|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
1-356 |
0e+00 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 602.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 1 MSEKVKFVERQALKEKPDTAGLGFGQYFTDYMLSYDYDIDKgWHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTND 80
Cdd:PRK13357 1 FTVTLKPNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 81 -EVVLFRPDQNFKRINDSLARLEMPKIDEDVLLEGLKQLVDVERDWV-PEGEGQSLYIRPFVFATEGILGVRPSHQYKLL 158
Cdd:PRK13357 80 gSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 159 IILSPSGAYYGGDtLKSTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQSNANKLGYDQVLWLDGVEQKYVEEVGSMNI 238
Cdd:PRK13357 160 VIASPVGAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 239 FFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAYDKGALTEVFGSGTAAVISPVGTLRYEDRE 318
Cdd:PRK13357 239 FFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 488390538 319 IVINNNEPGEITKKLYDTYTGIQSGKLEDKHGWRVVVP 356
Cdd:PRK13357 319 FVIGDGEVGPVTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
43-355 |
8.90e-149 |
|
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: 422.24 E-value: 8.90e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTND-EVVLFRPDQNFKRINDSLARLEMPKIDEDVLLEGLKQLVDV 121
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADgSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 122 ERDWVP-EGEGQSLYIRPFVFATEGILGVRPSHQYKLLIILSPSGAYYGGDtLKSTKIYVEDEYVRAVRGGVGFAKVAGN 200
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 201 YAASLLAQSNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVEN-GKVVTPALNGSILPGITRKSIIELAKELGYEVEERK 279
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGdGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488390538 280 VSVDELFEAYDKGAltEVFGSGTAAVISPVGTLRYEDREIVINNNEPGEITKKLYDTYTGIQSGKLEDKHGWRVVV 355
Cdd:TIGR01123 240 IDIDELKAFVEAGE--IVFACGTAAVITPVGEIQHGGKEVVFASGQPGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
55-343 |
1.06e-137 |
|
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: 392.71 E-value: 1.06e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 55 EVSPAAQGLHYGQAVFEGLKAYKTND-EVVLFRPDQNFKRINDSLARLEMPKIDEDVLLEGLKQLVDVERDWVPEGEGQS 133
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDgKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 134 LYIRPFVFATEGILGVRPSHQYKLLIILSPSGAYYGGdTLKSTKIYVEdEYVRAVRGGVGFAKVAGNYAASLLAQSNANK 213
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKG-GEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 214 LGYDQVLWLDGvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAydkga 293
Cdd:cd01557 159 KGYDQALWLDG-AHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEA----- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488390538 294 lTEVFGSGTAAVISPVGtlRYEDREIVINNNEPGEITKKLYDTYTGIQSG 343
Cdd:cd01557 233 -DEVFATGTAAVVTPVG--EIDYRGKEPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
43-347 |
5.11e-110 |
|
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: 322.52 E-value: 5.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTNdevvLFRPDQNFKRINDSLARLEMP-KIDEDVLLEGLKQLVDV 121
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGR----LFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 122 ERDwvpegegQSLYIRPFVFATEGILGVRPSH-QYKLLIILSPSGAYYGGDTLKSTKIYVEdEYVRAVRGGVGFAKvAGN 200
Cdd:COG0115 80 NGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITS-PYRRAAPGGLGGIK-TGN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 201 YAASLLAQSNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKV 280
Cdd:COG0115 151 YLNNVLAKQEAKEAGADEALLLD--TDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488390538 281 SVDELFEAydkgalTEVFGSGTAAVISPVGTLryedREIVINNNEPGEITKKLYDTYTGIQSGKLED 347
Cdd:COG0115 229 SLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
68-309 |
1.64e-41 |
|
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: 144.81 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 68 AVFEGLKAYktNDEVvlFRPDQNFKRINDSLARLEMP-KIDEDVLLEGLKQLVDVERDWVPegegqslYIRPFVFATEGI 146
Cdd:pfam01063 1 GVFETLRVY--NGKI--FFLDEHLARLRRSAKLLGIPlPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 147 LGVRPSHqYKLLIILSPSgaYYGGDTLKSTKIYveDEYVRAVRGGVGFAKVaGNYAASLLAQSNANKLGYDQVLWLDgvE 226
Cdd:pfam01063 70 FGLPTSD-PTLAIFVSAL--PPPPESKKKGVIS--SLVRRNPPSPLPGAKT-LNYLENVLARREAKAQGADDALLLD--E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 227 QKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAydkgalTEVFGSGTAAVI 306
Cdd:pfam01063 142 DGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEA------DEAFLTNSLRGV 215
|
...
