|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
81-420 |
4.32e-138 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 399.52 E-value: 4.32e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 81 KKKPDPSSLVFGASFTDHMLMVEWTSKyGWDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMK 160
Cdd:PRK13357 14 KRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFRPDANAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 161 RMCRSAVRTTLPEFDKEELLQCVLQLIQLDREWV-PYSTSASLYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNG 239
Cdd:PRK13357 93 RLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVGAYFKGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 240 tFSPVSLWANPKFVRSWKGGTGDFKMGCNYGSSLLAQCEAAENGCHQVLWLYGKENR-ITEVGTMNLFLywINKDGEEel 318
Cdd:PRK13357 173 -VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITKDGTV-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 319 aTPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTALEENRVKEMFGSGTACVVCPVASILYKGQMLHIPTME 398
Cdd:PRK13357 248 -TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEFVIGDGE 325
|
330 340
....*....|....*....|..
gi 672051359 399 NGhKLSSRIMAKLTDIQYGRIK 420
Cdd:PRK13357 326 VG-PVTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
122-417 |
1.59e-126 |
|
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.
Pssm-ID: 238798 Cd Length: 279 Bit Score: 366.91 E-value: 1.59e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 122 SIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMKRMCRSAVRTTLPEFDKEELLQCVLQLIQLDREWVPYSTSAS 201
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 202 LYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNGtFSPVSLWANPkFVRSWKGGTGDFKMGCNYGSSLLAQCEAAE 281
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 282 NGCHQVLWLYGKENRITEVGTMNLFLYWINkdgeeELATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTA 361
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 672051359 362 leenrvKEMFGSGTACVVCPVASILYKGQmlhIPTMENGHKLSSRIMAKLTDIQYG 417
Cdd:cd01557 233 ------DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
110-427 |
4.49e-102 |
|
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: 305.91 E-value: 4.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 110 WDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMKRMCRSAVRTTLPEFDKEELLQCVLQLIQL 189
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 190 DREWVP-YSTSASLYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNGtFSPVSLWANPKFVRSWKGGTGDFKMGCN 268
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 269 YGSSLLAQCEAAENGCHQVLWLYGKENR-ITEVGTMNLFLywINKDGeeELATPPLDGVILPGVTRQSILELGEEWGeFK 347
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTyIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 348 VCERHITMDDLSTALEenRVKEMFGSGTACVVCPVASILYKGQMLHIPTMENGhKLSSRIMAKLTDIQYGRIKSE--WTL 425
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPG-EVTKALYDELTDIQYGDFEDPygWIV 311
|
..
gi 672051359 426 EL 427
Cdd:TIGR01123 312 EV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
110-419 |
3.78e-72 |
|
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: 228.15 E-value: 3.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 110 WDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMKRMCRSAVRTTLP-EFDKEELLQCVLQLIQ 188
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 189 LDREwvpystsASLYIRPTFIGIEPSLGVKKP-SKALLFVILSPVGSYFSNGTFSPVSLWANPkFVRSWKGGTGDFKmGC 267
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 268 NYGSSLLAQCEAAENGCHQVLWLyGKENRITEVGTMNLFLYwinKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFK 347
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672051359 348 VCERHITMDDLSTAleenrvKEMFGSGTACVVCPVASIlyKGQmlHIPTMENGhKLSSRIMAKLTDIQYGRI 419
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGR--PIGDGKPG-PVTRRLRELYTDIVRGEA 283
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
136-385 |
3.41e-33 |
|
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: 124.39 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 136 LFEGLKAFRGvdnkiRLFRPDLNMKRMCRSAVRTTLP-EFDKEELLQCVLQLIQLDREWVPYstsaslyIRPT-FIGIEP 213
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPlPFDEEDLRKIIEELLKANGLGVGR-------LRLTvSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 214 SLGVKKPSKALLFVILSPVGSYFSNGTFSPVSLWANPKFVRSwkggtgDFKmGCNYGSSLLAQCEAAENGCHQVLwLYGK 293
Cdd:pfam01063 70 FGLPTSDPTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 294 ENRITEVGTMNLFLYwinKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTAleenrvKEMFGS 373
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 672051359 374 GTACVVCPVASI 385
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
81-420 |
4.32e-138 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 399.52 E-value: 4.32e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 81 KKKPDPSSLVFGASFTDHMLMVEWTSKyGWDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMK 160
Cdd:PRK13357 14 KRAIDWANLGFGYVFTDHMVVIDYKDG-KWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFRPDANAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 161 RMCRSAVRTTLPEFDKEELLQCVLQLIQLDREWV-PYSTSASLYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNG 239
Cdd:PRK13357 93 RLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVGAYFKGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 240 tFSPVSLWANPKFVRSWKGGTGDFKMGCNYGSSLLAQCEAAENGCHQVLWLYGKENR-ITEVGTMNLFLywINKDGEEel 318
Cdd:PRK13357 173 -VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTyIEEVGGMNFFF--ITKDGTV-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 319 aTPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTALEENRVKEMFGSGTACVVCPVASILYKGQMLHIPTME 398
Cdd:PRK13357 248 -TPPLSGSILPGITRDSLLQLAEDLG-LTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKEFVIGDGE 325
|
330 340
....*....|....*....|..
