|
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: 598.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 1 MSQAVKVERRETLKQKPNTSQLGFGKYFTDYMLSYDYDADKgWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYKR-D 79
Cdd:PRK13357 1 FTVTLKPNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHkD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 80 GEVALFRPEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDIERDWI-PEGEGQSLYIRPFVFATEGALGVGASHQYKLL 158
Cdd:PRK13357 80 GSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 159 IILSPSGAYYGGEtLKPTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYIEEVGSMNI 238
Cdd:PRK13357 160 VIASPVGAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 239 FFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFESYDKGELTEVFGSGTAAVISPVGTLRYEDRE 318
Cdd:PRK13357 239 FFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 600881035 319 IVINNNETGEITQKLYDVYTGIQNGTLEDKNGWRVVVP 356
Cdd:PRK13357 319 FVIGDGEVGPVTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
43-355 |
3.82e-142 |
|
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: 405.30 E-value: 3.82e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 43 WHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYK-RDGEVALFRPEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDI 121
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRcADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 122 ERDWIP-EGEGQSLYIRPFVFATEGALGVGASHQYKLLIILSPSGAYYGGEtLKPTKIYVEDEYVRAVRGGVGFAKVAGN 200
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 201 YAASLLAQTNANKLGYDQVLWLDGVEQKYIEEVGSMNIFFVEN-GKVITPELNGSILPGITRKSIIELAKNLGYEVEERR 279
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGdGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600881035 280 VSIDELFESYDKGEltEVFGSGTAAVISPVGTLRYEDREIVINNNETGEITQKLYDVYTGIQNGTLEDKNGWRVVV 355
Cdd:TIGR01123 240 IDIDELKAFVEAGE--IVFACGTAAVITPVGEIQHGGKEVVFASGQPGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
55-343 |
1.24e-136 |
|
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: 390.02 E-value: 1.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 55 EISPAAQGVHYGQSVFEGLKAYKR-DGEVALFRPEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDIERDWIPEGEGQS 133
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTpDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 134 LYIRPFVFATEGALGVGASHQYKLLIILSPSGAYYGGEtLKPTKIYVEdEYVRAVRGGVGFAKVAGNYAASLLAQTNANK 213
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 214 LGYDQVLWLDGvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFesydkgE 293
Cdd:cd01557 159 KGYDQALWLDG-AHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELY------E 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 600881035 294 LTEVFGSGTAAVISPVGtlRYEDREIVINNNETGEITQKLYDVYTGIQNG 343
Cdd:cd01557 232 ADEVFATGTAAVVTPVG--EIDYRGKEPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
43-347 |
1.75e-109 |
|
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: 321.37 E-value: 1.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 43 WHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYkrDGEvaLFRPEENFKRLNNSLARLEMPQ-VDEAELLEGLKQLVDI 121
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAY--DGR--LFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 122 ERDwipegegQSLYIRPFVFATEGALGVGASH-QYKLLIILSPSGAYYGGETLKPTKIYVEdEYVRAVRGGVGFAKvAGN 200
Cdd:COG0115 80 NGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITS-PYRRAAPGGLGGIK-TGN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 201 YAASLLAQTNANKLGYDQVLWLDgvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRV 280
Cdd:COG0115 151 YLNNVLAKQEAKEAGADEALLLD--TDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600881035 281 SIDELFESydkgelTEVFGSGTAAVISPVGTLryedREIVINNNETGEITQKLYDVYTGIQNGTLED 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 |
2.06e-43 |
|
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: 149.82 E-value: 2.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 68 SVFEGLKAYkrDGEValFRPEENFKRLNNSLARLEMPQ-VDEAELLEGLKQLVDIERDWIPegegqslYIRPFVFATEGA 146
Cdd:pfam01063 1 GVFETLRVY--NGKI--FFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 147 LGVGASHqYKLLIILSPSgaYYGGETLKPTKIYveDEYVRAVRGGVGFAKVaGNYAASLLAQTNANKLGYDQVLWLDgvE 226
Cdd:pfam01063 70 FGLPTSD-PTLAIFVSAL--PPPPESKKKGVIS--SLVRRNPPSPLPGAKT-LNYLENVLARREAKAQGADDALLLD--E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 227 QKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFESydkgelTEVFGSGTAAVI 306
Cdd:pfam01063 142 DGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEA------DEAFLTNSLRGV 215
|
...
