|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
31-377 |
1.31e-138 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 399.14 E-value: 1.31e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 31 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLF 110
Cdd:PRK13357 7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 111 QPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 189
Cdd:PRK13357 86 RPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 190 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 268
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 269 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 348
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340
....*....|....*....|....*....
gi 296010906 349 IHIPTMENGPkLASRILSKLTDIQYGREE 377
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
79-374 |
6.58e-126 |
|
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: 363.82 E-value: 6.58e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 79 SLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSAS 158
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 159 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 238
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 239 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 318
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 296010906 319 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 374
Cdd:cd01557 233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
67-382 |
3.57e-100 |
|
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: 299.75 E-value: 3.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 67 WEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKL 146
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 147 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 225
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 226 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 304
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 305 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 382
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
67-377 |
2.89e-69 |
|
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: 219.29 E-value: 2.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 67 WEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVK 145
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 146 LDQEwvpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGG 224
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 225 NYGSSLFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFK 304
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296010906 305 VSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 377
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
93-342 |
2.30e-32 |
|
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: 121.31 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 93 LFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPS 171
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 172 LGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGE 250
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 251 DHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGS 330
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 296010906 331 GTACVVCPVSDI 342
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
31-377 |
1.31e-138 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 399.14 E-value: 1.31e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 31 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLF 110
Cdd:PRK13357 7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 111 QPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 189
Cdd:PRK13357 86 RPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 190 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 268
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 269 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 348
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340
....*....|....*....|....*....
gi 296010906 349 IHIPTMENGPkLASRILSKLTDIQYGREE 377
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
79-374 |
6.58e-126 |
|
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: 363.82 E-value: 6.58e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 79 SLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSAS 158
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 159 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 238
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 239 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 318
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 296010906 319 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 374
Cdd:cd01557 233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
67-382 |
3.57e-100 |
|
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: 299.75 E-value: 3.57e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 67 WEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKL 146
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 147 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 225
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 226 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 304
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 305 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 382
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
84-348 |
5.42e-74 |
|
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: 230.57 E-value: 5.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 84 SSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVKLdqewvpySTSASLYIR 162
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKG-----RLFRLDEHLDRLNRSAKRLGLPIpYDREELREALKELVAA-------NNGASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 163 PTFIGTEPSLGV--KKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLfAQCEAVDNG 240
Cdd:cd00449 69 PLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGG-EKGVRLITSPDRRRAAPGGTGDAKTGGNLNSVL-AKQEAAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 241 CQQVLWLYGEDHqITEVGTMNLFLYWineDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAle 320
Cdd:cd00449 147 ADEALLLDDNGY-VTEGSASNVFIVK---DGE--LVTPPLDGGILPGITRDSVIELAKELG-IKVEERPISLDELYAA-- 217
|
250 260
....*....|....*....|....*...
gi 296010906 321 gnrvREMFGSGTACVVCPVSDILYKGET 348
Cdd:cd00449 218 ----DEVFLTGTAAEVTPVTEIDGRGIG 241
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
67-377 |
2.89e-69 |
|
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: 219.29 E-value: 2.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 67 WEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVK 145
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 146 LDQEwvpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGG 224
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 225 NYGSSLFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFK 304
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296010906 305 VSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 377
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
42-385 |
1.80e-61 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 203.16 E-value: 1.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 42 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYR 121
Cdd:PLN02782 71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 122 SAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 201
Cdd:PLN02782 151 GAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGV-API 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 202 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL------YGEdhqitEVGTMNLFLYWINedgeeEL 275
Cdd:PLN02782 230 NLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvhkkYLE-----EVSSCNIFIVKDN-----VI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 276 ATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPtmE 355
Cdd:PLN02782 300 STPAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRVSYG--E 370
|
330 340 350
....*....|....*....|....*....|...
gi 296010906 356 NGPKLASRIL-SKLTDIQYGREES--DWTIVLS 385
Cdd:PLN02782 371 GGFGTVSQQLyTVLTSLQMGLIEDnmNWTVELS 403
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
46-384 |
6.88e-58 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 192.45 E-value: 6.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 46 LVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVR 125
Cdd:PLN03117 25 LGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGADR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 126 ATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYF--SSGtfnpVSL 203
Cdd:PLN03117 105 LCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHkaSSG----LNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 204 WANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLYWINedgeeELATPPLDG 282
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdAATGKNIEELSACNIFILKGN-----IVSTPPTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 283 IILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENGpkLAS 362
Cdd:PLN03117 256 TILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--LST 326
|
330 340
....*....|....*....|....
