|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
8-317 |
2.51e-114 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 334.81 E-value: 2.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 8 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVEVF---------------- 71
Cdd:PRK13357 7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFeglkayrhkdgsivlf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 72 ---------------------DKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 129
Cdd:PRK13357 86 rpdanakrlqrsadrllmpelPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 130 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 208
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 209 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 288
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340
....*....|....*....|....*....
gi 296010902 289 IHIPTMENGPkLASRILSKLTDIQYGREE 317
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
56-314 |
5.71e-99 |
|
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.
Pssm-ID: 238798 Cd Length: 279 Bit Score: 292.95 E-value: 5.71e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 56 SLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKLDQEWVPYSTSAS 98
Cdd:cd01557 1 SLHPATHALHYGQAVFeglkayrtpdgkivlfrpdenaerlnrsarrlglppfSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 99 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 178
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 179 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 258
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 296010902 259 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 314
Cdd:cd01557 233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
44-322 |
1.34e-78 |
|
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are two phylogenetically separable groups of branched-chain amino acid aminotransferase (IlvE). The last common ancestor of the two lineages appears also to have given rise to a family of D-amino acid aminotransferases (DAAT). This model represents the IlvE family less similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 233278 Cd Length: 313 Bit Score: 242.36 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 44 WEKPHIKPLQNLSLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKL 86
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFeglkayrcadgsivlfrpdanaarlrrsarrllmpelPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 87 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 165
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 166 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 244
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 245 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 322
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
44-317 |
2.93e-54 |
|
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439885 [Multi-domain] Cd Length: 285 Bit Score: 178.84 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 44 WEKPHIKPLQNLSLHPGSSALHYAVEVF---------------------------------DKEELLECIQQLVKLDQEw 90
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFegiraydgrlfrldehlarlnrsakrlgipipyTEEELLEAIRELVAANGL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 91 vpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGGNYGSS 169
Cdd:COG0115 83 ------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TGNYLNN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 170 LFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERY 249
Cdd:COG0115 155 VLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IPVEERP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010902 250 LTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 317
Cdd:COG0115 228 ISLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
71-282 |
2.35e-25 |
|
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.
Pssm-ID: 395844 [Multi-domain] Cd Length: 221 Bit Score: 101.28 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 71 FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKY 149
Cdd:pfam01063 36 FDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGGFGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 150 VRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGEDHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVT 229
Cdd:pfam01063 109 PLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDEDGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGIT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296010902 230 RRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 282
Cdd:pfam01063 176 RQALLDLAKALG-LEVEERPITLADLQEA------DEAFLTNSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
8-317 |
2.51e-114 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 334.81 E-value: 2.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 8 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVEVF---------------- 71
Cdd:PRK13357 7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFeglkayrhkdgsivlf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 72 ---------------------DKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 129
Cdd:PRK13357 86 rpdanakrlqrsadrllmpelPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 130 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 208
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 209 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 288
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340
....*....|....*....|....*....
gi 296010902 289 IHIPTMENGPkLASRILSKLTDIQYGREE 317
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
56-314 |
5.71e-99 |
|
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.
Pssm-ID: 238798 Cd Length: 279 Bit Score: 292.95 E-value: 5.71e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 56 SLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKLDQEWVPYSTSAS 98
Cdd:cd01557 1 SLHPATHALHYGQAVFeglkayrtpdgkivlfrpdenaerlnrsarrlglppfSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 99 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 178
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 179 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 258
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 296010902 259 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 314
Cdd:cd01557 233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
44-322 |
1.34e-78 |
|
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are two phylogenetically separable groups of branched-chain amino acid aminotransferase (IlvE). The last common ancestor of the two lineages appears also to have given rise to a family of D-amino acid aminotransferases (DAAT). This model represents the IlvE family less similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 233278 Cd Length: 313 Bit Score: 242.36 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 44 WEKPHIKPLQNLSLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKL 86
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFeglkayrcadgsivlfrpdanaarlrrsarrllmpelPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 87 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 165
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 166 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 244
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 245 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 322
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
71-288 |
4.40e-58 |
|
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.