gi 600881035 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: 598.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 1 MSQAVKVERRETLKQKPNTSQLGFGKYFTDYMLSYDYDADKgWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYKR-D 79
Cdd:PRK13357 1 FTVTLKPNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHkD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 80 GEVALFRPEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDIERDWI-PEGEGQSLYIRPFVFATEGALGVGASHQYKLL 158
Cdd:PRK13357 80 GSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 159 IILSPSGAYYGGEtLKPTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYIEEVGSMNI 238
Cdd:PRK13357 160 VIASPVGAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 239 FFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFESYDKGELTEVFGSGTAAVISPVGTLRYEDRE 318
Cdd:PRK13357 239 FFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 600881035 319 IVINNNETGEITQKLYDVYTGIQNGTLEDKNGWRVVVP 356
Cdd:PRK13357 319 FVIGDGEVGPVTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
43-355 |
3.82e-142 |
|
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: 405.30 E-value: 3.82e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 43 WHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYK-RDGEVALFRPEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDI 121
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRcADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 122 ERDWIP-EGEGQSLYIRPFVFATEGALGVGASHQYKLLIILSPSGAYYGGEtLKPTKIYVEDEYVRAVRGGVGFAKVAGN 200
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 201 YAASLLAQTNANKLGYDQVLWLDGVEQKYIEEVGSMNIFFVEN-GKVITPELNGSILPGITRKSIIELAKNLGYEVEERR 279
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGdGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 600881035 280 VSIDELFESYDKGEltEVFGSGTAAVISPVGTLRYEDREIVINNNETGEITQKLYDVYTGIQNGTLEDKNGWRVVV 355
Cdd:TIGR01123 240 IDIDELKAFVEAGE--IVFACGTAAVITPVGEIQHGGKEVVFASGQPGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
55-343 |
1.24e-136 |
|
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: 390.02 E-value: 1.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 55 EISPAAQGVHYGQSVFEGLKAYKR-DGEVALFRPEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDIERDWIPEGEGQS 133
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTpDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 134 LYIRPFVFATEGALGVGASHQYKLLIILSPSGAYYGGEtLKPTKIYVEdEYVRAVRGGVGFAKVAGNYAASLLAQTNANK 213
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGG-EKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 214 LGYDQVLWLDGvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFesydkgE 293
Cdd:cd01557 159 KGYDQALWLDG-AHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELY------E 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 600881035 294 LTEVFGSGTAAVISPVGtlRYEDREIVINNNETGEITQKLYDVYTGIQNG 343
Cdd:cd01557 232 ADEVFATGTAAVVTPVG--EIDYRGKEPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
43-347 |
1.75e-109 |
|
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: 321.37 E-value: 1.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 43 WHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYkrDGEvaLFRPEENFKRLNNSLARLEMPQ-VDEAELLEGLKQLVDI 121
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAY--DGR--LFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 122 ERDwipegegQSLYIRPFVFATEGALGVGASH-QYKLLIILSPSGAYYGGETLKPTKIYVEdEYVRAVRGGVGFAKvAGN 200
Cdd:COG0115 80 NGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITS-PYRRAAPGGLGGIK-TGN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 201 YAASLLAQTNANKLGYDQVLWLDgvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRV 280
Cdd:COG0115 151 YLNNVLAKQEAKEAGADEALLLD--TDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600881035 281 SIDELFESydkgelTEVFGSGTAAVISPVGTLryedREIVINNNETGEITQKLYDVYTGIQNGTLED 347
Cdd:COG0115 229 SLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
22-353 |
2.10e-102 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 307.55 E-value: 2.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 22 LGFGKYFTDYMLSYDYDADKGWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAY-KRDGEVALFRPEENFKRLNNSLAR 100
Cdd:PLN02782 75 LGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYrKEDGNILLFRPEENAIRMRNGAER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 101 LEMPQVDEAELLEGLKQLVDIERDWIPEGEGQSLYIRPFVFATEGALGVGASHQYKLLIILSPSGAYYGgETLKPTKIYV 180
Cdd:PLN02782 155 MCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFK-EGVAPINLIV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 181 EDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYIEEVGSMNIFFVENGKVITPELNGSILPGIT 260
Cdd:PLN02782 234 ENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIVKDNVISTPAIKGTILPGIT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 261 RKSIIELAKNLGYEVEERRVSIDELFESydkgelTEVFGSGTAAVISPVGTLRYEDREIVINNNETGEITQKLYDVYTGI 340
Cdd:PLN02782 314 RKSIIDVARSQGFQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRVSYGEGGFGTVSQQLYTVLTSL 387
|
330
....*....|...
