|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
32-341 |
6.00e-114 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 334.81 E-value: 6.00e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 32 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVEVF---------------- 95
Cdd:PRK13357 7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFeglkayrhkdgsivlf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 96 ---------------------DKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 153
Cdd:PRK13357 86 rpdanakrlqrsadrllmpelPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 154 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 232
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 233 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 312
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340
....*....|....*....|....*....
gi 296010900 313 IHIPTMENGPkLASRILSKLTDIQYGREE 341
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
80-338 |
1.33e-98 |
|
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: 1.33e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 80 SLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKLDQEWVPYSTSAS 122
Cdd:cd01557 1 SLHPATHALHYGQAVFeglkayrtpdgkivlfrpdenaerlnrsarrlglppfSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 123 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 202
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 203 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 282
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 296010900 283 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 338
Cdd:cd01557 233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
68-346 |
2.97e-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: 2.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 68 WEKPHIKPLQNLSLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKL 110
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFeglkayrcadgsivlfrpdanaarlrrsarrllmpelPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 111 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 189
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 190 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 268
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 269 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 346
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
68-341 |
5.87e-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: 5.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 68 WEKPHIKPLQNLSLHPGSSALHYAVEVF---------------------------------DKEELLECIQQLVKLDQEw 114
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFegiraydgrlfrldehlarlnrsakrlgipipyTEEELLEAIRELVAANGL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 115 vpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGGNYGSS 193
Cdd:COG0115 83 ------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TGNYLNN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 194 LFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERY 273
Cdd:COG0115 155 VLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IPVEERP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010900 274 LTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 341
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 ... |
95-306 |
3.55e-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: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 95 FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKY 173
Cdd:pfam01063 36 FDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGGFGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 174 VRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGEDHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVT 253
Cdd:pfam01063 109 PLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDEDGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGIT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296010900 254 RRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 306
Cdd:pfam01063 176 RQALLDLAKALG-LEVEERPITLADLQEA------DEAFLTNSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
32-341 |
6.00e-114 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 334.81 E-value: 6.00e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 32 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVEVF---------------- 95
Cdd:PRK13357 7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFeglkayrhkdgsivlf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 96 ---------------------DKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 153
Cdd:PRK13357 86 rpdanakrlqrsadrllmpelPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 154 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 232
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 233 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 312
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340
....*....|....*....|....*....
gi 296010900 313 IHIPTMENGPkLASRILSKLTDIQYGREE 341
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
80-338 |
1.33e-98 |
|
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: 1.33e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 80 SLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKLDQEWVPYSTSAS 122
Cdd:cd01557 1 SLHPATHALHYGQAVFeglkayrtpdgkivlfrpdenaerlnrsarrlglppfSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 123 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 202
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 203 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 282
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 296010900 283 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 338
Cdd:cd01557 233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
68-346 |
2.97e-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: 2.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 68 WEKPHIKPLQNLSLHPGSSALHYAVEVF-------------------------------------DKEELLECIQQLVKL 110
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFeglkayrcadgsivlfrpdanaarlrrsarrllmpelPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 111 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 189
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 190 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 268
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 269 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 346
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
95-312 |
8.97e-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: 8.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 95 FDKEELLECIQQLVKLdqewvpySTSASLYIRPTFIGTEPSLGV--KKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPK 172
Cdd:cd00449 44 YDREELREALKELVAA-------NNGASLYIRPLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGG-EKGVRLITSPD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 173 YVRAWKGGTGDCKMGGNYGSSLfAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYWineDGEeeLATPPLDGIILPGV 252
Cdd:cd00449 116 RRRAAPGGTGDAKTGGNLNSVL-AKQEAAEAGADEALLLDDNGY-VTEGSASNVFIVK---DGE--LVTPPLDGGILPGI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 253 TRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGET 312
Cdd:cd00449 189 TRDSVIELAKELG-IKVEERPISLDELYAA------DEVFLTGTAAEVTPVTEIDGRGIG 241
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
68-341 |
5.87e-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: 5.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 68 WEKPHIKPLQNLSLHPGSSALHYAVEVF---------------------------------DKEELLECIQQLVKLDQEw 114
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFegiraydgrlfrldehlarlnrsakrlgipipyTEEELLEAIRELVAANGL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 115 vpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGGNYGSS 193
Cdd:COG0115 83 ------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TGNYLNN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 194 LFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERY 273
Cdd:COG0115 155 VLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IPVEERP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010900 274 LTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 341
Cdd:COG0115 228 ISLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
43-349 |
1.79e-42 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 151.92 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 43 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK------------------------- 97
Cdd:PLN02782 71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGlkayrkedgnillfrpeenairmrn 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 98 ------------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 165
Cdd:PLN02782 151 gaermcmpaptvEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGV-API 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 166 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL------YGEdhqitEVGTMNLFLYWINedgeeEL 239
Cdd:PLN02782 230 NLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvhkkYLE-----EVSSCNIFIVKDN-----VI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 240 ATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPtmE 319
Cdd:PLN02782 300 STPAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRVSYG--E 370
|
330 340 350
....*....|....*....|....*....|...
