|
Name |
Accession |
Description |
Interval |
E-value |
| tyrA |
PRK11199 |
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional |
1-373 |
0e+00 |
|
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
Pssm-ID: 183035 [Multi-domain] Cd Length: 374 Bit Score: 805.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 1 MVAELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMR 80
Cdd:PRK11199 1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 81 ESYAHENDKGFKTLCPTLRPVVIVGGRGQMGRLFEKMLTLSGYQVRILDKGDWDRSDELLKDAGMVIISVPIHLTEQIIG 160
Cdd:PRK11199 81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 161 ELPKLPEDCILVDLASVKNRPLQAMLAAHTGPVLGLHPMFGPDSGSLAKQVVVWCDGRQPEAYQWFLEQIQVWGARLHRI 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVNLDQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIKRY 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2509134745 321 YQRFGDAIKLLEQGDKQAFIDSFERVEHWFGDYAKRFLVESRSMLRSANDSRQ 373
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQ 373
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
101-352 |
7.92e-49 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 170.55 E-value: 7.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 101 VVIVGGRGQMGRLFEKMLTLSGYQV----RILDKGD----------WDRSDELLKDAGMVIISVPIHLTEQIIGEL-PKL 165
Cdd:PRK08655 3 ISIIGGTGGLGKWFARFLKEKGFEVivtgRDPKKGKevakelgveyANDNIDAAKDADIVIISVPINVTEDVIKEVaPHV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 166 PEDCILVDLASVKNRPLQAML--AAHTGPVLGLHPMFGPDSGSLAKQVVVWC--DGRQ----PEAYQWFLEQiqvwGARL 237
Cdd:PRK08655 83 KEGSLLMDVTSVKERPVEAMEeyAPEGVEILPTHPMFGPRTPSLKGQVVILTptEKRSnpwfDKVKNFLEKE----GARV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 238 HRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVNLDQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMssesNLALI 317
Cdd:PRK08655 159 IVTSPEEHDRIMSVVQGLTHFAYISIASTLKRLGVDIKESRKFASPIYELMIDIIGRILGQNPYLYASIQM----NNPQI 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 2509134745 318 KRYYQRFGDAI----KLLEQGDKQAFIDSFERVEHWFGD 352
Cdd:PRK08655 235 PEIHETFIKECeelsELVKNGDREEFVERMKEAAKHFGD 273
|
|
| CM_T |
TIGR01799 |
chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of ... |
5-87 |
2.91e-43 |
|
chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of the gamma proteobacterial "T-protein" which consists of an N-terminal chorismate mutase domain and a C-terminal prephenate dehydrogenase domain. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 130858 [Multi-domain] Cd Length: 83 Bit Score: 145.04 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRESYA 84
Cdd:TIGR01799 1 LEDLRGEIDGVDQELLHLLAKRLELVAQVGKVKHAAGLPIYAPEREAAMLAARREEAEKAGIAPDLIEDVLRRFMRESYA 80
|
...
gi 2509134745 85 HEN 87
Cdd:TIGR01799 81 NEN 83
|
|
| PheA |
COG1605 |
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ... |
3-168 |
1.59e-34 |
|
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 441213 [Multi-domain] Cd Length: 166 Bit Score: 124.88 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 3 AELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRES 82
Cdd:COG1605 5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 83 YAHENDKGFKTLCptlrPVVIVGGRGQMGRLFEKMLTLSGYQVRILDKGDWDRSDELLKDAGMVIISVPIHLTEQIIGEL 162
Cdd:COG1605 85 IALQEKLLAEVAY----LGPEGGFTGQAAGKHFGGSAASLPAAAIDEVFREVEAGGAAYGVVPVENSTEGGVVETLDLLL 160
|
....*.
