|
Name |
Accession |
Description |
Interval |
E-value |
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
78-378 |
1.55e-134 |
|
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: 386.17 E-value: 1.55e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 78 SLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYS 157
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 158 LYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYaTRAWPGGVGDKKLGANYAPCILPQLQAAKR 237
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVSSF-RRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 238 GYQQNLWLFGPEKNITEVGTMNVFFVFlnkvtgKKELVTAPLDGTILEGVTRDSVLTLARDKldpqEWDINERYYTITEV 317
Cdd:cd01557 160 GYDQALWLDGAHGYVAEVGTMNIFFVK------DGELITPPLDGSILPGITRDSILELARDL----GIKVEERPITRDEL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768811323 318 AtrakqgELLEAFGSGTAAVVSPIKEIGWNNEDIhvpllPGEQCGALTKQVAQWIADIQYG 378
Cdd:cd01557 230 Y------EADEVFATGTAAVVTPVGEIDYRGKEP-----GEGEVGPVTKKLYDLLTDIQYG 279
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
29-380 |
1.26e-132 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 384.11 E-value: 1.26e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 29 KITRNPNPSKPRPNEE----LVFGQTFTDHMLTIPWSAEEgWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQN 104
Cdd:PRK13357 2 TVTLKPNPTSDEKRAIdwanLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 105 TITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLV-PQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYV 183
Cdd:PRK13357 81 SIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 184 ITSPVGPYYKTGFKAVR-LEATDYaTRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPE-KNITEVGTMNVF 261
Cdd:PRK13357 161 IASPVGAYFKGGVKPVSiWVSDEY-DRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEhTYIEEVGGMNFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 262 FVFlnkvtgKKELVTAPLDGTILEGVTRDSVLTLARDkldpqeWDIN--ERYYTITEVATRAKQGELLEAFGSGTAAVVS 339
Cdd:PRK13357 240 FIT------KDGTVTPPLSGSILPGITRDSLLQLAED------LGLTveERPVSIDEWQADAASGEFTEAFACGTAAVIT 307
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 768811323 340 PIKEIGWNNEDIHVpllPGEQCGALTKQVAQWIADIQYGRV 380
Cdd:PRK13357 308 PIGGIKYKDKEFVI---GDGEVGPVTQKLYDELTGIQFGDV 345
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
66-380 |
8.85e-96 |
|
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: 288.58 E-value: 8.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 66 WGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQ 145
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 146 DKHLVP-QGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGANY 224
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVTTEYDRAAPGGTGAVKVGGNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 225 APCILPQLQAAKRGYQQNLWLFGPE-KNITEVGTMNVFFvflnkVTGKKELVTAPLDGTILEGVTRDSVLTLARDKLDPQ 303
Cdd:TIGR01123 161 AASLLAQAKAAEQGCDQVVYLDPVEhTYIEEVGAMNFFF-----ITGDGELVTPPLSGSILPGITRDSLLQLAKDLGMEV 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768811323 304 EwdinERYYTITEVATRAKQGEllEAFGSGTAAVVSPIKEIGWNNEDIHVpllPGEQCGALTKQVAQWIADIQYGRV 380
Cdd:TIGR01123 236 E----ERRIDIDELKAFVEAGE--IVFACGTAAVITPVGEIQHGGKEVVF---ASGQPGEVTKALYDELTDIQYGDF 303
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
66-380 |
1.54e-71 |
|
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: 225.45 E-value: 1.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 66 WGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPqntitMFRPDKNMARMNKSAARICLP-TFESEELIKLTGKLIE 144
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGR-----LFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 145 QDKHLvpqgngySLYIRPTMIGTSKGLGVGTP-SEALLYVITSPVGPYYKTGF-KAVRLEATDYaTRAWPGGVGDKKlGA 222
Cdd:COG0115 79 ANGLE-------DGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYeKGVRVITSPY-RRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 223 NYAPCILPQLQAAKRGYQQNLWLfGPEKNITEVGTMNVFFVFlnkvtgKKELVTAPLDGTILEGVTRDSVLTLARDkldp 302