gi 296010906 363 RILSKLTDIQYGREESD--WTIVL 384
Cdd:PLN03117 327 KLHLILTNIQMGVVEDKkgWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
42-379 |
5.83e-47 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 164.51 E-value: 5.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 42 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYR 121
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 122 SAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPV 201
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 202 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYG-EDHQITEVGTMNLFLYwinedGEEELATPPL 280
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 281 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 360
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
|
330
....*....|....*....
gi 296010906 361 ASRILSKLTDIQYGREESD 379
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
42-385 |
2.07e-46 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 162.96 E-value: 2.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 42 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYR 121
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 122 SAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 201
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 202 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGED-HQITEVGTMNLFLYWINedgeeELATPPL 280
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTgKNIEEVSAANIFLVKGN-----IIVTPAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 281 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 360
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
|
330 340
....*....|....*....|....*..
gi 296010906 361 ASRILSKLTDIQYG--REESDWTIVLS 385
Cdd:PLN02883 358 TQQLRSILLGIQTGsiQDTKDWVLQIA 384
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
93-342 |
2.30e-32 |
|
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: 121.31 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 93 LFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPS 171
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 172 LGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGE 250
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 251 DHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGS 330
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 296010906 331 GTACVVCPVSDI 342
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
86-380 |
6.50e-27 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 108.70 E-value: 6.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 86 ALHYAVELFEGLKAFRGVDNKIrLFQPNLNMDRMYRSA--VRATLPvFDKEELLECIQQLVKLDQewvpystSASLYIRP 163
Cdd:PRK06606 29 ALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAkiLRMEIP-YSVDELMEAQREVVRKNN-------LKSAYIRP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 164 -TFIGTEpSLGV---KKPTKALLFVLlsPVGPYFSSGTFNP-----VSLWA----NPKYVRAwkggtgdcKMGGNYGSSL 230
Cdd:PRK06606 100 lVFVGDE-GLGVrphGLPTDVAIAAW--PWGAYLGEEALEKgirvkVSSWTrhapNSIPTRA--------KASGNYLNSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 231 FAQCEAVDNGCQQVLWLygeDHQ--ITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSER 308
Cdd:PRK06606 169 LAKTEARRNGYDEALLL---DVEgyVSEGSGENIF---IVRDGV--LYTPPLTSSILEGITRDTVITLAKDLG-IEVIER 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296010906 309 YLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE--SDW 380
Cdd:PRK06606 240 RITRDELYIA------DEVFFTGTAAEVTPIREV----DGRQIGNGKRGP-ITEKLQSAYFDIVRGRTEkyAHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
74-380 |
1.20e-23 |
|
branched-chain amino acid aminotransferase, group I; 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 more strongly similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130192 Cd Length: 298 Bit Score: 99.36 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 74 PLQNLSLHPGSSALHYAVELFEGLKAFRGvDNKIRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVKLdqewvp 152
Cdd:TIGR01122 8 DWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEIpYSKEELMEATRETLRK------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 153 ySTSASLYIRP-TFIGTEpSLGV--KKPTKALLFVLLSPVGPY-----FSSGTFNPVSLW--ANPKYVrawkggTGDCKM 222
Cdd:TIGR01122 81 -NNLRSAYIRPlVFRGDG-DLGLnpRAGYKPDVIIAAWPWGAYlgeeaLEKGIDAKVSSWrrNAPNTI------PTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 223 GGNYGSSLFAQCEAVDNGCQQVLWLyGEDHQITEVGTMNLFlywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGe 302
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILL-DVEGYVAEGSGENIF---IVKDG--VLFTPPVTSSILPGITRDTVITLAKELG- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010906 303 FKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREESDW 380
Cdd:TIGR01122 226 IEVVEQPISREELYTA------DEAFFTGTAAEITPIREV----DGRKIGNGRRGP-VTKKLQEAFFDLVTGGTEDYW 292
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
72-342 |
1.16e-18 |
|
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: 84.96 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 72 IKPLQNLSLHPGSSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSA--VRATLPvFDKEELLECIQQLVKLDQe 149
Cdd:cd01558 6 YVPREEAKVSVFDRGFLFGDGVYEVIRVYNG-----KPFALDEHLDRLYRSAkeLRIDIP-YTREELKELIRELVAKNE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 150 wvpySTSASLYIRPTFiGTEP-SLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPkyVRAWkggtGDCKM-GGNYG 227
Cdd:cd01558 79 ----GGEGDVYIQVTR-GVGPrGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVP--DIRW----LRCDIkSLNLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 228 SSLFAQCEAVDNGCQQVlWLYGEDHQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSE 307
Cdd:cd01558 148 NNVLAKQEAKEAGADEA-ILLDADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGITRATVIELAKELG-IPVEE 220
|
250 260 270
....*....|....*....|....*....|....*
gi 296010906 308 RYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 342
Cdd:cd01558 221 RPFSLEELYTA------DEVFLTSTTAEVMPVVEI 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
94-342 |
3.09e-12 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 66.43 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 94 FEGLKAFRGvdnkiRLFQPNLNMDRMYRSA--VRATLPVfDKEELLECIQQLVKLDQewvpySTSAslYIRPTFIGTEPS 171
Cdd:PRK08320 33 FEGIRAYNG-----RVFRLKEHIDRLYDSAkaIMLEIPL-SKEEMTEIVLETLRKNN-----LRDA--YIRLVVSRGVGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 172 LGV--KKPTKALLFVLLSPVGPYF------------SSGTFNPV-SLWANPKYVrawkggtgdckmggNYGSSLFAQCEA 236
Cdd:PRK08320 100 LGLdpRKCPKPTVVCIAEPIGLYPgelyekglkvitVSTRRNRPdALSPQVKSL--------------NYLNNILAKIEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 237 VDNGCQQVLWLygeDHQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDD 314
Cdd:PRK08320 166 NLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG-IPVREELFTLHD 236
|
250 260
....*....|....*....|....*...