gi 2509134745 163 PKLPED 168
Cdd:COG1605 161 ASPLKI 166
|
|
| FDXACB |
COG4937 |
Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis]; |
101-356 |
2.19e-26 |
|
Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443964 [Multi-domain] Cd Length: 443 Bit Score: 109.34 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 101 VVIVGGRGQMGRLFEKMLTLSGYQVRILDKGDWDRSDELLK------------DAGMVIISVPIHLTEQIIGEL-PKLPE 167
Cdd:COG4937 7 IGIIGGTGEMGQWFAKFFKDFGFEVTIWGRGGKVEIAEKLGvgfandndaaiaDADIIIVSVPIVITETTIVEVaPKMPK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 168 DCILVDLASVKNRPLQAMLAAHTGPV--LGLHPMFGPDSGSLAKQVVVW------CDGRQPEAYQWFLEQiqvwGARLHR 239
Cdd:COG4937 87 GSLLMDLTSTKVKPVEAMEKYAPVDVeiLGTHPMFGPTPPTLSGQIVILtpiegrCDKWFPKIRNLLEEE----GARIII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 240 ISAVEHDQNMAFIQALRHFATFAYGLHLAEENVNLDQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIKR 319
Cdd:COG4937 163 ITPEEHDRMMSVVQGLTHFAYISIGATIKRLDFDVKESRKFASPVYELMLDIIGRIIGQNPYLYASIQMENPEVKKVHET 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 2509134745 320 YYQRFGDAIKLLEQGDKQAFIDSFERVEHWFGDYAKR 356
Cdd:COG4937 243 FIEECNELSNIVRKDDEEGFVEIMKEAAKHFGDTESA 279
|
|
| CM_2 |
pfam01817 |
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ... |
9-87 |
1.06e-25 |
|
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine.
Pssm-ID: 460345 [Multi-domain] Cd Length: 79 Bit Score: 98.72 E-value: 1.06e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509134745 9 RDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRESYAHEN 87
Cdd:pfam01817 1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
|
|
| CM_2 |
smart00830 |
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ... |
9-87 |
3.26e-24 |
|
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to prephenate in the pathway of tyrosine and phenylalanine biosynthesis. This enzyme is negatively regulated by tyrosine, tryptophan and phenylalanine..
Pssm-ID: 214841 [Multi-domain] Cd Length: 79 Bit Score: 94.57 E-value: 3.26e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509134745 9 RDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRESYAHEN 87
Cdd:smart00830 1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
127-345 |
3.67e-20 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 89.03 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 127 ILDKGDWDrSDELLKDAGMVIISVPIHLTEQIIGEL-PKLPEDCILVDLASVKNRPLQAMLAAHTGPV--LGLHPMFGPD 203
Cdd:COG0287 47 VIDRAATD-LEEAVADADLVVLAVPVGATIEVLAELaPHLKPGAIVTDVGSVKGAVVEAAEALLPDGVrfVGGHPMAGTE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 204 -SGSLA--------KQVVVwC--DGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENV 272
Cdd:COG0287 126 kSGPEAadadlfegAPYIL-TptEGTDPEALERVEELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLED 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509134745 273 NlDQLLALSSPIYRlelAMVgRLFAQDPQLYADIIMS-SESNLALIKRYYQRFGDAIKLLEQGDKQAFIDSFER 345
Cdd:COG0287 205 E-EEILRLAAGGFR---DTT-RIAASDPEMWRDIFLAnREALLEALDRFIEELDALRDALEAGDGEALEELLER 273
|
|
| PRK08818 |
PRK08818 |
prephenate dehydrogenase; Provisional |
98-338 |
1.36e-19 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 181561 [Multi-domain] Cd Length: 370 Bit Score: 89.15 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 98 LRPVV-IVGGRGQMGRLFEKML-TLSGYQVRILDKGDWDRSDE--LLKDAGMVIISVPIHLTEQIIGELPKLP----EDC 169
Cdd:PRK08818 3 AQPVVgIVGSAGAYGRWLARFLrTRMQLEVIGHDPADPGSLDPatLLQRADVLIFSAPIRHTAALIEEYVALAggraAGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 170 ILVDLASVKNRPLQAMLAAHtGPVLGLHPMFG-PDSGSLAKQVVVWCDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQN 248
Cdd:PRK08818 83 LWLDVTSIKQAPVAAMLASQ-AEVVGLHPMTApPKSPTLKGRVMVVCEARLQHWSPWVQSLCSALQAECVYATPEHHDRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 249 MAFIQALRHfATfayglHLAEENV---------NLDQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSESNLALIKR 319
Cdd:PRK08818 162 MALVQAMVH-AT-----HLAQAGVlrdyapllgELRALMPYRSASFELDTAVIARILSLNPSIYEDIQFGNPYVGEMLDR 235
|
250
....*....|....*....