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIVK------DGVLVTPPLSGGILPGITRDSVIELARE---- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768811323 303 QEWDINERYYTITEVATrAKqgellEAFGSGTAAVVSPIKEIGwnneDIHVpllPGEQCGALTKQVAQWIADIQYGRV 380
Cdd:COG0115 219 LGIPVEERPISLEELYT-AD-----EVFLTGTAAEVTPVTEID----GRPI---GDGKPGPVTRRLRELYTDIVRGEA 283
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
92-344 |
2.51e-30 |
|
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: 115.92 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 92 LFEGLKAYRtpqNTItmFRPDKNMARMNKSAARICLPTFESEELIKltgKLIEQdkhLVPQGNGYSLYIRPTMIGTSKGL 171
Cdd:pfam01063 2 VFETLRVYN---GKI--FFLDEHLARLRRSAKLLGIPLPFDEEDLR---KIIEE---LLKANGLGVGRLRLTVSRGPGGF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 172 GVGTPS-EALLYVITSPVGPYYKtgfkavRLEATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLwLFGPEK 250
Cdd:pfam01063 71 GLPTSDpTLAIFVSALPPPPESK------KKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDAL-LLDEDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 251 NITEVGTMNVFFVflnkvtgK-KELVTAPLDGTILEGVTRDSVLTLARdkldPQEWDINERYYTITEVAtRAKqgellEA 329
Cdd:pfam01063 144 NVTEGSTSNVFLV-------KgGTLYTPPLESGILPGITRQALLDLAK----ALGLEVEERPITLADLQ-EAD-----EA 206
|
250
....*....|....*
gi 768811323 330 FGSGTAAVVSPIKEI 344
Cdd:pfam01063 207 FLTNSLRGVTPVSSI 221
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
78-378 |
1.55e-134 |
|
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: 386.17 E-value: 1.55e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 78 SLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYS 157
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 158 LYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYaTRAWPGGVGDKKLGANYAPCILPQLQAAKR 237
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVSSF-RRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 238 GYQQNLWLFGPEKNITEVGTMNVFFVFlnkvtgKKELVTAPLDGTILEGVTRDSVLTLARDKldpqEWDINERYYTITEV 317
Cdd:cd01557 160 GYDQALWLDGAHGYVAEVGTMNIFFVK------DGELITPPLDGSILPGITRDSILELARDL----GIKVEERPITRDEL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768811323 318 AtrakqgELLEAFGSGTAAVVSPIKEIGWNNEDIhvpllPGEQCGALTKQVAQWIADIQYG 378
Cdd:cd01557 230 Y------EADEVFATGTAAVVTPVGEIDYRGKEP-----GEGEVGPVTKKLYDLLTDIQYG 279
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
29-380 |
1.26e-132 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 384.11 E-value: 1.26e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 29 KITRNPNPSKPRPNEE----LVFGQTFTDHMLTIPWSAEEgWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQN 104
Cdd:PRK13357 2 TVTLKPNPTSDEKRAIdwanLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 105 TITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLV-PQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYV 183
Cdd:PRK13357 81 SIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 184 ITSPVGPYYKTGFKAVR-LEATDYaTRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPE-KNITEVGTMNVF 261
Cdd:PRK13357 161 IASPVGAYFKGGVKPVSiWVSDEY-DRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEhTYIEEVGGMNFF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 262 FVFlnkvtgKKELVTAPLDGTILEGVTRDSVLTLARDkldpqeWDIN--ERYYTITEVATRAKQGELLEAFGSGTAAVVS 339
Cdd:PRK13357 240 FIT------KDGTVTPPLSGSILPGITRDSLLQLAED------LGLTveERPVSIDEWQADAASGEFTEAFACGTAAVIT 307
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 768811323 340 PIKEIGWNNEDIHVpllPGEQCGALTKQVAQWIADIQYGRV 380
Cdd:PRK13357 308 PIGGIKYKDKEFVI---GDGEVGPVTQKLYDELTGIQFGDV 345
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
66-380 |
8.85e-96 |
|
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: 288.58 E-value: 8.85e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 66 WGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQ 145