gi 296010900 320 NGPKLASRIL-SKLTDIQYGREES--DWTIVLS 349
Cdd:PLN02782 371 GGFGTVSQQLyTVLTSLQMGLIEDnmNWTVELS 403
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
47-348 |
9.99e-39 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 140.84 E-value: 9.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 47 LVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK----------------------------- 97
Cdd:PLN03117 25 LGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGlkayrtedgritlfrpdqnalrmqtgadr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 98 --------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYF--SSGtfnpVSL 167
Cdd:PLN03117 105 lcmtppslEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHkaSSG----LNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 168 WANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLYWINedgeeELATPPLDG 246
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdAATGKNIEELSACNIFILKGN-----IVSTPPTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 247 IILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENGpkLAS 326
Cdd:PLN03117 256 TILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--LST 326
|
330 340
....*....|....*....|....
gi 296010900 327 RILSKLTDIQYGREESD--WTIVL 348
Cdd:PLN03117 327 KLHLILTNIQMGVVEDKkgWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
43-343 |
2.08e-31 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 122.14 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 43 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVEVFDK------------------------- 97
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGtkayrkengklllfrpdhnairmkl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 98 ------------EELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPV 165
Cdd:PLN02259 137 gaermlmpspsvDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 166 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYG-EDHQITEVGTMNLFLYwinedGEEELATPPL 244
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 245 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 324
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
|
330
....*....|....*....
gi 296010900 325 ASRILSKLTDIQYGREESD 343
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
43-349 |
1.92e-29 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 116.35 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 43 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYA----------------VEVFDKE-------- 98
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGqgliegmkayrgedgrILLFRPElnamrmki 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 99 -------------ELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 165
Cdd:PLN02883 133 gaermcmhspsvhQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 166 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGED-HQITEVGTMNLFLYWINedgeeELATPPL 244
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTgKNIEEVSAANIFLVKGN-----IIVTPAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 245 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 324
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
|
330 340
....*....|....*....|....*..
gi 296010900 325 ASRILSKLTDIQYG--REESDWTIVLS 349
Cdd:PLN02883 358 TQQLRSILLGIQTGsiQDTKDWVLQIA 384
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
95-306 |
3.55e-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: 3.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 95 FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKY 173
Cdd:pfam01063 36 FDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGGFGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 174 VRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGEDHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVT 253
Cdd:pfam01063 109 PLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDEDGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGIT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296010900 254 RRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 306
Cdd:pfam01063 176 RQALLDLAKALG-LEVEERPITLADLQEA------DEAFLTNSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
95-344 |
8.72e-20 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 88.28 E-value: 8.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 95 FDKEELLECIQQLVKLDQewvpystSASLYIRP-TFIGTEpSLGV---KKPTKALLFVLlsPVGPYFSSGTFNP-----V 165
Cdd:PRK06606 74 YSVDELMEAQREVVRKNN-------LKSAYIRPlVFVGDE-GLGVrphGLPTDVAIAAW--PWGAYLGEEALEKgirvkV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 166 SLWA----NPKYVRAwkggtgdcKMGGNYGSSLFAQCEAVDNGCQQVLWLygeDHQ--ITEVGTMNLFlywINEDGEeeL 239
Cdd:PRK06606 144 SSWTrhapNSIPTRA--------KASGNYLNSILAKTEARRNGYDEALLL---DVEgyVSEGSGENIF---IVRDGV--L 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 240 ATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTME 319
Cdd:PRK06606 208 YTPPLTSSILEGITRDTVITLAKDLG-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREV----DGRQIGNGK 276
|
250 260
....*....|....*....|....*..
