|
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: 809.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 1 MVAELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVMR 80
Cdd:PRK11199 1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 81 ESYSSENDKGFKTLHPNLRPVVIVGGGGQMGRLFEKMLTLSGYQVRILEKDDWARAADIVADAGMVIVSVPIHTTVETIG 160
Cdd:PRK11199 81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 161 RLPPLPADCILVDLASVKAEPLQAMLAAHQGPVLGLHPMFGPDSGSLAKQVVVYCDGRQPEAYQWFLEQIQVWGARLHRI 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVRLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSENNLALIKRY 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1030991022 321 YQRFGEAIGLLEQGDKQAFINSFRKVEHWFGDYAQRFQSESRTLLRQANDNRQ 373
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQ 373
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
101-352 |
6.47e-46 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 162.46 E-value: 6.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 101 VVIVGGGGQMGRLFEKMLTLSGYQVRILEKD--DWARAA------------DIVADAGMVIVSVPIHTTVETIGRLPP-L 165
Cdd:PRK08655 3 ISIIGGTGGLGKWFARFLKEKGFEVIVTGRDpkKGKEVAkelgveyandniDAAKDADIVIISVPINVTEDVIKEVAPhV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 166 PADCILVDLASVKAEPLQAML--AAHQGPVLGLHPMFGPDSGSLAKQVVV------YCDGRQPEAYQWFLEQiqvwGARL 237
Cdd:PRK08655 83 KEGSLLMDVTSVKERPVEAMEeyAPEGVEILPTHPMFGPRTPSLKGQVVIltptekRSNPWFDKVKNFLEKE----GARV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 238 HRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVRLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSENnlalI 317
Cdd:PRK08655 159 IVTSPEEHDRIMSVVQGLTHFAYISIASTLKRLGVDIKESRKFASPIYELMIDIIGRILGQNPYLYASIQMNNPQ----I 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 1030991022 318 KRYYQRFGEAI----GLLEQGDKQAFINSFRKVEHWFGD 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 |
6.00e-44 |
|
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: 146.97 E-value: 6.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 5 LTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVMRESYS 84
Cdd:TIGR01799 1 LEDLRGEIDGVDQELLHLLAKRLELVAQVGKVKHAAGLPIYAPEREAAMLAARREEAEKAGIAPDLIEDVLRRFMRESYA 80
|
...
gi 1030991022 85 SEN 87
Cdd:TIGR01799 81 NEN 83
|
|
| PheA |
COG1605 |
Chorismate mutase [Amino acid transport and metabolism]; Chorismate mutase is part of the ... |
3-168 |
2.10e-35 |
|
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: 127.19 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 3 AELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVMRES 82
Cdd:COG1605 5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 83 YSSENDKGFKTLHpnlrPVVIVGGGGQMGRLFEKMLTLSGYQVRILEKDDWARAADIVADAGMVIVSVPIHTTVETIGRL 162
Cdd:COG1605 85 IALQEKLLAEVAY----LGPEGGFTGQAAGKHFGGSAASLPAAAIDEVFREVEAGGAAYGVVPVENSTEGGVVETLDLLL 160
|
....*.