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 146 DKHLVP-QGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGANY 224
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVTTEYDRAAPGGTGAVKVGGNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 225 APCILPQLQAAKRGYQQNLWLFGPE-KNITEVGTMNVFFvflnkVTGKKELVTAPLDGTILEGVTRDSVLTLARDKLDPQ 303
Cdd:TIGR01123 161 AASLLAQAKAAEQGCDQVVYLDPVEhTYIEEVGAMNFFF-----ITGDGELVTPPLSGSILPGITRDSLLQLAKDLGMEV 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768811323 304 EwdinERYYTITEVATRAKQGEllEAFGSGTAAVVSPIKEIGWNNEDIHVpllPGEQCGALTKQVAQWIADIQYGRV 380
Cdd:TIGR01123 236 E----ERRIDIDELKAFVEAGE--IVFACGTAAVITPVGEIQHGGKEVVF---ASGQPGEVTKALYDELTDIQYGDF 303
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
85-372 |
1.32e-79 |
|
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: 245.20 E-value: 1.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 85 VFHYAFELFEGLKAYRtpqntITMFRPDKNMARMNKSAARICLP-TFESEELIKLTGKLIEQdkhlvpqGNGYSLYIRPT 163
Cdd:cd00449 3 GLHYGDGVFEGLRAGK-----GRLFRLDEHLDRLNRSAKRLGLPiPYDREELREALKELVAA-------NNGASLYIRPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 164 MIGTSKGLGVGTP--SEALLYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGaNYAPCILPQLQAAKRGYQQ 241
Cdd:cd00449 71 LTRGVGGLGVAPPpsPEPTFVVFASPVGAYAKGGEKGVRLITSPDRRRAAPGGTGDAKTG-GNLNSVLAKQEAAEAGADE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 242 NLWLFGpEKNITEVGTMNVFFVFlnkvtgKKELVTAPLDGTILEGVTRDSVLTLARDKLdpqeWDINERYYTITEVAtra 321
Cdd:cd00449 150 ALLLDD-NGYVTEGSASNVFIVK------DGELVTPPLDGGILPGITRDSVIELAKELG----IKVEERPISLDELY--- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 768811323 322 kqgELLEAFGSGTAAVVSPIKEIGWNNEdihvpllPGEQCGALTKQVAQWI 372
Cdd:cd00449 216 ---AADEVFLTGTAAEVTPVTEIDGRGI-------GDGKPGPVTRKLRELL 256
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
66-380 |
1.54e-71 |
|
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: 225.45 E-value: 1.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 66 WGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPqntitMFRPDKNMARMNKSAARICLP-TFESEELIKLTGKLIE 144
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGR-----LFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 145 QDKHLvpqgngySLYIRPTMIGTSKGLGVGTP-SEALLYVITSPVGPYYKTGF-KAVRLEATDYaTRAWPGGVGDKKlGA 222
Cdd:COG0115 79 ANGLE-------DGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYeKGVRVITSPY-RRAAPGGLGGIK-TG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 223 NYAPCILPQLQAAKRGYQQNLWLfGPEKNITEVGTMNVFFVFlnkvtgKKELVTAPLDGTILEGVTRDSVLTLARDkldp 302
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLL-DTDGYVAEGSGSNVFIVK------DGVLVTPPLSGGILPGITRDSVIELARE---- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768811323 303 QEWDINERYYTITEVATrAKqgellEAFGSGTAAVVSPIKEIGwnneDIHVpllPGEQCGALTKQVAQWIADIQYGRV 380
Cdd:COG0115 219 LGIPVEERPISLEELYT-AD-----EVFLTGTAAEVTPVTEID----GRPI---GDGKPGPVTRRLRELYTDIVRGEA 283
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
43-380 |
2.13e-59 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 196.69 E-value: 2.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 43 EELVFGQTFTDHMLTIPWSAEEGWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSA 122
Cdd:PLN03117 23 EELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 123 ARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGfKAVRLE 202
Cdd:PLN03117 103 DRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKAS-SGLNLK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 203 ATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPE-KNITEVGTMNVFFVFLNKVTgkkelvTAPLDG 281
Cdd:PLN03117 182 VDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATgKNIEELSACNIFILKGNIVS------TPPTSG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 282 TILEGVTRDSVLTLARDKldpqEWDINERYYTITEVAtrakqgELLEAFGSGTAAVVSPIKEIGWNneDIHVPLLPGEQc 361
Cdd:PLN03117 256 TILPGVTRKSISELARDI----GYQVEERDVSVDELL------EAEEVFCTGTAVVVKAVETVTFH--DKKVKYRTGEE- 322
|
330
....*....|....*....