gi 600881035 341 QNGTLEDKNGWRV 353
Cdd:PLN02782 388 QMGLIEDNMNWTV 400
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
62-337 |
2.19e-92 |
|
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: 276.79 E-value: 2.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 62 GVHYGQSVFEGLKAYKRdgevALFRPEENFKRLNNSLARLEMPQ-VDEAELLEGLKQLVDierdwipEGEGQSLYIRPFV 140
Cdd:cd00449 3 GLHYGDGVFEGLRAGKG----RLFRLDEHLDRLNRSAKRLGLPIpYDREELREALKELVA-------ANNGASLYIRPLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 141 FATEGALGV--GASHQYKLLIILSPSGAYYGGEtLKPTKIYVEDEYVRAVRGGVGFAKvAGNYAASLLAQTNANKLGYDQ 218
Cdd:cd00449 72 TRGVGGLGVapPPSPEPTFVVFASPVGAYAKGG-EKGVRLITSPDRRRAAPGGTGDAK-TGGNLNSVLAKQEAAEAGADE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 219 VLWLDGveQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFESydkgelTEVF 298
Cdd:cd00449 150 ALLLDD--NGYVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAA------DEVF 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 600881035 299 GSGTAAVISPVGTLRYEDreivINNNETGEITQKLYDVY 337
Cdd:cd00449 222 LTGTAAEVTPVTEIDGRG----IGDGKPGPVTRKLRELL 256
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
21-355 |
4.83e-84 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 259.09 E-value: 4.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 21 QLGFGKYFTDYMLSYDYDADKGWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYK-RDGEVALFRPEENFKRLNNSLA 99
Cdd:PLN03117 24 ELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRtEDGRITLFRPDQNALRMQTGAD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 100 RLEMPQVDEAELLEGLKQLVDIERDWIPEGEGQSLYIRPFVFATEGALGVGASHQYKLLIILSPSGAYY---GGETLKpt 176
Cdd:PLN03117 104 RLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHkasSGLNLK-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 177 kiyVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYIEEVGSMNIFFVENGKVITPELNGSIL 256
Cdd:PLN03117 182 ---VDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNIFILKGNIVSTPPTSGTIL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 257 PGITRKSIIELAKNLGYEVEERRVSIDELFESydkgelTEVFGSGTAAVISPVGTLRYEDREIvinNNETGE--ITQKLY 334
Cdd:PLN03117 259 PGVTRKSISELARDIGYQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKV---KYRTGEeaLSTKLH 329
|
330 340
....*....|....*....|.
