|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
44-390 |
2.11e-138 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 399.14 E-value: 2.11e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 44 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLF 123
Cdd:PRK13357 7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 124 QPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 202
Cdd:PRK13357 86 RPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 203 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 281
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 282 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 361
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340
....*....|....*....|....*....
gi 296010904 362 IHIPTMENGPkLASRILSKLTDIQYGREE 390
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
92-387 |
1.05e-125 |
|
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: 1.05e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 92 SLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSAS 171
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 172 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 251
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 252 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 331
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 296010904 332 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 387
Cdd:cd01557 233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
80-395 |
5.53e-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: 5.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 80 WEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKL 159
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 160 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 238
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 239 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 317
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 318 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 395
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
80-390 |
4.25e-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: 4.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 80 WEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVK 158
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 159 LDQEwvpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGG 237
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 238 NYGSSLFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFK 317
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296010904 318 VSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 390
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 ... |
106-355 |
2.89e-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: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 106 LFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPS 184
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 185 LGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGE 263
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 264 DHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGS 343
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 296010904 344 GTACVVCPVSDI 355
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
44-390 |
2.11e-138 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 399.14 E-value: 2.11e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 44 VTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEfGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLF 123
Cdd:PRK13357 7 PNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 124 QPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPV 202
Cdd:PRK13357 86 RPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 203 GPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQ-ITEVGTMNLFLywIN 281
Cdd:PRK13357 166 GAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--IT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 282 EDGEEelaTPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGET 361
Cdd:PRK13357 243 KDGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340
....*....|....*....|....*....
gi 296010904 362 IHIPTMENGPkLASRILSKLTDIQYGREE 390
Cdd:PRK13357 319 FVIGDGEVGP-VTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
92-387 |
1.05e-125 |
|
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: 1.05e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 92 SLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSAS 171
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 172 LYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPkYVRAWKGGTGDCKMGGNYGSSLFAQCEAVD 251
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 252 NGCQQVLWLYGEDHQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 331
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 296010904 332 LegnrvrEMFGSGTACVVCPVSDILYKGETihiPTMENGPKLASRILSKLTDIQYG 387
Cdd:cd01557 233 D------EVFATGTAAVVTPVGEIDYRGKE---PGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
80-395 |
5.53e-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: 5.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 80 WEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKL 159
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 160 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGN 238
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 239 YGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGeFK 317
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLdPVEHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 318 VSERYLTMDDLTTALEgnRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPkLASRILSKLTDIQYGREES--DWTI 395
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
97-361 |
8.04e-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: 8.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 97 SSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVKLdqewvpySTSASLYIR 175
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKG-----RLFRLDEHLDRLNRSAKRLGLPIpYDREELREALKELVAA-------NNGASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 176 PTFIGTEPSLGV--KKPTKALLFVLLSPVGPYFSSGtFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLfAQCEAVDNG 253
Cdd:cd00449 69 PLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGG-EKGVRLITSPDRRRAAPGGTGDAKTGGNLNSVL-AKQEAAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 254 CQQVLWLYGEDHqITEVGTMNLFLYWineDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAle 333
Cdd:cd00449 147 ADEALLLDDNGY-VTEGSASNVFIVK---DGE--LVTPPLDGGILPGITRDSVIELAKELG-IKVEERPISLDELYAA-- 217
|
250 260
....*....|....*....|....*...
