|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
45-398 |
2.30e-139 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 401.45 E-value: 2.30e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 45 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 124
Cdd:PRK13357 8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 125 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 203
Cdd:PRK13357 87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 204 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 282
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 283 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 362
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 12851429 363 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 398
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
93-387 |
1.30e-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: 1.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 93 IHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASL 172
Cdd:cd01557 2 LHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 173 YIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPkYIRAWKGGTGDCKMGGNYGASLLAQCEAVEN 252
Cdd:cd01557 82 YIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGE-KGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 253 GCQQVLWLYGKDNQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAl 332
Cdd:cd01557 160 GYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 12851429 333 egnrvKEMFGSGTACVVCPVSDILYKGQmlhIPTMENGPKLASRILGKLTDIQYG 387
Cdd:cd01557 233 -----DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
80-397 |
6.71e-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: 6.71e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 80 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQI 159
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 160 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGN 238
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 239 YGASLLAQCEAVENGCQQVLWLYGK-DNQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGeFK 317
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVeHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 318 VCERHLTMDDLATALEgnRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPkLASRILGKLTDIQYGRVES--DWTI 395
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
..
gi 12851429 396 EL 397
Cdd:TIGR01123 312 EV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
80-390 |
5.62e-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: 5.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 80 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQ 158
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 159 IDQEwvpystsASLYIRPTFIGTEPSLGVKKP-SKALLFVILSPVGPYFSSGSFTPVSLWANPkYIRAWKGGTGDCKmGG 237
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 238 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFK 317
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12851429 318 VCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDIlyKGQmlHIPTMENGPkLASRILGKLTDIQYGRVE 390
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 ... |
106-355 |
4.60e-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: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 106 LFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIDQEWVPYstsaslyIRPTFIGTEPS 184
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 185 LGVKKPS-KALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAwkggtgDCKmGGNYGASLLAQCEAVENGCQQVLwLYGK 263
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 264 DNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGS 343
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 12851429 344 GTACVVCPVSDI 355
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
45-398 |
2.30e-139 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 401.45 E-value: 2.30e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 45 TPATVLKEKPDPDSLVFGATFTDHMLTVEWSsASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFR 124
Cdd:PRK13357 8 NPTSDEKRAIDWANLGFGYVFTDHMVVIDYK-DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 125 PDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWV-PYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVG 203
Cdd:PRK13357 87 PDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 204 PYFSSGsFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLywINE 282
Cdd:PRK13357 167 AYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 283 DGEEelaTPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQML 362
Cdd:PRK13357 244 DGTV---TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEF 319
|
330 340 350
....*....|....*....|....*....|....*...
gi 12851429 363 HIPTMENGPkLASRILGKLTDIQYGRVES--DWTIELP 398
Cdd:PRK13357 320 VIGDGEVGP-VTQKLYDELTGIQFGDVEDphGWIVKVD 356
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
93-387 |
1.30e-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: 1.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 93 IHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASL 172
Cdd:cd01557 2 LHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGASL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 173 YIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPkYIRAWKGGTGDCKMGGNYGASLLAQCEAVEN 252
Cdd:cd01557 82 YIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGE-KGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 253 GCQQVLWLYGKDNQITEVGTMNLFLYWINedgeeELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAl 332
Cdd:cd01557 160 GYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 12851429 333 egnrvKEMFGSGTACVVCPVSDILYKGQmlhIPTMENGPKLASRILGKLTDIQYG 387
Cdd:cd01557 233 -----DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
80-397 |
6.71e-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: 6.71e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 80 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQI 159
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 160 DQEWVP-YSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGN 238
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGL-APVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 239 YGASLLAQCEAVENGCQQVLWLYGK-DNQITEVGTMNLFLywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGeFK 317
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVeHTYIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 318 VCERHLTMDDLATALEgnRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPkLASRILGKLTDIQYGRVES--DWTI 395
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGE-VTKALYDELTDIQYGDFEDpyGWIV 311
|
..