gi 672051359 399 NGhKLSSRIMAKLTDIQYGRIK 420
Cdd:PRK13357 326 VG-PVTQKLYDELTGIQFGDVE 346
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
122-417 |
1.59e-126 |
|
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.
Pssm-ID: 238798 Cd Length: 279 Bit Score: 366.91 E-value: 1.59e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 122 SIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMKRMCRSAVRTTLPEFDKEELLQCVLQLIQLDREWVPYSTSAS 201
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 202 LYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNGtFSPVSLWANPkFVRSWKGGTGDFKMGCNYGSSLLAQCEAAE 281
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 282 NGCHQVLWLYGKENRITEVGTMNLFLYWINkdgeeELATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTA 361
Cdd:cd01557 159 KGYDQALWLDGAHGYVAEVGTMNIFFVKDG-----ELITPPLDGSILPGITRDSILELARDLG-IKVEERPITRDELYEA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 672051359 362 leenrvKEMFGSGTACVVCPVASILYKGQmlhIPTMENGHKLSSRIMAKLTDIQYG 417
Cdd:cd01557 233 ------DEVFATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
110-427 |
4.49e-102 |
|
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: 305.91 E-value: 4.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 110 WDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMKRMCRSAVRTTLPEFDKEELLQCVLQLIQL 189
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 190 DREWVP-YSTSASLYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNGtFSPVSLWANPKFVRSWKGGTGDFKMGCN 268
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 269 YGSSLLAQCEAAENGCHQVLWLYGKENR-ITEVGTMNLFLywINKDGeeELATPPLDGVILPGVTRQSILELGEEWGeFK 347
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTyIEEVGAMNFFF--ITGDG--ELVTPPLSGSILPGITRDSLLQLAKDLG-ME 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 348 VCERHITMDDLSTALEenRVKEMFGSGTACVVCPVASILYKGQMLHIPTMENGhKLSSRIMAKLTDIQYGRIKSE--WTL 425
Cdd:TIGR01123 235 VEERRIDIDELKAFVE--AGEIVFACGTAAVITPVGEIQHGGKEVVFASGQPG-EVTKALYDELTDIQYGDFEDPygWIV 311
|
..