gi 2509134745 320 YYQRFGDAIKLLEQGDKQA 338
Cdd:PRK08818 236 LLAQLQELRALVAQGDDAA 254
|
|
| PRK08507 |
PRK08507 |
prephenate dehydrogenase; Validated |
136-349 |
1.17e-12 |
|
prephenate dehydrogenase; Validated
Pssm-ID: 181452 [Multi-domain] Cd Length: 275 Bit Score: 67.61 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 136 SDELLKDAGMVIISVPIhltEQIIGELPKL---PEDCILVDLASVKNRPLQAMLAAHTGPVLGLHPM-----FGPDS--- 204
Cdd:PRK08507 52 SFEELKKCDVIFLAIPV---DAIIEILPKLldiKENTTIIDLGSTKAKIIESVPKHIRKNFIAAHPMagtenSGPKAaik 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 205 GSLAKQVVVWCDGRQP-EAYQWFLEQI-QVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLH-LAEENVNldQLLALS 281
Cdd:PRK08507 129 GLYEGKVVVLCDVEKSgEKHQERAKEIfSGLGMRIVYMDAKEHDLHAAYISHLPHIISFALANTvLKEEDER--NIFDLA 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509134745 282 SPIYRlelAMVgRLFAQDPQLYADIIMSSESN-LALIKRYYQRFGDAIKLLEQgdkqafiDSFERVEHW 349
Cdd:PRK08507 207 GGGFR---SMS-RLAKSSPAMWSDIFKQNKENvLEAIDEFIKELEQFKQLIEN-------EDWEELEEW 264
|
|
| PRK09239 |
PRK09239 |
chorismate mutase; Provisional |
1-85 |
2.01e-12 |
|
chorismate mutase; Provisional
Pssm-ID: 181719 [Multi-domain] Cd Length: 104 Bit Score: 63.12 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 1 MVAELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMR 80
Cdd:PRK09239 8 APAELAALRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKDANLDPDFAEKFLNFIIK 87
|
....*
gi 2509134745 81 ESYAH 85
Cdd:PRK09239 88 EVIRH 92
|
|
| CM-like |
TIGR01803 |
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on ... |
5-86 |
5.89e-12 |
|
chorismate mutase related enzymes; This subfamily includes two enzymes which are variants on the mechanism of chorismate mutase and are likely to have evolved from an ancestral chorismate mutase enzyme. 4-amino-4-deoxy-chorismate mutase produces amino-deoxy-prephenate which is subsequently converted to para-dimethylamino-phenylalanine, a component of the natural product pristinamycin. Isochorismate-pyruvate lyase presumably catalyzes the same type of 2+2+2 cyclo-rearrangement as chorismate mutase, but acting on isochorismate, this results in two broken bonds instead of one broken and one made. The product of this reaction is salicylate (2-hydroxy-benzoate) which is also incorporated into various natural products.
Pssm-ID: 130862 [Multi-domain] Cd Length: 82 Bit Score: 61.07 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRESYA 84
Cdd:TIGR01803 1 LADIREAIDRIDLALVQALGRRMDYVKRASEFKRSHEAAIPAPERVAAVLPNAARWAEENGLDPPFVEGLFAQIIHWYIA 80
|
..