gi 1030991022 163 PPLPAD 168
Cdd:COG1605 161 ASPLKI 166
|
|
| FDXACB |
COG4937 |
Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis]; |
101-356 |
4.36e-29 |
|
Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443964 [Multi-domain] Cd Length: 443 Bit Score: 117.04 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 101 VVIVGGGGQMGRLFEKMLTLSGYQVRIL---EKDDWARAA---------DIVADAGMVIVSVPIHTTVETIGRLPPLPAD 168
Cdd:COG4937 7 IGIIGGTGEMGQWFAKFFKDFGFEVTIWgrgGKVEIAEKLgvgfandndAAIADADIIIVSVPIVITETTIVEVAPKMPK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 169 C-ILVDLASVKAEPLQAMLAAHQGPV--LGLHPMFGPDSGSLAKQVVVY------CDGRQPEAYQWFLEQiqvwGARLHR 239
Cdd:COG4937 87 GsLLMDLTSTKVKPVEAMEKYAPVDVeiLGTHPMFGPTPPTLSGQIVILtpiegrCDKWFPKIRNLLEEE----GARIII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 240 ISAVEHDQNMAFIQALRHFATFAYGLHLAEENVRLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSENNLALIKR 319
Cdd:COG4937 163 ITPEEHDRMMSVVQGLTHFAYISIGATIKRLDFDVKESRKFASPVYELMLDIIGRIIGQNPYLYASIQMENPEVKKVHET 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 1030991022 320 YYQRFGEAIGLLEQGDKQAFINSFRKVEHWFGDYAQR 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 |
4.98e-26 |
|
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: 99.49 E-value: 4.98e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1030991022 9 RDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVMRESYSSEN 87
Cdd:pfam01817 1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
|
|
| CM_2 |
smart00830 |
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ... |
9-87 |
4.30e-23 |
|
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: 91.49 E-value: 4.30e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1030991022 9 RDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVMRESYSSEN 87
Cdd:smart00830 1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
136-338 |
1.45e-21 |
|
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: 92.88 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 136 AADIVADAGMVIVSVPIHTTVETIGRLPP-LPADCILVDLASVKAEPLQAMLAAHQGPV--LGLHPMFGPD-SGSLA--- 208
Cdd:COG0287 55 LEEAVADADLVVLAVPVGATIEVLAELAPhLKPGAIVTDVGSVKGAVVEAAEALLPDGVrfVGGHPMAGTEkSGPEAada 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 209 ----KQVVVYC--DGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVRlEQLLALSS 282
Cdd:COG0287 135 dlfeGAPYILTptEGTDPEALERVEELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDE-EEILRLAA 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1030991022 283 PIYRlelAMVgRLFAQDPQLYADIIMS-SENNLALIKRYYQRFGEAIGLLEQGDKQA 338
Cdd:COG0287 214 GGFR---DTT-RIAASDPEMWRDIFLAnREALLEALDRFIEELDALRDALEAGDGEA 266
|
|
| PRK08818 |
PRK08818 |
prephenate dehydrogenase; Provisional |
98-361 |
5.52e-19 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 181561 [Multi-domain] Cd Length: 370 Bit Score: 87.23 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 98 LRPVV-IVGGGGQMGRLFEKMLTlSGYQVRILEKD----DWARAADIVADAGMVIVSVPIHTTVETIGRLPPLP----AD 168
Cdd:PRK08818 3 AQPVVgIVGSAGAYGRWLARFLR-TRMQLEVIGHDpadpGSLDPATLLQRADVLIFSAPIRHTAALIEEYVALAggraAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 169 CILVDLASVKAEPLQAMLAAhQGPVLGLHPMFGP-DSGSLAKQVVVYCDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQ 247
Cdd:PRK08818 82 QLWLDVTSIKQAPVAAMLAS-QAEVVGLHPMTAPpKSPTLKGRVMVVCEARLQHWSPWVQSLCSALQAECVYATPEHHDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 248 NMAFIQALRHfATfayglHLAEENV---------RLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSENNLALIK 318
Cdd:PRK08818 161 VMALVQAMVH-AT-----HLAQAGVlrdyapllgELRALMPYRSASFELDTAVIARILSLNPSIYEDIQFGNPYVGEMLD 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1030991022 319 RYYQRFGEAIGLLEQGDKQAFInSFRkvEHWFGDYAQRFQSES 361
Cdd:PRK08818 235 RLLAQLQELRALVAQGDDAARA-RFR--AQFLHANAQALQEDA 274
|
|
| PRK08507 |
PRK08507 |
prephenate dehydrogenase; Validated |
140-314 |
3.26e-13 |
|
prephenate dehydrogenase; Validated
Pssm-ID: 181452 [Multi-domain] Cd Length: 275 Bit Score: 69.15 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 140 VADAGMVIVSVPIHTTVETIGRLPPLPADCILVDLASVKAEPLQAMLAAHQGPVLGLHPM-----FGPDS---GSLAKQV 211
Cdd:PRK08507 56 LKKCDVIFLAIPVDAIIEILPKLLDIKENTTIIDLGSTKAKIIESVPKHIRKNFIAAHPMagtenSGPKAaikGLYEGKV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 212 VVYCDGRQP-EAYQWFLEQI-QVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLH-LAEENVRleQLLALSSPIYRle 288
Cdd:PRK08507 136 VVLCDVEKSgEKHQERAKEIfSGLGMRIVYMDAKEHDLHAAYISHLPHIISFALANTvLKEEDER--NIFDLAGGGFR-- 211
|
170 180
....*....|....*....|....*.
