|
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: 807.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 1 MVAELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMR 80
Cdd:PRK11199 1 MVAELTALRDQIDEVDKQLLELLAKRLELVAQVGEVKSRHGLPIYVPEREAAMLASRRAEAEALGVPPDLIEDVLRRVMR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 81 ESYSSENDKGFKTLCPALRPVVIVGGGGQMGRLFEKMLTLSGYQVRILEQHDWDRAADIVADAGMVIVSVPIHVTEQVIG 160
Cdd:PRK11199 81 ESYSSENDKGFKTLNPDLRPVVIVGGKGQLGRLFAKMLTLSGYQVRILEQDDWDRAEDILADAGMVIVSVPIHLTEEVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 161 KLPPLPKDCILVDLASVKNGPLQAMLAAHDGPVLGLHPMFGPDSGSLAKQVVVWCDGRKPEAYQWFLEQIQVWGARLHRI 240
Cdd:PRK11199 161 RLPPLPEDCILVDLTSVKNAPLQAMLAAHSGPVLGLHPMFGPDVGSLAKQVVVVCDGRQPEAYQWLLEQIQVWGARLHRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSERNLALIKRY 320
Cdd:PRK11199 241 SAVEHDQNMAFIQALRHFATFAYGLHLAKENVDLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSPENLALIKRY 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446147349 321 YKRFGEAIELLEQGDKQAFIDSFRKVEHWFGDYAQRFQSESRVLLRQANDNRQ 373
Cdd:PRK11199 321 YQRFGEALELLEQGDKQAFIDSFRKVEHWFGDYAEQFLKESRSLLQQANDNRQ 373
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
101-352 |
4.27e-50 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 173.63 E-value: 4.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 101 VVIVGGGGQMGRLFEKMLTLSGYQVrILEQHDWDRAADI---------------VADAGMVIVSVPIHVTEQVIGKLPP- 164
Cdd:PRK08655 3 ISIIGGTGGLGKWFARFLKEKGFEV-IVTGRDPKKGKEVakelgveyandnidaAKDADIVIISVPINVTEDVIKEVAPh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 165 LPKDCILVDLASVKNGPLQAML--AAHDGPVLGLHPMFGPDSGSLAKQVVVWC--DGRK----PEAYQWFLEQiqvwGAR 236
Cdd:PRK08655 82 VKEGSLLMDVTSVKERPVEAMEeyAPEGVEILPTHPMFGPRTPSLKGQVVILTptEKRSnpwfDKVKNFLEKE----GAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 237 LHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSERNLAL 316
Cdd:PRK08655 158 VIVTSPEEHDRIMSVVQGLTHFAYISIASTLKRLGVDIKESRKFASPIYELMIDIIGRILGQNPYLYASIQMNNPQIPEI 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 446147349 317 IKRYYKRFGEAIELLEQGDKQAFIDSFRKVEHWFGD 352
Cdd:PRK08655 238 HETFIKECEELSELVKNGDREEFVERMKEAAKHFGD 273
|
|
| CM_T |
TIGR01799 |
chorismate mutase domain of T-protein; This model represents the chorismate mutase domain of ... |
5-87 |
1.01e-45 |
|
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: 151.59 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 5 LTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYS 84
Cdd:TIGR01799 1 LEDLRGEIDGVDQELLHLLAKRLELVAQVGKVKHAAGLPIYAPEREAAMLAARREEAEKAGIAPDLIEDVLRRFMRESYA 80
|
...
gi 446147349 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 |
3.96e-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: 126.42 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 3 AELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRES 82
Cdd:COG1605 5 ESLEELRAEIDEIDRQLLELLAERAELAKEVGELKKEHGLPIYDPEREAEVLERLRELAEELGLDPEFVEAIFREIISES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 83 YSSENDKGFKTLCPAlrpvVIVGGGGQMGRLFEKMLTLSGYQVRILEQHDWDRAADIVADAGMVIVSVPIHVTEQVIGKL 162
Cdd:COG1605 85 IALQEKLLAEVAYLG----PEGGFTGQAAGKHFGGSAASLPAAAIDEVFREVEAGGAAYGVVPVENSTEGGVVETLDLLL 160
|
....*.