gi 672051359 426 EL 427
Cdd:TIGR01123 312 EV 313
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
127-411 |
2.91e-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: 235.19 E-value: 2.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 127 ASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMKRMCRSAVRTTLP-EFDKEELLQCVLQLIQLdrewvpySTSASLYIR 205
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKG-----RLFRLDEHLDRLNRSAKRLGLPiPYDREELREALKELVAA-------NNGASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 206 PTFIGIEPSLGV--KKPSKALLFVILSPVGSYFSNGtFSPVSLWANPKFVRSWKGGTGDFKMGCNYGSsLLAQCEAAENG 283
Cdd:cd00449 69 PLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGG-EKGVRLITSPDRRRAAPGGTGDAKTGGNLNS-VLAKQEAAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 284 CHQVLWLYGkENRITEVGTMNLFLYwinKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTAle 363
Cdd:cd00449 147 ADEALLLDD-NGYVTEGSASNVFIV---KDGE--LVTPPLDGGILPGITRDSVIELAKELG-IKVEERPISLDELYAA-- 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 672051359 364 enrvKEMFGSGTACVVCPVASILYKGQmlhipTMENGHKLSSRIMAKL 411
Cdd:cd00449 218 ----DEVFLTGTAAEVTPVTEIDGRGI-----GDGKPGPVTRKLRELL 256
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
110-419 |
3.78e-72 |
|
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: 228.15 E-value: 3.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 110 WDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMKRMCRSAVRTTLP-EFDKEELLQCVLQLIQ 188
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 189 LDREwvpystsASLYIRPTFIGIEPSLGVKKP-SKALLFVILSPVGSYFSNGTFSPVSLWANPkFVRSWKGGTGDFKmGC 267
Cdd:COG0115 79 ANGL-------EDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKGVRVITSP-YRRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 268 NYGSSLLAQCEAAENGCHQVLWLyGKENRITEVGTMNLFLYwinKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFK 347
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIV---KDGV--LVTPPLSGGILPGITRDSVIELARELG-IP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672051359 348 VCERHITMDDLSTAleenrvKEMFGSGTACVVCPVASIlyKGQmlHIPTMENGhKLSSRIMAKLTDIQYGRI 419
Cdd:COG0115 223 VEERPISLEELYTA------DEVFLTGTAAEVTPVTEI--DGR--PIGDGKPG-PVTRRLRELYTDIVRGEA 283
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
60-427 |
4.97e-64 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 211.25 E-value: 4.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 60 SEASTQTFRAKDLiitkadvlkkkpDPSSLVFGASFTDHMLMVEWTSKYGWDKPHIKPFENLSIHPAASVLHYAVELFEG 139
Cdd:PLN02782 58 SSSYTEVTELADI------------DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 140 LKAFRGVDNKIRLFRPDLNMKRMCRSAVRTTLPEFDKEELLQCVLQLIQLDREWVPYSTSASLYIRPTFIGIEPSLGVkK 219
Cdd:PLN02782 126 LKAYRKEDGNILLFRPEENAIRMRNGAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGL-A 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 220 PSKALLFVI-LSPVGSYFSNGTfSPVSLWANPKFVRSWKGGTGDFKMGCNYGSSLLAQCEAAENGCHQVLWLYGKENR-I 297
Cdd:PLN02782 205 PAPEYTFLIyVSPVGNYFKEGV-APINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKyL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 298 TEVGTMNLFlywINKDgeEELATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTAleenrvKEMFGSGTAC 377
Cdd:PLN02782 284 EEVSSCNIF---IVKD--NVISTPAIKGTILPGITRKSIIDVARSQG-FQVEERNVTVDELLEA------DEVFCTGTAV 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 672051359 378 VVCPVASILYKGQmlhipTMENGHK----LSSRIMAKLTDIQYGRIKS--EWTLEL 427
Cdd:PLN02782 352 VVSPVGSITYKGK-----RVSYGEGgfgtVSQQLYTVLTSLQMGLIEDnmNWTVEL 402
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
69-427 |
2.92e-60 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 199.77 E-value: 2.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 69 AKDLIITKADVLKKKPDPSSLVFGASFTDHMLMVEWTSKYGWDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGVDN 148
Cdd:PLN03117 5 SSPLPTSKADEKYANVKWEELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 149 KIRLFRPDLNMKRMCRSAVRTTLPEFDKEELLQCVLQLIQLDREWVPYSTSASLYIRPTFIGIEPSLGVKKPSKALLFVI 228