gi 2509134745 85 HE 86
Cdd:TIGR01803 81 EE 82
|
|
| CM_archaeal |
TIGR01791 |
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ... |
5-82 |
2.53e-11 |
|
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. Chorismate mutase catalyzes the conversion of chorismate into prephenate which is subsequently converted into either phenylalanine or tyrosine. In Sulfolobus this gene is found as a fusion with prephenate dehydrogenase (although the non-TIGR annotation contains a typographical error indicating it as a dehydratase OMNI|NTL02SS0274) which is the next enzyme in the tyrosine biosynthesis pathway. The Archaeoglobus gene contains an N-terminal prephenate dehydrogenase domain and a C-terminal prephenate dehydratase domain followed by a regulatory amino acid-binding ACT domain. The Thermoplasma volcanium gene is adjacent to prephenate dehydratase. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 130851 [Multi-domain] Cd Length: 83 Bit Score: 59.36 E-value: 2.53e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRES 82
Cdd:TIGR01791 1 IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEILMSLS 78
|
|
| PRK12595 |
PRK12595 |
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed |
1-55 |
6.26e-11 |
|
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
Pssm-ID: 183614 [Multi-domain] Cd Length: 360 Bit Score: 63.07 E-value: 6.26e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2509134745 1 MVAELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLA 55
Cdd:PRK12595 2 MNEELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLD 56
|
|
| PRK06285 |
PRK06285 |
chorismate mutase; Provisional |
4-79 |
5.28e-10 |
|
chorismate mutase; Provisional
Pssm-ID: 180509 [Multi-domain] Cd Length: 96 Bit Score: 55.81 E-value: 5.28e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2509134745 4 ELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLM 79
Cdd:PRK06285 8 RLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENIGLKIMKILM 83
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
138-348 |
6.32e-10 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 60.78 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 138 ELLKDAGMVIISVPIHLTEQIIGEL-PKLPEDCILVDLASVKNRPLQAMLAAH----TGPVLGlHPMFGPD-SGSLAKQV 211
Cdd:PRK14806 59 EAVSGADVIVLAVPVLAMEKVLADLkPLLSEHAIVTDVGSTKGNVVDAARAVFgelpAGFVPG-HPIAGSEkSGVHAANA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 212 VVWCDGR-----QPEAYQWFLEQI-QVW---GARLHRISAVEHDQNMAFIQALRHFatFAYGL--HLAEENVNLDqllal 280
Cdd:PRK14806 138 DLFRNHKviltpLAETDPAALARVdRLWravGADVLHMDVAHHDEVLAATSHLPHL--LAFSLvdQLANREDNLD----- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509134745 281 sspIYRleLAMVG-----RLFAQDPQLYADIIMSS-ESNLALIKRYYQRFGDAIKLLEQGDKQAFIDSFERVEH 348
Cdd:PRK14806 211 ---IFR--YAAGGfrdftRIAASDPVMWHDIFLANkEAVLRALDHFRDDLDALRAAIEAGDGHALLGVFTRARA 279
|
|
| CM_P2 |
TIGR01807 |
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of ... |
5-81 |
6.31e-09 |
|
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of two separate clades of the chorismate mutase domain of the gamma and beta and epsilon proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. It is also found in Aquifex aolicus. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 130866 [Multi-domain] Cd Length: 76 Bit Score: 52.07 E-value: 6.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRY--GLPIYVPEREASMLasRRQEAEALGVSPDlieDVLRRLMRE 81
Cdd:TIGR01807 1 LEELRNKIDAIDDRILDLLSERATYAQAVGELKGSGasGASFYRPEREAQVI--RRLQNLNKGPLDQ---EAIARIFRE 74
|
|
| PDH_C |
pfam20463 |
Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate ... |
241-343 |
6.62e-09 |
|
Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate dehydrogenases EC:1.3.1.12 (PDHs) involved in tyrosine biosynthesis. This is the C-terminal, helical dimerization domain of PDHs.
Pssm-ID: 466612 [Multi-domain] Cd Length: 102 Bit Score: 52.77 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVNLDQLLALSSPIYRLelamVGRLFAQDPQLYADIIMSSESNLALIKRY 320
Cdd:pfam20463 1 SPETHDRVVAVVSHLPHFVAIALAATLAELGVDIKEARKLASGGFRD----MTRIAGSNPELWADIQTHNARAVLEALDD 76
|
90 100
....*....|....*....|....
gi 2509134745 321 YQRFGDAIK-LLEQGDKQAFIDSF 343
Cdd:pfam20463 77 FIAELKQLKeLIRNGDWEELVEYM 100
|
|
| PDH_N |
pfam02153 |
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ... |
138-237 |
6.79e-09 |
|
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face.