gi 12851429 396 EL 397
Cdd:TIGR01123 312 EV 313
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
97-359 |
2.25e-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: 2.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 97 ASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIdqewvpySTSASLYIR 175
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKG-----RLFRLDEHLDRLNRSAKRLGLPIpYDREELREALKELVAA-------NNGASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 176 PTFIGTEPSLGV--KKPSKALLFVILSPVGPYFSSGSfTPVSLWANPKYIRAWKGGTGDCKMGGNYgASLLAQCEAVENG 253
Cdd:cd00449 69 PLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGGE-KGVRLITSPDRRRAAPGGTGDAKTGGNL-NSVLAKQEAAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 254 CQQVLWLYGkDNQITEVGTMNLFLYWineDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAle 333
Cdd:cd00449 147 ADEALLLDD-NGYVTEGSASNVFIVK---DGE--LVTPPLDGGILPGITRDSVIELAKELG-IKVEERPISLDELYAA-- 217
|
250 260
....*....|....*....|....*.
gi 12851429 334 gnrvKEMFGSGTACVVCPVSDILYKG 359
Cdd:cd00449 218 ----DEVFLTGTAAEVTPVTEIDGRG 239
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
80-390 |
5.62e-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: 5.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 80 WEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQ 158
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 159 IDQEwvpystsASLYIRPTFIGTEPSLGVKKP-SKALLFVILSPVGPYFSSGSFTPVSLWANPkYIRAWKGGTGDCKmGG 237
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 238 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFK 317
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12851429 318 VCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDIlyKGQmlHIPTMENGPkLASRILGKLTDIQYGRVE 390
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGR--PIGDGKPGP-VTRRLRELYTDIVRGEAE 284
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
55-397 |
7.21e-67 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 217.41 E-value: 7.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 55 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 134
Cdd:PLN02782 71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 135 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVkKPSKALLFVI-LSPVGPYFSSGsFTP 213
Cdd:PLN02782 151 GAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGL-APAPEYTFLIyVSPVGNYFKEG-VAP 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 214 VSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWL---YGKdnQITEVGTMNLFLYWINedgeeELAT 290
Cdd:PLN02782 229 INLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLdcvHKK--YLEEVSSCNIFIVKDN-----VIST 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 291 PPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQmlHIPTMENG 370
Cdd:PLN02782 302 PAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGK--RVSYGEGG 372
|
330 340 350
....*....|....*....|....*....|
gi 12851429 371 PKLASRIL-GKLTDIQYGRVES--DWTIEL 397
Cdd:PLN02782 373 FGTVSQQLyTVLTSLQMGLIEDnmNWTVEL 402
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
57-397 |
1.08e-62 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 205.16 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 57 DSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSA 136
Cdd:PLN03117 23 EELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 137 VRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSftPVSL 216
Cdd:PLN03117 103 DRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASS--GLNL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 217 WANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWL---YGKDnqITEVGTMNLFLYWINedgeeELATPPL 293
Cdd:PLN03117 181 KVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLdaaTGKN--IEELSACNIFILKGN-----IVSTPPT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 294 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGpkL 373
Cdd:PLN03117 254 SGTILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA--L 324
|
330 340
....*....|....*....|....*.
gi 12851429 374 ASRILGKLTDIQYGRVESD--WTIEL 397
Cdd:PLN03117 325 STKLHLILTNIQMGVVEDKkgWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
55-392 |
7.08e-54 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 183.38 E-value: 7.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 55 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 134
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 135 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGsFTPV 214
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 215 SLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYG-KDNQITEVGTMNLFLYwinedGEEELATPPL 293
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 294 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENgpKL 373
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SV 361
|
330
....*....|....*....
gi 12851429 374 ASRILGKLTDIQYGRVESD 392
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIEDN 380
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
55-397 |
1.35e-48 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 169.13 E-value: 1.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 55 DPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCR 134
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 135 SAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSfTPV 214
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 215 SLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQ-ITEVGTMNLFLYWINedgeeELATPPL 293
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKnIEEVSAANIFLVKGN-----IIVTPAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 294 DGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDILYKGQMLHIPTMENgpKL 373
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
|
330 340
....*....|....*....|....*.