Pssm-ID: 238254 [Multi-domain] Cd Length: 256 Bit Score: 187.81 E-value: 4.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 71 FDKEELLECIQQLVKLdqewvpySTSASLYIRPTFIGTEPSLGV--KKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPK 148
Cdd:cd00449 44 YDREELREALKELVAA-------NNGASLYIRPLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGG-EKGVRLITSPD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 149 YVRAWKGGTGDCKMGGNYGSSLfAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYWineDGEeeLATPPLDGIILPGV 228
Cdd:cd00449 116 RRRAAPGGTGDAKTGGNLNSVL-AKQEAAEAGADEALLLDDNGY-VTEGSASNVFIVK---DGE--LVTPPLDGGILPGI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 229 TRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGET 288
Cdd:cd00449 189 TRDSVIELAKELG-IKVEERPISLDELYAA------DEVFLTGTAAEVTPVTEIDGRGIG 241
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
44-317 |
2.93e-54 |
|
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439885 [Multi-domain] Cd Length: 285 Bit Score: 178.84 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 44 WEKPHIKPLQNLSLHPGSSALHYAVEVF---------------------------------DKEELLECIQQLVKLDQEw 90
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFegiraydgrlfrldehlarlnrsakrlgipipyTEEELLEAIRELVAANGL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 91 vpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGGNYGSS 169
Cdd:COG0115 83 ------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TGNYLNN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 170 LFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERY 249
Cdd:COG0115 155 VLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IPVEERP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010902 250 LTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 317
Cdd:COG0115 228 ISLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
19-325 |
6.71e-43 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 152.31 E-value: 6.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 19 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK------------------------- 73
Cdd:PLN02782 71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGlkayrkedgnillfrpeenairmrn 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 74 ------------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 141
Cdd:PLN02782 151 gaermcmpaptvEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGV-API 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 142 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL------YGEdhqitEVGTMNLFLYWINedgeeEL 215
Cdd:PLN02782 230 NLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvhkkYLE-----EVSSCNIFIVKDN-----VI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 216 ATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPtmE 295
Cdd:PLN02782 300 STPAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRVSYG--E 370
|
330 340 350
....*....|....*....|....*....|...
gi 296010902 296 NGPKLASRIL-SKLTDIQYGREES--DWTIVLS 325
Cdd:PLN02782 371 GGFGTVSQQLyTVLTSLQMGLIEDnmNWTVELS 403
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
23-324 |
4.62e-39 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 141.22 E-value: 4.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 23 LVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK----------------------------- 73
Cdd:PLN03117 25 LGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGlkayrtedgritlfrpdqnalrmqtgadr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 74 --------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYF--SSGtfnpVSL 143
Cdd:PLN03117 105 lcmtppslEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHkaSSG----LNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 144 WANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLYWINedgeeELATPPLDG 222
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdAATGKNIEELSACNIFILKGN-----IVSTPPTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 223 IILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENGpkLAS 302
Cdd:PLN03117 256 TILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--LST 326
|
330 340
....*....|....*....|....
gi 296010902 303 RILSKLTDIQYGREESD--WTIVL 324
Cdd:PLN03117 327 KLHLILTNIQMGVVEDKkgWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
19-319 |
1.24e-31 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 122.14 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 19 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK------------------------- 73
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGtkayrkengklllfrpdhnairmkl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 74 ------------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPV 141
Cdd:PLN02259 137 gaermlmpspsvDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 142 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYG-EDHQITEVGTMNLFLYwinedGEEELATPPL 220
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 221 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 300
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
|
330
....*....|....*....
gi 296010902 301 ASRILSKLTDIQYGREESD 319
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
19-325 |
1.03e-29 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 116.74 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 19 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYA----------------VEVFDKE-------- 74
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGqgliegmkayrgedgrILLFRPElnamrmki 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 75 -------------ELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 141
Cdd:PLN02883 133 gaermcmhspsvhQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 142 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGED-HQITEVGTMNLFLYWINedgeeELATPPL 220
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTgKNIEEVSAANIFLVKGN-----IIVTPAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 221 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 300
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
|
330 340
....*....|....*....|....*..
gi 296010902 301 ASRILSKLTDIQYG--REESDWTIVLS 325
Cdd:PLN02883 358 TQQLRSILLGIQTGsiQDTKDWVLQIA 384
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
71-282 |
2.35e-25 |
|
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.