Pssm-ID: 460467 [Multi-domain] Cd Length: 154 Bit Score: 54.31 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 138 ELLKDAGMVIISVPIHLTEQIIGEL-PKLPEDCILVDLASVKN---RPLQAMLAAHTgpVLGLHPMFGPDS--------G 205
Cdd:pfam02153 41 EAVREADIVFLAVPVEQTLPVLKELaPHLKEDALITDVGSVKVkiiRELEQHLPDKS--FVPGHPMAGTEKsgpdaaraN 118
|
90 100 110
....*....|....*....|....*....|....*
gi 2509134745 206 SLAKQVVVWCDGRQPEAyQWFLEQIQVW---GARL 237
Cdd:pfam02153 119 LFENAPVILTPTEKTDT-EALNCVKELLegvGARV 152
|
|
| PRK07248 |
PRK07248 |
chorismate mutase; |
4-62 |
9.57e-09 |
|
chorismate mutase;
Pssm-ID: 168880 [Multi-domain] Cd Length: 87 Bit Score: 51.99 E-value: 9.57e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2509134745 4 ELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAE 62
Cdd:PRK07248 2 DLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDKVSSLVE 60
|
|
| CM_mono_grmpos |
TIGR01805 |
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade ... |
5-82 |
1.70e-08 |
|
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade of chorismate mutase proteins/domains from gram positive species. The sequence from Enterococcus is fused to the C-terminus of an aparrent acetyltransferase, and the seuence from Clostridium acetobutylicum (but not perfringens) is fused to the N-terminus of shikimate-5-dehydrogenase, another enzyme of the chorismate pathway. All the other members of this clade are mono-functional. Members of this clade from Streptococcus and Lactococcus have been found which represent the sole chorismate mutase domain in their respective genomes which also exhibit evidence of the enzymes of both the upstream and downstream branches of the chorismate pathways. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 130864 [Multi-domain] Cd Length: 81 Bit Score: 51.31 E-value: 1.70e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSpDLIEDVLRRLMRES 82
Cdd:TIGR01805 1 LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCTKNVENKEYR-ETIEEFFRNIMDIS 77
|
|
| PRK07075 |
PRK07075 |
isochorismate lyase; |
5-79 |
2.25e-08 |
|
isochorismate lyase;
Pssm-ID: 136191 [Multi-domain] Cd Length: 101 Bit Score: 51.27 E-value: 2.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRyGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLM 79
Cdd:PRK07075 10 LDDIREAIDRLDRDIIAALGRRMQYVKAASRFKPS-EASIPAPERVAAMLPERRRWAEQAGLDADFVEKLFAQLI 83
|
|
| PLN02712 |
PLN02712 |
arogenate dehydrogenase |
106-257 |
5.71e-08 |
|
arogenate dehydrogenase
Pssm-ID: 215382 [Multi-domain] Cd Length: 667 Bit Score: 54.60 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 106 GRGQMGRLFEKMLTLSGYQVRILDKGDW------------DRSDELLKDAGMVII-SVPIHLTEQIIGELP--KLPEDCI 170
Cdd:PLN02712 376 GFGNFGQFLAKTMVKQGHTVLAYSRSDYsdeaqklgvsyfSDADDLCEEHPEVILlCTSILSTEKVLKSLPfqRLKRSTL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 171 LVDLASVKNRPlQAMLAAHTGP---VLGLHPMFGPDSGS--------LAKQVVVWCDGRQPEAYQWFLEQIQVWGARLHR 239
Cdd:PLN02712 456 FVDVLSVKEFP-RNLFLQHLPQdfdILCTHPMFGPESGKngwnnlafVFDKVRIGSDDRRVSRCDSFLDIFAREGCRMVE 534
|
170
....*....|....*...
gi 2509134745 240 ISAVEHDQNMAFIQALRH 257
Cdd:PLN02712 535 MSCAEHDWHAAGSQFITH 552
|
|
| PLN02256 |
PLN02256 |
arogenate dehydrogenase |
146-257 |
6.32e-07 |
|
arogenate dehydrogenase
Pssm-ID: 215144 [Multi-domain] Cd Length: 304 Bit Score: 50.43 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 146 VIISVPIHLTEQIIGELP--KLPEDCILVDLASVKNRPLQAMLAA--HTGPVLGLHPMFGPDSG--SLAKQVVVW----- 214