gi 446147349 163 PPLPKD 168
Cdd:COG1605 161 ASPLKI 166
|
|
| FDXACB |
COG4937 |
Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis]; |
101-356 |
1.40e-29 |
|
Ferredoxin-fold anticodon binding domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443964 [Multi-domain] Cd Length: 443 Bit Score: 118.20 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 101 VVIVGGGGQMGRLFEKMLTLSGYQVRILEQHDWDRAA------------DIVADAGMVIVSVPIHVTEQVIGKLPPLPKD 168
Cdd:COG4937 7 IGIIGGTGEMGQWFAKFFKDFGFEVTIWGRGGKVEIAeklgvgfandndAAIADADIIIVSVPIVITETTIVEVAPKMPK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 169 C-ILVDLASVKNGPLQAMLAAHDGPV--LGLHPMFGPDSGSLAKQVVVWC--DGRKPEayqWFLEQIQVW---GARLHRI 240
Cdd:COG4937 87 GsLLMDLTSTKVKPVEAMEKYAPVDVeiLGTHPMFGPTPPTLSGQIVILTpiEGRCDK---WFPKIRNLLeeeGARIIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSERNLALIKRY 320
Cdd:COG4937 164 TPEEHDRMMSVVQGLTHFAYISIGATIKRLDFDVKESRKFASPVYELMLDIIGRIIGQNPYLYASIQMENPEVKKVHETF 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 446147349 321 YKRFGEAIELLEQGDKQAFIDSFRKVEHWFGDYAQR 356
Cdd:COG4937 244 IEECNELSNIVRKDDEEGFVEIMKEAAKHFGDTESA 279
|
|
| CM_2 |
pfam01817 |
Chorismate mutase type II; Chorismate mutase EC:5.4.99.5 catalyzes the conversion of ... |
9-87 |
8.79e-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: 96.02 E-value: 8.79e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446147349 9 RDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYSSEN 87
Cdd:pfam01817 1 RAEIDEIDREILELLAERMELAREIGEYKKENGLPVYDPEREEEVLERLRAGAEELGLDPDFIEAIFREIISESRALQK 79
|
|
| CM_2 |
smart00830 |
Chorismate mutase type II; Chorismate mutase, catalyses the conversion of chorismate to ... |
9-87 |
3.29e-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: 91.87 E-value: 3.29e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446147349 9 RDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYSSEN 87
Cdd:smart00830 1 RAEIDAIDDQILALLAERAALAREVARLKAKNGLPIRDPEREAEVLERLRALAEGPGLDPELVERIFREIIEASIALQK 79
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
136-345 |
8.23e-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: 88.26 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 136 AADIVADAGMVIVSVPIHVTEQVIGKLPP-LPKDCILVDLASVKNGPLQAM--LAAHDGPVLGLHPMFGPD-SGSLA--- 208
Cdd:COG0287 55 LEEAVADADLVVLAVPVGATIEVLAELAPhLKPGAIVTDVGSVKGAVVEAAeaLLPDGVRFVGGHPMAGTEkSGPEAada 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 209 -----KQVVVwC--DGRKPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVQlEQLLALS 281
Cdd:COG0287 135 dlfegAPYIL-TptEGTDPEALERVEELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDE-EEILRLA 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446147349 282 SPIYRlelAMVgRLFAQDPQLYADIIMS-SERNLALIKRYYKRFGEAIELLEQGDKQAFIDSFRK 345
Cdd:COG0287 213 AGGFR---DTT-RIAASDPEMWRDIFLAnREALLEALDRFIEELDALRDALEAGDGEALEELLER 273
|
|
| PRK08818 |
PRK08818 |
prephenate dehydrogenase; Provisional |
98-361 |
5.92e-18 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 181561 [Multi-domain] Cd Length: 370 Bit Score: 84.14 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 98 LRPVV-IVGGGGQMGR-----LFEKM-LTLSGYQVRILEQHDwdrAADIVADAGMVIVSVPIHVTEQVIGKLPPLP---- 166