Pssm-ID: 395844 [Multi-domain] Cd Length: 221 Bit Score: 101.28 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 71 FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKY 149
Cdd:pfam01063 36 FDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGGFGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 150 VRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGEDHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVT 229
Cdd:pfam01063 109 PLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDEDGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGIT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296010902 230 RRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 282
Cdd:pfam01063 176 RQALLDLAKALG-LEVEERPITLADLQEA------DEAFLTNSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
71-320 |
6.20e-20 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 88.28 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 71 FDKEELLECIQQLVKLDQewvpystSASLYIRP-TFIGTEpSLGV---KKPTKALLFVLlsPVGPYFSSGTFNP-----V 141
Cdd:PRK06606 74 YSVDELMEAQREVVRKNN-------LKSAYIRPlVFVGDE-GLGVrphGLPTDVAIAAW--PWGAYLGEEALEKgirvkV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 142 SLWA----NPKYVRAwkggtgdcKMGGNYGSSLFAQCEAVDNGCQQVLWLygeDHQ--ITEVGTMNLFlywINEDGEeeL 215
Cdd:PRK06606 144 SSWTrhapNSIPTRA--------KASGNYLNSILAKTEARRNGYDEALLL---DVEgyVSEGSGENIF---IVRDGV--L 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 216 ATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTME 295
Cdd:PRK06606 208 YTPPLTSSILEGITRDTVITLAKDLG-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREV----DGRQIGNGK 276
|
250 260
....*....|....*....|....*..
gi 296010902 296 NGPkLASRILSKLTDIQYGREE--SDW 320
Cdd:PRK06606 277 RGP-ITEKLQSAYFDIVRGRTEkyAHW 302
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
71-282 |
2.65e-13 |
|
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.
Pssm-ID: 238799 [Multi-domain] Cd Length: 270 Bit Score: 68.78 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 71 FDKEELLECIQQLVKLDQewvpySTSASLYIRPTFiGTEP-SLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPky 149
Cdd:cd01558 61 YTREELKELIRELVAKNE-----GGEGDVYIQVTR-GVGPrGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVP-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 150 VRAWkggtGDCKM-GGNYGSSLFAQCEAVDNGCQQVlWLYGEDHQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGV 228
Cdd:cd01558 133 DIRW----LRCDIkSLNLLNNVLAKQEAKEAGADEA-ILLDADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGI 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296010902 229 TRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 282
Cdd:cd01558 203 TRATVIELAKELG-IPVEERPFSLEELYTA------DEVFLTSTTAEVMPVVEI 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
165-282 |
6.57e-10 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 59.11 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 165 NYGSSLFAQCEAVDNGCQQVLWLygeDHQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGe 242
Cdd:PRK08320 154 NYLNNILAKIEANLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG- 224
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 296010902 243 FKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 282
Cdd:PRK08320 225 IPVREELFTLHDLYTA------DEVFLTGTAAEVIPVVKV 258
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
165-266 |
5.70e-09 |
|
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.
Pssm-ID: 238800 [Multi-domain] Cd Length: 249 Bit Score: 55.78 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 165 NYGSSLFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRRCILDLAHQWGEfK 244
Cdd:cd01559 127 NYLENVLAKREARDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGY-A 199
|
90 100
....*....|....*....|....*
gi 296010902 245 VSERYLTMDDLTTALE---GNRVRE 266
Cdd:cd01559 200 VDERPLRLEDLLAADEaflTNSLLG 224
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
187-268 |
8.46e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 46.12 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 187 LYGEDHQITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRRCILDlahqwgEFKVSERYLTMDDLTTA---LEGNR 263
Cdd:PRK07546 130 LLNERGEVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSAraiWVGNS 199
|
....*
gi 296010902 264 VREMF 268
Cdd:PRK07546 200 LRGLI 204
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
180-282 |
5.55e-05 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 44.20 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 180 GCQQVLWLygeDH--QITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTT 257
Cdd:PRK07544 176 GYADALML---DYrgYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIELAKRRG-IEVVERHIMPEELAG 245
|
90 100
....*....|....*....|....*
gi 296010902 258 AlegnrvREMFGSGTACVVCPVSDI 282
Cdd:PRK07544 246 F------SECFLTGTAAEVTPVSEI 264
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
176-289 |
7.09e-05 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 43.77 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 176 AVDNGCQQVlWlYGEDHQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDl 255
Cdd:PRK06680 163 AKEAGAQEA-W-MVDDGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPFTLQE- 234
|
90 100 110
....*....|....*....|....*....|....
gi 296010902 256 ttALEgnrVREMFGSGTACVVCPVSDIlyKGETI 289
Cdd:PRK06680 235 --AYA---AREAFITAASSFVFPVVQI--DGKQI 261
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
165-279 |
2.20e-03 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 39.23 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010902 165 NYGSSLFAQCEAVDNGCQQVLWLyGEDHQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRRCILDLAHQWGEF 243
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 296010902 244 K----VSERYLTMDdlttalEGNRVREMFGSGTACVVCPV 279
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
215-258 |
4.89e-03 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 38.02 E-value: 4.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 296010902 215 LATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 258
Cdd:PRK07849 206 LLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
|
|
| |
