|
Name |
Accession |
Description |
Interval |
E-value |
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-358 |
0e+00 |
|
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: 599.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 6 ATLYITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFSEPWYTEETVKTALHVLQDFLLPDLLKAEISHPN 85
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFYTEETNATAWHILKDYLLPLLLGREFSHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 86 EVPGLFQHIKRNRMAKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEVGVVIGIN-TIPVMLKQIEKYAEEGYERFKVKI 164
Cdd:cd03317 81 EVSERLAPIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQdDVEQLLKQIERYLEEGYKRIKLKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 165 KPEHDYELLKEIRKEFPHIPLMADANSAYTLADTEKLKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSL 244
Cdd:cd03317 161 KPGWDVEPLKAVRERFPDIPLMADANSAYTLADIPLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 245 EDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALASLPNFTIPGDISASSRHWQ 324
Cdd:cd03317 241 EDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVALASLPNFTYPGDISASSRYFE 320
|
330 340 350
....*....|....*....|....*....|....
gi 446325458 325 RDIISPEVTLEGGKVMVPQSVDAEYEVDRGRLAE 358
Cdd:cd03317 321 EDIITPPFELENGIISVPTGPGIGVTVDREALKK 354
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-332 |
2.13e-136 |
|
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: 391.51 E-value: 2.13e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 9 YITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFSEPWYTEETVKTALHVLQDFLLPDLLKaEISHPNEVP 88
Cdd:TIGR01928 1 YHVSEPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGEVVAFQTPWYTHETIATVKHIIEDFFEPNINK-EFEHPSEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 89 GLFQHIKRNRMAKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEVGVVIGINTIPVMLKQIEKYAEEGYERFKVKIKPEH 168
Cdd:TIGR01928 80 ELVRSLKGTPMAKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSGLANDEQMLKQIESLKATGYKRIKLKITPQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 169 DYELLKEIRKEFPHIPLMADANSAYTLADTEKLKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSLEDAR 248
Cdd:TIGR01928 160 MHQLVKLRRLRFPQIPLVIDANESYDLQDFPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSLDDAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 249 VAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALASLPNFTIPGDISASSRHWQRDII 328
Cdd:TIGR01928 240 NLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGISRAFNVALASLGGNDYPGDVSPSGYYFDQDIV 319
|
....
gi 446325458 329 SPEV 332
Cdd:TIGR01928 320 APSI 323
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-343 |
1.54e-110 |
|
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: 327.16 E-value: 1.54e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 1 MEIKKATLYITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFSEPwyteetVKTALHVLQDFLLPDLLKAE 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTG------AEAVAAALEEALAPLLIGRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 81 ISHPNEVPG-LFQHIKRNRMAKAGIEGAIWDLYAKRQKKSLATVLGGASPE-IEVGVVIGINTIPVMLKQIEKYAEEGYE 158
Cdd:COG4948 75 PLDIEALWQrLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDrVPVYATLGIDTPEEMAEEAREAVARGFR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 159 RFKVKIK---PEHDYELLKEIRKEF-PHIPLMADANSAYTLADTEKL-KRLDEFQLMMIEQPLADYDFLDHAQLQKKIET 233
Cdd:COG4948 155 ALKLKVGgpdPEEDVERVRAVREAVgPDARLRVDANGAWTLEEAIRLlRALEDLGLEWIEQPLPAEDLEGLAELRRATPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 234 PICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALAS-LPNFTI 312
Cdd:COG4948 235 PIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAaLPNFDI 314
|
330 340 350
....*....|....*....|....*....|.
gi 446325458 313 pGDISAsSRHWQRDIISPEVTLEGGKVMVPQ 343
Cdd:COG4948 315 -VELDG-PLLLADDLVEDPLRIEDGYLTVPD 343
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
150-343 |
5.52e-51 |
|
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: 169.28 E-value: 5.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 150 EKYAEEGYERFKVKI---KPEHDYELLKEIRKEF-PHIPLMADANSAYTLADT-EKLKRLDEFQLMMIEQPLADYDFLDH 224
Cdd:pfam13378 8 RAVEARGFRAFKLKVggpDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAiRLARALEELGLLWIEEPVPPDDLEGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 225 AQLQKKIETPICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMvEMGISRAQNVAL 304
Cdd:pfam13378 88 ARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSG-GGPIGLAASLHL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446325458 305 -ASLPNFTIpGDISASSRHWQRDIISPEVTLEGGKVMVPQ 343
Cdd:pfam13378 167 aAAVPNLLI-QEYFLDPLLLEDDLLTEPLEVEDGRVAVPD 205
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
14-305 |
9.73e-22 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 94.31 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 14 PLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFsePWYTEETVKTALhvlqDF---LLPDLLKAEI-SHPNEVPG 89