Cdd:PRK08818 3 AQPVVgIVGSAGAYGRwlarfLRTRMqLEVIGHDPADPGSLD---PATLLQRADVLIFSAPIRHTAALIEEYVALAggra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 167 KDCILVDLASVKNGPLQAMLAAHdGPVLGLHPMFGP-DSGSLAKQVVVWCDGRKPEAYQWFLEQIQVWGARLHRISAVEH 245
Cdd:PRK08818 80 AGQLWLDVTSIKQAPVAAMLASQ-AEVVGLHPMTAPpKSPTLKGRVMVVCEARLQHWSPWVQSLCSALQAECVYATPEHH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 246 DQNMAFIQALRHfATfayglHLAEENV---------QLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSERNLAL 316
Cdd:PRK08818 159 DRVMALVQAMVH-AT-----HLAQAGVlrdyapllgELRALMPYRSASFELDTAVIARILSLNPSIYEDIQFGNPYVGEM 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446147349 317 IKRYYKRFGEAIELLEQGDKQAFIdSFRkvEHWFGDYAQRFQSES 361
Cdd:PRK08818 233 LDRLLAQLQELRALVAQGDDAARA-RFR--AQFLHANAQALQEDA 274
|
|
| PRK08507 |
PRK08507 |
prephenate dehydrogenase; Validated |
140-335 |
4.16e-12 |
|
prephenate dehydrogenase; Validated
Pssm-ID: 181452 [Multi-domain] Cd Length: 275 Bit Score: 65.69 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 140 VADAGMVIVSVPIHVTEQVIGKLPPLPKDCILVDLASVKNGPLQAMLAAHDGPVLGLHPM-----FGPDS---GSLAKQV 211
Cdd:PRK08507 56 LKKCDVIFLAIPVDAIIEILPKLLDIKENTTIIDLGSTKAKIIESVPKHIRKNFIAAHPMagtenSGPKAaikGLYEGKV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 212 VVWCDGRKP-EAYQWFLEQI-QVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLH-LAEENVQleQLLALSSPIYRle 288
Cdd:PRK08507 136 VVLCDVEKSgEKHQERAKEIfSGLGMRIVYMDAKEHDLHAAYISHLPHIISFALANTvLKEEDER--NIFDLAGGGFR-- 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446147349 289 lAMVgRLFAQDPQLYADIIMSSERN-LALIKRYYKRFGEAIELLEQGD 335
Cdd:PRK08507 212 -SMS-RLAKSSPAMWSDIFKQNKENvLEAIDEFIKELEQFKQLIENED 257
|
|
| CM_archaeal |
TIGR01791 |
chorismate mutase, archaeal type; This model represents a clade of archaeal chorismate mutases. ... |
5-82 |
1.04e-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: 60.13 E-value: 1.04e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446147349 5 LTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRES 82
Cdd:TIGR01791 1 IEELRQEIEEIDKSILDLIEKRIKIARKIGEIKHNNGLPITDEEREERVIERLRNTARNLGLDVLKLKEIFEILMSLS 78
|
|
| PDH_C |
pfam20463 |
Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate ... |
241-344 |
1.29e-11 |
|
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: 60.48 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 241 SAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLelamVGRLFAQDPQLYADIIMSSERNLA-LIKR 319
Cdd:pfam20463 1 SPETHDRVVAVVSHLPHFVAIALAATLAELGVDIKEARKLASGGFRD----MTRIAGSNPELWADIQTHNARAVLeALDD 76
|
90 100
....*....|....*....|....*
gi 446147349 320 YYKRFGEAIELLEQGDKQAFIDSFR 344
Cdd:pfam20463 77 FIAELKQLKELIRNGDWEELVEYMK 101
|
|
| PRK09239 |
PRK09239 |
chorismate mutase; Provisional |
1-81 |
2.62e-11 |
|
chorismate mutase; Provisional
Pssm-ID: 181719 [Multi-domain] Cd Length: 104 Bit Score: 59.65 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 1 MVAELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMR 80
Cdd:PRK09239 8 APAELAALRQSIDNIDAALIHMLAERFKCTQAVGVLKAEHGLPPADPAREAYQIERLRQLAKDANLDPDFAEKFLNFIIK 87
|
.