Cdd:PLN03117 85 RITLFRPDQNALRMQTGADRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 229 LSPVGSYFSNGtfSPVSLWANPKFVRSWKGGTGDFKMGCNYGSSLLAQCEAAENGCHQVLWLYGKENR-ITEVGTMNLFL 307
Cdd:PLN03117 165 ASPVGNYHKAS--SGLNLKVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKnIEELSACNIFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 308 YWINKdgeeeLATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTAleenrvKEMFGSGTACVVCPVASILY 387
Cdd:PLN03117 243 LKGNI-----VSTPPTSGTILPGVTRKSISELARDIG-YQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTF 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 672051359 388 KGQMLHIPTMENGhkLSSRIMAKLTDIQYGRI--KSEWTLEL 427
Cdd:PLN03117 311 HDKKVKYRTGEEA--LSTKLHLILTNIQMGVVedKKGWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
85-420 |
5.81e-50 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 173.75 E-value: 5.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 85 DPSSLVFGASFTDHMLMVEWTSKYGWDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMKRMCR 164
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 165 SAVRTTLPEFDKEELLQCVLQLIQLDREWVPYSTSASLYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNGtFSPV 244
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG-MAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 245 SLWANPKFVRSWKGGTGDFKMGCNYGSSLLAQCEAAENGCHQVLWLYG-KENRITEVGTMNLFLYwinkdGEEELATPPL 323
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSvKKKYLEEASSCNVFVV-----KGRTISTPAT 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 324 DGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTAleenrvKEMFGSGTACVVCPVASILYKGQMLHIPTMEngHKL 403
Cdd:PLN02259 291 NGTILEGITRKSVMEIASDQG-YQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGD--ESV 361
|
330
....*....|....*..
gi 672051359 404 SSRIMAKLTDIQYGRIK 420
Cdd:PLN02259 362 CQKLRSVLVGIQTGLIE 378
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
85-427 |
2.47e-48 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 169.51 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 85 DPSSLVFGASFTDHMLMVEWTSKYGWDKPHIKPFENLSIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMKRMCR 164
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 165 SAVRTTLPEFDKEELLQCVLQLIQLDREWVPYSTSASLYIRPTFIGIEPSLGVKKPSKALLFVILSPVGSYFSNGTfSPV 244
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 245 SLWANPKFVRSWKGGTGDFKMGCNYGSSLLAQCEAAENGCHQVLWLYGKENR-ITEVGTMNLFLYWINKdgeeeLATPPL 323
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKnIEEVSAANIFLVKGNI-----IVTPAT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 324 DGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTAleenrvKEMFGSGTACVVCPVASILYKGQMLHIPTMENghKL 403
Cdd:PLN02883 287 SGTILGGITRKSIIEIALDLG-YKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGDG--IV 357
|
330 340
....*....|....*....|....*.
gi 672051359 404 SSRIMAKLTDIQYGRIK--SEWTLEL 427
Cdd:PLN02883 358 TQQLRSILLGIQTGSIQdtKDWVLQI 383
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
136-385 |
3.41e-33 |
|
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: 124.39 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 136 LFEGLKAFRGvdnkiRLFRPDLNMKRMCRSAVRTTLP-EFDKEELLQCVLQLIQLDREWVPYstsaslyIRPT-FIGIEP 213
Cdd:pfam01063 2 VFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIPlPFDEEDLRKIIEELLKANGLGVGR-------LRLTvSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 214 SLGVKKPSKALLFVILSPVGSYFSNGTFSPVSLWANPKFVRSwkggtgDFKmGCNYGSSLLAQCEAAENGCHQVLwLYGK 293
Cdd:pfam01063 70 FGLPTSDPTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLP------GAK-TLNYLENVLARREAKAQGADDAL-LLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 294 ENRITEVGTMNLFLYwinKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTAleenrvKEMFGS 373
Cdd:pfam01063 142 DGNVTEGSTSNVFLV---KGGT--LYTPPLESGILPGITRQALLDLAKALG-LEVEERPITLADLQEA------DEAFLT 209
|
250
....*....|..
