGGITET 268
Cdd:cd03324 256 AIEWVKQLAEFKPWWIEEPTSPDDILGhaaiRKALAPL-PIGVATGEHCQNRVVFKQLLQAGAIDVVQIDSCRLGGVNEN 334
|
330
....*....|....*....
gi 489306207 269 RKIANMAEAYDVALalhCP 287
Cdd:cd03324 335 LAVLLMAAKFGVPV---CP 350
|
|
| MR_like_1 |
cd03326 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 1. Enzymes of this ... |
82-351 |
3.27e-15 |
|
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: 76.28 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 82 ALAGIDQALWD----IKGKALGVSVSDLLG-GQVRDKIRVYSWIGGDRPADTARAAKEA----VARGFTAVKMN-GTEEL 151
Cdd:cd03326 109 AVGALDMAVWDavakIAGLPLYRLLARRYGrGQADPRVPVYAAGGYYYPGDDLGRLRDEmrryLDRGYTVVKIKiGGAPL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 152 qfldsfekvDQALANVAAVRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAPLTSTPI 231
Cdd:cd03326 189 ---------DEDLRRIEAALDVLGDGARLAVDANGRFDLETAIAYAKALAPYGLRWYEEPGDPLDYALQAELADHYDGPI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 232 ALGERLFSRWDFKRVLSEGYV----DIIQPDASHAGGITETRKIANMAEAYDVALALHCPLGPIALAacLQLDAvcynaf 307
Cdd:cd03326 260 ATGENLFSLQDARNLLRYGGMrpdrDVLQFDPGLSYGLPEYLRMLDVLEAHGWSRRRFFPHGGHLMS--LHIAA------ 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489306207 308 iqeqSLGIHYNESNdlldyvrdPGVFD----------YDQGFVKIPNGPGLGIE 351
Cdd:cd03326 332 ----GLGLGGNESY--------PDVFQpfggfadgckVENGYVRLPDAPGIGFE 373
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
17-303 |
1.48e-10 |
|
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: 61.12 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 17 FLKVETDQGVTGWGE--PVvegrahTVAAAVEelsdyligkdprniediwtvlyrggfyrggaihmSALAGIDQALWDIK 94
Cdd:cd03320 28 LLRLEDLTGPVGWGEiaPL------PLAFGIE----------------------------------SALANLEALLVGFT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 95 GKALGVSVSDLLGGQvrdkirvyswiggdrPADTARAAKEAVARGFTAVKMngteelqfldsfeKV-----DQALANVAA 169
Cdd:cd03320 68 RPRNRIPVNALLPAG---------------DAAALGEAKAAYGGGYRTVKL-------------KVgatsfEEDLARLRA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 170 VRDAVGPNVGIGVDFHGRVHKPMAKVLMKELDPYKLMFIEEPVLSENYEALKELAplTSTPIALGERLFSRWDFKRVLSE 249
Cdd:cd03320 120 LREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPPDDLAELRRLA--AGVPIALDESLRRLDDPLALAAA 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489306207 250 GYVD--IIQPdaSHAGGITETRKIANMAEAYDVALALHCPL-GPIALAACLQLDAVC 303
Cdd:cd03320 198 GALGalVLKP--ALLGGPRALLELAEEARARGIPAVVSSALeSSIGLGALAHLAAAL 252
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
22-277 |
3.68e-04 |
|
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: 42.10 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 22 TDQGVTGWGE--PVVEGRAHTVAAAVEELsdyligkdpRNIEDIWTvlyRGGFYRGGAIHMSALAGIDQALWDIkGKALG 99
Cdd:TIGR01927 29 TDEGRTGWGEiaPLPGFGTETLAEALDFC---------RALIEEIT---RGDIEAIDDQLPSVAFGFESALIEL-ESGDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 100 VSVSdllggqvrDKIRVYSWIGGDRPADTARAAKEAVARGFTaVKMNGTEELQFLDSFEKVDQALANVAAVRdavgpnvg 179
Cdd:TIGR01927 96 LPPA--------SNYYVALLPAGDPALLLLRSAKAEGFRTFK-WKVGVGELAREGMLVNLLLEALPDKAELR-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489306207 180 igVDFHGRVHKPMAKVLMKELDPY---KLMFIEEPVLSENyeALKELAPLTSTPIALGERLFSRWDFKRVLSEGYVDIIQ 256
Cdd:TIGR01927 159 --LDANGGLSPDEAQQFLKALDPNlrgRIAFLEEPLPDAD--EMSAFSEATGTAIALDESLWELPQLADEYGPGWRGALV 234
|
250 260
....*....|....*....|.
gi 489306207 257 PDASHAGGITETRKIANMAEA 277
Cdd:TIGR01927 235 IKPAIIGSPAKLRDLAQKAHR 255
|
|
| |