gi 296010900 320 NGPkLASRILSKLTDIQYGREE--SDW 344
Cdd:PRK06606 277 RGP-ITEKLQSAYFDIVRGRTEkyAHW 302
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
95-306 |
3.26e-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: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 95 FDKEELLECIQQLVKLDQewvpySTSASLYIRPTFiGTEP-SLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPky 173
Cdd:cd01558 61 YTREELKELIRELVAKNE-----GGEGDVYIQVTR-GVGPrGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVP-- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 174 VRAWkggtGDCKM-GGNYGSSLFAQCEAVDNGCQQVlWLYGEDHQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGV 252
Cdd:cd01558 133 DIRW----LRCDIkSLNLLNNVLAKQEAKEAGADEA-ILLDADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGI 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296010900 253 TRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 306
Cdd:cd01558 203 TRATVIELAKELG-IPVEERPFSLEELYTA------DEVFLTSTTAEVMPVVEI 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
189-306 |
7.74e-10 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 59.11 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 189 NYGSSLFAQCEAVDNGCQQVLWLygeDHQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGe 266
Cdd:PRK08320 154 NYLNNILAKIEANLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG- 224
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 296010900 267 FKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 306
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 ... |
189-290 |
6.56e-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: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 189 NYGSSLFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRRCILDLAHQWGEfK 268
Cdd:cd01559 127 NYLENVLAKREARDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGY-A 199
|
90 100
....*....|....*....|....*
gi 296010900 269 VSERYLTMDDLTTALE---GNRVRE 290
Cdd:cd01559 200 VDERPLRLEDLLAADEaflTNSLLG 224
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
211-292 |
9.45e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 46.12 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 211 LYGEDHQITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRRCILDlahqwgEFKVSERYLTMDDLTTA---LEGNR 287
Cdd:PRK07546 130 LLNERGEVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSAraiWVGNS 199
|
....*
gi 296010900 288 VREMF 292
Cdd:PRK07546 200 LRGLI 204
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
204-306 |
6.29e-05 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 44.20 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 204 GCQQVLWLygeDH--QITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTT 281
Cdd:PRK07544 176 GYADALML---DYrgYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIELAKRRG-IEVVERHIMPEELAG 245
|
90 100
....*....|....*....|....*
gi 296010900 282 AlegnrvREMFGSGTACVVCPVSDI 306
Cdd:PRK07544 246 F------SECFLTGTAAEVTPVSEI 264
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
200-313 |
8.01e-05 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 43.77 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 200 AVDNGCQQVlWlYGEDHQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDl 279
Cdd:PRK06680 163 AKEAGAQEA-W-MVDDGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPFTLQE- 234
|
90 100 110
....*....|....*....|....*....|....
gi 296010900 280 ttALEgnrVREMFGSGTACVVCPVSDIlyKGETI 313
Cdd:PRK06680 235 --AYA---AREAFITAASSFVFPVVQI--DGKQI 261
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
189-303 |
2.48e-03 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 39.23 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010900 189 NYGSSLFAQCEAVDNGCQQVLWLyGEDHQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRRCILDLAHQWGEF 267
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 296010900 268 K----VSERYLTMDdlttalEGNRVREMFGSGTACVVCPV 303
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
239-282 |
5.47e-03 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 38.02 E-value: 5.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 296010900 239 LATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 282
Cdd:PRK07849 206 LLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
|
|
| |