gi 768811323 362 gALTKQVAQWIADIQYGRV 380
Cdd:PLN03117 323 -ALSTKLHLILTNIQMGVV 340
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
43-386 |
2.60e-53 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 181.97 E-value: 2.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 43 EELVFGQTFTDHMLTIPWSAEEGWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSA 122
Cdd:PLN02782 73 DNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRNGA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 123 ARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLE 202
Cdd:PLN02782 153 ERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPINLI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 203 ATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPEKN-ITEVGTMNVFFVFLNKVTgkkelvTAPLDG 281
Cdd:PLN02782 233 VENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKyLEEVSSCNIFIVKDNVIS------TPAIKG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 282 TILEGVTRDSVLTLARDkldpQEWDINERYYTITevatrakqgELLEA---FGSGTAAVVSPIKEIGWNNEDIHVpllpG 358
Cdd:PLN02782 307 TILPGITRKSIIDVARS----QGFQVEERNVTVD---------ELLEAdevFCTGTAVVVSPVGSITYKGKRVSY----G 369
|
330 340 350
....*....|....*....|....*....|
gi 768811323 359 EQ-CGALTKQVAQWIADIQYGRV-NYGNWS 386
Cdd:PLN02782 370 EGgFGTVSQQLYTVLTSLQMGLIeDNMNWT 399
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
14-351 |
7.22e-49 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 169.90 E-value: 7.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 14 IRTLATGAPLDASKLKITRNPNPSKPRPN----------EELVFGQTFTDHMLTIPWSAEEGWGTPHIKPYGNLSLDPSA 83
Cdd:PLN02259 20 IRTLQTFAKYNAQAASALREERKKPLYQNgddvyadldwDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 84 CVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSAARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPT 163
Cdd:PLN02259 100 GVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 164 MIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLEATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNL 243
Cdd:PLN02259 180 LMGSGPILGLGPAPEYTFIVYASPVGNYFKEGMAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 244 WLFGPEKN-ITEVGTMNVFfvflnkVTGKKELVTAPLDGTILEGVTRDSVLTLARDkldpQEWDINERYYTITEVAtrak 322
Cdd:PLN02259 260 YLDSVKKKyLEEASSCNVF------VVKGRTISTPATNGTILEGITRKSVMEIASD----QGYQVVEKAVHVDEVM---- 325
|
330 340
....*....|....*....|....*....