Cdd:PLN02256 96 VLLCTSILSTEAVLRSLPlqRLKRSTLFVDVLSVKEFPKNLLLQVlpEEFDILCTHPMFGPESGkgGWAGLPFVYdkvri 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2509134745 215 -CDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRH 257
Cdd:PLN02256 176 gDEGEREARCERFLDIFEEEGCRMVEMSCEEHDRYAAGSQFITH 219
|
|
| PRK06545 |
PRK06545 |
prephenate dehydrogenase; Validated |
99-345 |
1.21e-06 |
|
prephenate dehydrogenase; Validated
Pssm-ID: 235824 [Multi-domain] Cd Length: 359 Bit Score: 49.90 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 99 RPVVIVG--------GRGqmgrlfekmLTLSGYQVRILDkgdWDRSDELL--------------------KDAGMVIISV 150
Cdd:PRK06545 1 RTVLIVGlgliggslALA---------IKAAGPDVFIIG---YDPSAAQLaralgfgvidelaadlqraaAEADLIVLAV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 151 PIHLTEQIIGELP--KLPEDCILVDLASVKNRPLQAmLAAHTGPV---LGLHPMFGPD-SGSLAKQ---------VVVWC 215
Cdd:PRK06545 69 PVDATAALLAELAdlELKPGVIVTDVGSVKGAILAE-AEALLGDLirfVGGHPMAGSHkSGVAAARadlfenapwVLTPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 216 DGRQPEAyqwfLEQIQVW----GARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENvnldqLLALSspiyrleLAM 291
Cdd:PRK06545 148 DHTDPDA----VAELKDLlsgtGAKFVVLDAEEHDRAVALVSHLPHILASSLAARLAGEH-----PLALR-------LAA 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2509134745 292 VG-----RLFAQDPQLYADIImssESN----LALIKRYYQRFGDAIKLLEQGDKQAFIDSFER 345
Cdd:PRK06545 212 GGfrditRIASSDPGMWRDIL---ESNaealLDALDEWIEDLDRARDALESGDAEAIAELFDA 271
|
|
| PRK06444 |
PRK06444 |
prephenate dehydrogenase; Provisional |
101-255 |
1.68e-06 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 102381 [Multi-domain] Cd Length: 197 Bit Score: 48.31 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 101 VVIVGGRGQMGRLFEKMLTLSGYQVRIldkgdwdrsdellKDAGMVIISVPIHLTEQIIGElpklpEDCILVDLASVKnr 180
Cdd:PRK06444 3 EIIIGKNGRLGRVLCSILDDNGLGVYI-------------KKADHAFLSVPIDAALNYIES-----YDNNFVEISSVK-- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509134745 181 plqAMLAAHTGPVLGLHPMFGPDS--GSLAKQVVVWCDGRQPEaYQWFLEQIqVWGARLHRISAVEHDQNMAFIQAL 255
Cdd:PRK06444 63 ---WPFKKYSGKIVSIHPLFGPMSynDGVHRTVIFINDISRDN-YLNEINEM-FRGYHFVEMTADEHDLLMSEIMVK 134
|
|
| CM_mono2 |
TIGR01806 |
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ... |
19-120 |
4.33e-06 |
|
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from alpha, beta and gamma proteobacteria as well as Mycobacterium tuberculosis and a clade of nematodes. Although the most likely function for the enzymes represented by this model is as a chorismate mutase, in no species are these enzymes the sole chorismate mutase in the genome. Also, in no case are these enzymes located in a region of the genome proximal to any other enzymes involved in chorismate pathways. Although the Pantoea enzyme has been shown to complement a CM-free mutant of E. coli, this was also shown to be the case with isochorismate-pyruvate lyase which only has a secondary (non-physiologically relevant) chorismate mutase activity. This enzyme is believed to be a homodimer and be localized to the periplasm. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 130865 Cd Length: 114 Bit Score: 45.11 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 19 LLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRES----YAHENDkGFKTL 94
Cdd:TIGR01806 9 LVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANkaiqYRLVSD-WLNPP 87
|
90 100
....*....|....*....|....*.