gi 672051359 374 GTACVVCPVASI 385
Cdd:pfam01063 210 NSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
117-385 |
1.57e-29 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 116.78 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 117 PFENLSIHPAASVLHYAVELFEGLKAFRGVDNKIrLFRPDLNMKRMCRSA--VRTTLPeFDKEELLQCVLQLIQ---LDr 191
Cdd:PRK06606 17 PWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAkiLRMEIP-YSVDELMEAQREVVRknnLK- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 192 ewvpystsaSLYIRP-TFIGIEpSLGVKKPS-KALLFVILSPVGSY-----FSNGTFSPVSLWA----NPKFVRSwkggt 260
Cdd:PRK06606 94 ---------SAYIRPlVFVGDE-GLGVRPHGlPTDVAIAAWPWGAYlgeeaLEKGIRVKVSSWTrhapNSIPTRA----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 261 gdfKMGCNYGSSLLAQCEAAENGCHQVLWLyGKENRITEVGTMNLFlywINKDGEeeLATPPLDGVILPGVTRQSILELG 340
Cdd:PRK06606 159 ---KASGNYLNSILAKTEARRNGYDEALLL-DVEGYVSEGSGENIF---IVRDGV--LYTPPLTSSILEGITRDTVITLA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 672051359 341 EEWGeFKVCERHITMDDLSTAleenrvKEMFGSGTACVVCPVASI 385
Cdd:PRK06606 230 KDLG-IEVIERRITRDELYIA------DEVFFTGTAAEVTPIREV 267
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
117-385 |
1.05e-27 |
|
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: 111.30 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 117 PFENLSIHPAASVLHYAVELFEGLKAFRGvDNKIRLFRPDLNMKRMCRSAVRTTLP-EFDKEELLQCVLQLIQLdrewvp 195
Cdd:TIGR01122 8 DWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEiPYSKEELMEATRETLRK------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 196 ySTSASLYIRP-TFIGIEpSLGVKKPSKAL--LFVILSPVGSY-----FSNGTFSPVSLW--ANPKFVrswkggTGDFKM 265
Cdd:TIGR01122 81 -NNLRSAYIRPlVFRGDG-DLGLNPRAGYKpdVIIAAWPWGAYlgeeaLEKGIDAKVSSWrrNAPNTI------PTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 266 GCNYGSSLLAQCEAAENGCHQVLWLyGKENRITEVGTMNLFlywINKDGeeELATPPLDGVILPGVTRQSILELGEEWGe 345
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILL-DVEGYVAEGSGENIF---IVKDG--VLFTPPVTSSILPGITRDTVITLAKELG- 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 672051359 346 FKVCERHITMDDLSTAleenrvKEMFGSGTACVVCPVASI 385
Cdd:TIGR01122 226 IEVVEQPISREELYTA------DEAFFTGTAAEITPIREV 259
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
115-385 |
2.37e-23 |
|
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: 98.82 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 115 IKPFENLSIHPAASVLHYAVELFEGLKAFRGvdnkiRLFRPDLNMKRMCRSA--VRTTLPeFDKEELLQCVLQLIQLDRe 192
Cdd:cd01558 6 YVPREEAKVSVFDRGFLFGDGVYEVIRVYNG-----KPFALDEHLDRLYRSAkeLRIDIP-YTREELKELIRELVAKNE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 193 wvpySTSASLYIRPTFiGIEP-SLGVKKPSKALLFVILSPVGSYFSNGTFSPVSL-------WANPkfvrswkggtgDFK 264
Cdd:cd01558 79 ----GGEGDVYIQVTR-GVGPrGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVitvpdirWLRC-----------DIK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 265 MgCNYGSSLLAQCEAAENGCHQVlWLYGKENRITEVGTMNLFlywINKDGEeeLATPPLDGVILPGVTRQSILELGEEWG 344
Cdd:cd01558 143 S-LNLLNNVLAKQEAKEAGADEA-ILLDADGLVTEGSSSNVF---IVKNGV--LVTPPLDNGILPGITRATVIELAKELG 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 672051359 345 eFKVCERHITMDDLSTAleenrvKEMFGSGTACVVCPVASI 385