gi 768811323 323 qgELLEAFGSGTAAVVSPIKEIGWNNEDI 351
Cdd:PLN02259 326 --DADEVFCTGTAVVVAPVGTITYQEKRV 352
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
43-390 |
2.84e-44 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 157.57 E-value: 2.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 43 EELVFGQTFTDHMLTIPWSAEEGWGTPHIKPYGNLSLDPSACVFHYAFELFEGLKAYRTPQNTITMFRPDKNMARMNKSA 122
Cdd:PLN02883 55 DKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKIGA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 123 ARICLPTFESEELIKLTGKLIEQDKHLVPQGNGYSLYIRPTMIGTSKGLGVGTPSEALLYVITSPVGPYYKTGFKAVRLE 202
Cdd:PLN02883 135 ERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGTAALNLY 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 203 ATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLWLFGPE-KNITEVGTMNVFFVFLNKVtgkkelVTAPLDG 281
Cdd:PLN02883 215 VEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTgKNIEEVSAANIFLVKGNII------VTPATSG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 282 TILEGVTRDSVLTLARDkldpQEWDINERYYTITEVatraKQGEllEAFGSGTAAVVSPIKEIGWNNEDIHVPLlpGEqc 361
Cdd:PLN02883 289 TILGGITRKSIIEIALD----LGYKVEERRVPVEEL----KEAE--EVFCTGTAAGVASVGSITFKNTRTEYKV--GD-- 354
|
330 340 350
....*....|....*....|....*....|
gi 768811323 362 GALTKQVAQWIADIQYGRV-NYGNWSKTVA 390
Cdd:PLN02883 355 GIVTQQLRSILLGIQTGSIqDTKDWVLQIA 384
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
92-344 |
2.51e-30 |
|
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: 115.92 E-value: 2.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 92 LFEGLKAYRtpqNTItmFRPDKNMARMNKSAARICLPTFESEELIKltgKLIEQdkhLVPQGNGYSLYIRPTMIGTSKGL 171
Cdd:pfam01063 2 VFETLRVYN---GKI--FFLDEHLARLRRSAKLLGIPLPFDEEDLR---KIIEE---LLKANGLGVGRLRLTVSRGPGGF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 172 GVGTPS-EALLYVITSPVGPYYKtgfkavRLEATDYATRAWPGGVGDKKLGANYAPCILPQLQAAKRGYQQNLwLFGPEK 250
Cdd:pfam01063 71 GLPTSDpTLAIFVSALPPPPESK------KKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDAL-LLDEDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 251 NITEVGTMNVFFVflnkvtgK-KELVTAPLDGTILEGVTRDSVLTLARdkldPQEWDINERYYTITEVAtRAKqgellEA 329
Cdd:pfam01063 144 NVTEGSTSNVFLV-------KgGTLYTPPLESGILPGITRQALLDLAK----ALGLEVEERPITLADLQ-EAD-----EA 206
|
250
....*....|....*
gi 768811323 330 FGSGTAAVVSPIKEI 344
Cdd:pfam01063 207 FLTNSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
86-385 |
9.54e-27 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 108.31 E-value: 9.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 86 FHYAFELFEGLKAYRTPQNTiTMFRPDKNMARMNKSAA--RICLPtFESEELIKLTGKLIEQdkhlvpqgNGY-SLYIRP 162
Cdd:PRK06606 30 LHYGTGVFEGIRAYDTPKGP-AIFRLREHTKRLFNSAKilRMEIP-YSVDELMEAQREVVRK--------NNLkSAYIRP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 163 -TMIGtSKGLGV---GTPSEALLYVItsPVGPY-----YKTGFKA-----VRLEATDYATRAwpggvgdkKLGANYAPCI 228
Cdd:PRK06606 100 lVFVG-DEGLGVrphGLPTDVAIAAW--PWGAYlgeeaLEKGIRVkvsswTRHAPNSIPTRA--------KASGNYLNSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 229 LPQLQAAKRGYQQNLwLFGPEKNITEVGTMNVFFVflnkvtGKKELVTAPLDGTILEGVTRDSVLTLARDkldpqewdin 308
Cdd:PRK06606 169 LAKTEARRNGYDEAL-LLDVEGYVSEGSGENIFIV------RDGVLYTPPLTSSILEGITRDTVITLAKD---------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 309 eRYYTITEvaTRAKQGELL---EAFGSGTAAVVSPIKEIgwnneDIHVplLPGEQCGALTKQVAQWIADIQYGRV-NYGN 384
Cdd:PRK06606 232 -LGIEVIE--RRITRDELYiadEVFFTGTAAEVTPIREV-----DGRQ--IGNGKRGPITEKLQSAYFDIVRGRTeKYAH 301
|
.