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDETGKIGWGEIAPL--PWFGSETLEEAL----AFcqqLPGEITPEQIfSIPDALPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 90 lfqhikrnrmAKAGIEGAIWDLYAKRQKKSLA----TVLGGASPEIevgvvigintipvmLKQIEKYAEEGYERFKVKI- 164
Cdd:PRK02714 87 ----------CQFGFESALENESGSRSNVTLNplsySALLPAGEAA--------------LQQWQTLWQQGYRTFKWKIg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 165 --KPEHDYELLKEIRKEFP-HIPLMADANSAYTLADTEK-LKRLD-------EFqlmmIEQPLADYDFLDHAQLQKKIET 233
Cdd:PRK02714 143 vdPLEQELKIFEQLLERLPaGAKLRLDANGGLSLEEAKRwLQLCDrrlsgkiEF----IEQPLPPDQFDEMLQLSQDYQT 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325458 234 PICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTesvQIHNYCMEHNIPVWCGGMVEMGISRAQNVALA 305
Cdd:PRK02714 219 PIALDESVANLAQLQQCYQQGWRGIFVIKPAIAGSPS---RLRQFCQQHPLDAVFSSVFETAIGRKAALALA 287
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
144-233 |
7.85e-20 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 83.10 E-value: 7.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 144 VMLKQIEKYAEE-GYERFKVKI--KPEHDYELLKEIRKEF-PHIPLMADANSAYTLADT-EKLKRLDEFQLMMIEQPLAD 218
Cdd:smart00922 3 ELAEAARRAVAEaGFRAVKVKVggGPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAiRALEALDELGLEWIEEPVPP 82
|
90
....*....|....*
gi 446325458 219 YDFLDHAQLQKKIET 233
Cdd:smart00922 83 DDLEGLAELRRATPI 97
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
6-358 |
0e+00 |
|
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: 599.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 6 ATLYITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFSEPWYTEETVKTALHVLQDFLLPDLLKAEISHPN 85
Cdd:cd03317 1 IELFHVRMPLKFPFETSFGTLNEREFLIVELTDEEGITGYGEVVAFEGPFYTEETNATAWHILKDYLLPLLLGREFSHPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 86 EVPGLFQHIKRNRMAKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEVGVVIGIN-TIPVMLKQIEKYAEEGYERFKVKI 164
Cdd:cd03317 81 EVSERLAPIKGNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGTRDSIPVGVSIGIQdDVEQLLKQIERYLEEGYKRIKLKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 165 KPEHDYELLKEIRKEFPHIPLMADANSAYTLADTEKLKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSL 244
Cdd:cd03317 161 KPGWDVEPLKAVRERFPDIPLMADANSAYTLADIPLLKRLDEYGLLMIEQPLAADDLIDHAELQKLLKTPICLDESIQSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 245 EDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALASLPNFTIPGDISASSRHWQ 324
Cdd:cd03317 241 EDARKAIELGACKIINIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVALASLPNFTYPGDISASSRYFE 320
|
330 340 350
....*....|....*....|....*....|....
gi 446325458 325 RDIISPEVTLEGGKVMVPQSVDAEYEVDRGRLAE 358
Cdd:cd03317 321 EDIITPPFELENGIISVPTGPGIGVTVDREALKK 354
|
|
| menC_lowGC/arch |
TIGR01928 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-332 |
2.13e-136 |
|
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: 391.51 E-value: 2.13e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 9 YITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFSEPWYTEETVKTALHVLQDFLLPDLLKaEISHPNEVP 88
Cdd:TIGR01928 1 YHVSEPFKSPFKTSKGTLNHRDCLIIELIDDKGNAGFGEVVAFQTPWYTHETIATVKHIIEDFFEPNINK-EFEHPSEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 89 GLFQHIKRNRMAKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEVGVVIGINTIPVMLKQIEKYAEEGYERFKVKIKPEH 168
Cdd:TIGR01928 80 ELVRSLKGTPMAKAGLEMALWDMYHKLPSFSLAYGQGKLRDKAPAGAVSGLANDEQMLKQIESLKATGYKRIKLKITPQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 169 DYELLKEIRKEFPHIPLMADANSAYTLADTEKLKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSLEDAR 248
Cdd:TIGR01928 160 MHQLVKLRRLRFPQIPLVIDANESYDLQDFPRLKELDRYQLLYIEEPFKIDDISMLDELAKGTITPICLDESITSLDDAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 249 VAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALASLPNFTIPGDISASSRHWQRDII 328
Cdd:TIGR01928 240 NLIELGNVKVINIKPGRLGGLTEVQKAIDTCKEHGAKVWIGGMLETGISRAFNVALASLGGNDYPGDVSPSGYYFDQDIV 319
|
....
gi 446325458 329 SPEV 332
Cdd:TIGR01928 320 APSI 323
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
1-343 |
1.54e-110 |
|
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: 327.16 E-value: 1.54e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 1 MEIKKATLYITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFSEPwyteetVKTALHVLQDFLLPDLLKAE 80
Cdd:COG4948 1 MKITDIEVYPVRLPLKRPFTISRGTRTERDVVLVRVETDDGITGWGEAVPGGTG------AEAVAAALEEALAPLLIGRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 81 ISHPNEVPG-LFQHIKRNRMAKAGIEGAIWDLYAKRQKKSLATVLGGASPE-IEVGVVIGINTIPVMLKQIEKYAEEGYE 158
Cdd:COG4948 75 PLDIEALWQrLYRALPGNPAAKAAVDMALWDLLGKALGVPVYQLLGGKVRDrVPVYATLGIDTPEEMAEEAREAVARGFR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 159 RFKVKIK---PEHDYELLKEIRKEF-PHIPLMADANSAYTLADTEKL-KRLDEFQLMMIEQPLADYDFLDHAQLQKKIET 233
Cdd:COG4948 155 ALKLKVGgpdPEEDVERVRAVREAVgPDARLRVDANGAWTLEEAIRLlRALEDLGLEWIEQPLPAEDLEGLAELRRATPV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 234 PICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALAS-LPNFTI 312
Cdd:COG4948 235 PIAADESLTSRADFRRLIEAGAVDIVNIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAAaLPNFDI 314
|
330 340 350
....*....|....*....|....*....|.
