|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
100-453 |
1.64e-138 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 401.45 E-value: 1.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 100 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 179
Cdd:PRK13357 8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 180 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 258
Cdd:PRK13357 87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 259 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 337
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 338 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 417
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 66792792 418 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 453
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
148-442 |
8.92e-129 |
|
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: 373.84 E-value: 8.92e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 148 IHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASL 227
Cdd:cd01557 2 LHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 228 YIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPkYIRAWKGGTGDCKMGGNYGASLLAQCEAVEN 307
Cdd:cd01557 82 YIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGE-KGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 308 GCQQVLWLYGKDNQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAl 387
Cdd:cd01557 160 GYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 66792792 388 egnrvKEMFGSGTACVVCPVSDILYKGQmlhIPTMENGPKLASRILGKLTDIQYG 442
Cdd:cd01557 233 -----DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
135-452 |
4.12e-103 |
|
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: 309.77 E-value: 4.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 135 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQI 214
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 215 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGN 293
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 294 YGASLLAQCEAVENGCQQVLWLYGK-DNQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGeFK 372
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVeHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 373 VCERHLTMDDLATALEgnRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPkLASRILGKLTDIQYGRVES--DWTI 450
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
..
gi 66792792 451 EL 452
Cdd:TIGR01123 312 EV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
135-445 |
2.81e-74 |
|
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: 234.70 E-value: 2.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 135 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQ 213
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 214 IDQEwvpystsASLYIRPTFIGTEPSLGVKKP-SKALLFVILSPVGPYFSSGSFTPVSLWANPkYIRAWKGGTGDCKmGG 292
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 293 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFK 372
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66792792 373 VCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDIlyKGQmlHIPTMENGPkLASRILGKLTDIQYGRVE 445
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGR--PIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
161-410 |
1.20e-35 |
|
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: 131.33 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 161 LFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIDQEWVPYstsaslyIRPTFIGTEPS 239
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 240 LGVKKPS-KALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAwkggtgDCKmGGNYGASLLAQCEAVENGCQQVLwLYGK 318
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 319 DNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGS 398
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 66792792 399 GTACVVCPVSDI 410
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
100-453 |
1.64e-138 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 401.45 E-value: 1.64e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 100 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 179
Cdd:PRK13357 8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 180 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 258
Cdd:PRK13357 87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 259 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 337
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 338 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 417
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 66792792 418 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 453
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
148-442 |
8.92e-129 |
|
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: 373.84 E-value: 8.92e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 148 IHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASL 227
Cdd:cd01557 2 LHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 228 YIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPkYIRAWKGGTGDCKMGGNYGASLLAQCEAVEN 307
Cdd:cd01557 82 YIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGE-KGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 308 GCQQVLWLYGKDNQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAl 387
Cdd:cd01557 160 GYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 66792792 388 egnrvKEMFGSGTACVVCPVSDILYKGQmlhIPTMENGPKLASRILGKLTDIQYG 442
Cdd:cd01557 233 -----DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
135-452 |
4.12e-103 |
|
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: 309.77 E-value: 4.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 135 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQI 214
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 215 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGN 293
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 294 YGASLLAQCEAVENGCQQVLWLYGK-DNQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGeFK 372
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVeHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 373 VCERHLTMDDLATALEgnRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPkLASRILGKLTDIQYGRVES--DWTI 450
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
..
gi 66792792 451 EL 452
Cdd:TIGR01123 312 EV 313
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
152-414 |
1.14e-75 |
|
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: 237.11 E-value: 1.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 152 ASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIdqewvpySTSASLYIR 230
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKG-----RLFRLDEHLDRLNRSAKRLGLPIpYDREELREALKELVAA-------NNGASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 231 PTFIGTEPSLGV--KKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGNYgASLLAQCEAVENG 308
Cdd:cd00449 69 PLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGGE-KGVRLITSPDRRRAAPGGTGDAKTGGNL-NSVLAKQEAAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 309 CQQVLWLYGkDNQITEVGTMNLFLYWineDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAle 388
Cdd:cd00449 147 ADEALLLDD-NGYVTEGSASNVFIVK---DGE--LVTPPLDGGILPGITRDSVIELAKELG-IKVEERPISLDELYAA-- 217
|
250 260
....*....|....*....|....*.