gi 1030991022 289 lAMVgRLFAQDPQLYADIIMSSENNL 314
Cdd:PRK08507 212 -SMS-RLAKSSPAMWSDIFKQNKENV 235
|
|
| CM_archaeal |
TIGR01791 |
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ... |
5-82 |
9.57e-13 |
|
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: 63.22 E-value: 9.57e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1030991022 5 LTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVMRES 82
Cdd:TIGR01791 1 IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEILMSLS 78
|
|
| PRK12595 |
PRK12595 |
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed |
1-55 |
2.69e-11 |
|
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
Pssm-ID: 183614 [Multi-domain] Cd Length: 360 Bit Score: 64.23 E-value: 2.69e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1030991022 1 MVAELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLA 55
Cdd:PRK12595 2 MNEELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLD 56
|
|
| PRK09239 |
PRK09239 |
chorismate mutase; Provisional |
1-81 |
3.39e-11 |
|
chorismate mutase; Provisional
Pssm-ID: 181719 [Multi-domain] Cd Length: 104 Bit Score: 59.65 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 1 MVAELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVMR 80
Cdd:PRK09239 8 APAELAALRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKDANLDPDFAEKFLNFIIK 87
|
.
gi 1030991022 81 E 81
Cdd:PRK09239 88 E 88
|
|
| CM_P2 |
TIGR01807 |
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of ... |
5-79 |
1.75e-10 |
|
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: 56.69 E-value: 1.75e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1030991022 5 LTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQY--GLPIYVPEREAAMLasRREEAAALG-VPPDLIEDVLRRVM 79
Cdd:TIGR01807 1 LEELRNKIDAIDDRILDLLSERATYAQAVGELKGSGasGASFYRPEREAQVI--RRLQNLNKGpLDQEAIARIFREIM 76
|
|
| PDH_C |
pfam20463 |
Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate ... |
241-344 |
3.31e-10 |
|
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: 56.62 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVRLEQLLALSSPIYRLelamVGRLFAQDPQLYADIIMSSENNLA-LIKR 319
Cdd:pfam20463 1 SPETHDRVVAVVSHLPHFVAIALAATLAELGVDIKEARKLASGGFRD----MTRIAGSNPELWADIQTHNARAVLeALDD 76
|
90 100
....*....|....*....|....*
gi 1030991022 320 YYQRFGEAIGLLEQGDKQAFINSFR 344
Cdd:pfam20463 77 FIAELKQLKELIRNGDWEELVEYMK 101
|
|
| PRK06285 |
PRK06285 |
chorismate mutase; Provisional |
4-79 |
6.48e-10 |
|
chorismate mutase; Provisional
Pssm-ID: 180509 [Multi-domain] Cd Length: 96 Bit Score: 55.43 E-value: 6.48e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1030991022 4 ELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVM 79
Cdd:PRK06285 8 RLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENIGLKIMKILM 83
|
|
| PRK07075 |
PRK07075 |
isochorismate lyase; |
5-73 |
7.06e-09 |
|
isochorismate lyase;
Pssm-ID: 136191 [Multi-domain] Cd Length: 101 Bit Score: 52.81 E-value: 7.06e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 5 LTALRDQIDEVDKALLSLLAKRLELVAEVGEVK-SQYGLPiyVPEREAAMLASRREEAAALGVPPDLIED 73
Cdd:PRK07075 10 LDDIREAIDRLDRDIIAALGRRMQYVKAASRFKpSEASIP--APERVAAMLPERRRWAEQAGLDADFVEK 77
|
|
| PRK07248 |
PRK07248 |
chorismate mutase; |
4-56 |
8.03e-09 |
|
chorismate mutase;