gi 296010904 334 gnrvREMFGSGTACVVCPVSDILYKGET 361
Cdd:cd00449 218 ----DEVFLTGTAAEVTPVTEIDGRGIG 241
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
80-390 |
4.25e-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: 4.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 80 WEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVK 158
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 159 LDQEwvpystsASLYIRPTFIGTEPSLGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPkYVRAWKGGTGDCKmGG 237
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 238 NYGSSLFAQCEAVDNGCQQVLWLYGEDHqITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFK 317
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLLDTDGY-VAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296010904 318 VSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE 390
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
55-398 |
3.06e-61 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 202.77 E-value: 3.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 55 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYR 134
Cdd:PLN02782 71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 135 SAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 214
Cdd:PLN02782 151 GAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGV-API 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 215 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL------YGEdhqitEVGTMNLFLYWINedgeeEL 288
Cdd:PLN02782 230 NLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvhkkYLE-----EVSSCNIFIVKDN-----VI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 289 ATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPtmE 368
Cdd:PLN02782 300 STPAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRVSYG--E 370
|
330 340 350
....*....|....*....|....*....|...
gi 296010904 369 NGPKLASRIL-SKLTDIQYGREES--DWTIVLS 398
Cdd:PLN02782 371 GGFGTVSQQLyTVLTSLQMGLIEDnmNWTVELS 403
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
59-397 |
9.83e-58 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 192.45 E-value: 9.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 59 LVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVR 138
Cdd:PLN03117 25 LGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGADR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 139 ATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYF--SSGtfnpVSL 216
Cdd:PLN03117 105 LCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHkaSSG----LNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 217 WANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWL-YGEDHQITEVGTMNLFLYWINedgeeELATPPLDG 295
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdAATGKNIEELSACNIFILKGN-----IVSTPPTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 296 IILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENGpkLAS 375
Cdd:PLN03117 256 TILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--LST 326
|
330 340
....*....|....*....|....
gi 296010904 376 RILSKLTDIQYGREESD--WTIVL 397
Cdd:PLN03117 327 KLHLILTNIQMGVVEDKkgWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
55-392 |
8.02e-47 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 164.51 E-value: 8.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 55 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYR 134
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 135 SAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGtFNPV 214
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 215 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYG-EDHQITEVGTMNLFLYwinedGEEELATPPL 293
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 294 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 373
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
|
330
....*....|....*....
gi 296010904 374 ASRILSKLTDIQYGREESD 392
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
55-398 |
4.59e-46 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 162.58 E-value: 4.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 55 DPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYR 134
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 135 SAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTfNPV 214
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 215 SLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGED-HQITEVGTMNLFLYWINedgeeELATPPL 293
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTgKNIEEVSAANIFLVKGN-----IIVTPAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 294 DGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDILYKGETIHIPTMENgpKL 373
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
|
330 340
....*....|....*....|....*..
gi 296010904 374 ASRILSKLTDIQYG--REESDWTIVLS 398
Cdd:PLN02883 358 TQQLRSILLGIQTGsiQDTKDWVLQIA 384
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