gi 446147349 81 E 81
Cdd:PRK09239 88 E 88
|
|
| PRK12595 |
PRK12595 |
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed |
1-55 |
8.15e-11 |
|
bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed
Pssm-ID: 183614 [Multi-domain] Cd Length: 360 Bit Score: 62.69 E-value: 8.15e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446147349 1 MVAELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLA 55
Cdd:PRK12595 2 MNEELEQLRKEIDEINLQLLELLSKRGELVQEIGEEKTKQGTKRYDPVREREMLD 56
|
|
| PRK06285 |
PRK06285 |
chorismate mutase; Provisional |
4-79 |
5.60e-10 |
|
chorismate mutase; Provisional
Pssm-ID: 180509 [Multi-domain] Cd Length: 96 Bit Score: 55.81 E-value: 5.60e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446147349 4 ELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVM 79
Cdd:PRK06285 8 RLNEIRKRIDEIDEQIIDLIAERTSLAKEIAELKKSLGMPIFDPEREDYIHEKIRKLCEEHNIDENIGLKIMKILM 83
|
|
| CM_P2 |
TIGR01807 |
chorismate mutase domain of proteobacterial P-protein, clade 2; This model represents one of ... |
5-79 |
3.61e-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: 52.84 E-value: 3.61e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446147349 5 LTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRF--GLPIYVPEREASMLasRRAEAEALG-VPPDLIEDVLRRVM 79
Cdd:TIGR01807 1 LEELRNKIDAIDDRILDLLSERATYAQAVGELKGSGasGASFYRPEREAQVI--RRLQNLNKGpLDQEAIARIFREIM 76
|
|
| CM_mono_grmpos |
TIGR01805 |
monofunctional chorismate mutase, gram positive-type, clade 2; This model represents a clade ... |
5-62 |
1.21e-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: 51.70 E-value: 1.21e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446147349 5 LTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAE 62
Cdd:TIGR01805 1 LELIRKKIDEIDDKLVVLFEERMEVVKEIAAYKKKNGIPIFDSKREQEIIDKCTKNVE 58
|
|
| PLN02712 |
PLN02712 |
arogenate dehydrogenase |
106-257 |
1.55e-08 |
|
arogenate dehydrogenase
Pssm-ID: 215382 [Multi-domain] Cd Length: 667 Bit Score: 56.53 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 106 GGGQMGRLFEKMLTLSGYQVRILEQHDW-DRAADI----VADAG--------MVIVSVPIHVTEQVIGKLP--PLPKDCI 170
Cdd:PLN02712 376 GFGNFGQFLAKTMVKQGHTVLAYSRSDYsDEAQKLgvsyFSDADdlceehpeVILLCTSILSTEKVLKSLPfqRLKRSTL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 171 LVDLASVKNGPLQAMLAA--HDGPVLGLHPMFGPDSGS--------LAKQVVVWCDGRKPEAYQWFLEQIQVWGARLHRI 240
Cdd:PLN02712 456 FVDVLSVKEFPRNLFLQHlpQDFDILCTHPMFGPESGKngwnnlafVFDKVRIGSDDRRVSRCDSFLDIFAREGCRMVEM 535
|
170
....*....|....*..
gi 446147349 241 SAVEHDQNMAFIQALRH 257
Cdd:PLN02712 536 SCAEHDWHAAGSQFITH 552
|
|
| PRK07248 |
PRK07248 |
chorismate mutase; |
4-62 |
3.76e-08 |
|
chorismate mutase;
Pssm-ID: 168880 [Multi-domain] Cd Length: 87 Bit Score: 50.45 E-value: 3.76e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446147349 4 ELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAE 62
Cdd:PRK07248 2 DLEEIRQEIDQIDDQLVALLEKRMALVEQVVAYKKATGKPVLDTKREQVILDKVSSLVE 60
|
|
| PRK06545 |
PRK06545 |
prephenate dehydrogenase; Validated |
99-338 |
1.27e-07 |
|
prephenate dehydrogenase; Validated
Pssm-ID: 235824 [Multi-domain] Cd Length: 359 Bit Score: 52.99 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 99 RPVVIVG-G--GGQMGRlfekMLTLSGYQVRIleqHDWDRAA---------DIVADAG-----------MVIVSVPIHVT 155