Cdd:cd01558 216 -IPVEERPFSLEELYTA------DEVFLTSTTAEVMPVVEI 249
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
130-385 |
2.05e-14 |
|
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: 72.73 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 130 LHYAVELFEGLKAFRGvdnkiRLFRPDLNMKRMCRSAVRTTLPEFDKEELLQCVLQLIQLdrewvpySTSASLYIRPTFI 209
Cdd:cd01559 4 FAYGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAA-------NDIDEGRIRLILS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 210 ------GIEPSLGvkkPSKALLFVILSPVGSYFSNGT---FSPVSLWANPKFVRswkggtgdFKMgCNYGSSLLAQCEAA 280
Cdd:cd01559 72 rgpggrGYAPSVC---PGPALYVSVIPLPPAWRQDGVrliTCPVRLGEQPLLAG--------LKH-LNYLENVLAKREAR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 281 ENGCHQVLWLYGkENRITEVGTMNLFlyWInKDGEeeLATPPLDGVILPGVTRQSILELGEEWGEFKVcERHITMDDLST 360
Cdd:cd01559 140 DRGADEALFLDT-DGRVIEGTASNLF--FV-KDGE--LVTPSLDRGGLAGITRQRVIELAAAKGYAVD-ERPLRLEDLLA 212
|
250 260
....*....|....*....|....*
gi 672051359 361 AleenrvKEMFGSGTACVVCPVASI 385
Cdd:cd01559 213 A------DEAFLTNSLLGVAPVTAI 231
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
137-385 |
1.05e-13 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 71.06 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 137 FEGLKAFRGvdnkiRLFRPDLNMKRMCRSA--VRTTLPeFDKEELLQCVLQLIQLDRewvpySTSAslYIRPTF------ 208
Cdd:PRK08320 33 FEGIRAYNG-----RVFRLKEHIDRLYDSAkaIMLEIP-LSKEEMTEIVLETLRKNN-----LRDA--YIRLVVsrgvgd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 209 IGIEPslgvKKPSKALLFVILSPVGSY----FSNG----TFS-----PVSLwaNPKfVRSwkggtgdfkmgCNYGSSLLA 275
Cdd:PRK08320 100 LGLDP----RKCPKPTVVCIAEPIGLYpgelYEKGlkviTVStrrnrPDAL--SPQ-VKS-----------LNYLNNILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 276 QCEAAENGCHQVLWLyGKENRITEVGTMNLFLYwinKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITM 355
Cdd:PRK08320 162 KIEANLAGVDEAIML-NDEGYVAEGTGDNIFIV---KNGK--LITPPTYAGALEGITRNAVIEIAKELG-IPVREELFTL 234
|
250 260 270
....*....|....*....|....*....|
gi 672051359 356 DDLSTAleenrvKEMFGSGTACVVCPVASI 385
Cdd:PRK08320 235 HDLYTA------DEVFLTGTAAEVIPVVKV 258
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
137-385 |
5.76e-13 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 68.83 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 137 FEGLKAFRGVdnkirlfRPDLNM--KRMCRSAVRTTL-PEFDKEELLQCVLQLIQldrewvPYSTSASLYIRPTFIGIEP 213
Cdd:PRK13356 37 FDGARAFEGV-------TPDLDLhcARVNRSAEALGLkPTVSAEEIEALAREGLK------RFDPDTALYIRPMYWAEDG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 214 SLGVKKPSK-----AL-LFVILSPVGSYFSnGTFSPvslwanpkFVRSW-KGGTGDFKMGCNYGSSLLAQCEAAENGCHQ 286
Cdd:PRK13356 104 FASGVAPDPestrfALcLEEAPMPEPTGFS-LTLSP--------FRRPTlEMAPTDAKAGCLYPNNARALREARSRGFDN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 287 VLWLYGKENrITEVGTMNLFlywINKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITMDDLSTAleenr 366
Cdd:PRK13356 175 ALVLDMLGN-VAETATSNVF---MVKDGV--VFTPVPNGTFLNGITRQRVIALLREDG-VTVVETTLTYEDFLEA----- 242
|
250
....*....|....*....