gi 2509134745 95 CPTLRPVVIVGGRGQMGRLFEKMLTL 120
Cdd:TIGR01806 88 SPPPQVPDLTDTRSAIDQLNTEMLSA 113
|
|
| CM_M_hiGC-arch |
TIGR01808 |
monofunctional chorismate mutase, high GC gram positive type; This model represents the ... |
4-76 |
7.09e-06 |
|
monofunctional chorismate mutase, high GC gram positive type; This model represents the monofunctional chorismate mutase from high GC gram-positive bacteria and archaea. Trusted annotations from Corynebacterium and Pyrococcus are aparrently the sole chorismate mutase enzymes in their respective genomes. This is coupled with the presence in those genomes of the enzymes of the chorismate pathways both up- and downstream of chorismate mutase. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 130867 [Multi-domain] Cd Length: 74 Bit Score: 43.36 E-value: 7.09e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2509134745 4 ELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLasrRQEAEALGVSPDLIEDVLR 76
Cdd:TIGR01808 1 EIDTLREEIDRLDAEILALVKRRAEISQAIGKARMASGGTRLVHSREMKVI---ERYSELGPEGKDLAIKLLR 70
|
|
| CM_P_1 |
TIGR01797 |
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ... |
5-84 |
8.41e-06 |
|
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the chorismate mutase domain of the gamma and beta proteobacterial "P-protein" which contains an N-terminal chorismate mutase domain and a C-terminal prephenate dehydratase domain. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 130856 [Multi-domain] Cd Length: 83 Bit Score: 43.65 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRESYA 84
Cdd:TIGR01797 1 LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLLQRLITLGKAYHLDAHYITRLFQLIIEDSVL 80
|
|
| PRK07417 |
PRK07417 |
prephenate/arogenate dehydrogenase; |
138-281 |
2.07e-05 |
|
prephenate/arogenate dehydrogenase;
Pssm-ID: 180970 [Multi-domain] Cd Length: 279 Bit Score: 45.65 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 138 ELLKDAGMVIISVPIHLTEQIIGEL-PKLPEDCILVDLASVKNRPLQAMLAAHTGPVlGLHPMFG-PDSGSLAKQ----- 210
Cdd:PRK07417 53 SLLKDCDLVILALPIGLLLPPSEQLiPALPPEAIVTDVGSVKAPIVEAWEKLHPRFV-GSHPMAGtAESGVEAGQrglfk 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509134745 211 ----VVVWCDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEEN----VNLDQLLALS 281
Cdd:PRK07417 132 nrpwVLTPTENTDLNALAIVEELAVSLGSKIYTADPEEHDRAVALISHLPVMVSAALIQTCGTEKdpsvLKLAQNLASS 210
|
|
| PRK08055 |
PRK08055 |
chorismate mutase; Provisional |
13-84 |
6.12e-05 |
|
chorismate mutase; Provisional
Pssm-ID: 236143 Cd Length: 181 Bit Score: 43.14 E-value: 6.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2509134745 13 DEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRESYA 84
Cdd:PRK08055 24 AVSLGALATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLDPESIKPFIVAQMDAAKA 95
|
|
| PRK09269 |
PRK09269 |
chorismate mutase; Provisional |
19-119 |
1.35e-04 |
|
chorismate mutase; Provisional
Pssm-ID: 236441 Cd Length: 193 Bit Score: 42.28 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 19 LLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLASRRQEAEALGVSPDLIEDVLRRLMRES----YAHENDKGFKTL 94
Cdd:PRK09269 37 LVDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAPAHGVDPDYVRRFFRDQIEANklvqYALLARWRLAGA 116
|
90 100
....*....|....*....|....*
gi 2509134745 95 CPTLRPVVIVGGRGQMGRLFEKMLT 119
Cdd:PRK09269 117 APPGPRPDLASIRPRLDRLQQELLD 141
|
|
| PRK07502 |
PRK07502 |
prephenate/arogenate dehydrogenase family protein; |
138-345 |
1.36e-04 |
|
prephenate/arogenate dehydrogenase family protein;
Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 43.42 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 138 ELLKDAGMVIISVPIHLTEQIIGEL-PKLPEDCILVDLASVKNRPLQAM---LAAHTGPVLGlHPMF-----GPDSGSLA 208