gi 768811323 385 W 385
Cdd:PRK06606 302 W 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
85-385 |
2.22e-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: 107.06 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 85 VFHYAFELFEGLKAYRTPQNTItMFRPDKNMARMNKSAARICLP-TFESEELIKLTGKLIEQDkhlvpqgNGYSLYIRPT 163
Cdd:TIGR01122 20 ALHYGTGVFEGIRAYDTDKGPA-IFRLKEHIQRLYDSAKIYRMEiPYSKEELMEATRETLRKN-------NLRSAYIRPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 164 MIGTSKGLGV----GTPSEalLYVITSPVGPYYKT-----GFKAVRLEATDYATRAWPGGVgdkKLGANYAPCILPQLQA 234
Cdd:TIGR01122 92 VFRGDGDLGLnpraGYKPD--VIIAAWPWGAYLGEealekGIDAKVSSWRRNAPNTIPTAA---KAGGNYLNSLLAKSEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 235 AKRGYQQNLWLfGPEKNITEvGTMNVFFVFLNKVtgkkeLVTAPLDGTILEGVTRDSVLTLARdkldpqewdinERYYTI 314
Cdd:TIGR01122 167 RRHGYDEAILL-DVEGYVAE-GSGENIFIVKDGV-----LFTPPVTSSILPGITRDTVITLAK-----------ELGIEV 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768811323 315 TEvaTRAKQGELL---EAFGSGTAAVVSPIKEIgwNNEDIHvpllPGeQCGALTKQVAQWIADIQYGRV-NYGNW 385
Cdd:TIGR01122 229 VE--QPISREELYtadEAFFTGTAAEITPIREV--DGRKIG----NG-RRGPVTKKLQEAFFDLVTGGTeDYWGW 294
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
85-344 |
7.79e-18 |
|
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes transamination between D-amino acids and their respective alpha-keto acids. It plays a major role in the synthesis of bacterial cell wall components like D-alanine and D-glutamate in addition to other D-amino acids. The enzyme like other members of this superfamily requires PLP as a cofactor. Members of this subgroup are found in all three forms of life.
Pssm-ID: 238799 [Multi-domain] Cd Length: 270 Bit Score: 82.65 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 85 VFHYAFELFEGLKAYRTpqntiTMFRPDKNMARMNKSAARICLPT-FESEELIKLTGKLIEQDKhlvpQGNGYsLYIRPT 163
Cdd:cd01558 20 GFLFGDGVYEVIRVYNG-----KPFALDEHLDRLYRSAKELRIDIpYTREELKELIRELVAKNE----GGEGD-VYIQVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 164 MiGTSK-GLGVGTPSEALLYVITSP----VGPYYKTGFKAVRLEatdyaTRAWpgGVGDKKLGaNYAPCILPQLQAAKRG 238
Cdd:cd01558 90 R-GVGPrGHDFPKCVKPTVVIITQPlplpPAELLEKGVRVITVP-----DIRW--LRCDIKSL-NLLNNVLAKQEAKEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 239 YQQnLWLFGPEKNITEVGTMNVFFVflnkvtGKKELVTAPLDGTILEGVTRDSVLTLARDKldpqEWDINERYYTITEVA 318
Cdd:cd01558 161 ADE-AILLDADGLVTEGSSSNVFIV------KNGVLVTPPLDNGILPGITRATVIELAKEL----GIPVEERPFSLEELY 229
|
250 260
....*....|....*....|....*.
gi 768811323 319 TrAKqgellEAFGSGTAAVVSPIKEI 344
Cdd:cd01558 230 T-AD-----EVFLTSTTAEVMPVVEI 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
93-344 |
1.35e-10 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 61.81 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 93 FEGLKAYrtpQNTItmFRPDKNMARMNKSAARICL-PTFESEELiklTGKLIEQdkhlVPQGNGYSLYIRPTMigtSKGL 171
Cdd:PRK08320 33 FEGIRAY---NGRV--FRLKEHIDRLYDSAKAIMLeIPLSKEEM---TEIVLET----LRKNNLRDAYIRLVV---SRGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 172 G--------VGTPSealLYVITSPVGPY----YKTGFKAVRLeatdyATRAWPGGVGD---KKLgaNYAPCILPQLQAAK 236
Cdd:PRK08320 98 GdlgldprkCPKPT---VVCIAEPIGLYpgelYEKGLKVITV-----STRRNRPDALSpqvKSL--NYLNNILAKIEANL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 237 RGYQQNLwLFGPEKNITEVGTMNVFFVflnkvtGKKELVTAPLDGTILEGVTRDSVLTLARDKldpqEWDINERYYTITE 316
Cdd:PRK08320 168 AGVDEAI-MLNDEGYVAEGTGDNIFIV------KNGKLITPPTYAGALEGITRNAVIEIAKEL----GIPVREELFTLHD 236
|
250 260
....*....|....*....|....*...