Pssm-ID: 168880 [Multi-domain] Cd Length: 87 Bit Score: 52.37 E-value: 8.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1030991022 4 ELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLAS 56
Cdd:PRK07248 2 DLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDK 54
|
|
| CM_mono_grmpos |
TIGR01805 |
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade ... |
5-58 |
9.65e-09 |
|
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: 51.70 E-value: 9.65e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1030991022 5 LTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRR 58
Cdd:TIGR01805 1 LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCT 54
|
|
| PRK06545 |
PRK06545 |
prephenate dehydrogenase; Validated |
131-338 |
3.50e-08 |
|
prephenate dehydrogenase; Validated
Pssm-ID: 235824 [Multi-domain] Cd Length: 359 Bit Score: 54.53 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 131 DDWARAAdivADAGMVIVSVPIHTTVETIGRLP--PLPADCILVDLASVKAEPLQA--MLAAHQGPVLGLHPMFGPD-SG 205
Cdd:PRK06545 52 ADLQRAA---AEADLIVLAVPVDATAALLAELAdlELKPGVIVTDVGSVKGAILAEaeALLGDLIRFVGGHPMAGSHkSG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 206 SLAKQ---------VVVYCDGRQPEAyqwfLEQIQVW----GARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENv 272
Cdd:PRK06545 129 VAAARadlfenapwVLTPDDHTDPDA----VAELKDLlsgtGAKFVVLDAEEHDRAVALVSHLPHILASSLAARLAGEH- 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1030991022 273 rleqLLALSspiyrleLAMVG-----RLFAQDPQLYADIIMSSENNLA-LIKRYYQRFGEAIGLLEQGDKQA 338
Cdd:PRK06545 204 ----PLALR-------LAAGGfrditRIASSDPGMWRDILESNAEALLdALDEWIEDLDRARDALESGDAEA 264
|
|
| PLN02256 |
PLN02256 |
arogenate dehydrogenase |
146-257 |
3.10e-07 |
|
arogenate dehydrogenase
Pssm-ID: 215144 [Multi-domain] Cd Length: 304 Bit Score: 51.59 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 146 VIVSVPIHTTVETIGRLP--PLPADCILVDLASVKAEPLQAMLAA--HQGPVLGLHPMFGPDSG--SLAKQVVVY----- 214
Cdd:PLN02256 96 VLLCTSILSTEAVLRSLPlqRLKRSTLFVDVLSVKEFPKNLLLQVlpEEFDILCTHPMFGPESGkgGWAGLPFVYdkvri 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1030991022 215 -CDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRH 257
Cdd:PLN02256 176 gDEGEREARCERFLDIFEEEGCRMVEMSCEEHDRYAAGSQFITH 219
|
|
| PRK06444 |
PRK06444 |
prephenate dehydrogenase; Provisional |
101-255 |
5.64e-07 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 102381 [Multi-domain] Cd Length: 197 Bit Score: 49.46 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 101 VVIVGGGGQMGRLFEKMLTLSGYQVRIlekddwaRAADIvadagmVIVSVPIHTTVETIGRLpplpaDCILVDLASVKAe 180
Cdd:PRK06444 3 EIIIGKNGRLGRVLCSILDDNGLGVYI-------KKADH------AFLSVPIDAALNYIESY-----DNNFVEISSVKW- 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1030991022 181 PLQamlaAHQGPVLGLHPMFGPDS--GSLAKQVVVYCDGRQPEaYQWFLEQIqVWGARLHRISAVEHDQNMAFIQAL 255
Cdd:PRK06444 64 PFK----KYSGKIVSIHPLFGPMSynDGVHRTVIFINDISRDN-YLNEINEM-FRGYHFVEMTADEHDLLMSEIMVK 134
|
|
| PDH_N |
pfam02153 |
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ... |
130-237 |
8.77e-07 |
|
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: 48.15 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 130 KDDWARAADIVADAGMVIVSVPIHTTVETIGRL-PPLPADCILVDLASVKAEP---LQAMLAAHQgpVLGLHPMFGPDS- 204