gi 12851429 374 ASRILGKLTDIQYGRVE--SDWTIEL 397
Cdd:PLN02883 358 TQQLRSILLGIQTGSIQdtKDWVLQI 383
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
106-355 |
4.60e-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: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 106 LFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIDQEWVPYstsaslyIRPTFIGTEPS 184
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVGR-------LRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 185 LGVKKPS-KALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAwkggtgDCKmGGNYGASLLAQCEAVENGCQQVLwLYGK 263
Cdd:pfam01063 70 FGLPTSDpTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 264 DNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFGS 343
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 12851429 344 GTACVVCPVSDI 355
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
87-393 |
5.53e-30 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 117.17 E-value: 5.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 87 PFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIrLFRPDLNMDRMCRSA--VRTTLPmFDKEELLKCILQLLQIDQewv 164
Cdd:PRK06606 17 PWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAkiLRMEIP-YSVDELMEAQREVVRKNN--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 165 pystSASLYIRP-TFIGTEpSLGVKKPS-KALLFVILSPVGPYFSSGSFTP-----VSLW--ANPKYI--RAwkggtgdc 233
Cdd:PRK06606 92 ----LKSAYIRPlVFVGDE-GLGVRPHGlPTDVAIAAWPWGAYLGEEALEKgirvkVSSWtrHAPNSIptRA-------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 234 KMGGNYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQW 313
Cdd:PRK06606 159 KASGNYLNSILAKTEARRNGYDEALLL-DVEGYVSEGSGENIF---IVRDGV--LYTPPLTSSILEGITRDTVITLAKDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 314 GeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI-LYKgqmlhIPTMENGPkLASRILGKLTDIQYGRVE-- 390
Cdd:PRK06606 233 G-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREVdGRQ-----IGNGKRGP-ITEKLQSAYFDIVRGRTEky 299
|
...
gi 12851429 391 SDW 393
Cdd:PRK06606 300 AHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
87-355 |
8.45e-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: 8.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 87 PFGNLPIHPAASVLHYAVELFEGLKAFRGvDNKIRLFRPDLNMDRMCRSAVRTTLPM-FDKEELLKCILQLLQIdqewvp 165
Cdd:TIGR01122 8 DWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEIpYSKEELMEATRETLRK------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 166 ySTSASLYIRP-TFIGTEpSLGVKKPSKAL--LFVILSPVGPY-----FSSGSFTPVSLW--ANPKYIrawkggTGDCKM 235
Cdd:TIGR01122 81 -NNLRSAYIRPlVFRGDG-DLGLNPRAGYKpdVIIAAWPWGAYlgeeaLEKGIDAKVSSWrrNAPNTI------PTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 236 GGNYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGeeELATPPLDGIILPGVTRQSILELAQQWGe 315
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILL-DVEGYVAEGSGENIF---IVKDG--VLFTPPVTSSILPGITRDTVITLAKELG- 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 12851429 316 FKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 355
Cdd:TIGR01122 226 IEVVEQPISREELYTA------DEAFFTGTAAEITPIREV 259
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
107-355 |
3.41e-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: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 107 FEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpySTSASLYIRPTFiGTEP- 183
Cdd:cd01558 28 YEVIRVYNG-----KPFALDEHLDRLYRSAkeLRIDIPY-TREELKELIRELVAKNE-----GGEGDVYIQVTR-GVGPr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 184 SLGVKKPSKALLFVILSPVGPYFSSGSFTPVSLwANPKYIRaWkggtGDCKM-GGNYGASLLAQCEAVENGCQQVlWLYG 262
Cdd:cd01558 96 GHDFPKCVKPTVVIITQPLPLPPAELLEKGVRV-ITVPDIR-W----LRCDIkSLNLLNNVLAKQEAKEAGADEA-ILLD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 263 KDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATAlegnrvKEMFG 342
Cdd:cd01558 169 ADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGITRATVIELAKELG-IPVEERPFSLEELYTA------DEVFL 236
|
250
....*....|...