gi 488390538 307 SPV 309
Cdd:pfam01063 216 TPV 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
1-356 |
0e+00 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 602.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 1 MSEKVKFVERQALKEKPDTAGLGFGQYFTDYMLSYDYDIDKgWHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTND 80
Cdd:PRK13357 1 FTVTLKPNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 81 -EVVLFRPDQNFKRINDSLARLEMPKIDEDVLLEGLKQLVDVERDWV-PEGEGQSLYIRPFVFATEGILGVRPSHQYKLL 158
Cdd:PRK13357 80 gSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 159 IILSPSGAYYGGDtLKSTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQSNANKLGYDQVLWLDGVEQKYVEEVGSMNI 238
Cdd:PRK13357 160 VIASPVGAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 239 FFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAYDKGALTEVFGSGTAAVISPVGTLRYEDRE 318
Cdd:PRK13357 239 FFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 488390538 319 IVINNNEPGEITKKLYDTYTGIQSGKLEDKHGWRVVVP 356
Cdd:PRK13357 319 FVIGDGEVGPVTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
43-355 |
8.90e-149 |
|
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: 422.24 E-value: 8.90e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTND-EVVLFRPDQNFKRINDSLARLEMPKIDEDVLLEGLKQLVDV 121
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADgSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 122 ERDWVP-EGEGQSLYIRPFVFATEGILGVRPSHQYKLLIILSPSGAYYGGDtLKSTKIYVEDEYVRAVRGGVGFAKVAGN 200
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 201 YAASLLAQSNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVEN-GKVVTPALNGSILPGITRKSIIELAKELGYEVEERK 279
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGdGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488390538 280 VSVDELFEAYDKGAltEVFGSGTAAVISPVGTLRYEDREIVINNNEPGEITKKLYDTYTGIQSGKLEDKHGWRVVV 355
Cdd:TIGR01123 240 IDIDELKAFVEAGE--IVFACGTAAVITPVGEIQHGGKEVVFASGQPGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
55-343 |
1.06e-137 |
|
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: 392.71 E-value: 1.06e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 55 EVSPAAQGLHYGQAVFEGLKAYKTND-EVVLFRPDQNFKRINDSLARLEMPKIDEDVLLEGLKQLVDVERDWVPEGEGQS 133
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDgKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 134 LYIRPFVFATEGILGVRPSHQYKLLIILSPSGAYYGGdTLKSTKIYVEdEYVRAVRGGVGFAKVAGNYAASLLAQSNANK 213
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKG-GEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 214 LGYDQVLWLDGvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAydkga 293
Cdd:cd01557 159 KGYDQALWLDG-AHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEA----- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488390538 294 lTEVFGSGTAAVISPVGtlRYEDREIVINNNEPGEITKKLYDTYTGIQSG 343
Cdd:cd01557 233 -DEVFATGTAAVVTPVG--EIDYRGKEPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
43-347 |
5.11e-110 |
|
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: 322.52 E-value: 5.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTNdevvLFRPDQNFKRINDSLARLEMP-KIDEDVLLEGLKQLVDV 121
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGR----LFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 122 ERDwvpegegQSLYIRPFVFATEGILGVRPSH-QYKLLIILSPSGAYYGGDTLKSTKIYVEdEYVRAVRGGVGFAKvAGN 200
Cdd:COG0115 80 NGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITS-PYRRAAPGGLGGIK-TGN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 201 YAASLLAQSNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKV 280
Cdd:COG0115 151 YLNNVLAKQEAKEAGADEALLLD--TDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488390538 281 SVDELFEAydkgalTEVFGSGTAAVISPVGTLryedREIVINNNEPGEITKKLYDTYTGIQSGKLED 347
Cdd:COG0115 229 SLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
18-353 |
1.69e-99 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 300.23 E-value: 1.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 18 DTAGLGFGQYFTDYMLSYDYDIDKGWHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAY-KTNDEVVLFRPDQNFKRIND 96
Cdd:PLN02782 71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYrKEDGNILLFRPEENAIRMRN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 97 SLARLEMPKIDEDVLLEGLKQLVDVERDWVPEGEGQSLYIRPFVFATEGILGVRPSHQYKLLIILSPSGAYYGgDTLKST 176
Cdd:PLN02782 151 GAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFK-EGVAPI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 177 KIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQSNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSIL 256
Cdd:PLN02782 230 NLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIVKDNVISTPAIKGTIL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 257 PGITRKSIIELAKELGYEVEERKVSVDELFEAydkgalTEVFGSGTAAVISPVGTLRYEDREIVINNNEPGEITKKLYDT 336
Cdd:PLN02782 310 PGITRKSIIDVARSQGFQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRVSYGEGGFGTVSQQLYTV 383
|
330
....*....|....*..