gi 66792792 389 gnrvKEMFGSGTACVVCPVSDILYKG 414
Cdd:cd00449 218 ----DEVFLTGTAAEVTPVTEIDGRG 239
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
135-445 |
2.81e-74 |
|
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: 234.70 E-value: 2.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 135 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQ 213
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 214 IDQEwvpystsASLYIRPTFIGTEPSLGVKKP-SKALLFVILSPVGPYFSSGSFTPVSLWANPkYIRAWKGGTGDCKmGG 292
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 293 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFK 372
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66792792 373 VCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDIlyKGQmlHIPTMENGPkLASRILGKLTDIQYGRVE 445
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGR--PIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
22-452 |
6.38e-66 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 217.02 E-value: 6.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 22 LSPATPNCSPGLSGSAVRHESPLCHVFPRSRSFVMACLPRATATLarqdCSNGCSAPFagergSEEVAETFRAKDLiitp 101
Cdd:PLN02782 4 LCPSRAFSTRLHSSSRRLNFPPPSSLSLRHSNSSVSSNPISSKAI----SLTRCDAVS-----SSSYTEVTELADI---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 102 atvlkekpDPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPD 181
Cdd:PLN02782 71 --------DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 182 LNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVkKPSKALLFVI-LSPVGPY 260
Cdd:PLN02782 143 ENAIRMRNGAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGL-APAPEYTFLIyVSPVGNY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 261 FSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWL---YGKdnQITEVGTMNLFLYWINe 337
Cdd:PLN02782 222 FKEG-VAPINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvHKK--YLEEVSSCNIFIVKDN- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 338 dgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQml 417
Cdd:PLN02782 298 ----VISTPAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGK-- 364
|
410 420 430
....*....|....*....|....*....|....*...
gi 66792792 418 HIPTMENGPKLASRIL-GKLTDIQYGRVES--DWTIEL 452
Cdd:PLN02782 365 RVSYGEGGFGTVSQQLyTVLTSLQMGLIEDnmNWTVEL 402
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
112-452 |
4.77e-62 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 205.16 E-value: 4.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 112 DSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSA 191
Cdd:PLN03117 23 EELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 192 VRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSftPVSL 271
Cdd:PLN03117 103 DRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASS--GLNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 272 WANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWL---YGKDnqITEVGTMNLFLYWINedgeeELATPPL 348
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdaaTGKN--IEELSACNIFILKGN-----IVSTPPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 349 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGpkL 428
Cdd:PLN03117 254 SGTILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--L 324
|
330 340
....*....|....*....|....*.
gi 66792792 429 ASRILGKLTDIQYGRVESD--WTIEL 452
Cdd:PLN03117 325 STKLHLILTNIQMGVVEDKkgWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
110-447 |
2.78e-53 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 183.38 E-value: 2.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 110 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 189
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 190 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGsFTPV 269
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 270 SLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYG-KDNQITEVGTMNLFLYwinedGEEELATPPL 348
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 349 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENgpKL 428
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
|
330
....*....|....*....
gi 66792792 429 ASRILGKLTDIQYGRVESD 447
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
110-452 |
4.86e-48 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 169.13 E-value: 4.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 110 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 189
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 190 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPV 269
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 270 SLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLYWINedgeeELATPPL 348
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKnIEEVSAANIFLVKGN-----IIVTPAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 349 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENgpKL 428
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
|
330 340
....*....|....*....|....*.
gi 66792792 429 ASRILGKLTDIQYGRVE--SDWTIEL 452
Cdd:PLN02883 358 TQQLRSILLGIQTGSIQdtKDWVLQI 383
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
161-410 |
1.20e-35 |
|
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: 131.33 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 161 LFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIDQEWVPYstsaslyIRPTFIGTEPS 239
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 240 LGVKKPS-KALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAwkggtgDCKmGGNYGASLLAQCEAVENGCQQVLwLYGK 318
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 319 DNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGS 398
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 66792792 399 GTACVVCPVSDI 410
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
142-448 |
1.24e-29 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 117.17 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 142 PFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIrLFRPDLNMDRMCRSA--VRTTLPmFDKEELLKCILQLLQIDQewv 219
Cdd:PRK06606 17 PWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAkiLRMEIP-YSVDELMEAQREVVRKNN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 220 pystSASLYIRP-TFIGTEpSLGVKKPS-KALLFVILSPVGPYFSSGSFTP-----VSLW--ANPKYI--RAwkggtgdc 288
Cdd:PRK06606 92 ----LKSAYIRPlVFVGDE-GLGVRPHGlPTDVAIAAWPWGAYLGEEALEKgirvkVSSWtrHAPNSIptRA-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 289 KMGGNYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQW 368
Cdd:PRK06606 159 KASGNYLNSILAKTEARRNGYDEALLL-DVEGYVSEGSGENIF---IVRDGV--LYTPPLTSSILEGITRDTVITLAKDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 369 GeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI-LYKgqmlhIPTMENGPkLASRILGKLTDIQYGRVE-- 445
Cdd:PRK06606 233 G-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREVdGRQ-----IGNGKRGP-ITEKLQSAYFDIVRGRTEky 299
|
...