gi 600881035 335 DVYTGIQNGTLEDKNGWRVVV 355
Cdd:PLN03117 330 LILTNIQMGVVEDKKGWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
2-351 |
1.12e-78 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 246.17 E-value: 1.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 2 SQAVKVERRETLKQKPNTS-------QLGFGKYFTDYMLSYDYDADKGWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLK 74
Cdd:PLN02259 34 ASALREERKKPLYQNGDDVyadldwdNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 75 AYKRD-GEVALFRPEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDIERDWIPEGEGQSLYIRPFVFATEGALGVGASH 153
Cdd:PLN02259 114 AYRKEnGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 154 QYKLLIILSPSGAYYGgETLKPTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYIEEV 233
Cdd:PLN02259 194 EYTFIVYASPVGNYFK-EGMAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 234 GSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFESydkgelTEVFGSGTAAVISPVGTLR 313
Cdd:PLN02259 273 SSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTIT 346
|
330 340 350
....*....|....*....|....*....|....*...
gi 600881035 314 YEDREIVINNNETgEITQKLYDVYTGIQNGTLEDKNGW 351
Cdd:PLN02259 347 YQEKRVEYKTGDE-SVCQKLRSVLVGIQTGLIEDNKGW 383
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
8-351 |
1.17e-69 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 223.05 E-value: 1.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 8 ERRETLKQKPNTSQLGFGKYFTDYMLSYDYDADKGWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYK-RDGEVALFR 86
Cdd:PLN02883 43 EREDEEYADVDWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRgEDGRILLFR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 87 PEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDIERDWIPEGEGQSLYIRPFVFATEGALGVGASHQYKLLIILSPSGA 166
Cdd:PLN02883 123 PELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 167 YYGgETLKPTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYIEEVGSMNIFFVENGKV 246
Cdd:PLN02883 203 YFK-EGTAALNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNII 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 247 ITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFESydkgelTEVFGSGTAAVISPVGTLRYEDREIVINNNEt 326
Cdd:PLN02883 282 VTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEA------EEVFCTGTAAGVASVGSITFKNTRTEYKVGD- 354
|
330 340
....*....|....*....|....*
gi 600881035 327 GEITQKLYDVYTGIQNGTLEDKNGW 351
Cdd:PLN02883 355 GIVTQQLRSILLGIQTGSIQDTKDW 379
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
38-351 |
8.95e-68 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 215.40 E-value: 8.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 38 DADKGWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYKRDGEVALFRPEENFKRLNNS--LARLEMPQ-VDEaelleg 114
Cdd:PRK06606 5 RAGYIWFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPAIFRLREHTKRLFNSakILRMEIPYsVDE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 115 lkqLVDIERDWIPEGEGQSLYIRPFVFATEGALGVGAsHQYK--LLIILSPSGAYYGGETLKP---TKIyveDEYVR-AV 188
Cdd:PRK06606 79 ---LMEAQREVVRKNNLKSAYIRPLVFVGDEGLGVRP-HGLPtdVAIAAWPWGAYLGEEALEKgirVKV---SSWTRhAP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 189 RGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDgvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELA 268
Cdd:PRK06606 152 NSIPTRAKASGNYLNSILAKTEARRNGYDEALLLD--VEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 269 KNLGYEVEERRVSIDELFESydkgelTEVFGSGTAAVISPVgtlRYEDReIVINNNETGEITQKLYDVYTGIQNGTLEDK 348
Cdd:PRK06606 230 KDLGIEVIERRITRDELYIA------DEVFFTGTAAEVTPI---REVDG-RQIGNGKRGPITEKLQSAYFDIVRGRTEKY 299
|
...
gi 600881035 349 NGW 351
Cdd:PRK06606 300 AHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
43-355 |
1.68e-63 |
|
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: 204.13 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 43 WHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYKRDGEVALFRPEENFKRLNNS--LARLEMPQVDEaelleglkQLVD 120
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTDKGPAIFRLKEHIQRLYDSakIYRMEIPYSKE--------ELME 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 121 IERDWIPEGEGQSLYIRPFVFATEGALGVGASHQYK--LLIILSPSGAYYGGETL-KPTKIYVEDEYVRAVRGGVGFAKV 197
Cdd:TIGR01122 73 ATRETLRKNNLRSAYIRPLVFRGDGDLGLNPRAGYKpdVIIAAWPWGAYLGEEALeKGIDAKVSSWRRNAPNTIPTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 198 AGNYAASLLAQTNANKLGYDQVLWLDgvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEE 277
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILLD--VEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 278 RRVSIDELFESydkgelTEVFGSGTAAVISPVgtlryedREI---VINNNETGEITQKLYDVYTGIQNGTLEDKNGWRVV 354
Cdd:TIGR01122 231 QPISREELYTA------DEAFFTGTAAEITPI-------REVdgrKIGNGRRGPVTKKLQEAFFDLVTGGTEDYWGWLTY 297
|
.