gi 768811323 317 VATrAKqgellEAFGSGTAAVVSPIKEI 344
Cdd:PRK08320 237 LYT-AD-----EVFLTGTAAEVIPVVKV 258
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
87-345 |
3.50e-10 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 60.37 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 87 HYAFELFEGLKAYrtpQNTItmFRPDKNMARMNKSAARIclpTFEseelIKLTGKLIEQDKHLVPQGNGYS-LYIRPTMI 165
Cdd:PRK07544 33 HYASSVFEGERAY---GGKI--FKLREHSERLRRSAELL---DFE----IPYSVAEIDAAKKETLAANGLTdAYVRPVAW 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 166 GTSKGLGVGTPSEAL-LYVITSPVGPYY--KTGFKAVRLEATDY---ATRAWPggVGDKKLGAnYAPCILPQLQAAKRGY 239
Cdd:PRK07544 101 RGSEMMGVSAQQNKIhLAIAAWEWPSYFdpEAKMKGIRLDIAKWrrpDPETAP--SAAKAAGL-YMICTISKHAAEAKGY 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 240 QQNLwLFGPEKNITEVGTMNVFFVflnkvtgKKELVTAPLDGTILEGVTRDSVLTLARDKldpqEWDINERYYTITEVAT 319
Cdd:PRK07544 178 ADAL-MLDYRGYVAEATGANIFFV-------KDGVIHTPTPDCFLDGITRQTVIELAKRR----GIEVVERHIMPEELAG 245
|
250 260
....*....|....*....|....*.
gi 768811323 320 rakqgeLLEAFGSGTAAVVSPIKEIG 345
Cdd:PRK07544 246 ------FSECFLTGTAAEVTPVSEIG 265
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
86-345 |
7.38e-09 |
|
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: 55.78 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 86 FHYAFELFEGLKAYRTpqntitmfRP---DKNMARMNKSAARICLPTFESEELIKLTGKLIEQDkhlvPQGNGYslyIRP 162
Cdd:cd01559 4 FAYGDGVFETMRALDG--------RLfllDAHLARLERSARRLGIPEPDLPRLRAALESLLAAN----DIDEGR---IRL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 163 TMIGTSKGLGVGTPSEA--LLYVITSPVGPyyKTGFKAVRLEATDYATRAWPGGVGDKKLgaNYAPCILPQLQAAKRGYQ 240
Cdd:cd01559 69 ILSRGPGGRGYAPSVCPgpALYVSVIPLPP--AWRQDGVRLITCPVRLGEQPLLAGLKHL--NYLENVLAKREARDRGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 241 QNLWLfGPEKNITEVGTMNVFFVFLNkvtgkkELVTAPLDGTILEGVTRDSVLTLARDkldpQEWDINERYytitEVATR 320
Cdd:cd01559 145 EALFL-DTDGRVIEGTASNLFFVKDG------ELVTPSLDRGGLAGITRQRVIELAAA----KGYAVDERP----LRLED 209
|
250 260
....*....|....*....|....*
gi 768811323 321 AKQGEllEAFGSGTAAVVSPIKEIG 345
Cdd:cd01559 210 LLAAD--EAFLTNSLLGVAPVTAID 232
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
86-345 |
1.84e-07 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 52.26 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 86 FHYAFELFEGLKAYRTpqntiTMFRPDKNMARMNKSAARICLPtfeseelIKLTGKLIEQDKHLVPQGNGYS-LYIRpTM 164
Cdd:PRK12479 27 FLYGDGVFEGIRSYGG-----NVFCLKEHVKRLYESAKSILLT-------IPLTVDEMEEAVLQTLQKNEYAdAYIR-LI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 165 IGTSKG-LGVG--TPSEALLYVITSPVGPY----YKTGFKAVRLEATdyatRAWPGGVGDKKLGANYAPCILPQLQAAKR 237
Cdd:PRK12479 94 VSRGKGdLGLDprSCVKPSVIIIAEQLKLFpqefYDNGLSVVSVASR----RNTPDALDPRIKSMNYLNNVLVKIEAAQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 238 GYQQNLWLfGPEKNITEVGTMNVFFVFLNKVtgkkelVTAPLDGTILEGVTRDSVLTLARDKLDPQEwdinERYYTITEV 317
Cdd:PRK12479 170 GVLEALML-NQQGYVCEGSGDNVFVVKDGKV------LTPPSYLGALEGITRNSVIELCERLSIPCE----ERPFTRHDV 238
|
250 260 270
....*....|....*....|....*....|...
