|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
33-386 |
1.48e-139 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 401.45 E-value: 1.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 33 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 112
Cdd:PRK13357 8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 113 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 191
Cdd:PRK13357 87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 192 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 270
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 271 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 350
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 1705437 351 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 386
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
81-375 |
8.46e-130 |
|
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: 8.46e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 81 IHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASL 160
Cdd:cd01557 2 LHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 161 YIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPkYIRAWKGGTGDCKMGGNYGASLLAQCEAVEN 240
Cdd:cd01557 82 YIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGE-KGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 241 GCQQVLWLYGKDNQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAl 320
Cdd:cd01557 160 GYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1705437 321 egnrvKEMFGSGTACVVCPVSDILYKGQmlhIPTMENGPKLASRILGKLTDIQYG 375
Cdd:cd01557 233 -----DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
68-385 |
4.46e-104 |
|
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: 4.46e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 68 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQI 147
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 148 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGN 226
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 227 YGASLLAQCEAVENGCQQVLWLYGK-DNQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGeFK 305
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVeHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 306 VCERHLTMDDLATALEgnRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPkLASRILGKLTDIQYGRVES--DWTI 383
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
..
gi 1705437 384 EL 385
Cdd:TIGR01123 312 EV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
68-378 |
3.89e-75 |
|
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: 3.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 68 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQ 146
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 147 IDQEwvpystsASLYIRPTFIGTEPSLGVKKP-SKALLFVILSPVGPYFSSGSFTPVSLWANPkYIRAWKGGTGDCKmGG 225
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 226 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFK 305
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705437 306 VCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDIlyKGQmlHIPTMENGPkLASRILGKLTDIQYGRVE 378
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 ... |
94-343 |
3.63e-36 |
|
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: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 94 LFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIDQEWVPYstsaslyIRPTFIGTEPS 172
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 173 LGVKKPS-KALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAwkggtgDCKmGGNYGASLLAQCEAVENGCQQVLwLYGK 251
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 252 DNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGS 331
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 1705437 332 GTACVVCPVSDI 343
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
33-386 |
1.48e-139 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 401.45 E-value: 1.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 33 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 112
Cdd:PRK13357 8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 113 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 191
Cdd:PRK13357 87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 192 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 270
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 271 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 350
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 1705437 351 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 386
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
81-375 |
8.46e-130 |
|
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: 8.46e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 81 IHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASL 160
Cdd:cd01557 2 LHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 161 YIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPkYIRAWKGGTGDCKMGGNYGASLLAQCEAVEN 240
Cdd:cd01557 82 YIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGE-KGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 241 GCQQVLWLYGKDNQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAl 320
Cdd:cd01557 160 GYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1705437 321 egnrvKEMFGSGTACVVCPVSDILYKGQmlhIPTMENGPKLASRILGKLTDIQYG 375
Cdd:cd01557 233 -----DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
68-385 |
4.46e-104 |
|
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: 4.46e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 68 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQI 147
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 148 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGN 226
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 227 YGASLLAQCEAVENGCQQVLWLYGK-DNQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGeFK 305
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVeHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 306 VCERHLTMDDLATALEgnRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPkLASRILGKLTDIQYGRVES--DWTI 383
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
..
gi 1705437 384 EL 385
Cdd:TIGR01123 312 EV 313
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
85-347 |
1.56e-76 |
|
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: 1.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 85 ASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIdqewvpySTSASLYIR 163
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKG-----RLFRLDEHLDRLNRSAKRLGLPIpYDREELREALKELVAA-------NNGASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 164 PTFIGTEPSLGV--KKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGNYgASLLAQCEAVENG 241
Cdd:cd00449 69 PLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGGE-KGVRLITSPDRRRAAPGGTGDAKTGGNL-NSVLAKQEAAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 242 CQQVLWLYGkDNQITEVGTMNLFLYWineDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAle 321
Cdd:cd00449 147 ADEALLLDD-NGYVTEGSASNVFIVK---DGE--LVTPPLDGGILPGITRDSVIELAKELG-IKVEERPISLDELYAA-- 217
|
250 260
....*....|....*....|....*.