gi 446325458 313 pGDISAsSRHWQRDIISPEVTLEGGKVMVPQ 343
Cdd:COG4948 315 -VELDG-PLLLADDLVEDPLRIEDGYLTVPD 343
|
|
| 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 ... |
5-307 |
6.72e-61 |
|
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: 198.18 E-value: 6.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 5 KATLYITEMPLVIPFAASYGTYEKRESIVIELEdTDGYIGFGEVVAFsePWYTEETVKTALHVLQDFLlPDLLKAEISHP 84
Cdd:cd03319 1 KISLRPERLPLKRPFTIARGSRTEAENVIVEIE-LDGITGYGEAAPT--PRVTGETVESVLAALKSVR-PALIGGDPRLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 85 NEVPGLFQHIKRNRMAKAGIEGAIWDLYAKRQKKSLATVLGGASPE-IEVGVVIGINTIPVMLKQIEKYAEEGYERFKVK 163
Cdd:cd03319 77 KLLEALQELLPGNGAARAAVDIALWDLEAKLLGLPLYQLWGGGAPRpLETDYTISIDTPEAMAAAAKKAAKRGFPLLKIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 164 I--KPEHDYELLKEIRKEFPHIPLMADANSAYTLADT-EKLKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDES 240
Cdd:cd03319 157 LggDLEDDIERIRAIREAAPDARLRVDANQGWTPEEAvELLRELAELGVELIEQPVPAGDDDGLAYLRDKSPLPIMADES 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325458 241 IHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALASL 307
Cdd:cd03319 237 CFSAADAARLAGGGAYDGINIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLAAA 303
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
100-316 |
2.56e-55 |
|
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: 182.16 E-value: 2.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 100 AKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEVGVVIGINTIPVMLKQIEKYAEEGYERFKVKIK--PEHDYELLKEIR 177
Cdd:cd03315 44 TKAAVDMALWDLWGKRLGVPVYLLLGGYRDRVRVAHMLGLGEPAEVAEEARRALEAGFRTFKLKVGrdPARDVAVVAALR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 178 KEFPH-IPLMADANSAYT-LADTEKLKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSLEDARVAITLGS 255
Cdd:cd03315 124 EAVGDdAELRVDANRGWTpKQAIRALRALEDLGLDYVEQPLPADDLEGRAALARATDTPIMADESAFTPHDAFRELALGA 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325458 256 CRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVAL-ASLPNFTIPGDI 316
Cdd:cd03315 204 ADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLaAALRAVTLPGEL 265
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
150-343 |
5.52e-51 |
|
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: 169.28 E-value: 5.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 150 EKYAEEGYERFKVKI---KPEHDYELLKEIRKEF-PHIPLMADANSAYTLADT-EKLKRLDEFQLMMIEQPLADYDFLDH 224
Cdd:pfam13378 8 RAVEARGFRAFKLKVggpDPEEDVERVRAVREAVgPGVDLMVDANGAWSVAEAiRLARALEELGLLWIEEPVPPDDLEGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 225 AQLQKKIETPICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMvEMGISRAQNVAL 304
Cdd:pfam13378 88 ARLRRATPVPIATGESLYSREDFRRLLEAGAVDIVQPDVTRVGGITEALKIAALAEAFGVPVAPHSG-GGPIGLAASLHL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446325458 305 -ASLPNFTIpGDISASSRHWQRDIISPEVTLEGGKVMVPQ 343
Cdd:pfam13378 167 aAAVPNLLI-QEYFLDPLLLEDDLLTEPLEVEDGRVAVPD 205
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
3-342 |
4.26e-44 |
|
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: 155.85 E-value: 4.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 3 IKKATLYITEMPLVIPFaasyGTYEKRESIVIELEDTDGYIGFGEVVafsePWYTEETVKtalHVLQDFLLPDLLKAEIS 82
Cdd:cd03316 2 ITDVETFVLRVPLPEPG----GAVTWRNLVLVRVTTDDGITGWGEAY----PGGRPSAVA---AAIEDLLAPLLIGRDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 83 HPNEVPGLFQHIKRNRM-------AKAGIEGAIWDLYAKRQKKSLATVLGGAS-PEIEV---GVVIGInTIPVMLKQIEK 151
Cdd:cd03316 71 DIERLWEKLYRRLFWRGrggvamaAISAVDIALWDIKGKAAGVPVYKLLGGKVrDRVRVyasGGGYDD-SPEELAEEAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 152 YAEEGYERFKVKI--------KPEHDYELLKEIRKEF-PHIPLMADANSAYTLADTEKL-KRLDEFQLMMIEQPLADYDF 221
Cdd:cd03316 150 AVAEGFTAVKLKVggpdsggeDLREDLARVRAVREAVgPDVDLMVDANGRWDLAEAIRLaRALEEYDLFWFEEPVPPDDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 222 LDHAQLQKKIETPICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPV---WCGGMVEMGISr 298
Cdd:cd03316 230 EGLARLRQATSVPIAAGENLYTRWEFRDLLEAGAVDIIQPDVTKVGGITEAKKIAALAEAHGVRVaphGAGGPIGLAAS- 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446325458 299 AQnvALASLPNFTI---PGDisasSRHWQRDIISPEVTLEGGKVMVP 342
Cdd:cd03316 309 LH--LAAALPNFGIleyHLD----DLPLREDLFKNPPEIEDGYVTVP 349
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