gi 12851429 343 SGTACVVCPVSDI 355
Cdd:cd01558 237 TSTTAEVMPVVEI 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
107-355 |
2.86e-14 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 72.60 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 107 FEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpySTSAslYIRPTFIGTEPS 184
Cdd:PRK08320 33 FEGIRAYNG-----RVFRLKEHIDRLYDSAkaIMLEIPL-SKEEMTEIVLETLRKNN-----LRDA--YIRLVVSRGVGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 185 LGV--KKPSKALLFVILSPVGPYFssGSF---------------TPVSLWANPKYIrawkggtgdckmggNYGASLLAQC 247
Cdd:PRK08320 100 LGLdpRKCPKPTVVCIAEPIGLYP--GELyekglkvitvstrrnRPDALSPQVKSL--------------NYLNNILAKI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 248 EAVENGCQQVLWLygkDNQ--ITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTM 325
Cdd:PRK08320 164 EANLAGVDEAIML---NDEgyVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG-IPVREELFTL 234
|
250 260 270
....*....|....*....|....*....|
gi 12851429 326 DDLATAlegnrvKEMFGSGTACVVCPVSDI 355
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 ... |
100-333 |
2.90e-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: 63.10 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 100 LHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIdqewvpySTSASLYIRPTFI 179
Cdd:cd01559 4 FAYGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAA-------NDIDEGRIRLILS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 180 -GTEP----SLGVKKPSkALLFVILSPVGPYFSSGS--FTPVSLWANP-----KYIrawkggtgdckmggNYGASLLAQC 247
Cdd:cd01559 72 rGPGGrgyaPSVCPGPA-LYVSVIPLPPAWRQDGVRliTCPVRLGEQPllaglKHL--------------NYLENVLAKR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 248 EAVENGCQQVLWLYGKDNqITEVGTMNLFlyWINEdgeEELATPPLDGIILPGVTRQSILELAQQWGEFKVcERHLTMDD 327
Cdd:cd01559 137 EARDRGADEALFLDTDGR-VIEGTASNLF--FVKD---GELVTPSLDRGGLAGITRQRVIELAAAKGYAVD-ERPLRLED 209
|
....*.
gi 12851429 328 LATALE 333
Cdd:cd01559 210 LLAADE 215
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
89-355 |
1.84e-09 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 58.04 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 89 GNLPIHPAASvlH---YAVELFEGLKAFRGVdnkirlfRPDLNM--DRMCRSAVRTTL-PMFDKEELLKCILQLLQidqe 162
Cdd:PRK13356 18 GNVPIMGPAD--HaawLGSTVFDGARAFEGV-------TPDLDLhcARVNRSAEALGLkPTVSAEEIEALAREGLK---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 163 wvPYSTSASLYIRPTFIGTEPSLGVKKPSK-----AL-LFVILSPvGPYFSSGSFTPvslwanpkYIRAW-KGGTGDCKM 235
Cdd:PRK13356 85 --RFDPDTALYIRPMYWAEDGFASGVAPDPestrfALcLEEAPMP-EPTGFSLTLSP--------FRRPTlEMAPTDAKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 236 GGNYGASLLAQCEAVENGCQQVLWLYGKDNqITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGe 315
Cdd:PRK13356 154 GCLYPNNARALREARSRGFDNALVLDMLGN-VAETATSNVF---MVKDGV--VFTPVPNGTFLNGITRQRVIALLREDG- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 12851429 316 FKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 355
Cdd:PRK13356 227 VTVVETTLTYEDFLEA------DEVFSTGNYSKVVPVTRF 260
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
93-355 |
5.59e-07 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 50.74 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 93 IHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSAvrttlpmfdkeellkcilQLLQIDqewVPYS----- 167
Cdd:PRK07544 25 VHVLTHGLHYASSVFEGERAYGG-----KIFKLREHSERLRRSA------------------ELLDFE---IPYSvaeid 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 168 --TSASL--------YIRPT-FIGTEpSLGVKKPSKALLFVILS-PVGPYFSS-----GSFTPVSLWANPkyirAWKGGT 230
Cdd:PRK07544 79 aaKKETLaangltdaYVRPVaWRGSE-MMGVSAQQNKIHLAIAAwEWPSYFDPeakmkGIRLDIAKWRRP----DPETAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 231 GDCKMGGNYGASLLAQCEAVENGCQQVLWL-YgkDNQITEVGTMNLFLYwinEDGEeeLATPPLDgIILPGVTRQSILEL 309
Cdd:PRK07544 154 SAAKAAGLYMICTISKHAAEAKGYADALMLdY--RGYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIEL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 12851429 310 AQQWGeFKVCERHLTMDDLATAlegnrvKEMFGSGTACVVCPVSDI 355
Cdd:PRK07544 226 AKRRG-IEVVERHIMPEELAGF------SECFLTGTAAEVTPVSEI 264
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
102-355 |
3.33e-06 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 48.41 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 102 YAVELFEGLKAFRGvdnkiRLFRPDLNMDRMCRSA--VRTTLPMfDKEELLKCILQLLQIDQewvpystSASLYIR---- 175
Cdd:PRK12479 29 YGDGVFEGIRSYGG-----NVFCLKEHVKRLYESAksILLTIPL-TVDEMEEAVLQTLQKNE-------YADAYIRlivs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 176 --PTFIGTEPSlGVKKPSKALLFVILSPVGPYFSSGSFTPVSLWA---NPKYIrawkggtgDCKMGG-NYGASLLAQCEA 249
Cdd:PRK12479 96 rgKGDLGLDPR-SCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASrrnTPDAL--------DPRIKSmNYLNNVLVKIEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 250 VENGCQQVLWLyGKDNQITEVGTMNLFlywINEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLA 329
Cdd:PRK12479 167 AQAGVLEALML-NQQGYVCEGSGDNVF---VVKDGK--VLTPPSYLGALEGITRNSVIELCERLS-IPCEERPFTRHDVY 239
|
250 260
....*....|....*....|....*.