gi 600881035 355 V 355
Cdd:TIGR01122 298 V 298
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
68-309 |
2.06e-43 |
|
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: 149.82 E-value: 2.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 68 SVFEGLKAYkrDGEValFRPEENFKRLNNSLARLEMPQ-VDEAELLEGLKQLVDIERDWIPegegqslYIRPFVFATEGA 146
Cdd:pfam01063 1 GVFETLRVY--NGKI--FFLDEHLARLRRSAKLLGIPLpFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 147 LGVGASHqYKLLIILSPSgaYYGGETLKPTKIYveDEYVRAVRGGVGFAKVaGNYAASLLAQTNANKLGYDQVLWLDgvE 226
Cdd:pfam01063 70 FGLPTSD-PTLAIFVSAL--PPPPESKKKGVIS--SLVRRNPPSPLPGAKT-LNYLENVLARREAKAQGADDALLLD--E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 227 QKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFESydkgelTEVFGSGTAAVI 306
Cdd:pfam01063 142 DGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEA------DEAFLTNSLRGV 215
|
...
gi 600881035 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 |
1.33e-36 |
|
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: 133.11 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 43 WHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYkrDGEValFRPEENFKRLNNSLA--RLEMPqVDEAELLEGLKQLVD 120
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVY--NGKP--FALDEHLDRLYRSAKelRIDIP-YTREELKELIRELVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 121 IErdwipEGEGQSLYIRPfvfaTEGALGVG----ASHQYKLLIILSPSGAYYGGETLKPTK-IYVEDeyvraVRGGVGFA 195
Cdd:cd01558 76 KN-----EGGEGDVYIQV----TRGVGPRGhdfpKCVKPTVVIITQPLPLPPAELLEKGVRvITVPD-----IRWLRCDI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 196 KvAGNYAASLLAQTNANKLGYDQVLWLDgvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEV 275
Cdd:cd01558 142 K-SLNLLNNVLAKQEAKEAGADEAILLD--ADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPV 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 600881035 276 EERRVSIDELFESydkgelTEVFGSGTAAVISPVGTLryEDReiVINNNETGEITQKLYDVY 337
Cdd:cd01558 219 EERPFSLEELYTA------DEVFLTSTTAEVMPVVEI--DGR--PIGDGKPGPVTKRLREAY 270
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
32-338 |
1.51e-33 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 125.86 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 32 MLSYDYDADKGWHDLKIVPYGPIEISPAAQGVHYGQSVFEGLKAYkrDGEValFRPEENFKRLNNSlARL---EMP-QVD 107
Cdd:PRK07544 1 VIPFDDRDGFIWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAY--GGKI--FKLREHSERLRRS-AELldfEIPySVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 108 EaelLEGLKQLVdIERDWIPEGegqslYIRPFVFATEGALGVGASH-QYKLLIILSPSGAYYGGET-LKPTKIYVEdEYV 185
Cdd:PRK07544 76 E---IDAAKKET-LAANGLTDA-----YVRPVAWRGSEMMGVSAQQnKIHLAIAAWEWPSYFDPEAkMKGIRLDIA-KWR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 186 R-AVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDgvEQKYIEEVGSMNIFFVENGKVITPELNgSILPGITRKSI 264
Cdd:PRK07544 146 RpDPETAPSAAKAAGLYMICTISKHAAEAKGYADALMLD--YRGYVAEATGANIFFVKDGVIHTPTPD-CFLDGITRQTV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 600881035 265 IELAKNLGYEVEERRVSIDELfesydkGELTEVFGSGTAAVISPVGtlryedrEIVINNNETGEITQKLYDVYT 338
Cdd:PRK07544 223 IELAKRRGIEVVERHIMPEEL------AGFSECFLTGTAAEVTPVS-------EIGEYRFTPGAITRDLMDDYE 283
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
62-333 |