10-314 |
3.56e-37 |
|
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: 137.45 E-value: 3.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 10 ITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFSEPWYTEETVKTALHVLQDFLLPDLLKAEISHPNEV-P 88
Cdd:cd03318 9 IVDLPTRRPHQFAGTTMHTQSLVLVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDRYLAPLLIGRDATNIGAAmA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 89 GLFQHIKRNRMAKAGIEGAIWDLYAKRQKKSLATVLGGA-SPEIEVGVVIGINTIPVMLKQIEKYAEEG-YERFKVKI-- 164
Cdd:cd03318 89 LLDRAVAGNLFAKAAIEMALLDAQGRRLGLPVSELLGGRvRDSLPVAWTLASGDTERDIAEAEEMLEAGrHRRFKLKMga 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 165 -KPEHDYELLKEIRKEFP-HIPLMADANSAYTLADTEK-LKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESI 241
Cdd:cd03318 169 rPPADDLAHVEAIAKALGdRASVRVDVNQAWDESTAIRaLPRLEAAGVELIEQPVPRENLDGLARLRSRNRVPIMADESV 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446325458 242 HSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALASlpnfTIPG 314
Cdd:cd03318 249 SGPADAFELARRGAADVFSLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAHLFA----TLPS 317
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
6-313 |
2.15e-36 |
|
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: 131.68 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 6 ATLYITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVvafsepwyteetvktalhvlqdfllpdllkaeishpn 85
Cdd:cd00308 1 VEVYAVRLPTSRPFYLAGGTADTNDTVLVKLTTDSGVVGWGEV------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 86 evpglfqhikrnrmaKAGIEGAIWDLYAKRQKKSLATVLGGASpeievgvvigINTIPVmlkqiekYAEEgyerfkvkik 165
Cdd:cd00308 44 ---------------ISGIDMALWDLAAKALGVPLAELLGGGS----------RDRVPA-------YGSI---------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 166 pehdyELLKEIRKEFPH-IPLMADANSAYTLADTEKL-KRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHS 243
Cdd:cd00308 82 -----ERVRAVREAFGPdARLAVDANGAWTPKEAIRLiRALEKYGLAWIEEPCAPDDLEGYAALRRRTGIPIAADESVTT 156
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446325458 244 LEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVAL-ASLPNFTIP 313
Cdd:cd00308 157 VDDALEALELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAAALHLaAALPNDRAI 227
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
6-314 |
1.83e-26 |
|
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: 106.19 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 6 ATLYITEMPLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFSepwyteetVKTALHvlqdfllpdllkaeishpn 85
Cdd:cd03320 1 ARLYPYSLPLSRPLGTSRGRLTRRRGLLLRLEDLTGPVGWGEIAPLP--------LAFGIE------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 86 evpglfqhikrnrMAKAGIEGAIWDLYAKRQKKSL-ATVLGGASPEIEvgvvigintipvmlkQIEKYAEEGYERFKVKI 164
Cdd:cd03320 54 -------------SALANLEALLVGFTRPRNRIPVnALLPAGDAAALG---------------EAKAAYGGGYRTVKLKV 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 165 ---KPEHDYELLKEIRKEFP-HIPLMADANSAYTLADT-EKLKRLDEFQLMMIEQPLADYDFLDHAQLQKKIetPICLDE 239
Cdd:cd03320 106 gatSFEEDLARLRALREALPaDAKLRLDANGGWSLEEAlAFLEALAAGRIEYIEQPLPPDDLAELRRLAAGV--PIALDE 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446325458 240 SIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALASL--PNFTIPG 314
Cdd:cd03320 184 SLRRLDDPLALAAAGALGALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGALAHLAAAlpPLPAACG 260
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
14-270 |
9.43e-24 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 100.63 E-value: 9.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 14 PLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAfsepwYTEETVKTALHVLQDflLPDLLKAEISHPNEV----PG 89
Cdd:cd03321 14 PMQYPVHTSVGTVATAPLVLIDLATDEGVTGHSYLFT-----YTPAALKSLKQLLDD--MAALLVGEPLAPAELeralAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 90 LFQHIKRN---RMAKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEVGVVIGINTIPVMLKQIEKYAEEGYERFKVKI-K 165
Cdd:cd03321 87 RFRLLGYTglvRMAAAGIDMAAWDALAKVHGLPLAKLLGGNPRPVQAYDSHGLDGAKLATERAVTAAEEGFHAVKTKIgY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 166 P--EHDYELLKEIRKEFP-HIPLMADANSAYTLADT-EKLKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESI 241
Cdd:cd03321 167 PtaDEDLAVVRSIRQAVGdGVGLMVDYNQSLTVPEAiERGQALDQEGLTWIEEPTLQHDYEGHARIASALRTPVQMGENW 246
|
250 260
....*....|....*....|....*....