gi 488390538 337 YTGIQSGKLEDKHGWRV 353
Cdd:PLN02782 384 LTSLQMGLIEDNMNWTV 400
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
62-337 |
7.08e-95 |
|
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: 282.95 E-value: 7.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 62 GLHYGQAVFEGLKAYKtndeVVLFRPDQNFKRINDSLARLEMPK-IDEDVLLEGLKQLVDVerdwvpeGEGQSLYIRPFV 140
Cdd:cd00449 3 GLHYGDGVFEGLRAGK----GRLFRLDEHLDRLNRSAKRLGLPIpYDREELREALKELVAA-------NNGASLYIRPLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 141 FATEGILGV--RPSHQYKLLIILSPSGAYYGGdTLKSTKIYVEDEYVRAVRGGVGFAKvAGNYAASLLAQSNANKLGYDQ 218
Cdd:cd00449 72 TRGVGGLGVapPPSPEPTFVVFASPVGAYAKG-GEKGVRLITSPDRRRAAPGGTGDAK-TGGNLNSVLAKQEAAEAGADE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 219 VLWLDGveQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAydkgalTEVF 298
Cdd:cd00449 150 ALLLDD--NGYVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAA------DEVF 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 488390538 299 GSGTAAVISPVGTLRYEDreivINNNEPGEITKKLYDTY 337
Cdd:cd00449 222 LTGTAAEVTPVTEIDGRG----IGDGKPGPVTRKLRELL 256
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
22-355 |
3.86e-87 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 266.80 E-value: 3.86e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 22 LGFGQYFTDYMLSYDYDIDKGWHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTND-EVVLFRPDQNFKRINDSLAR 100
Cdd:PLN03117 25 LGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDgRITLFRPDQNALRMQTGADR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 101 LEMPKIDEDVLLEGLKQLVDVERDWVPEGEGQSLYIRPFVFATEGILGVRPSHQYKLLIILSPSGAYYGGDTLKSTKiyV 180
Cdd:PLN03117 105 LCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASSGLNLK--V 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 181 EDEYVRAVRGGVGFAKVAGNYAASLLAQSNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGIT 260
Cdd:PLN03117 183 DHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNIFILKGNIVSTPPTSGTILPGVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 261 RKSIIELAKELGYEVEERKVSVDELFEAydkgalTEVFGSGTAAVISPVGTLRYEDREIVINNNEPGeITKKLYDTYTGI 340
Cdd:PLN03117 263 RKSISELARDIGYQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA-LSTKLHLILTNI 335
|
330
....*....|....*
gi 488390538 341 QSGKLEDKHGWRVVV 355
Cdd:PLN03117 336 QMGVVEDKKGWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
18-351 |
1.97e-80 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 250.79 E-value: 1.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 18 DTAGLGFGQYFTDYMLSYDYDIDKGWHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAY-KTNDEVVLFRPDQNFKRIND 96
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYrKENGKLLLFRPDHNAIRMKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 97 SLARLEMPKIDEDVLLEGLKQLVDVERDWVPEGEGQSLYIRPFVFATEGILGVRPSHQYKLLIILSPSGAYYGgDTLKST 176
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFK-EGMAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 177 KIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQSNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSIL 256
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPATNGTIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 257 PGITRKSIIELAKELGYEVEERKVSVDELFEAydkgalTEVFGSGTAAVISPVGTLRYEDREIVINNNEPgEITKKLYDT 336
Cdd:PLN02259 296 EGITRKSVMEIASDQGYQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE-SVCQKLRSV 368
|
330
....*....|....*
gi 488390538 337 YTGIQSGKLEDKHGW 351
Cdd:PLN02259 369 LVGIQTGLIEDNKGW 383
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
43-351 |
3.31e-69 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 219.25 E-value: 3.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTNDEVVLFRPDQNFKRINDSlARLEMPKIDEDVlleglKQLVDVE 122