Cdd:pfam02153 33 GDEATDDIEAVREADIVFLAVPVEQTLPVLKELaPHLKEDALITDVGSVKVKIireLEQHLPDKS--FVPGHPMAGTEKs 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1030991022 205 -------GSLAKQVVVYCDGRQPEAyQWFLEQIQVW---GARL 237
Cdd:pfam02153 111 gpdaaraNLFENAPVILTPTEKTDT-EALNCVKELLegvGARV 152
|
|
| PLN02712 |
PLN02712 |
arogenate dehydrogenase |
106-365 |
9.19e-07 |
|
arogenate dehydrogenase
Pssm-ID: 215382 [Multi-domain] Cd Length: 667 Bit Score: 50.75 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 106 GGGQMGRLFEKMLTLSGYQVRILEKDDWARAA------------DIVADAGMVIV-SVPIHTTVETIGRLP--PLPADCI 170
Cdd:PLN02712 376 GFGNFGQFLAKTMVKQGHTVLAYSRSDYSDEAqklgvsyfsdadDLCEEHPEVILlCTSILSTEKVLKSLPfqRLKRSTL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 171 LVDLASVKAEPlQAMLAAHQGP---VLGLHPMFGPDSGS--------LAKQVVVYCDGRQPEAYQWFLEQIQVWGARLHR 239
Cdd:PLN02712 456 FVDVLSVKEFP-RNLFLQHLPQdfdILCTHPMFGPESGKngwnnlafVFDKVRIGSDDRRVSRCDSFLDIFAREGCRMVE 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 240 ISAVEHDQNMAFIQalrhFATFAYGLhlaeenvRLEQLLALSSPI----YRLELAMVGRLFAQDPQLYADIIMSSENNLA 315
Cdd:PLN02712 535 MSCAEHDWHAAGSQ----FITHTMGR-------LLEKLGLESTPIntkgYETLLNLVENTAGDSFDLYYGLFMYNVNAME 603
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1030991022 316 LIKRYY--------QRFGEAIGLLEqgdKQAFINSFRKVEHWFGDYAQRFQSESRTLL 365
Cdd:PLN02712 604 QLERLDlafeslkkQLFGRLHGVLR---KQLFKSSEKSQVLREESLVSKVSQKTAALL 658
|
|
| CM_M_hiGC-arch |
TIGR01808 |
monofunctional chorismate mutase, high GC gram positive type; This model represents the ... |
4-76 |
1.05e-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: 46.05 E-value: 1.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1030991022 4 ELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLaSRREEAAALGvpPDLIEDVLR 76
Cdd:TIGR01808 1 EIDTLREEIDRLDAEILALVKRRAEISQAIGKARMASGGTRLVHSREMKVI-ERYSELGPEG--KDLAIKLLR 70
|
|
| PRK07417 |
PRK07417 |
prephenate/arogenate dehydrogenase; |
139-338 |
1.91e-06 |
|
prephenate/arogenate dehydrogenase;
Pssm-ID: 180970 [Multi-domain] Cd Length: 279 Bit Score: 48.74 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 139 IVADAGMVIVSVPIHTTVETIGRL-PPLPADCILVDLASVKAEPLQAMLAAHQGPVlGLHPMFG-PDSGSLAKQ------ 210
Cdd:PRK07417 54 LLKDCDLVILALPIGLLLPPSEQLiPALPPEAIVTDVGSVKAPIVEAWEKLHPRFV-GSHPMAGtAESGVEAGQrglfkn 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 211 ---VVVYCDGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEEN----VRLEQLLALSSp 283
Cdd:PRK07417 133 rpwVLTPTENTDLNALAIVEELAVSLGSKIYTADPEEHDRAVALISHLPVMVSAALIQTCGTEKdpsvLKLAQNLASSG- 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1030991022 284 iyrleLAMVGRLFAQDPQLYADiiMSSENNLAL---IKRYYQRFGEAIGLLEQGDKQA 338
Cdd:PRK07417 212 -----FADTSRVGGGNPELGVM--MAEYNRAALlrsLASYRQSLDQLEELIEQENWSA 262
|
|
| PRK14806 |
PRK14806 |
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ... |
137-343 |
4.38e-06 |
|
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 237820 [Multi-domain] Cd Length: 735 Bit Score: 48.84 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 137 ADIVADAGMVIVSVPIHTTVETIGRLPPLPA-DCILVDLASVKAEPLQAMLAAHQG-P---VLGlHPMFGPD-SGSLAKQ 210
Cdd:PRK14806 58 AEAVSGADVIVLAVPVLAMEKVLADLKPLLSeHAIVTDVGSTKGNVVDAARAVFGElPagfVPG-HPIAGSEkSGVHAAN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 211 VVVYCDGR-----QPEAYQWFLEQI-QVW---GARLHRISAVEHDQNMAFIQALRHFatFAYGL--HLAEENVRLEqlla 279