Cdd:PRK07502 62 EAVKGADLVILCVPVGASGAVAAEIaPHLKPGAIVTDVGSVKASVIAAMaphLPEGVHFIPG-HPLAgtehsGPDAGFAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 209 KQVVVWC-----DGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFatFAYGL-----HLaeENVNLDQLL 278
Cdd:PRK07502 141 LFENRWCiltppEGTDPAAVARLTAFWRALGARVEEMDPEHHDLVLAITSHLPHL--IAYTIvgtadDL--ERVTESEVI 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2509134745 279 ALSSPIYRlelaMVGRLFAQDPQLYADIIMSS-ESNLALIkryyQRFGDAIKLLEQ----GDKQAFIDSFER 345
Cdd:PRK07502 217 KYSASGFR----DFTRIAASDPTMWRDVFLHNkDAVLEML----GRFTEDLAALQRairwGDGDALFDLFTR 280
|
|
| pheA |
PRK10622 |
bifunctional chorismate mutase/prephenate dehydratase; Provisional |
5-54 |
1.90e-04 |
|
bifunctional chorismate mutase/prephenate dehydratase; Provisional
Pssm-ID: 182594 [Multi-domain] Cd Length: 386 Bit Score: 43.18 E-value: 1.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASML 54
Cdd:PRK10622 7 LLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLL 56
|
|
| PRK06443 |
PRK06443 |
chorismate mutase; Validated |
1-51 |
3.55e-04 |
|
chorismate mutase; Validated
Pssm-ID: 235801 Cd Length: 177 Bit Score: 41.04 E-value: 3.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2509134745 1 MVA--ELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREA 51
Cdd:PRK06443 1 MVHfiDMEDLRSEILENTMDIIELIEKRRELARMIGIIKMRNGLSIRDSEREN 53
|
|
| PLN02712 |
PLN02712 |
arogenate dehydrogenase |
96-355 |
3.81e-04 |
|
arogenate dehydrogenase
Pssm-ID: 215382 [Multi-domain] Cd Length: 667 Bit Score: 42.66 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 96 PTLRPVVIvgGRGQMGRLFEKMLTLSGYQVRILDKGD-------------WDRSDELLKDAGMVIISVPIHLTEQIIGEL 162
Cdd:PLN02712 51 TQLKIAII--GFGNYGQFLAKTLISQGHTVLAHSRSDhslaarslgvsffLDPHDLCERHPDVILLCTSIISTENVLKSL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 163 P--KLPEDCILVDLASVKN--RPLQAMLAAHTGPVLGLHPMFGPDSGSLA--------KQVVVWCDGRQPEAYQWFLEQI 230
Cdd:PLN02712 129 PlqRLKRNTLFVDVLSVKEfaKNLLLDYLPEDFDIICSHPMFGPQSAKHGwdglrfvyEKVRIGNEELRVSRCKSFLEVF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509134745 231 QVWGARLHRISAVEHDQNMAFIQalrhFATFAYGLHLaeenvnldQLLAL-SSPI----YRLELAMVGRLFAQDPQLYAD 305
Cdd:PLN02712 209 EREGCKMVEMSCTEHDKYAAESQ----FITHTVGRVL--------EMLKLeSTPIntkgYESLLDLVENTCGDSFDLYYG 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2509134745 306 IIMSSESNLALIKRYYQRFGDAIKLL-----EQGDKQAFiDSFERVEHWFGDYAK 355
Cdd:PLN02712 277 LFMYNKNSLEMLERLDLAFEALRKQLfgrlhGVVRKQLF-GNEEKKVHVQPNHAE 330
|
|
| PRK07857 |
PRK07857 |
chorismate mutase; |
3-65 |
1.06e-03 |
|
chorismate mutase;
Pssm-ID: 236117 Cd Length: 106 Bit Score: 38.13 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2509134745 3 AELTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGLPIYVPEREASMLAsrrQEAEALG 65
Cdd:PRK07857 28 AEIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIE---RYREELG 87
|
|
| PRK06034 |
PRK06034 |
hypothetical protein; Provisional |
5-79 |
1.91e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235680 [Multi-domain] Cd Length: 279 Bit Score: 39.69 E-value: 1.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509134745 5 LTALRDQIDEVDKALLGLLAKRLELVAEVGEVKSRYGL-PIYVPEREASMLasRR-QEAEALGVSPDLIEDVLRRLM 79
Cdd:PRK06034 11 LAELRWEIDAIDEELHQLLMERGDIIDRLIAVKRTQEVgSAFRPGREADMM--RRlVSRHRGILPLDTVESIWRVII 85
|
|
| DUF2325 |
pfam10087 |
Uncharacterized protein conserved in bacteria (DUF2325); Members of this family of ... |
101-148 |
5.69e-03 |
|
Uncharacterized protein conserved in bacteria (DUF2325); Members of this family of hypothetical bacterial proteins have no known function.
Pssm-ID: 431042 Cd Length: 94 Bit Score: 35.98 E-value: 5.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2509134745 101 VVIVGGRGQMGRLFEKMLTLSGYQVRILDKGDWDRSDEL---LKDAGMVII 148
Cdd:pfam10087 2 VLIVGGHDRMVRQYRDLCEKYGGKFKVFDGMKGGGVKRLekkIGSADLVVL 52
|
|
| |