gi 768811323 318 ATRAkqgellEAFGSGTAAVVSPI-----KEIG 345
Cdd:PRK12479 239 YVAD------EVFLTGTAAELIPVvkvdsREIG 265
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
227-345 |
3.23e-07 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 51.47 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 227 CILPQL---QAAK-RGYQQnLWLFGpEKNITEVGTMNVFFVflnkvTGKKELVTAPLDGTILEGVTRDSVLTLARdkldP 302
Cdd:PRK06680 152 GLLPNVlakQAAKeAGAQE-AWMVD-DGFVTEGASSNAWIV-----TKDGKLVTRPADNFILPGITRHTLIDLAK----E 220
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 768811323 303 QEWDINERYYTITEvATRAKqgellEAFGSGTAAVVSPIKEIG 345
Cdd:PRK06680 221 LGLEVEERPFTLQE-AYAAR-----EAFITAASSFVFPVVQID 257
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
177-351 |
2.88e-05 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 45.78 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 177 SEALLY--VITSPVGPYYKTGFKAVR----LEATDYATrawpggvgdkKLGANYAPCILPQLQAAKRGYQQNLWLFGpEK 250
Cdd:PLN02845 146 SEPAFYavVIEDTYAQDRPEGVKVVTssvpIKPPQFAT----------VKSVNYLPNALSQMEAEERGAFAGIWLDE-EG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 251 NITEVGTMNVFFvflnkVTGKKELVTAPLDgTILEGVTRDSVLTLARDKLDPQEW-DINERYYTITEvATRAKqgellEA 329
Cdd:PLN02845 215 FVAEGPNMNVAF-----LTNDGELVLPPFD-KILSGCTARRVLELAPRLVSPGDLrGVKQRKISVEE-AKAAD-----EM 282
|
170 180
....*....|....*....|..
gi 768811323 330 FGSGTAAVVSPIkeIGWNNEDI 351
Cdd:PLN02845 283 MLIGSGVPVLPI--VSWDGQPI 302
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
112-344 |
1.02e-04 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 43.79 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 112 DKNMARMNKSAARICL-PTFESEELIKLTgklIEQDKHLVPQGngySLYIRPTMIGTSKGLGVGTPSEA----LLYVITS 186
Cdd:PRK13356 51 DLHCARVNRSAEALGLkPTVSAEEIEALA---REGLKRFDPDT---ALYIRPMYWAEDGFASGVAPDPEstrfALCLEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 187 PVGPyyKTGFKAVRleaTDYAtRAWPG-GVGDKKlganyAPCILPQ-----LQAAKRGYQQNLWLfGPEKNITEVGTMNV 260
Cdd:PRK13356 125 PMPE--PTGFSLTL---SPFR-RPTLEmAPTDAK-----AGCLYPNnaralREARSRGFDNALVL-DMLGNVAETATSNV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768811323 261 FFVflnkvtgKKELVTAPLD-GTILEGVTRDSVLTLARDkldpQEWDINERYYTITEVAtrakqgELLEAFGSGTAAVVS 339
Cdd:PRK13356 193 FMV-------KDGVVFTPVPnGTFLNGITRQRVIALLRE----DGVTVVETTLTYEDFL------EADEVFSTGNYSKVV 255
|
....*
gi 768811323 340 PIKEI 344
Cdd:PRK13356 256 PVTRF 260
|
|
|