gi 12851429 330 TAlegnrvKEMFGSGTACVVCPVSDI 355
Cdd:PRK12479 240 VA------DEVFLTGTAAELIPVVKV 259
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
244-355 |
1.04e-05 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 46.85 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 244 LAQCEAVENGCQQVlWLYGkDNQITEVGTMNlflYWInEDGEEELATPPLDGIILPGVTRQSILELAQQWGeFKVCERHL 323
Cdd:PRK06680 158 LAKQAAKEAGAQEA-WMVD-DGFVTEGASSN---AWI-VTKDGKLVTRPADNFILPGITRHTLIDLAKELG-LEVEERPF 230
|
90 100 110
....*....|....*....|....*....|..
gi 12851429 324 TmddLATALEgnrVKEMFGSGTACVVCPVSDI 355
Cdd:PRK06680 231 T---LQEAYA---AREAFITAASSFVFPVVQI 256
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
238-352 |
2.01e-05 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 46.16 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 238 NYGASLLAQCEAVENGCQQVLWLyGKDNQITEVGTMNL-FLywineDGEEELATPPLDGIiLPGVTRQSILELAQQWGEF 316
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL-----TNDGELVLPPFDKI-LSGCTARRVLELAPRLVSP 260
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 12851429 317 K----VCERHLTMDdlatalEGNRVKEMFGSGTACVVCPV 352
Cdd:PLN02845 261 GdlrgVKQRKISVE------EAKAADEMMLIGSGVPVLPI 294
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
266-331 |
4.96e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 44.20 E-value: 4.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12851429 266 QITEVGTMNLFLywinEDGEEELATPPLDGIILPGVTRQSILElaqqwgEFKVCERHLTMDDLATA 331
Cdd:PRK07546 136 EVCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLD------AGRAREAVLTVDDLKSA 191
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
107-331 |
1.49e-03 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 40.33 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 107 FEGLKAFRGvdnKIRLFRPDLnmDRMCRSAVRTTLPMFDKEELLKCILQLLQidqEWvpYSTSASLYIRPTFigtepSLG 186
Cdd:PRK07849 42 FETLLVRDG---RPCNLEAHL--ERLARSAALLDLPEPDLDRWRRAVELAIE---EW--RAPEDEAALRLVY-----SRG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12851429 187 VKKPSKALLFVILSPVGPYFSSGSFTPVSLWANPkyiRAWKGGTGDCK---MGG----NYGASLLAQCEAVENGCQQVLW 259
Cdd:PRK07849 107 RESGGAPTAWVTVSPVPERVARARREGVSVITLD---RGYPSDAAERApwlLAGaktlSYAVNMAALRYAARRGADDVIF 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12851429 260 LYGkDNQITEVGTMNLFLYwinEDGEeeLATPPLDGIILPGVTRQSILELAQQWGeFKVCERHLTMDDLATA 331
Cdd:PRK07849 184 TST-DGYVLEGPTSTVVIA---TDDR--LLTPPPWYGILPGTTQAALFEVAREKG-WDCEYRALRPADLFAA 248
|
|
| |