106-355 |
2.89e-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: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 106 LFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVKLDQEWVPYstsaslyIRPTFIGTEPS 184
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 185 LGVKKPT-KALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAwkggtgDCKmGGNYGSSLFAQCEAVDNGCQQVLwLYGE 263
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 264 DHQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTAlegnrvREMFGS 343
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 296010904 344 GTACVVCPVSDI 355
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
99-393 |
7.91e-27 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 108.70 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 99 ALHYAVELFEGLKAFRGVDNKIrLFQPNLNMDRMYRSA--VRATLPvFDKEELLECIQQLVKLDQewvpystSASLYIRP 176
Cdd:PRK06606 29 ALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAkiLRMEIP-YSVDELMEAQREVVRKNN-------LKSAYIRP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 177 -TFIGTEpSLGV---KKPTKALLFVLlsPVGPYFSSGTFNP-----VSLWA----NPKYVRAwkggtgdcKMGGNYGSSL 243
Cdd:PRK06606 100 lVFVGDE-GLGVrphGLPTDVAIAAW--PWGAYLGEEALEKgirvkVSSWTrhapNSIPTRA--------KASGNYLNSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 244 FAQCEAVDNGCQQVLWLygeDHQ--ITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSER 321
Cdd:PRK06606 169 LAKTEARRNGYDEALLL---DVEgyVSEGSGENIF---IVRDGV--LYTPPLTSSILEGITRDTVITLAKDLG-IEVIER 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296010904 322 YLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREE--SDW 393
Cdd:PRK06606 240 RITRDELYIA------DEVFFTGTAAEVTPIREV----DGRQIGNGKRGP-ITEKLQSAYFDIVRGRTEkyAHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
87-393 |
1.41e-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: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 87 PLQNLSLHPGSSALHYAVELFEGLKAFRGvDNKIRLFQPNLNMDRMYRSAVRATLPV-FDKEELLECIQQLVKLdqewvp 165
Cdd:TIGR01122 8 DWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEIpYSKEELMEATRETLRK------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 166 ySTSASLYIRP-TFIGTEpSLGV--KKPTKALLFVLLSPVGPY-----FSSGTFNPVSLW--ANPKYVrawkggTGDCKM 235
Cdd:TIGR01122 81 -NNLRSAYIRPlVFRGDG-DLGLnpRAGYKPDVIIAAWPWGAYlgeeaLEKGIDAKVSSWrrNAPNTI------PTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 236 GGNYGSSLFAQCEAVDNGCQQVLWLyGEDHQITEVGTMNLFlywINEDGeeELATPPLDGIILPGVTRRCILDLAHQWGe 315
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILL-DVEGYVAEGSGENIF---IVKDG--VLFTPPVTSSILPGITRDTVITLAKELG- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296010904 316 FKVSERYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDIlykgETIHIPTMENGPkLASRILSKLTDIQYGREESDW 393
Cdd:TIGR01122 226 IEVVEQPISREELYTA------DEAFFTGTAAEITPIREV----DGRKIGNGRRGP-VTKKLQEAFFDLVTGGTEDYW 292
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
85-355 |
1.30e-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: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 85 IKPLQNLSLHPGSSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSA--VRATLPvFDKEELLECIQQLVKLDQe 162
Cdd:cd01558 6 YVPREEAKVSVFDRGFLFGDGVYEVIRVYNG-----KPFALDEHLDRLYRSAkeLRIDIP-YTREELKELIRELVAKNE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 163 wvpySTSASLYIRPTFiGTEP-SLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPkyVRAWkggtGDCKM-GGNYG 240
Cdd:cd01558 79 ----GGEGDVYIQVTR-GVGPrGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVP--DIRW----LRCDIkSLNLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 241 SSLFAQCEAVDNGCQQVlWLYGEDHQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSE 320
Cdd:cd01558 148 NNVLAKQEAKEAGADEA-ILLDADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGITRATVIELAKELG-IPVEE 220
|
250 260 270
....*....|....*....|....*....|....*
gi 296010904 321 RYLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 355
Cdd:cd01558 221 RPFSLEELYTA------DEVFLTSTTAEVMPVVEI 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
107-355 |
3.32e-12 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 66.43 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 107 FEGLKAFRGvdnkiRLFQPNLNMDRMYRSA--VRATLPVfDKEELLECIQQLVKLDQewvpySTSAslYIRPTFIGTEPS 184
Cdd:PRK08320 33 FEGIRAYNG-----RVFRLKEHIDRLYDSAkaIMLEIPL-SKEEMTEIVLETLRKNN-----LRDA--YIRLVVSRGVGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 185 LGV--KKPTKALLFVLLSPVGPYF------------SSGTFNPV-SLWANPKYVrawkggtgdckmggNYGSSLFAQCEA 249
Cdd:PRK08320 100 LGLdpRKCPKPTVVCIAEPIGLYPgelyekglkvitVSTRRNRPdALSPQVKSL--------------NYLNNILAKIEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 250 VDNGCQQVLWLygeDHQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDD 327
Cdd:PRK08320 166 NLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG-IPVREELFTLHD 236
|
250 260
....*....|....*....|....*...