1.56e-29 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 114.97 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 62 GVHYGQSVFEGLKAYkrDGEValFRPEENFKRLNNSlAR---LEMPqVDEAELLEGLKQLVdiERDWIPEGegqslYIRP 138
Cdd:PRK08320 25 GFLYGDGVFEGIRAY--NGRV--FRLKEHIDRLYDS-AKaimLEIP-LSKEEMTEIVLETL--RKNNLRDA-----YIRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 139 FVFATEGALGVGASHQYK--LLIILSPSGAYYGgeTLKPTKIYVEDEYVRAVRGGVGFAKVAG-NYAASLLAQTNANKLG 215
Cdd:PRK08320 92 VVSRGVGDLGLDPRKCPKptVVCIAEPIGLYPG--ELYEKGLKVITVSTRRNRPDALSPQVKSlNYLNNILAKIEANLAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 216 YDQVLWLDgvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEErrvsidELFESYDKGELT 295
Cdd:PRK08320 170 VDEAIMLN--DEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVRE------ELFTLHDLYTAD 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 600881035 296 EVFGSGTAAVISPVGTLryEDReiVINNNETGEITQKL 333
Cdd:PRK08320 242 EVFLTGTAAEVIPVVKV--DGR--VIGDGKPGPITKKL 275
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
62-288 |
1.14e-22 |
|
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: 95.07 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 62 GVHYGQSVFEGLKAYkrDGEVALFrpEENFKRLNNSLARLEMPQVDEAELLEGLKQLvdIERDWIPEGegqslYIRpfVF 141
Cdd:cd01559 3 GFAYGDGVFETMRAL--DGRLFLL--DAHLARLERSARRLGIPEPDLPRLRAALESL--LAANDIDEG-----RIR--LI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 142 ATEGALGVGAShqykllIILSPSGAYYGgeTLKPTKIYVEDEYVRAVRGGVGFAK---VAG----NYAASLLAQTNANKL 214
Cdd:cd01559 70 LSRGPGGRGYA------PSVCPGPALYV--SVIPLPPAWRQDGVRLITCPVRLGEqplLAGlkhlNYLENVLAKREARDR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 600881035 215 GYDQVLWLDgVEQKYIEEVGSmNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFES 288
Cdd:cd01559 142 GADEALFLD-TDGRVIEGTAS-NLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAA 213
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
43-337 |
4.16e-22 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 94.64 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 43 WHDLKIvpygPIeISPAAQGVHYGQSVFEGLKAYkrDGeVAlfrP--EENFKRLNNSLARLEM-PQVDEAEL----LEGL 115
Cdd:PRK13356 15 WHEGNV----PI-MGPADHAAWLGSTVFDGARAF--EG-VT---PdlDLHCARVNRSAEALGLkPTVSAEEIealaREGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 116 KQLvdierdwipeGEGQSLYIRPFVFATEGALGVGA----SHQYKLLIILSPSGAYYGGE-TLKPtkiyvedeYVRAVRG 190
Cdd:PRK13356 84 KRF----------DPDTALYIRPMYWAEDGFASGVApdpeSTRFALCLEEAPMPEPTGFSlTLSP--------FRRPTLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 191 -GVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQkyIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAK 269
Cdd:PRK13356 146 mAPTDAKAGCLYPNNARALREARSRGFDNALVLDMLGN--VAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 600881035 270 NLGYEVEERRVSIDElFESYDkgeltEVFGSGTAAVISPVgtLRYEDREIvinnnETGEITQKLYDVY 337
Cdd:PRK13356 224 EDGVTVVETTLTYED-FLEAD-----EVFSTGNYSKVVPV--TRFDDRSL-----QPGPVTRRARELY 278
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
56-337 |
1.67e-18 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 84.62 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 56 ISPAAQGVHYGQSVFEGLKAYKRDgevaLFRPEENFKRLNNSLAR--LEMPQVDEaELLEGLKQLVDierdwipEGEGQS 133