Cdd:PRK14806 137 ADLFRNHKviltpLAETDPAALARVdRLWravGADVLHMDVAHHDEVLAATSHLPHL--LAFSLvdQLANREDNLD---- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1030991022 280 lsspIYRleLAMVG-----RLFAQDPQLYADIIMSSE----NNLALIKRYYQRFGEAIgllEQGDKQAFINSF 343
Cdd:PRK14806 211 ----IFR--YAAGGfrdftRIAASDPVMWHDIFLANKeavlRALDHFRDDLDALRAAI---EAGDGHALLGVF 274
|
|
| PRK09269 |
PRK09269 |
chorismate mutase; Provisional |
19-76 |
2.03e-05 |
|
chorismate mutase; Provisional
Pssm-ID: 236441 Cd Length: 193 Bit Score: 44.98 E-value: 2.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1030991022 19 LLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLR 76
Cdd:PRK09269 37 LVDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAPAHGVDPDYVRRFFR 94
|
|
| pheA |
PRK10622 |
bifunctional chorismate mutase/prephenate dehydratase; Provisional |
5-54 |
2.66e-05 |
|
bifunctional chorismate mutase/prephenate dehydratase; Provisional
Pssm-ID: 182594 [Multi-domain] Cd Length: 386 Bit Score: 45.88 E-value: 2.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1030991022 5 LTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAML 54
Cdd:PRK10622 7 LLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLL 56
|
|
| CM_P_1 |
TIGR01797 |
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ... |
5-54 |
2.75e-05 |
|
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: 42.11 E-value: 2.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1030991022 5 LTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAML 54
Cdd:TIGR01797 1 LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLL 50
|
|
| PLN02712 |
PLN02712 |
arogenate dehydrogenase |
96-355 |
4.86e-05 |
|
arogenate dehydrogenase
Pssm-ID: 215382 [Multi-domain] Cd Length: 667 Bit Score: 45.36 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 96 PNLRPVVIvgGGGQMGRLFEKMLTLSGYQVRILEKDDWARAA-----DIVAD--------AGMVIVSVPIHTTVETIGRL 162
Cdd:PLN02712 51 TQLKIAII--GFGNYGQFLAKTLISQGHTVLAHSRSDHSLAArslgvSFFLDphdlcerhPDVILLCTSIISTENVLKSL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 163 P--PLPADCILVDLASVK--AEPLQAMLAAHQGPVLGLHPMFGPDSGSLA--------KQVVVYCDGRQPEAYQWFLEQI 230
Cdd:PLN02712 129 PlqRLKRNTLFVDVLSVKefAKNLLLDYLPEDFDIICSHPMFGPQSAKHGwdglrfvyEKVRIGNEELRVSRCKSFLEVF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 231 QVWGARLHRISAVEHDQNMAFIQalrhFATFAYGlhlaeenvRLEQLLAL-SSPI----YRLELAMVGRLFAQDPQLYAD 305
Cdd:PLN02712 209 EREGCKMVEMSCTEHDKYAAESQ----FITHTVG--------RVLEMLKLeSTPIntkgYESLLDLVENTCGDSFDLYYG 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1030991022 306 IIMSSENNLALIKRY--------YQRFGEAIGLLEqgdKQAFINSFRKVeHWFGDYAQ 355
Cdd:PLN02712 277 LFMYNKNSLEMLERLdlafealrKQLFGRLHGVVR---KQLFGNEEKKV-HVQPNHAE 330
|
|
| CM_mono2 |
TIGR01806 |
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ... |
19-72 |
1.15e-04 |
|
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: 41.26 E-value: 1.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1030991022 19 LLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIE 72
Cdd:TIGR01806 9 LVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVT 62
|
|
| PRK08055 |
PRK08055 |
chorismate mutase; Provisional |
13-79 |
1.35e-04 |
|
chorismate mutase; Provisional