gi 296010904 328 LTTAlegnrvREMFGSGTACVVCPVSDI 355
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 ... |
99-339 |
6.91e-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: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 99 ALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSAVRATLPVFDKEELLeciQQLVKLDQEWVPYSTSASLYI-Rpt 177
Cdd:cd01559 3 GFAYGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLR---AALESLLAANDIDEGRIRLILsR-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 178 fiGTEP----SLGVKKPTkallfvLLSPVGPYFSSGTFNPVSLWANPkyVRAWKGGTgdckMGG----NYGSSLFAQCEA 249
Cdd:cd01559 73 --GPGGrgyaPSVCPGPA------LYVSVIPLPPAWRQDGVRLITCP--VRLGEQPL----LAGlkhlNYLENVLAKREA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 250 VDNGCQQVLWLYGEDHqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRRCILDLAHQWGEfKVSERYLTMDDLT 329
Cdd:cd01559 139 RDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGY-AVDERPLRLEDLL 211
|
250
....*....|...
gi 296010904 330 TALE---GNRVRE 339
Cdd:cd01559 212 AADEaflTNSLLG 224
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
93-355 |
1.08e-05 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 46.89 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 93 LHPGSSALHYAVELFEGLKAFRGvdnkiRLFQPNLNMDRMYRSA--VRATLPvFDKEELLECIQQLVKLdqewvpySTSA 170
Cdd:PRK07544 25 VHVLTHGLHYASSVFEGERAYGG-----KIFKLREHSERLRRSAelLDFEIP-YSVAEIDAAKKETLAA-------NGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 171 SLYIRPT-FIGTEpSLGVKKP-TKALLFVLLSPVGPYFSS-----GTFNPVSLWANPkyvrAWKGGTGDCKMGGNYGSSL 243
Cdd:PRK07544 92 DAYVRPVaWRGSE-MMGVSAQqNKIHLAIAAWEWPSYFDPeakmkGIRLDIAKWRRP----DPETAPSAAKAAGLYMICT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 244 FAQCEAVDNGCQQVLWLygeDH--QITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRRCILDLAHQWGeFKVSER 321
Cdd:PRK07544 167 ISKHAAEAKGYADALML---DYrgYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIELAKRRG-IEVVER 236
|
250 260 270
....*....|....*....|....*....|....
gi 296010904 322 YLTMDDLTTAlegnrvREMFGSGTACVVCPVSDI 355
Cdd:PRK07544 237 HIMPEELAGF------SECFLTGTAAEVTPVSEI 264
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
260-341 |
1.15e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 46.12 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 260 LYGEDHQITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRRCILDlahqwgEFKVSERYLTMDDLTTA---LEGNR 336
Cdd:PRK07546 130 LLNERGEVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSAraiWVGNS 199
|
....*
gi 296010904 337 VREMF 341
Cdd:PRK07546 200 LRGLI 204
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
249-362 |
9.90e-05 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 43.77 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 249 AVDNGCQQVlWlYGEDHQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDl 328
Cdd:PRK06680 163 AKEAGAQEA-W-MVDDGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPFTLQE- 234
|
90 100 110
....*....|....*....|....*....|....
gi 296010904 329 ttALEgnrVREMFGSGTACVVCPVSDIlyKGETI 362
Cdd:PRK06680 235 --AYA---AREAFITAASSFVFPVVQI--DGKQI 261
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
238-352 |
3.04e-03 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 39.23 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296010904 238 NYGSSLFAQCEAVDNGCQQVLWLyGEDHQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRRCILDLAHQWGEF 316
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 296010904 317 K----VSERYLTMDdlttalEGNRVREMFGSGTACVVCPV 352
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
288-331 |
6.66e-03 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 38.02 E-value: 6.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 296010904 288 LATPPLDGIILPGVTRRCILDLAHQWGeFKVSERYLTMDDLTTA 331
Cdd:PRK07849 206 LLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
|
|
| |