gi 296010906 315 LTTAlegnrvREMFGSGTACVVCPVSDI 342
Cdd:PRK08320 237 LYTA------DEVFLTGTAAEVIPVVKV 258
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
86-326 |
6.48e-12 |
|
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: 65.02 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 86 ALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPVFDKEELLeciQQLVKLDQEWVPYSTSASLYI-Rpt 164
Cdd:cd01559 3 GFAYGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLR---AALESLLAANDIDEGRIRLILsR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 165 fiGTEP----SLGVKKPTkallfvLLSPVGPYFSSGTFNPVSLWANPkyVRAWKGGTgdckMGG----NYGSSLFAQCEA 236
Cdd:cd01559 73 --GPGGrgyaPSVCPGPA------LYVSVIPLPPAWRQDGVRLITCP--VRLGEQPL----LAGlkhlNYLENVLAKREA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 237 VDNGCQQVLWLYGEDHqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRRCILDLAHQWGEfKVSERYLTMDDLT 316
Cdd:cd01559 139 RDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGY-AVDERPLRLEDLL 211
|
250
....*....|...
gi 296010906 317 TALE---GNRVRE 326
Cdd:cd01559 212 AADEaflTNSLLG 224
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
80-342 |
1.02e-05 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 46.89 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 80 LHPGSSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSA--VRATLPvFDKEELLECIQQLVKLdqewvpySTSA 157
Cdd:PRK07544 25 VHVLTHGLHYASSVFEGERAYGG-----KIFKLREHSERLRRSAelLDFEIP-YSVAEIDAAKKETLAA-------NGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 158 SLYIRPT-FIGTEpSLGVKKP-TKALLFVLLSPVGPYFSS-----GTFNPVSLWANPkyvrAWKGGTGDCKMGGNYGSSL 230
Cdd:PRK07544 92 DAYVRPVaWRGSE-MMGVSAQqNKIHLAIAAWEWPSYFDPeakmkGIRLDIAKWRRP----DPETAPSAAKAAGLYMICT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 231 FAQCEAVDNGCQQVLWLygeDH--QITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRRCILDLAHQWGeFKVSER 308
Cdd:PRK07544 167 ISKHAAEAKGYADALML---DYrgYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIELAKRRG-IEVVER 236
|
250 260 270
....*....|....*....|....*....|....
gi 296010906 309 YLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 342
Cdd:PRK07544 237 HIMPEELAGF------SECFLTGTAAEVTPVSEI 264
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
247-328 |
1.09e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 46.12 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 247 LYGEDHQITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRRCILDlahqwgEFKVSERYLTMDDLTTA---LEGNR 323
Cdd:PRK07546 130 LLNERGEVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSAraiWVGNS 199
|
....*
gi 296010906 324 VREMF 328
Cdd:PRK07546 200 LRGLI 204
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
236-349 |
9.40e-05 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 43.77 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 236 AVDNGCQQVlWlYGEDHQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDl 315
Cdd:PRK06680 163 AKEAGAQEA-W-MVDDGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPFTLQE- 234
|
90 100 110
....*....|....*....|....*....|....
gi 296010906 316 ttALEgnrVREMFGSGTACVVCPVSDIlyKGETI 349
Cdd:PRK06680 235 --AYA---AREAFITAASSFVFPVVQI--DGKQI 261
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
225-339 |
2.89e-03 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 39.23 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010906 225 NYGSSLFAQCEAVDNGCQQVLWLyGEDHQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRRCILDLAHQWGEF 303
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 296010906 304 K----VSERYLTMDdlttalEGNRVREMFGSGTACVVCPV 339
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
275-318 |
6.34e-03 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 38.02 E-value: 6.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 296010906 275 LATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 318
Cdd:PRK07849 206 LLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
|
|
| |