Cdd:PRK12479 20 VSVYDHGFLYGDGVFEGIRSYGGN----VFCLKEHVKRLYESAKSilLTIPLTVD-EMEEAVLQTLQ-------KNEYAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 134 LYIRPFVFATEGALGVGASHQYKLLII-------LSPSGAYYGGETLK--PTKIYVEDEYVRAVRggvgfakvAGNYAAS 204
Cdd:PRK12479 88 AYIRLIVSRGKGDLGLDPRSCVKPSVIiiaeqlkLFPQEFYDNGLSVVsvASRRNTPDALDPRIK--------SMNYLNN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 205 LLAQTNANKLGYDQVLWLDgvEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRvside 284
Cdd:PRK12479 160 VLVKIEAAQAGVLEALMLN--QQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERP----- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 600881035 285 lFESYDKGELTEVFGSGTAAVISPVgtLRYEDREivINNNETGEITQKLYDVY 337
Cdd:PRK12479 233 -FTRHDVYVADEVFLTGTAAELIPV--VKVDSRE--IGDGKPGSVTKQLTEEF 280
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
206-337 |
2.86e-14 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 72.27 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 206 LAQTNANKLGYDQVlWLdgVEQKYIEEVGSMNIFFV-ENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDE 284
Cdd:PRK06680 158 LAKQAAKEAGAQEA-WM--VDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQE 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 600881035 285 LFESydkgelTEVFGSGTAAVISPVGTLryeDREiVINNNETGEITQKLYDVY 337
Cdd:PRK06680 235 AYAA------REAFITAASSFVFPVVQI---DGK-QIGNGKPGPIAKRLREAY 277
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
56-352 |
1.84e-13 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 70.00 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 56 ISPAAQGVHYGQSVFEGLKAYkrDGEValFRPEENFKRLNNSLARLEMP-QVDEAELLEGLKQLvdIERDWIPEGegqsl 134
Cdd:PRK07650 16 ISPFDHGYLYGLGVFETFRIY--NGHP--FLLDDHYDRLNDALDTLQIEwTMTKDEVLLILKNL--LEKNGLENA----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 135 YIRPFVFATEGALGVGAShQYK---LLIILSPsgayyggetLKPTKIYVEDEYV--RAVR----GGVGFAkvAGNYAASL 205
Cdd:PRK07650 85 YVRFNVSAGIGEIGLQTE-MYEeptVIVYMKP---------LAPPGLPAEKEGVvlKQRRntpeGAFRLK--SHHYLNNI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 206 LAQtnaNKLGYDQVLwlDGV---EQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSI 282
Cdd:PRK07650 153 LGK---REIGNDPNK--EGIfltEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTK 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 283 DELFESydkgelTEVFGSGTAAVISPVgtLRYEDREIvinNNETGEITQKLYDVYtgiqngTLEDKNGWR 352
Cdd:PRK07650 228 EELLSA------DEVFVTNSIQEIVPL--TRIEERDF---PGKVGMVTKRLQNLY------EMQREKLWS 280
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
62-285 |
1.43e-12 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 66.79 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 62 GVHYGQSVFEGLKAykRDGEVALFrpEENFKRLNNSLARLEMPQVDEAELLEGLKQL----------VDIERdwipeGEG 131
Cdd:PRK06092 18 STQYGDGCFTTARV--RDGQVSLL--SRHLQRLQDACERLAIPLDDWAQLEQEMKQLaaelengvlkVIISR-----GSG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 132 QSLYirpfvfATEGAlgvgasHQYKLLIILSPSGAYYG-----GETLKPTkiyvedeyvrAVRGGVGfAKVAG----NYA 202
Cdd:PRK06092 89 GRGY------SPAGC------AAPTRILSVSPYPAHYSrwreqGITLALC----------PTRLGRN-PLLAGikhlNRL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 203 ASLLAQTNANKLGYDQVLWLDgVEQKYIEEVGSmNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSI 282
Cdd:PRK06092 146 EQVLIRAELEQTEADEALVLD-SEGWVIECCAA-NLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASL 223
|
...