gi 446325458 242 HSLEDARVAITLGSCRIVNIKPGRVGGLT 270
Cdd:cd03321 247 LGPEEMFKALSAGACDLVMPDLMKIGGVT 275
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
14-305 |
9.73e-22 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 94.31 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 14 PLVIPFAASYGTYEKRESIVIELEDTDGYIGFGEVVAFsePWYTEETVKTALhvlqDF---LLPDLLKAEI-SHPNEVPG 89
Cdd:PRK02714 13 PFRQPLQTAHGLWRIREGIILRLTDETGKIGWGEIAPL--PWFGSETLEEAL----AFcqqLPGEITPEQIfSIPDALPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 90 lfqhikrnrmAKAGIEGAIWDLYAKRQKKSLA----TVLGGASPEIevgvvigintipvmLKQIEKYAEEGYERFKVKI- 164
Cdd:PRK02714 87 ----------CQFGFESALENESGSRSNVTLNplsySALLPAGEAA--------------LQQWQTLWQQGYRTFKWKIg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 165 --KPEHDYELLKEIRKEFP-HIPLMADANSAYTLADTEK-LKRLD-------EFqlmmIEQPLADYDFLDHAQLQKKIET 233
Cdd:PRK02714 143 vdPLEQELKIFEQLLERLPaGAKLRLDANGGLSLEEAKRwLQLCDrrlsgkiEF----IEQPLPPDQFDEMLQLSQDYQT 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446325458 234 PICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTesvQIHNYCMEHNIPVWCGGMVEMGISRAQNVALA 305
Cdd:PRK02714 219 PIALDESVANLAQLQQCYQQGWRGIFVIKPAIAGSPS---RLRQFCQQHPLDAVFSSVFETAIGRKAALALA 287
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
144-233 |
7.85e-20 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 83.10 E-value: 7.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 144 VMLKQIEKYAEE-GYERFKVKI--KPEHDYELLKEIRKEF-PHIPLMADANSAYTLADT-EKLKRLDEFQLMMIEQPLAD 218
Cdd:smart00922 3 ELAEAARRAVAEaGFRAVKVKVggGPLEDLARVAAVREAVgPDADLMVDANGAWTAEEAiRALEALDELGLEWIEEPVPP 82
|
90
....*....|....*
gi 446325458 219 YDFLDHAQLQKKIET 233
Cdd:smart00922 83 DDLEGLAELRRATPI 97
|
|
| PRK15129 |
PRK15129 |
L-Ala-D/L-Glu epimerase; Provisional |
14-308 |
9.28e-20 |
|
L-Ala-D/L-Glu epimerase; Provisional
Pssm-ID: 185083 [Multi-domain] Cd Length: 321 Bit Score: 88.65 E-value: 9.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 14 PLVIPFAASYGTYEKRESIVIELEDtDGYIGFGEVVAFsePWYTEETVKTALHVLQdfLLPDLLKaeishpnevpGLFQH 93
Cdd:PRK15129 12 PLHTPFVIARGSRSEARVVVVELEE-EGIKGTGECTPY--PRYGESDASVMAQIMS--VVPQLEK----------GLTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 94 IKRNRM----AKAGIEGAIWDLYAKRQKKSLATVLGGASPE-IEVGVVIGINTIPVMLKQIEKYAEEGYERFKVKIKPEH 168
Cdd:PRK15129 77 ALQKLLpagaARNAVDCALWDLAARQQQQSLAQLIGITLPEtVTTAQTVVIGTPEQMANSASALWQAGAKLLKVKLDNHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 169 DYELLKEIRKEFPHIPLMADANSAYT---LADTEKLkrLDEFQLMMIEQPL-ADydflDHAQLQKKIET-PICLDESIHS 243
Cdd:PRK15129 157 ISERMVAIRSAVPDATLIVDANESWRaegLAARCQL--LADLGVAMLEQPLpAQ----DDAALENFIHPlPICADESCHT 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325458 244 LEDarVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMveMGISRAQNVALASLP 308
Cdd:PRK15129 231 RSS--LKALKGRYEMVNIKLDKTGGLTEALALATEARAQGFALMLGCM--LCTSRAISAALPLVP 291
|
|
| MR_like_2 |
cd03327 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 2. Enzymes of this ... |
30-286 |
4.28e-19 |
|
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: 87.00 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 30 ESIVIELEDTDGYIGFGeVVAFSEP--WYTEETVK--------TALHVLQDFLLpdllkaEISHPNEVPGLFQHikrnrm 99
Cdd:cd03327 10 GWLFVEIETDDGTVGYA-NTTGGPVacWIVDQHLArfligkdpSDIEKLWDQMY------RATLAYGRKGIAMA------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 100 AKAGIEGAIWDLYAKRQKKSLATVLGGASPE-IEV-GVVIGINTIPVMLKQIEKYAEEGYERFKVKIK--PEH------- 168
Cdd:cd03327 77 AISAVDLALWDLLGKIRGEPVYKLLGGRTRDkIPAyASGLYPTDLDELPDEAKEYLKEGYRGMKMRFGygPSDghaglrk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 169 DYELLKEIRKEF-PHIPLMADANSAYTLADTEKL-KRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSLED 246
Cdd:cd03327 157 NVELVRAIREAVgYDVDLMLDCYMSWNLNYAIKMaRALEKYELRWIEEPLIPDDIEGYAELKKATGIPISTGEHEYTVYG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446325458 247 ARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPV 286
Cdd:cd03327 237 FKRLLEGRAVDILQPDVNWVGGITELKKIAALAEAYGVPV 276
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
9-322 |
1.27e-13 |
|
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: 70.61 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 9 YITEMPLVIPFAASYGTYEKRESIVIELEDTdGYIGFGEVVAFsePWYTEETVKTALHVLQDfLLPDLLKAEISHPNEVP 88