Pssm-ID: 236143 Cd Length: 181 Bit Score: 42.37 E-value: 1.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1030991022 13 DEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEAAALGVPPDLIEDVLRRVM 79
Cdd:PRK08055 24 AVSLGALATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLDPESIKPFIVAQM 90
|
|
| PRK07857 |
PRK07857 |
chorismate mutase; |
3-76 |
1.90e-04 |
|
chorismate mutase;
Pssm-ID: 236117 Cd Length: 106 Bit Score: 40.44 E-value: 1.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1030991022 3 AELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAMLASRREEaaaLGVP-PDLIEDVLR 76
Cdd:PRK07857 28 AEIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIERYREE---LGPEgKDLAMLLLR 99
|
|
| PRK06443 |
PRK06443 |
chorismate mutase; Validated |
1-53 |
2.61e-04 |
|
chorismate mutase; Validated
Pssm-ID: 235801 Cd Length: 177 Bit Score: 41.43 E-value: 2.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1030991022 1 MVA--ELTALRDQIDEVDKALLSLLAKRLELVAEVGEVKSQYGLPIYVPEREAAM 53
Cdd:PRK06443 1 MVHfiDMEDLRSEILENTMDIIELIEKRRELARMIGIIKMRNGLSIRDSERENYV 55
|
|
| PRK06034 |
PRK06034 |
hypothetical protein; Provisional |
5-79 |
5.76e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235680 [Multi-domain] Cd Length: 279 Bit Score: 41.23 E-value: 5.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1030991022 5 LTALRDQIDEVDKALLSLLAKRLELVAEVGEVK-SQYGLPIYVPEREAAM---LASRREEAAalgvPPDLIEDVLRRVM 79
Cdd:PRK06034 11 LAELRWEIDAIDEELHQLLMERGDIIDRLIAVKrTQEVGSAFRPGREADMmrrLVSRHRGIL----PLDTVESIWRVII 85
|
|
| PRK11861 |
PRK11861 |
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional |
146-314 |
1.19e-03 |
|
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
Pssm-ID: 183343 [Multi-domain] Cd Length: 673 Bit Score: 40.84 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 146 VIVSVPIHTTVETIGRLPP-LPADCILVDLASVKAEPL---QAMLAAHQGPVLGLHPMFGPDSGSLAKQVVVYCDGRQ-- 219
Cdd:PRK11861 1 VLLAAPVAQTGPLLARIAPfLDASTIVTDAGSTKSDVVaaaRAALGARIGQFVPGHPIAGRESSGVDAALADLYVGRNvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 220 ----PEAYQWFLEQIQ-VWGAR---LHRISAVEHDQNMAFIQALRHFATFAYglhlaeenvrLEQLLALSSPIYRLELAM 291
Cdd:PRK11861 81 lcalPENAPDALARVEaMWRAAradVRAMSAEQHDRVFAAVSHLPHVLSFAL----------VEQILGESDAELKFSYAA 150
|
170 180
....*....|....*....|....*...
gi 1030991022 292 VG-----RLFAQDPQLYADIIMSSENNL 314
Cdd:PRK11861 151 GGfrdftRIAASSPEMWRDVCLANRAAL 178
|
|
| PRK07502 |
PRK07502 |
prephenate/arogenate dehydrogenase family protein; |
136-343 |
1.67e-03 |
|
prephenate/arogenate dehydrogenase family protein;
Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 39.95 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 136 AADIVADAGMVIVSVPIHTTVE---TIGrlPPLPADCILVDLASVKAEPLQAM---LAAHQGPVLGlHPMF-----GPDS 204
Cdd:PRK07502 60 AAEAVKGADLVILCVPVGASGAvaaEIA--PHLKPGAIVTDVGSVKASVIAAMaphLPEGVHFIPG-HPLAgtehsGPDA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030991022 205 GSLAKQVVVYC-----DGRQPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFatFAYGL-----HLaeENVRL 274
Cdd:PRK07502 137 GFAELFENRWCiltppEGTDPAAVARLTAFWRALGARVEEMDPEHHDLVLAITSHLPHL--IAYTIvgtadDL--ERVTE 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1030991022 275 EQLLALSSPIYRlelaMVGRLFAQDPQLYADIIMsseNNLALIKRYYQRFGEAIGLLEQ----GDKQAFINSF 343
Cdd:PRK07502 213 SEVIKYSASGFR----DFTRIAASDPTMWRDVFL---HNKDAVLEMLGRFTEDLAALQRairwGDGDALFDLF 278
|
|
| |