gi 600881035 283 DEL 285
Cdd:PRK06092 224 EEL 226
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
66-288 |
1.11e-10 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 61.51 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 66 GQSVFEGLKAykRDGEVALFrpEENFKRLNNSLARLEMPQVDEAELLEGLKQLVDierDWIPEGEGQSL---YIR----- 137
Cdd:PRK07849 38 GDGVFETLLV--RDGRPCNL--EAHLERLARSAALLDLPEPDLDRWRRAVELAIE---EWRAPEDEAALrlvYSRgresg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 138 --PFVFATEGALGVGASHQYKLLI--ILSPSGayyggetlkptkiYVEDEYVRA--VRGGvgfAKVAgNYAASLLAQTNA 211
Cdd:PRK07849 111 gaPTAWVTVSPVPERVARARREGVsvITLDRG-------------YPSDAAERApwLLAG---AKTL-SYAVNMAALRYA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 600881035 212 NKLGYDQVLWL--DGveqkYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEERRVSIDELFES 288
Cdd:PRK07849 174 ARRGADDVIFTstDG----YVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAA 248
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
61-333 |
3.65e-10 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 60.03 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 61 QGVHYGQSVFEGLKAYKrdGEVALFRPeeNFKRLNNSLARLEMP-QVDEAELLEGLKQLvdIERDWIPEgEGqSLYIrpf 139
Cdd:PRK12400 28 RGLQFGDGVYEVIRLYK--GNFHLLDP--HITRLYRSMEEIELTlPFSKAELITLLYKL--IENNNFHE-DG-TIYL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 140 vfatEGALGVGA-SHQYKLLIilSPSGAYYGGETLKPTkIYVE-------DEYVRAVRGGVGfakvAGNYAASLLAQTNA 211
Cdd:PRK12400 97 ----QVSRGVQArTHTFSYDV--PPTIYAYITKKERPA-LWIEygvraisEPDTRWLRCDIK----SLNLLPNILAATKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 212 NKLGYDQVLWldgVEQKYIEEVGSMNIFFVENGKVITPELNGSILPGITRKSIIELAKNLGYEVEErrvsidELFESYDK 291
Cdd:PRK12400 166 ERKGCKEALF---VRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQE------ELFSVRDV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 600881035 292 GELTEVFGSGTAAVISPVGTLryedREIVINNNETGEITQKL 333
Cdd:PRK12400 237 YQADECFFTGTTIEILPMTHL----DGTAIQDGQVGPITKML 274
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
161-335 |
5.80e-09 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 56.95 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 161 LSPSG----AYYGgETLKPTKIYVEDEYVRAVRGGV-----GFAKVAG-NYAASLLAQTNANKLGYDQVLWLDgvEQKYI 230
Cdd:PLN02845 140 LSPSGcsepAFYA-VVIEDTYAQDRPEGVKVVTSSVpikppQFATVKSvNYLPNALSQMEAEERGAFAGIWLD--EEGFV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600881035 231 EEVGSMNIFFVENGKV-ITPElNGSILPGITRKSIIELAKNLGYE-----VEERRVSIDELFESydkgelTEVFGSGTAA 304
Cdd:PLN02845 217 AEGPNMNVAFLTNDGElVLPP-FDKILSGCTARRVLELAPRLVSPgdlrgVKQRKISVEEAKAA------DEMMLIGSGV 289
|
170 180 190
....*....|....*....|....*....|.
gi 600881035 305 VISPVgtLRYEDReiVINNNETGEITQKLYD 335
Cdd:PLN02845 290 PVLPI--VSWDGQ--PIGDGKVGPITLALHD 316
|
|
| |