Cdd:TIGR01927 1 YRYQMPFDAPVVTRHGLLARREGLIVRLTDE-GRTGWGEIAPL--PGFGTETLAEALDFCRA-LIEEITRGDIEAIDDQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 89 GLFQHikrnrmakaGIEGAIWDLYAKR----QKKSLATVLGGASPEIEvgvvigintIPVMLKQiekyaeEGYERFKVKI 164
Cdd:TIGR01927 77 PSVAF---------GFESALIELESGDelppASNYYVALLPAGDPALL---------LLRSAKA------EGFRTFKWKV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 165 -KPEHD-----YELLKEIRKEFPHIPLmaDANSAYTLADTEK-LKRLDEF---QLMMIEQPLADYDflDHAQLQKKIETP 234
Cdd:TIGR01927 133 gVGELAregmlVNLLLEALPDKAELRL--DANGGLSPDEAQQfLKALDPNlrgRIAFLEEPLPDAD--EMSAFSEATGTA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 235 ICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALA--SLPNFTI 312
Cdd:TIGR01927 209 IALDESLWELPQLADEYGPGWRGALVIKPAIIGSPAKLRDLAQKAHRLGLQAVFSSVFESSIALGQLARLAakLSPDPAA 288
|
330
....*....|
gi 446325458 313 PGDISASSRH 322
Cdd:TIGR01927 289 VGFTTALLRA 298
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
32-358 |
6.11e-13 |
|
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: 69.27 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 32 IVIELEDTDGYIGFGEVVAFSEPWYTEETVKTALHVLQDFL-----LPDLLKAEISHPNEVPGLFQHIKRNRM-AKAGIE 105
Cdd:cd03323 31 NIVELTDDNGNTGVGESPGGAEALEALLEAARSLVGGDVFGaylavLESVRVAFADRDAGGRGLQTFDLRTTVhVVTAFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 106 GAIWDLYAKRQKKSLATVLGGA-------------------------SPEIEVGVVIginTIPVMLKQIEK-YAEEGYER 159
Cdd:cd03323 111 VALLDLLGQALGVPVADLLGGGqrdsvpflaylfykgdrhktdlpypWFRDRWGEAL---TPEGVVRLARAaIDRYGFKS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 160 FKVK---IKPEHDYELLKEIRKEFPHIPLMADANSAYTLADTEKLKRLDEFQLMMIEQPLADYDFLdhAQLQKKIETPIC 236
Cdd:cd03323 188 FKLKggvLPGEEEIEAVKALAEAFPGARLRLDPNGAWSLETAIRLAKELEGVLAYLEDPCGGREGM--AEFRRATGLPLA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 237 LDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALASlpnfTIPGDI 316
Cdd:cd03323 266 TNMIVTDFRQLGHAIQLNAVDIPLADHHFWGGMRGSVRVAQVCETWGLGWGMHSNNHLGISLAMMTHVAA----AAPGLI 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446325458 317 SASSRHW---QRDIISPE-VTLEGGKVMVPQSVDAEYEVDRGRLAE 358
Cdd:cd03323 342 TACDTHWiwqDGQVITGEpLRIKDGKVAVPDKPGLGVELDRDKLAK 387
|
|
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
29-306 |
2.59e-12 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 68.34 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 29 RESIVIELEDTDGYIGFGEVVAFS----EPWYTEETVKTALHVLQD----FLLPdLLKAEISH---------PNEVpglF 91
Cdd:PLN02980 961 REGFILSLSLEDGSVGFGEVAPLEiheeDLLDVEEQLRFLLHVIKGakisFMLP-LLKGSFSSwiwselgipPSSI---F 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 92 QHIkrnrmaKAGIEGAIWDLYAKRQKKSLATVL--------GGASP-EIEVGVVIGINTIPVMLKQI-EKYAEEGYERFK 161
Cdd:PLN02980 1037 PSV------RCGLEMAILNAIAVRHGSSLLNILdpyqkdenGSEQShSVQICALLDSNGSPLEVAYVaRKLVEEGFSAIK 1110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 162 VKI----KPEHDYELLKEIRKEFP-HIPLMADANSAYTLADTEKL-KRLDEFQLMMIEQPLADYDflDHAQLQKKIETPI 235
Cdd:PLN02980 1111 LKVgrrvSPIQDAAVIQEVRKAVGyQIELRADANRNWTYEEAIEFgSLVKSCNLKYIEEPVQDED--DLIKFCEETGLPV 1188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446325458 236 CLDESIHSLED----ARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMGISRAQNVALAS 306
Cdd:PLN02980 1189 ALDETIDKFEEcplrMLTKYTHPGIVAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYIQFAS 1263
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
98-270 |
1.69e-11 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239445 [Multi-domain] Cd Length: 368 Bit Score: 64.73 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 98 RMAKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEV-------GVVIGINTIPVMLKQIEKYAEEGYERFKVKI----KP 166
Cdd:cd03329 93 DRGLGLVDIALWDLAGKYLGLPVHRLLGGYREKIPAyastmvgDDLEGLESPEAYADFAEECKALGYRAIKLHPwgpgVV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 167 EHDYELLKEIRKEF-PHIPLMADANSAYTLADTEKLKR-LDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSL 244
Cdd:cd03329 173 RRDLKACLAVREAVgPDMRLMHDGAHWYSRADALRLGRaLEELGFFWYEDPLREASISSYRWLAEKLDIPILGTEHSRGA 252
|
170 180
....*....|....*....|....*..