Cdd:PRK06606 10 WFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPAIFRLREHTKRLFNS-AKILRMEIPYSV-----DELMEAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 123 RDWVPEGEGQSLYIRPFVFATEGILGVRPsHQYK--LLIILSPSGAYYGGDTLK---STKIyveDEYVR-AVRGGVGFAK 196
Cdd:PRK06606 84 REVVRKNNLKSAYIRPLVFVGDEGLGVRP-HGLPtdVAIAAWPWGAYLGEEALEkgiRVKV---SSWTRhAPNSIPTRAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 197 VAGNYAASLLAQSNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVE 276
Cdd:PRK06606 160 ASGNYLNSILAKTEARRNGYDEALLLD--VEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVI 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390538 277 ERKVSVDELFEAydkgalTEVFGSGTAAVISPVgtlRYEDReIVINNNEPGEITKKLYDTYTGIQSGKLEDKHGW 351
Cdd:PRK06606 238 ERRITRDELYIA------DEVFFTGTAAEVTPI---REVDG-RQIGNGKRGPITEKLQSAYFDIVRGRTEKYAHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
43-355 |
4.19e-67 |
|
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: 213.38 E-value: 4.19e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTNDEVVLFRPDQNFKRINDS--LARLEMPKIDEdvlleglkQLVD 120
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTDKGPAIFRLKEHIQRLYDSakIYRMEIPYSKE--------ELME 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 121 VERDWVPEGEGQSLYIRPFVFATEGILGVRPSHQYK--LLIILSPSGAYYGGDTL-KSTKIYVEDEYVRAVRGGVGFAKV 197
Cdd:TIGR01122 73 ATRETLRKNNLRSAYIRPLVFRGDGDLGLNPRAGYKpdVIIAAWPWGAYLGEEALeKGIDAKVSSWRRNAPNTIPTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 198 AGNYAASLLAQSNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEE 277
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILLD--VEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 278 RKVSVDELFEAydkgalTEVFGSGTAAVISPVgtlryedREI---VINNNEPGEITKKLYDTYTGIQSGKLEDKHGWRVV 354
Cdd:TIGR01122 231 QPISREELYTA------DEAFFTGTAAEITPI-------REVdgrKIGNGRRGPVTKKLQEAFFDLVTGGTEDYWGWLTY 297
|
.
gi 488390538 355 V 355
Cdd:TIGR01122 298 V 298
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
18-351 |
9.24e-67 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 215.35 E-value: 9.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 18 DTAGLGFGQYFTDYMLSYDYDIDKGWHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTND-EVVLFRPDQNFKRIND 96
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDgRILLFRPELNAMRMKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 97 SLARLEMPKIDEDVLLEGLKQLVDVERDWVPEGEGQSLYIRPFVFATEGILGVRPSHQYKLLIILSPSGAYYGGDTlKST 176
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 177 KIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQSNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSIL 256
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNIIVTPATSGTIL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 257 PGITRKSIIELAKELGYEVEERKVSVDELFEAydkgalTEVFGSGTAAVISPVGTLRYEDREIVINNNEpGEITKKLYDT 336
Cdd:PLN02883 292 GGITRKSIIEIALDLGYKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGD-GIVTQQLRSI 364
|
330
....*....|....*
gi 488390538 337 YTGIQSGKLEDKHGW 351
Cdd:PLN02883 365 LLGIQTGSIQDTKDW 379
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
68-309 |
1.64e-41 |
|
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: 144.81 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 68 AVFEGLKAYktNDEVvlFRPDQNFKRINDSLARLEMP-KIDEDVLLEGLKQLVDVERDWVPegegqslYIRPFVFATEGI 146
Cdd:pfam01063 1 GVFETLRVY--NGKI--FFLDEHLARLRRSAKLLGIPlPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 147 LGVRPSHqYKLLIILSPSgaYYGGDTLKSTKIYveDEYVRAVRGGVGFAKVaGNYAASLLAQSNANKLGYDQVLWLDgvE 226
Cdd:pfam01063 70 FGLPTSD-PTLAIFVSAL--PPPPESKKKGVIS--SLVRRNPPSPLPGAKT-LNYLENVLARREAKAQGADDALLLD--E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 227 QKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAydkgalTEVFGSGTAAVI 306
Cdd:pfam01063 142 DGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEA------DEAFLTNSLRGV 215
|
...