gi 66792792 446 SDW 448
Cdd:PRK06606 300 AHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
142-410 |
1.64e-25 |
|
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: 105.52 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 142 PFGNLPIHPAASVLHYAVELFEGLKAFRGvDNKIRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIdqewvp 220
Cdd:TIGR01122 8 DWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEIpYSKEELMEATRETLRK------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 221 ySTSASLYIRP-TFIGTEpSLGVKKPSKAL--LFVILSPVGPY-----FSSGSFTPVSLW--ANPKYIrawkggTGDCKM 290
Cdd:TIGR01122 81 -NNLRSAYIRPlVFRGDG-DLGLNPRAGYKpdVIIAAWPWGAYlgeeaLEKGIDAKVSSWrrNAPNTI------PTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 291 GGNYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGe 370
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILL-DVEGYVAEGSGENIF---IVKDG--VLFTPPVTSSILPGITRDTVITLAKELG- 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 66792792 371 FKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 410
Cdd:TIGR01122 226 IEVVEQPISREELYTA------DEAFFTGTAAEITPIREV 259
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
162-410 |
5.51e-21 |
|
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: 92.28 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 162 FEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpySTSASLYIRPTFiGTEP- 238
Cdd:cd01558 28 YEVIRVYNG-----KPFALDEHLDRLYRSAkeLRIDIPY-TREELKELIRELVAKNE-----GGEGDVYIQVTR-GVGPr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 239 SLGVKKPSKALLFVILSPVGPYFSSGSFTPVSLwANPKYIRaWkggtGDCKM-GGNYGASLLAQCEAVENGCQQVlWLYG 317
Cdd:cd01558 96 GHDFPKCVKPTVVIITQPLPLPPAELLEKGVRV-ITVPDIR-W----LRCDIkSLNLLNNVLAKQEAKEAGADEA-ILLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 318 KDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFG 397
Cdd:cd01558 169 ADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGITRATVIELAKELG-IPVEERPFSLEELYTA------DEVFL 236
|
250
....*....|...
gi 66792792 398 SGTACVVCPVSDI 410
Cdd:cd01558 237 TSTTAEVMPVVEI 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
162-410 |
3.79e-14 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 72.60 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 162 FEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpySTSAslYIRPTFIGTEPS 239
Cdd:PRK08320 33 FEGIRAYNG-----RVFRLKEHIDRLYDSAkaIMLEIPL-SKEEMTEIVLETLRKNN-----LRDA--YIRLVVSRGVGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 240 LGV--KKPSKALLFVILSPVGPYFssGSF---------------TPVSLWANPKYIrawkggtgdckmggNYGASLLAQC 302
Cdd:PRK08320 100 LGLdpRKCPKPTVVCIAEPIGLYP--GELyekglkvitvstrrnRPDALSPQVKSL--------------NYLNNILAKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 303 EAVENGCQQVLWLygkDNQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTM 380
Cdd:PRK08320 164 EANLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG-IPVREELFTL 234
|
250 260 270
....*....|....*....|....*....|
gi 66792792 381 DDLATAlegnrvKEMFGSGTACVVCPVSDI 410
Cdd:PRK08320 235 HDLYTA------DEVFLTGTAAEVIPVVKV 258
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
155-388 |
8.13e-11 |
|
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: 61.94 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 155 LHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIdqewvpySTSASLYIRPTFI 234
Cdd:cd01559 4 FAYGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAA-------NDIDEGRIRLILS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 235 -GTEP----SLGVKKPSkALLFVILSPVGPYFSSGS--FTPVSLWANP-----KYIrawkggtgdckmggNYGASLLAQC 302
Cdd:cd01559 72 rGPGGrgyaPSVCPGPA-LYVSVIPLPPAWRQDGVRliTCPVRLGEQPllaglKHL--------------NYLENVLAKR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 303 EAVENGCQQVLWLYGKDNqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRQSILELAQQWGEFKVcERHLTMDD 382
Cdd:cd01559 137 EARDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGYAVD-ERPLRLED 209
|
....*.