gi 446325458 245 EDARVA-ITLGSCRIVNIKPGRVGGLT 270
Cdd:cd03329 253 LESRADwVLAGATDFLRADVNLVGGIT 279
|
|
| MR_MLE_N |
pfam02746 |
Mandelate racemase / muconate lactonizing enzyme, N-terminal domain; SCOP reports fold ... |
5-125 |
3.96e-11 |
|
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: 59.79 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 5 KATLYITEMPLVI-PFAASYGTYEKRESIVIELEDTDGYIGFGEvvAFSEPWyTEETVKTALHvlqDFLLPDLLKAEish 83
Cdd:pfam02746 1 AIEVFVVDVGWPLrPIQMAFGTVQQQSLVIVRIETSEGVVGIGE--ATSYGG-RAETIKAILD---DHLAPLLIGRD--- 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446325458 84 PNEVPGLFQHIKR----NRMAKAGIEGAIWDLYAKRQKKSLATVLG 125
Cdd:pfam02746 72 AANISDLWQLMYRaalgNMSAKAAIDMALWDLKAKVLNLPLADLLG 117
|
|
| RspA |
cd03322 |
The starvation sensing protein RspA from E.coli and its homologs are lactonizing enzymes whose ... |
29-312 |
9.83e-10 |
|
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: 59.38 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 29 RESIVIELEDTDGYIGFGEVvAFSEpwyTEETVKTALhvlQDFLLPDLLKAEishPNEVPGLFQHIKRNRM--------- 99
Cdd:cd03322 14 RNFVTLKITTDQGVTGLGDA-TLNG---RELAVKAYL---REHLKPLLIGRD---ANRIEDIWQYLYRGAYwrrgpvtmn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 100 AKAGIEGAIWDLYAKRQKKSLATVLGGASPE-IEVGVVIGINTIPVMLKQIEKYAEEGYERFKVKIKpehdyELLKEIRK 178
Cdd:cd03322 84 AIAAVDMALWDIKGKAAGMPLYQLLGGKSRDgIMVYSHASGRDIPELLEAVERHLAQGYRAIRVQLP-----KLFEAVRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 179 EF-PHIPLMADANSAYTLADTEKL-KRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSLEDARVAITLGSC 256
Cdd:cd03322 159 KFgFEFHLLHDVHHRLTPNQAARFgKDVEPYRLFWMEDPTPAENQEAFRLIRQHTATPLAVGEVFNSIWDWQNLIQERLI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446325458 257 RIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMVEMG-ISRAQNVAL-ASLPNFTI 312
Cdd:cd03322 239 DYIRTTVSHAGGITPARKIADLASLYGVRTGWHGPTDLSpVGMAAALHLdLWVPNFGI 296
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
99-287 |
1.38e-09 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239440 [Multi-domain] Cd Length: 415 Bit Score: 59.28 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 99 MAKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEVGVV----IGINTIP----VMLKQIEK------------------- 151
Cdd:cd03324 109 LATAAVVNAVWDLWAKAEGKPLWKLLVDMTPEELVSCIdfryITDALTPeealEILRRGQPgkaareadllaegypaytt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 152 ------------------YAEEGYERFKVKI--KPEHDYELLKEIRKEF-PHIPLMADANSAYTLADT-EKLKRLDEFQL 209
Cdd:cd03324 189 sagwlgysdeklrrlckeALAQGFTHFKLKVgaDLEDDIRRCRLAREVIgPDNKLMIDANQRWDVPEAiEWVKQLAEFKP 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 210 MMIEQPLADYDFLDHAQLQKKIET---PICLDESIHSledaRVA----ITLGSCRIVNIKPGRVGGLTESVQIHNYCMEH 282
Cdd:cd03324 269 WWIEEPTSPDDILGHAAIRKALAPlpiGVATGEHCQN----RVVfkqlLQAGAIDVVQIDSCRLGGVNENLAVLLMAAKF 344
|
....*
gi 446325458 283 NIPVW 287
Cdd:cd03324 345 GVPVC 349
|
|
| D-galactonate_dehydratase |
cd03325 |
D-galactonate dehydratase catalyses the dehydration of galactonate to ... |
36-352 |
6.96e-09 |
|
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: 56.57 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 36 LEDTDGYIGFGEVVAFSEpwytEETVKTALHVLQDFLLPdllkaeiSHPNEVPGLFQHIKRNRM---------AKAGIEG 106