gi 672051359 367 vKEMFGSGTACVVCPVASI 385
Cdd:PRK13356 243 -DEVFSTGNYSKVVPVTRF 260
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
279-385 |
9.20e-09 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 56.14 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 279 AAEN-GCHQVLWL-YgkENRITEVGTMNLFLYwinKDGEeeLATPPLDgVILPGVTRQSILELGEEWGeFKVCERHITMD 356
Cdd:PRK07544 171 AAEAkGYADALMLdY--RGYVAEATGANIFFV---KDGV--IHTPTPD-CFLDGITRQTVIELAKRRG-IEVVERHIMPE 241
|
90 100
....*....|....*....|....*....
gi 672051359 357 DLSTAleenrvKEMFGSGTACVVCPVASI 385
Cdd:PRK07544 242 ELAGF------SECFLTGTAAEVTPVSEI 264
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
132-385 |
3.84e-08 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 54.57 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 132 YAVELFEGLKAFRGvdnkiRLFRPDLNMKRMCRSA--VRTTLPeFDKEELLQCVLQLIQLDrewvpysTSASLYIR---- 205
Cdd:PRK12479 29 YGDGVFEGIRSYGG-----NVFCLKEHVKRLYESAksILLTIP-LTVDEMEEAVLQTLQKN-------EYADAYIRlivs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 206 --PTFIGIEPSlGVKKPSKALLFVILSPVGSYFSNGTFSPVSLWA--------NPKfVRSwkggtgdfkmgCNYGSSLLA 275
Cdd:PRK12479 96 rgKGDLGLDPR-SCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASrrntpdalDPR-IKS-----------MNYLNNVLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 276 QCEAAENGCHQVLWLyGKENRITEVGTMNLFlywINKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFKVCERHITM 355
Cdd:PRK12479 163 KIEAAQAGVLEALML-NQQGYVCEGSGDNVF---VVKDGK--VLTPPSYLGALEGITRNSVIELCERLS-IPCEERPFTR 235
|
250 260 270
....*....|....*....|....*....|
gi 672051359 356 DDLSTAleenrvKEMFGSGTACVVCPVASI 385
Cdd:PRK12479 236 HDVYVA------DEVFLTGTAAELIPVVKV 259
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
268-384 |
3.68e-06 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 48.47 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 268 NYGSSLLAQCEAAENGCHQVLWLyGKENRITEVGTMNL-FLywiNKDGeeELATPPLDGvILPGVTRQSILELGEEWGEF 346
Cdd:PLN02845 188 NYLPNALSQMEAEERGAFAGIWL-DEEGFVAEGPNMNVaFL---TNDG--ELVLPPFDK-ILSGCTARRVLELAPRLVSP 260
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 672051359 347 K----VCERHITMDDLSTAleenrvKEMFGSGTACVVCPVAS 384
Cdd:PLN02845 261 GdlrgVKQRKISVEEAKAA------DEMMLIGSGVPVLPIVS 296
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
274-385 |
6.88e-06 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 47.62 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672051359 274 LAQCEAAENGCHQVlWLYGkENRITEVGTMNLFLywINKDGEeeLATPPLDGVILPGVTRQSILELGEEWGeFKVCERHI 353
Cdd:PRK06680 158 LAKQAAKEAGAQEA-WMVD-DGFVTEGASSNAWI--VTKDGK--LVTRPADNFILPGITRHTLIDLAKELG-LEVEERPF 230
|
90 100 110
....*....|....*....|....*....|..
gi 672051359 354 TMDDLSTAleenrvKEMFGSGTACVVCPVASI 385
Cdd:PRK06680 231 TLQEAYAA------REAFITAASSFVFPVVQI 256
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
297-361 |
1.33e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 43.04 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672051359 297 ITEVGTMNLFLywinKDGEEELATPPLDGVILPGVTRQSILELGeewgefKVCERHITMDDLSTA 361
Cdd:PRK07546 137 VCEGTITNVFL----DRGGGMLTTPPLSCGLLPGVLRAELLDAG------RAREAVLTVDDLKSA 191
|
|
| |