gi 66792792 383 LATALE 388
Cdd:cd01559 210 LLAADE 215
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
144-410 |
2.79e-09 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 58.04 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 144 GNLPIHPAASvlH---YAVELFEGLKAFRGVdnkirlfRPDLNM--DRMCRSAVRTTL-PMFDKEELLKCILQLLQidqe 217
Cdd:PRK13356 18 GNVPIMGPAD--HaawLGSTVFDGARAFEGV-------TPDLDLhcARVNRSAEALGLkPTVSAEEIEALAREGLK---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 218 wvPYSTSASLYIRPTFIGTEPSLGVKKPSK-----AL-LFVILSPvGPYFSSGSFTPvslwanpkYIRAW-KGGTGDCKM 290
Cdd:PRK13356 85 --RFDPDTALYIRPMYWAEDGFASGVAPDPestrfALcLEEAPMP-EPTGFSLTLSP--------FRRPTlEMAPTDAKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 291 GGNYGASLLAQCEAVENGCQQVLWLYGKDNqITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGe 370
Cdd:PRK13356 154 GCLYPNNARALREARSRGFDNALVLDMLGN-VAETATSNVF---MVKDGV--VFTPVPNGTFLNGITRQRVIALLREDG- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 66792792 371 FKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 410
Cdd:PRK13356 227 VTVVETTLTYEDFLEA------DEVFSTGNYSKVVPVTRF 260
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
148-410 |
6.89e-07 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 50.74 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 148 IHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAvrttlpmfdkeellkcilQLLQIDqewVPYS----- 222
Cdd:PRK07544 25 VHVLTHGLHYASSVFEGERAYGG-----KIFKLREHSERLRRSA------------------ELLDFE---IPYSvaeid 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 223 --TSASL--------YIRPT-FIGTEpSLGVKKPSKALLFVILS-PVGPYFSS-----GSFTPVSLWANPkyirAWKGGT 285
Cdd:PRK07544 79 aaKKETLaangltdaYVRPVaWRGSE-MMGVSAQQNKIHLAIAAwEWPSYFDPeakmkGIRLDIAKWRRP----DPETAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 286 GDCKMGGNYGASLLAQCEAVENGCQQVLWL-YgkDNQITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRQSILEL 364
Cdd:PRK07544 154 SAAKAAGLYMICTISKHAAEAKGYADALMLdY--RGYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIEL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 66792792 365 AQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 410
Cdd:PRK07544 226 AKRRG-IEVVERHIMPEELAGF------SECFLTGTAAEVTPVSEI 264
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
157-410 |
4.09e-06 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 48.41 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 157 YAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpystSASLYIR---- 230
Cdd:PRK12479 29 YGDGVFEGIRSYGG-----NVFCLKEHVKRLYESAksILLTIPL-TVDEMEEAVLQTLQKNE-------YADAYIRlivs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 231 --PTFIGTEPSlGVKKPSKALLFVILSPVGPYFSSGSFTPVSLWA---NPKYIrawkggtgDCKMGG-NYGASLLAQCEA 304
Cdd:PRK12479 96 rgKGDLGLDPR-SCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASrrnTPDAL--------DPRIKSmNYLNNVLVKIEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 305 VENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLA 384
Cdd:PRK12479 167 AQAGVLEALML-NQQGYVCEGSGDNVF---VVKDGK--VLTPPSYLGALEGITRNSVIELCERLS-IPCEERPFTRHDVY 239
|
250 260
....*....|....*....|....*.
gi 66792792 385 TAlegnrvKEMFGSGTACVVCPVSDI 410
Cdd:PRK12479 240 VA------DEVFLTGTAAELIPVVKV 259
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
299-410 |
1.28e-05 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 46.85 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 299 LAQCEAVENGCQQVlWLYGkDNQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHL 378
Cdd:PRK06680 158 LAKQAAKEAGAQEA-WMVD-DGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPF 230
|
90 100 110
....*....|....*....|....*....|..
gi 66792792 379 TmddLATALEgnrVKEMFGSGTACVVCPVSDI 410
Cdd:PRK06680 231 T---LQEAYA---AREAFITAASSFVFPVVQI 256
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
293-407 |
3.16e-05 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 45.78 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 293 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRQSILELAQQWGEF 371
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 66792792 372 K----VCERHLTMDdlatalEGNRVKEMFGSGTACVVCPV 407
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
321-386 |
9.49e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 43.43 E-value: 9.49e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66792792 321 QITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRQSILElaqqwgEFKVCERHLTMDDLATA 386
Cdd:PRK07546 136 EVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSA 191
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
162-386 |
3.15e-03 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 39.56 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 162 FEGLKAFRGvdnKIRLFRPDLnmDRMCRSAVRTTLPMFDKEELLKCILQLLQidqEWvpYSTSASLYIRPTFigtepSLG 241
Cdd:PRK07849 42 FETLLVRDG---RPCNLEAHL--ERLARSAALLDLPEPDLDRWRRAVELAIE---EW--RAPEDEAALRLVY-----SRG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66792792 242 VKKPSKALLFVILSPVGPYFSSGSFTPVSLWANPkyiRAWKGGTGDCK---MGG----NYGASLLAQCEAVENGCQQVLW 314
Cdd:PRK07849 107 RESGGAPTAWVTVSPVPERVARARREGVSVITLD---RGYPSDAAERApwlLAGaktlSYAVNMAALRYAARRGADDVIF 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66792792 315 LYGkDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATA 386
Cdd:PRK07849 184 TST-DGYVLEGPTSTVVIA---TDDR--LLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
|
|
| |