Cdd:cd03325 19 IETDEGVVGWGEPTVEGK----ARTVEAAVQELEDYLIG-------KDPMNIEHHWQVMYRGGFyrggpvlmsAISGIDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 107 AIWDLYAKRQKKSLATVLGGASPE-IEVGVVIGINTIPVMLKQIEKYAEEGYERFKVKI-----------KPEHDYELLK 174
Cdd:cd03325 88 ALWDIKGKVLGVPVHQLLGGQVRDrVRVYSWIGGDRPSDVAEAARARREAGFTAVKMNAteelqwidtskKVDAAVERVA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 175 EIRKEF-PHIPLMADA------NSAYTLAdteklKRLDEFQLMMIEQPLADYDFLDHAQLQKKIETPICLDESIHSLEDA 247
Cdd:cd03325 168 ALREAVgPDIDIGVDFhgrvskPMAKDLA-----KELEPYRLLFIEEPVLPENVEALAEIAARTTIPIATGERLFSRWDF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 248 RVAITLGSCRIVNIKPGRVGGLTESVQIhnycmehnipvwcGGMVEmgisrAQNVALA------------------SLPN 309
Cdd:cd03325 243 KELLEDGAVDIIQPDISHAGGITELKKI-------------AAMAE-----AYDVALAphcplgpialaaslhvdaSTPN 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446325458 310 FTIPgDISASSRHWQRD-----IISPEV-TLEGGKVMVPQSVDAEYEVD 352
Cdd:cd03325 305 FLIQ-EQSLGIHYNEGDdlldyLVDPEVfDMENGYVKLPTGPGLGIEID 352
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
99-286 |
2.46e-05 |
|
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: 45.87 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 99 MAKAGIEGAIWDLYAKRQKKSLATVLGGASPEIEVGVVIGINTIP--VMLKQIEKYAEEGYERFKVKI--KPEHDYELLK 174
Cdd:cd03328 94 MAISAVDIALWDLKARLLGLPLARLLGRAHDSVPVYGSGGFTSYDddRLREQLSGWVAQGIPRVKMKIgrDPRRDPDRVA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 175 EIRKEF-PHIPLMADANSAYTLADTEKLKR-LDEFQLMMIEQPLADYDFLDHAQLQKKIetPICLD----ESIHSLEDAR 248
Cdd:cd03328 174 AARRAIgPDAELFVDANGAYSRKQALALARaFADEGVTWFEEPVSSDDLAGLRLVRERG--PAGMDiaagEYAYTLAYFR 251
|
170 180 190
....*....|....*....|....*....|....*...
gi 446325458 249 VAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPV 286
Cdd:cd03328 252 RLLEAHAVDVLQADVTRCGGVTGFLQAAALAAAHHVDL 289
|
|
| MAL |
cd03314 |
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the ... |
235-314 |
4.35e-05 |
|
Methylaspartate ammonia lyase (3-methylaspartase, MAL) is a homodimeric enzyme, catalyzing the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. This reaction is part of the main catabolic pathway for glutamate. MAL 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: 239430 [Multi-domain] Cd Length: 369 Bit Score: 45.08 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 235 ICLDESIHSLEDARVAITLGSCRIVNIKPGRVGGLTESVQIHNYCMEHNIPVWCGGMV-EMGIS--RAQNVALASLPNFT 311
Cdd:cd03314 264 IVADEWCNTLEDIRDFADAGAAHMVQIKTPDLGGIDNTIDAVLYCKEHGVGAYLGGSCnETDISarVTVHVALATRADQM 343
|
....*
gi 446325458 312 I--PG 314
Cdd:cd03314 344 LakPG 348
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
188-355 |
1.10e-04 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 188 DANSAYTLADT-EKLKRLDE-FQLMMIEQPLADYDFLdhAQLQKKIETPICLDESIHSLEDA-RVAiTLGSCRIVNIKPG 264
Cdd:PRK02901 140 DANGGWSVDEAvAAARALDAdGPLEYVEQPCATVEEL--AELRRRVGVPIAADESIRRAEDPlRVA-RAGAADVAVLKVA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446325458 265 RVGGLTESVQIHNYCmehNIPVWCGGMVEMGISRAQNVALA-SLPNFTIPGDIsASSRHWQRDIISPEVTLEG----GKV 339
Cdd:PRK02901 217 PLGGVRAALDIAEQI---GLPVVVSSALDTSVGIAAGLALAaALPELDHACGL-ATGGLFEEDVADPLLPVDGflpvRRV 292
|
170
....*....|....*.
gi 446325458 340 MVPQSVDAEYEVDRGR 355
Cdd:PRK02901 293 TPDPARLAALAADPDR 308
|
|
| |