gi 1705437 322 gnrvKEMFGSGTACVVCPVSDILYKG 347
Cdd:cd00449 218 ----DEVFLTGTAAEVTPVTEIDGRG 239
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
68-378 |
3.89e-75 |
|
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: 3.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 68 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQ 146
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 147 IDQEwvpystsASLYIRPTFIGTEPSLGVKKP-SKALLFVILSPVGPYFSSGSFTPVSLWANPkYIRAWKGGTGDCKmGG 225
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 226 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFK 305
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705437 306 VCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDIlyKGQmlHIPTMENGPkLASRILGKLTDIQYGRVE 378
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGR--PIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
43-385 |
4.80e-67 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 217.79 E-value: 4.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 43 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 122
Cdd:PLN02782 71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 123 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVkKPSKALLFVI-LSPVGPYFSSGsFTP 201
Cdd:PLN02782 151 GAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGL-APAPEYTFLIyVSPVGNYFKEG-VAP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 202 VSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWL---YGKdnQITEVGTMNLFLYWINedgeeELAT 278
Cdd:PLN02782 229 INLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvHKK--YLEEVSSCNIFIVKDN-----VIST 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 279 PPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQmlHIPTMENG 358
Cdd:PLN02782 302 PAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGK--RVSYGEGG 372
|
330 340 350
....*....|....*....|....*....|
gi 1705437 359 PKLASRIL-GKLTDIQYGRVES--DWTIEL 385
Cdd:PLN02782 373 FGTVSQQLyTVLTSLQMGLIEDnmNWTVEL 402
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
45-385 |
7.66e-63 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 205.16 E-value: 7.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 45 DSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSA 124
Cdd:PLN03117 23 EELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 125 VRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSftPVSL 204
Cdd:PLN03117 103 DRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASS--GLNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 205 WANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWL---YGKDnqITEVGTMNLFLYWINedgeeELATPPL 281
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdaaTGKN--IEELSACNIFILKGN-----IVSTPPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 282 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGpkL 361
Cdd:PLN03117 254 SGTILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--L 324
|
330 340
....*....|....*....|....*.
gi 1705437 362 ASRILGKLTDIQYGRVESD--WTIEL 385
Cdd:PLN03117 325 STKLHLILTNIQMGVVEDKkgWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
43-380 |
5.14e-54 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 183.38 E-value: 5.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 43 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 122
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 123 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGsFTPV 202
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 203 SLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYG-KDNQITEVGTMNLFLYwinedGEEELATPPL 281
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 282 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENgpKL 361
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
|
330
....*....|....*....
gi 1705437 362 ASRILGKLTDIQYGRVESD 380
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
43-385 |
9.98e-49 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 169.13 E-value: 9.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 43 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 122
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 123 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPV 202
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 203 SLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLYWINedgeeELATPPL 281
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKnIEEVSAANIFLVKGN-----IIVTPAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 282 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENgpKL 361
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
|
330 340
....*....|....*....|....*.
gi 1705437 362 ASRILGKLTDIQYGRVE--SDWTIEL 385
Cdd:PLN02883 358 TQQLRSILLGIQTGSIQdtKDWVLQI 383
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
94-343 |
3.63e-36 |
|
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: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 94 LFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIDQEWVPYstsaslyIRPTFIGTEPS 172
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 173 LGVKKPS-KALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAwkggtgDCKmGGNYGASLLAQCEAVENGCQQVLwLYGK 251
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 252 DNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGS 331
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 1705437 332 GTACVVCPVSDI 343
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
75-381 |
4.51e-30 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 117.17 E-value: 4.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 75 PFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIrLFRPDLNMDRMCRSA--VRTTLPmFDKEELLKCILQLLQIDQewv 152
Cdd:PRK06606 17 PWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAkiLRMEIP-YSVDELMEAQREVVRKNN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 153 pystSASLYIRP-TFIGTEpSLGVKKPS-KALLFVILSPVGPYFSSGSFTP-----VSLW--ANPKYI--RAwkggtgdc 221
Cdd:PRK06606 92 ----LKSAYIRPlVFVGDE-GLGVRPHGlPTDVAIAAWPWGAYLGEEALEKgirvkVSSWtrHAPNSIptRA-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 222 KMGGNYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQW 301
Cdd:PRK06606 159 KASGNYLNSILAKTEARRNGYDEALLL-DVEGYVSEGSGENIF---IVRDGV--LYTPPLTSSILEGITRDTVITLAKDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 302 GeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI-LYKgqmlhIPTMENGPkLASRILGKLTDIQYGRVE-- 378
Cdd:PRK06606 233 G-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREVdGRQ-----IGNGKRGP-ITEKLQSAYFDIVRGRTEky 299
|
...