gi 488390538 307 SPV 309
Cdd:pfam01063 216 TPV 218
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
43-337 |
2.75e-40 |
|
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: 143.12 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTNdevvLFRPDQNFKRINDSLA--RLEMPkIDEDVLLEGLKQLVd 120
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGK----PFALDEHLDRLYRSAKelRIDIP-YTREELKELIRELV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 121 vERDWVPEGEGqslYIRPfvfaTEGIlGVRPSHQYK-----LLIILSPSGAYYGGDTLKSTK-IYVEDeyvraVRGGVGF 194
Cdd:cd01558 75 -AKNEGGEGDV---YIQV----TRGV-GPRGHDFPKcvkptVVIITQPLPLPPAELLEKGVRvITVPD-----IRWLRCD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 195 AKvAGNYAASLLAQSNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYE 274
Cdd:cd01558 141 IK-SLNLLNNVLAKQEAKEAGADEAILLD--ADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIP 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488390538 275 VEERKVSVDELFEAydkgalTEVFGSGTAAVISPVGTLryEDReiVINNNEPGEITKKLYDTY 337
Cdd:cd01558 218 VEERPFSLEELYTA------DEVFLTSTTAEVMPVVEI--DGR--PIGDGKPGPVTKRLREAY 270
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
47-333 |
1.08e-34 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 128.84 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 47 KIVPYAPLEVSPAAQGLHYGQAVFEGLKAYKTNdevvLFRPDQNFKRINDS---------LARLEMpkidEDVLLEGLKQ 117
Cdd:PRK08320 10 EFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGR----VFRLKEHIDRLYDSakaimleipLSKEEM----TEIVLETLRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 118 --LVDVerdwvpegegqslYIRPFVFATEGILGVRPSHQYK--LLIILSPSGAYYGgdTLKSTKIYVEDEYVRAVRGGVG 193
Cdd:PRK08320 82 nnLRDA-------------YIRLVVSRGVGDLGLDPRKCPKptVVCIAEPIGLYPG--ELYEKGLKVITVSTRRNRPDAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 194 FAKVAG-NYAASLLAQSNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELG 272
Cdd:PRK08320 147 SPQVKSlNYLNNILAKIEANLAGVDEAIMLN--DEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELG 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488390538 273 YEVEERKVSVDELFEAydkgalTEVFGSGTAAVISPVGTLryEDReiVINNNEPGEITKKL 333
Cdd:PRK08320 225 IPVREELFTLHDLYTA------DEVFLTGTAAEVIPVVKV--DGR--VIGDGKPGPITKKL 275
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
43-338 |
1.35e-31 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 120.47 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIVPYAPLEVSPAAQGLHYGQAVFEGLKAYktNDEVvlFRPDQNFKRINDSlARL---EMP-KIDEdvlLEGLKQL 118
Cdd:PRK07544 12 WMDGELVPWRDAKVHVLTHGLHYASSVFEGERAY--GGKI--FKLREHSERLRRS-AELldfEIPySVAE---IDAAKKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 119 VdVERDWVPEGegqslYIRPFVFATEGILGVRPSH-QYKLLIILSPSGAYYGGDT-LKSTKIYVEdEYVR-AVRGGVGFA 195
Cdd:PRK07544 84 T-LAANGLTDA-----YVRPVAWRGSEMMGVSAQQnKIHLAIAAWEWPSYFDPEAkMKGIRLDIA-KWRRpDPETAPSAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 196 KVAGNYAASLLAQSNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNgSILPGITRKSIIELAKELGYEV 275
Cdd:PRK07544 157 KAAGLYMICTISKHAAEAKGYADALMLD--YRGYVAEATGANIFFVKDGVIHTPTPD-CFLDGITRQTVIELAKRRGIEV 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488390538 276 EERKVSVDELfeaydkGALTEVFGSGTAAVISPVGtlryedrEIVINNNEPGEITKKLYDTYT 338
Cdd:PRK07544 234 VERHIMPEEL------AGFSECFLTGTAAEVTPVS-------EIGEYRFTPGAITRDLMDDYE 283
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
43-337 |