Cdd:PRK06545 1 RTVLIVGlGliGGSLAL----AIKAAGPDVFI---IGYDPSAaqlaralgfGVIDELAadlqraaaeadLIVLAVPVDAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 156 EQVIGKLP--PLPKDCILVDLASVKNGPLQAMLAAHDGPV--LGLHPMFGPD-SGSLAKQ---------VVVWCDGRKPE 221
Cdd:PRK06545 74 AALLAELAdlELKPGVIVTDVGSVKGAILAEAEALLGDLIrfVGGHPMAGSHkSGVAAARadlfenapwVLTPDDHTDPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 222 AyqwfLEQIQVW----GARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENvqleqLLALSspiyrleLAMVG---- 293
Cdd:PRK06545 154 A----VAELKDLlsgtGAKFVVLDAEEHDRAVALVSHLPHILASSLAARLAGEH-----PLALR-------LAAGGfrdi 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446147349 294 -RLFAQDPQLYADIIMS-SERNLALIKRYYKRFGEAIELLEQGDKQA 338
Cdd:PRK06545 218 tRIASSDPGMWRDILESnAEALLDALDEWIEDLDRARDALESGDAEA 264
|
|
| PRK07075 |
PRK07075 |
isochorismate lyase; |
5-73 |
1.33e-07 |
|
isochorismate lyase;
Pssm-ID: 136191 [Multi-domain] Cd Length: 101 Bit Score: 49.35 E-value: 1.33e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446147349 5 LTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRfGLPIYVPEREASMLASRRAEAEALGVPPDLIED 73
Cdd:PRK07075 10 LDDIREAIDRLDRDIIAALGRRMQYVKAASRFKPS-EASIPAPERVAAMLPERRRWAEQAGLDADFVEK 77
|
|
| PLN02256 |
PLN02256 |
arogenate dehydrogenase |
146-257 |
1.47e-07 |
|
arogenate dehydrogenase
Pssm-ID: 215144 [Multi-domain] Cd Length: 304 Bit Score: 52.36 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 146 VIVSVPIHVTEQVIGKLP--PLPKDCILVDLASVKNGPLQAMLAA--HDGPVLGLHPMFGPDSG--SLAKQVVVW----- 214
Cdd:PLN02256 96 VLLCTSILSTEAVLRSLPlqRLKRSTLFVDVLSVKEFPKNLLLQVlpEEFDILCTHPMFGPESGkgGWAGLPFVYdkvri 175
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446147349 215 -CDGRKPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRH 257
Cdd:PLN02256 176 gDEGEREARCERFLDIFEEEGCRMVEMSCEEHDRYAAGSQFITH 219
|
|
| PDH_N |
pfam02153 |
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ... |
138-237 |
1.74e-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: 50.08 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 138 DIVADAGMVIVSVPIHVTEQVIGKL-PPLPKDCILVDLASVKNGP---LQAMLAAHDgpVLGLHPMFGPDS--------G 205
Cdd:pfam02153 41 EAVREADIVFLAVPVEQTLPVLKELaPHLKEDALITDVGSVKVKIireLEQHLPDKS--FVPGHPMAGTEKsgpdaaraN 118
|
90 100 110
....*....|....*....|....*....|....*
gi 446147349 206 SLAKQVVVWCDGRKPEAyQWFLEQIQVW---GARL 237
Cdd:pfam02153 119 LFENAPVILTPTEKTDT-EALNCVKELLegvGARV 152
|
|
| PRK06444 |
PRK06444 |
prephenate dehydrogenase; Provisional |
101-255 |
1.51e-06 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 102381 [Multi-domain] Cd Length: 197 Bit Score: 48.31 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 101 VVIVGGGGQMGRLFEKMLTLSGYQVrileqhdWDRAADIvadagmVIVSVPIHVTEQVIGKlpplpKDCILVDLASVKng 180
Cdd:PRK06444 3 EIIIGKNGRLGRVLCSILDDNGLGV-------YIKKADH------AFLSVPIDAALNYIES-----YDNNFVEISSVK-- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446147349 181 plqAMLAAHDGPVLGLHPMFGPDS--GSLAKQVVVWCDGRKPEaYQWFLEQIqVWGARLHRISAVEHDQNMAFIQAL 255
Cdd:PRK06444 63 ---WPFKKYSGKIVSIHPLFGPMSynDGVHRTVIFINDISRDN-YLNEINEM-FRGYHFVEMTADEHDLLMSEIMVK 134
|
|
| CM_M_hiGC-arch |
TIGR01808 |
monofunctional chorismate mutase, high GC gram positive type; This model represents the ... |
4-76 |
1.60e-05 |
|
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: 42.59 E-value: 1.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446147349 4 ELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLaSRRAEAEALGvpPDLIEDVLR 76
Cdd:TIGR01808 1 EIDTLREEIDRLDAEILALVKRRAEISQAIGKARMASGGTRLVHSREMKVI-ERYSELGPEG--KDLAIKLLR 70