gi 1705437 379 SDW 381
Cdd:PRK06606 300 AHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
75-343 |
7.12e-26 |
|
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: 7.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 75 PFGNLPIHPAASVLHYAVELFEGLKAFRGvDNKIRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIdqewvp 153
Cdd:TIGR01122 8 DWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEIpYSKEELMEATRETLRK------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 154 ySTSASLYIRP-TFIGTEpSLGVKKPSKAL--LFVILSPVGPY-----FSSGSFTPVSLW--ANPKYIrawkggTGDCKM 223
Cdd:TIGR01122 81 -NNLRSAYIRPlVFRGDG-DLGLNPRAGYKpdVIIAAWPWGAYlgeeaLEKGIDAKVSSWrrNAPNTI------PTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 224 GGNYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGe 303
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILL-DVEGYVAEGSGENIF---IVKDG--VLFTPPVTSSILPGITRDTVITLAKELG- 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1705437 304 FKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:TIGR01122 226 IEVVEQPISREELYTA------DEAFFTGTAAEITPIREV 259
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
95-343 |
2.99e-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: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 95 FEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpySTSASLYIRPTFiGTEP- 171
Cdd:cd01558 28 YEVIRVYNG-----KPFALDEHLDRLYRSAkeLRIDIPY-TREELKELIRELVAKNE-----GGEGDVYIQVTR-GVGPr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 172 SLGVKKPSKALLFVILSPVGPYFSSGSFTPVSLwANPKYIRaWkggtGDCKM-GGNYGASLLAQCEAVENGCQQVlWLYG 250
Cdd:cd01558 96 GHDFPKCVKPTVVIITQPLPLPPAELLEKGVRV-ITVPDIR-W----LRCDIkSLNLLNNVLAKQEAKEAGADEA-ILLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 251 KDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFG 330
Cdd:cd01558 169 ADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGITRATVIELAKELG-IPVEERPFSLEELYTA------DEVFL 236
|
250
....*....|...
gi 1705437 331 SGTACVVCPVSDI 343
Cdd:cd01558 237 TSTTAEVMPVVEI 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
95-343 |
2.64e-14 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 72.60 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 95 FEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpySTSAslYIRPTFIGTEPS 172
Cdd:PRK08320 33 FEGIRAYNG-----RVFRLKEHIDRLYDSAkaIMLEIPL-SKEEMTEIVLETLRKNN-----LRDA--YIRLVVSRGVGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 173 LGV--KKPSKALLFVILSPVGPYFssGSF---------------TPVSLWANPKYIrawkggtgdckmggNYGASLLAQC 235
Cdd:PRK08320 100 LGLdpRKCPKPTVVCIAEPIGLYP--GELyekglkvitvstrrnRPDALSPQVKSL--------------NYLNNILAKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 236 EAVENGCQQVLWLygkDNQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTM 313
Cdd:PRK08320 164 EANLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG-IPVREELFTL 234
|
250 260 270
....*....|....*....|....*....|
gi 1705437 314 DDLATAlegnrvKEMFGSGTACVVCPVSDI 343
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 ... |
88-321 |
1.87e-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: 63.48 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 88 LHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIdqewvpySTSASLYIRPTFI 167
Cdd:cd01559 4 FAYGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAA-------NDIDEGRIRLILS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 168 -GTEP----SLGVKKPSkALLFVILSPVGPYFSSGS--FTPVSLWANP-----KYIrawkggtgdckmggNYGASLLAQC 235
Cdd:cd01559 72 rGPGGrgyaPSVCPGPA-LYVSVIPLPPAWRQDGVRliTCPVRLGEQPllaglKHL--------------NYLENVLAKR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 236 EAVENGCQQVLWLYGKDNqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRQSILELAQQWGEFKVcERHLTMDD 315
Cdd:cd01559 137 EARDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGYAVD-ERPLRLED 209
|
....*.