4.41e-25 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 102.73 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 43 WHDLKIvpyaPLeVSPAAQGLHYGQAVFEGLKAYktndEVVLFRPDQNFKRINDSLARLEM-PKID----EDVLLEGLKQ 117
Cdd:PRK13356 15 WHEGNV----PI-MGPADHAAWLGSTVFDGARAF----EGVTPDLDLHCARVNRSAEALGLkPTVSaeeiEALAREGLKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 118 LvdverdwvpeGEGQSLYIRPFVFATEG-ILGVRP---SHQYKLLIILSPSGAYyGGDTLKSTkiyvedEYVRAVRG-GV 192
Cdd:PRK13356 86 F----------DPDTALYIRPMYWAEDGfASGVAPdpeSTRFALCLEEAPMPEP-TGFSLTLS------PFRRPTLEmAP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 193 GFAKVAGNYAASLLAQSNANKLGYDQVLWLDGVEQkyVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELG 272
Cdd:PRK13356 149 TDAKAGCLYPNNARALREARSRGFDNALVLDMLGN--VAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDG 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390538 273 YEVEERKVSVDElFEAYDkgaltEVFGSGTAAVISPVgtLRYEDREIvinnnEPGEITKKLYDTY 337
Cdd:PRK13356 227 VTVVETTLTYED-FLEAD-----EVFSTGNYSKVVPV--TRFDDRSL-----QPGPVTRRARELY 278
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
62-337 |
1.04e-23 |
|
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: 98.15 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 62 GLHYGQAVFEGLKAYKtnDEVVLFrpDQNFKRINDSLARLEMPKIDEDVLLEGLKQLVdvERDWVPEG----------EG 131
Cdd:cd01559 3 GFAYGDGVFETMRALD--GRLFLL--DAHLARLERSARRLGIPEPDLPRLRAALESLL--AANDIDEGrirlilsrgpGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 132 QSLYIRPFVFATEGIlGVRPShqyklliilsPSGAYYGGDTLKSTKIYVEDeyvravRGGVGFAKVAgNYAASLLAQSNA 211
Cdd:cd01559 77 RGYAPSVCPGPALYV-SVIPL----------PPAWRQDGVRLITCPVRLGE------QPLLAGLKHL-NYLENVLAKREA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 212 NKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAydk 291
Cdd:cd01559 139 RDRGADEALFLD--TDGRVIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAA--- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488390538 292 galTEVFGSGTAAVISPVgtLRYEDREIvinnnEPGEITKKLYDTY 337
Cdd:cd01559 214 ---DEAFLTNSLLGVAPV--TAIDDHDG-----PPGPLTRALRELL 249
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
56-353 |
2.23e-23 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 98.49 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 56 VSPAAQGLHYGQAVFEGLKAYKTNdevvLFRPDQNFKRINDSLAR--LEMPkidedVLLEGLKQLVdveRDWVPEGEGQS 133
Cdd:PRK12479 20 VSVYDHGFLYGDGVFEGIRSYGGN----VFCLKEHVKRLYESAKSilLTIP-----LTVDEMEEAV---LQTLQKNEYAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 134 LYIRPFVFATEGILGVRPSHQYKLLIILspsgayyggdTLKSTKIYVEDEYvravRGGVGFAKVAG-------------- 199
Cdd:PRK12479 88 AYIRLIVSRGKGDLGLDPRSCVKPSVII----------IAEQLKLFPQEFY----DNGLSVVSVASrrntpdaldpriks 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 200 -NYAASLLAQSNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEER 278
Cdd:PRK12479 154 mNYLNNVLVKIEAAQAGVLEALMLN--QQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEER 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488390538 279 KVSVDELFEAydkgalTEVFGSGTAAVISPVgtLRYEDREivINNNEPGEITKKLYDTYTgiqsgKLEDKHGWRV 353
Cdd:PRK12479 232 PFTRHDVYVA------DEVFLTGTAAELIPV--VKVDSRE--IGDGKPGSVTKQLTEEFK-----KLTRERGVRV 291
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
206-337 |
5.18e-19 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 85.75 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 206 LAQSNANKLGYDQVlWLdgVEQKYVEEVGSMNIFFV-ENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDE 284