|
|
| PRK06034 |
PRK06034 |
hypothetical protein; Provisional |
5-79 |
1.88e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235680 [Multi-domain] Cd Length: 279 Bit Score: 45.86 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 5 LTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSR----FGLPiyvPEREASMLasRR-AEAEALGVPPDLIEDVLRRVM 79
Cdd:PRK06034 11 LAELRWEIDAIDEELHQLLMERGDIIDRLIAVKRTqevgSAFR---PGREADMM--RRlVSRHRGILPLDTVESIWRVII 85
|
|
| PRK07502 |
PRK07502 |
prephenate/arogenate dehydrogenase family protein; |
134-343 |
2.26e-05 |
|
prephenate/arogenate dehydrogenase family protein;
Pssm-ID: 236034 [Multi-domain] Cd Length: 307 Bit Score: 45.73 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 134 DRAADIVADAGMVIVSVPIHVTEQVIGKLPP-LPKDCILVDLASVKnGPLQAMLAAHDGPVLGL---HPMF-----GPDS 204
Cdd:PRK07502 58 TSAAEAVKGADLVILCVPVGASGAVAAEIAPhLKPGAIVTDVGSVK-ASVIAAMAPHLPEGVHFipgHPLAgtehsGPDA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 205 GSLAKQVVVWC-----DGRKPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFatFAYGL-----HLaeENVQL 274
Cdd:PRK07502 137 GFAELFENRWCiltppEGTDPAAVARLTAFWRALGARVEEMDPEHHDLVLAITSHLPHL--IAYTIvgtadDL--ERVTE 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446147349 275 EQLLALSSPIYRlelaMVGRLFAQDPQLYADIIMSserNLALIKRYYKRFGEAIELLEQ----GDKQAFIDSF 343
Cdd:PRK07502 213 SEVIKYSASGFR----DFTRIAASDPTMWRDVFLH---NKDAVLEMLGRFTEDLAALQRairwGDGDALFDLF 278
|
|
| CM_P_1 |
TIGR01797 |
chorismate mutase domain of proteobacterial P-protein, clade 1; This model represents the ... |
5-82 |
3.58e-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: 41.73 E-value: 3.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446147349 5 LTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRES 82
Cdd:TIGR01797 1 LLALREKISAIDEKLLKLLAERRELAFEVGKSKLLSHRPVRDIERERDLLQRLITLGKAYHLDAHYITRLFQLIIEDS 78
|
|
| PLN02712 |
PLN02712 |
arogenate dehydrogenase |
96-355 |
1.28e-04 |
|
arogenate dehydrogenase
Pssm-ID: 215382 [Multi-domain] Cd Length: 667 Bit Score: 43.82 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 96 PALRPVVIvgGGGQMGRLFEKMLTLSGYQVRILEQHDWDRAA-----DIVAD--------AGMVIVSVPIHVTEQVIGKL 162
Cdd:PLN02712 51 TQLKIAII--GFGNYGQFLAKTLISQGHTVLAHSRSDHSLAArslgvSFFLDphdlcerhPDVILLCTSIISTENVLKSL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 163 P--PLPKDCILVDLASVKNGPLQAMLA--AHDGPVLGLHPMFGPDSGSLA--------KQVVVWCDGRKPEAYQWFLEQI 230
Cdd:PLN02712 129 PlqRLKRNTLFVDVLSVKEFAKNLLLDylPEDFDIICSHPMFGPQSAKHGwdglrfvyEKVRIGNEELRVSRCKSFLEVF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 231 QVWGARLHRISAVEHDQNMAFIQalrhFATFAYGLhlaeenvQLEQLLALSSPI----YRLELAMVGRLFAQDPQLYADI 306
Cdd:PLN02712 209 EREGCKMVEMSCTEHDKYAAESQ----FITHTVGR-------VLEMLKLESTPIntkgYESLLDLVENTCGDSFDLYYGL 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446147349 307 IMSSERNLALIKRYYKRFgEAI------ELLEQGDKQAFIDSFRKVeHWFGDYAQ 355
Cdd:PLN02712 278 FMYNKNSLEMLERLDLAF-EALrkqlfgRLHGVVRKQLFGNEEKKV-HVQPNHAE 330
|
|
| pheA |
PRK10622 |
bifunctional chorismate mutase/prephenate dehydratase; Provisional |
5-54 |
1.38e-04 |
|
bifunctional chorismate mutase/prephenate dehydratase; Provisional
Pssm-ID: 182594 [Multi-domain] Cd Length: 386 Bit Score: 43.56 E-value: 1.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446147349 5 LTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASML 54