gi 1705437 316 LATALE 321
Cdd:cd01559 210 LLAADE 215
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
77-343 |
9.68e-10 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 58.81 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 77 GNLPIHPAASvlH---YAVELFEGLKAFRGVdnkirlfRPDLnmDRMC----RSAVRTTL-PMFDKEELLKCILQLLQid 148
Cdd:PRK13356 18 GNVPIMGPAD--HaawLGSTVFDGARAFEGV-------TPDL--DLHCarvnRSAEALGLkPTVSAEEIEALAREGLK-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 149 qewvPYSTSASLYIRPTFIGTEPSLGVKKPSK-----AL-LFVILSPvGPYFSSGSFTPvslwanpkYIRAW-KGGTGDC 221
Cdd:PRK13356 85 ----RFDPDTALYIRPMYWAEDGFASGVAPDPestrfALcLEEAPMP-EPTGFSLTLSP--------FRRPTlEMAPTDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 222 KMGGNYGASLLAQCEAVENGCQQVLWLYGKDNqITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQW 301
Cdd:PRK13356 152 KAGCLYPNNARALREARSRGFDNALVLDMLGN-VAETATSNVF---MVKDGV--VFTPVPNGTFLNGITRQRVIALLRED 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1705437 302 GeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:PRK13356 226 G-VTVVETTLTYEDFLEA------DEVFSTGNYSKVVPVTRF 260
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
81-343 |
5.31e-07 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 50.74 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 81 IHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAvrttlpmfdkeellkcilQLLQIDqewVPYS----- 155
Cdd:PRK07544 25 VHVLTHGLHYASSVFEGERAYGG-----KIFKLREHSERLRRSA------------------ELLDFE---IPYSvaeid 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 156 --TSASL--------YIRPT-FIGTEpSLGVKKPSKALLFVILS-PVGPYFSS-----GSFTPVSLWANPkyirAWKGGT 218
Cdd:PRK07544 79 aaKKETLaangltdaYVRPVaWRGSE-MMGVSAQQNKIHLAIAAwEWPSYFDPeakmkGIRLDIAKWRRP----DPETAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 219 GDCKMGGNYGASLLAQCEAVENGCQQVLWL-YgkDNQITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRQSILEL 297
Cdd:PRK07544 154 SAAKAAGLYMICTISKHAAEAKGYADALMLdY--RGYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIEL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1705437 298 AQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:PRK07544 226 AKRRG-IEVVERHIMPEELAGF------SECFLTGTAAEVTPVSEI 264
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
90-343 |
3.17e-06 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 48.41 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 90 YAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpystSASLYIR---- 163
Cdd:PRK12479 29 YGDGVFEGIRSYGG-----NVFCLKEHVKRLYESAksILLTIPL-TVDEMEEAVLQTLQKNE-------YADAYIRlivs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 164 --PTFIGTEPSlGVKKPSKALLFVILSPVGPYFSSGSFTPVSLWA---NPKYIrawkggtgDCKMGG-NYGASLLAQCEA 237
Cdd:PRK12479 96 rgKGDLGLDPR-SCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASrrnTPDAL--------DPRIKSmNYLNNVLVKIEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 238 VENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLA 317
Cdd:PRK12479 167 AQAGVLEALML-NQQGYVCEGSGDNVF---VVKDGK--VLTPPSYLGALEGITRNSVIELCERLS-IPCEERPFTRHDVY 239
|
250 260
....*....|....*....|....*.
gi 1705437 318 TAlegnrvKEMFGSGTACVVCPVSDI 343
Cdd:PRK12479 240 VA------DEVFLTGTAAELIPVVKV 259
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
232-343 |
9.94e-06 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 46.85 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 232 LAQCEAVENGCQQVlWLYGkDNQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHL 311
Cdd:PRK06680 158 LAKQAAKEAGAQEA-WMVD-DGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPF 230
|
90 100 110
....*....|....*....|....*....|..
gi 1705437 312 TmddLATALEgnrVKEMFGSGTACVVCPVSDI 343
Cdd:PRK06680 231 T---LQEAYA---AREAFITAASSFVFPVVQI 256
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
226-340 |
1.91e-05 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 46.16 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 226 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRQSILELAQQWGEF 304
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1705437 305 K----VCERHLTMDdlatalEGNRVKEMFGSGTACVVCPV 340
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
254-319 |
2.96e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 44.58 E-value: 2.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1705437 254 QITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRQSILElaqqwgEFKVCERHLTMDDLATA 319
Cdd:PRK07546 136 EVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSA 191
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
95-319 |
1.42e-03 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 40.33 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 95 FEGLKAFRGvdnKIRLFRPDLnmDRMCRSAVRTTLPMFDKEELLKCILQLLQidqEWvpYSTSASLYIRPTFigtepSLG 174
Cdd:PRK07849 42 FETLLVRDG---RPCNLEAHL--ERLARSAALLDLPEPDLDRWRRAVELAIE---EW--RAPEDEAALRLVY-----SRG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705437 175 VKKPSKALLFVILSPVGPYFSSGSFTPVSLWANPkyiRAWKGGTGDCK---MGG----NYGASLLAQCEAVENGCQQVLW 247
Cdd:PRK07849 107 RESGGAPTAWVTVSPVPERVARARREGVSVITLD---RGYPSDAAERApwlLAGaktlSYAVNMAALRYAARRGADDVIF 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1705437 248 LYGkDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATA 319
Cdd:PRK07849 184 TST-DGYVLEGPTSTVVIA---TDDR--LLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
|
|
|