Cdd:PRK06680 158 LAKQAAKEAGAQEA-WM--VDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQE 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488390538 285 LFEAydkgalTEVFGSGTAAVISPVGTLryeDREiVINNNEPGEITKKLYDTY 337
Cdd:PRK06680 235 AYAA------REAFITAASSFVFPVVQI---DGK-QIGNGKPGPIAKRLREAY 277
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
226-352 |
1.16e-13 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 70.38 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 226 EQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDELFEAydkgalTEVFGSGTAAV 305
Cdd:PRK07650 171 EEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSA------DEVFVTNSIQE 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488390538 306 ISPVgtLRYEDREIvinNNEPGEITKKLYDTYtgiqsgKLEDKHGWR 352
Cdd:PRK07650 245 IVPL--TRIEERDF---PGKVGMVTKRLQNLY------EMQREKLWS 280
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
200-288 |
2.73e-11 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 63.44 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 200 NYAASLLAQSNANKLGYDQVLWL--DGveqkYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEE 277
Cdd:PRK07849 162 SYAVNMAALRYAARRGADDVIFTstDG----YVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEY 237
|
90
....*....|.
gi 488390538 278 RKVSVDELFEA 288
Cdd:PRK07849 238 RALRPADLFAA 248
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
161-335 |
2.81e-11 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 63.88 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 161 LSPSG----AYYGgDTLKSTKIYVEDEYVRAVRGGV-----GFAKVAG-NYAASLLAQSNANKLGYDQVLWLDgvEQKYV 230
Cdd:PLN02845 140 LSPSGcsepAFYA-VVIEDTYAQDRPEGVKVVTSSVpikppQFATVKSvNYLPNALSQMEAEERGAFAGIWLD--EEGFV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 231 EEVGSMNIFFVENGKV-VTPAlNGSILPGITRKSIIELAKELGYE-----VEERKVSVDELfeaydKGAlTEVFGSGTAA 304
Cdd:PLN02845 217 AEGPNMNVAFLTNDGElVLPP-FDKILSGCTARRVLELAPRLVSPgdlrgVKQRKISVEEA-----KAA-DEMMLIGSGV 289
|
170 180 190
....*....|....*....|....*....|.
gi 488390538 305 VISPVgtLRYEDReiVINNNEPGEITKKLYD 335
Cdd:PLN02845 290 PVLPI--VSWDGQ--PIGDGKVGPITLALHD 316
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
206-298 |
1.52e-09 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 57.93 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 206 LAQSNANKLGYDQVLWLDgVEQKYVEEVGSmNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERKVSVDEL 285
Cdd:PRK06092 149 LIRAELEQTEADEALVLD-SEGWVIECCAA-NLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEEL 226
|
90
....*....|...
gi 488390538 286 FEAyDkgaltEVF 298
Cdd:PRK06092 227 LQA-D-----EVF 233
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
200-338 |
1.01e-08 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 55.79 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488390538 200 NYAASLLAQSNANKLGYDQVLWldgVEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIELAKELGYEVEERK 279
Cdd:PRK12400 154 NLLPNILAATKAERKGCKEALF---VRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEEL 230
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488390538 280 VSVDELFEAydkgalTEVFGSGTAAVISPVGTLryedREIVINNNEPGEITKKLYDTYT 338
Cdd:PRK12400 231 FSVRDVYQA------DECFFTGTTIEILPMTHL----DGTAIQDGQVGPITKMLQRSFS 279
|
|
| |