Cdd:PRK10622 7 LLALREKISALDEKLLALLAERRELAVEVAKAKLLSHRPVRDIDRERDLL 56
|
|
| PRK09269 |
PRK09269 |
chorismate mutase; Provisional |
19-76 |
1.84e-04 |
|
chorismate mutase; Provisional
Pssm-ID: 236441 Cd Length: 193 Bit Score: 41.89 E-value: 1.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446147349 19 LLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLR 76
Cdd:PRK09269 37 LVDLAAQRLALADPVALSKWDSGKPIEDPPREAQVLANVEAQAPAHGVDPDYVRRFFR 94
|
|
| CM_mono2 |
TIGR01806 |
chorismate mutase, putative; This model represents a clade of probable chorismate mutases from ... |
19-88 |
2.24e-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: 40.49 E-value: 2.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446147349 19 LLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRES----YSSEND 88
Cdd:TIGR01806 9 LVDAANERLQLADDVAGYKARNNLPIEDSPREEQVLDSLRAQAQSAGLDPDYVTRFFQAQINANkaiqYRLVSD 82
|
|
| PRK06443 |
PRK06443 |
chorismate mutase; Validated |
1-51 |
3.72e-04 |
|
chorismate mutase; Validated
Pssm-ID: 235801 Cd Length: 177 Bit Score: 41.04 E-value: 3.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446147349 1 MVA--ELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREA 51
Cdd:PRK06443 1 MVHfiDMEDLRSEILENTMDIIELIEKRRELARMIGIIKMRNGLSIRDSEREN 53
|
|
| PRK08055 |
PRK08055 |
chorismate mutase; Provisional |
13-79 |
9.42e-04 |
|
chorismate mutase; Provisional
Pssm-ID: 236143 Cd Length: 181 Bit Score: 39.68 E-value: 9.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446147349 13 DEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVM 79
Cdd:PRK08055 24 AVSLGALATLINERLSYMKDVAGYKAEHHLPIEDLTQEQKVLAEAEEEAASNGLDPESIKPFIVAQM 90
|
|
| PRK07857 |
PRK07857 |
chorismate mutase; |
3-76 |
1.74e-03 |
|
chorismate mutase;
Pssm-ID: 236117 Cd Length: 106 Bit Score: 37.75 E-value: 1.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446147349 3 AELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRaeaEALGVP-PDLIEDVLR 76
Cdd:PRK07857 28 AEIDELREEIDRLDAEILALVKRRTEVSQAIGKARMASGGTRLVHSREMKVIERYR---EELGPEgKDLAMLLLR 99
|
|
| PRK07417 |
PRK07417 |
prephenate/arogenate dehydrogenase; |
139-338 |
1.96e-03 |
|
prephenate/arogenate dehydrogenase;
Pssm-ID: 180970 [Multi-domain] Cd Length: 279 Bit Score: 39.49 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 139 IVADAGMVIVSVPIHVTEQVIGKL-PPLPKDCILVDLASVKNGPLQAMLAAHDGPVlGLHPMFG-PDSGSLAKQVVVWcD 216
Cdd:PRK07417 54 LLKDCDLVILALPIGLLLPPSEQLiPALPPEAIVTDVGSVKAPIVEAWEKLHPRFV-GSHPMAGtAESGVEAGQRGLF-K 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 217 GRK----------PEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEEN----VQLEQLLALSS 282
Cdd:PRK07417 132 NRPwvltptentdLNALAIVEELAVSLGSKIYTADPEEHDRAVALISHLPVMVSAALIQTCGTEKdpsvLKLAQNLASSG 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446147349 283 piyrleLAMVGRLFAQDPQLYADIIMSSERN-LALIKRYYKRFGEAIELLEQGDKQA 338
Cdd:PRK07417 212 ------FADTSRVGGGNPELGVMMAEYNRAAlLRSLASYRQSLDQLEELIEQENWSA 262
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
106-175 |
9.27e-03 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 35.29 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147349 106 GGGQMGR-LFEKMLTLSGYQVRILEQHDWDRAADIVADAG----------------MVIVSVPIHVTEQVIGKLPPLPKD 168
Cdd:pfam03807 4 GAGNMGEaLARGLVAAGPHEVVVANSRNPEKAEELAEEYGvgatavdneeaaeeadVVFLAVKPEDAPDVLSELSDLLKG 83
|
....*..
gi 446147349 169 CILVDLA 175
Cdd:pfam03807 84 KIVISIA 90
|
|
| |
