|
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: 609.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 1 MSEKVKFEKRESLKEKPDTANLGFGQYFTDYMLSVDYDADQgWHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYKH-N 79
Cdd:PRK13357 1 FTVTLKPNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHkD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 80 GEVVLFRPDQNFKRINNSLARLEMPEVDEEALLEGLKQLIDVERDWV-PEGEGQSLYIRPFVFATEGILGVRSSHQYKLL 158
Cdd:PRK13357 80 GSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 159 IILSPSGAYYGGDtLKSTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNI 238
Cdd:PRK13357 160 VIASPVGAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 239 FFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAYDKGELTEVFGSGTAAVISPVGTLRYEDRE 318
Cdd:PRK13357 239 FFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 394256726 319 IVINNNEPGKITQKLYDTYTGIQSGKLEDKYGWRVEVP 356
Cdd:PRK13357 319 FVIGDGEVGPVTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
43-355 |
4.75e-150 |
|
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: 425.33 E-value: 4.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 43 WHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYKH-NGEVVLFRPDQNFKRINNSLARLEMPEVDEEALLEGLKQLIDV 121
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCaDGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 122 ERDWVP-EGEGQSLYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGGDtLKSTKIYVEDEYVRAVRGGVGFAKVAGN 200
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 201 YAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVEN-GKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERR 279
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGdGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394256726 280 VSIEELFNAYDKGEltEVFGSGTAAVISPVGTLRYEDREIVINNNEPGKITQKLYDTYTGIQSGKLEDKYGWRVEV 355
Cdd:TIGR01123 240 IDIDELKAFVEAGE--IVFACGTAAVITPVGEIQHGGKEVVFASGQPGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
55-343 |
2.98e-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: 391.56 E-value: 2.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 55 EISPAAQGLHYGQAVFEGLKAYKH-NGEVVLFRPDQNFKRINNSLARLEMPEVDEEALLEGLKQLIDVERDWVPEGEGQS 133
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTpDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 134 LYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGGdTLKSTKIYVEdEYVRAVRGGVGFAKVAGNYAASLLAQTNANK 213
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKG-GEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 214 LGYDQVLWLDGvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFnaydkgE 293
Cdd:cd01557 159 KGYDQALWLDG-AHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELY------E 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 394256726 294 LTEVFGSGTAAVISPVGtlRYEDREIVINNNEPGKITQKLYDTYTGIQSG 343
Cdd:cd01557 232 ADEVFATGTAAVVTPVG--EIDYRGKEPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
43-347 |
1.35e-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: 324.06 E-value: 1.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 43 WHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYkhNGEvvLFRPDQNFKRINNSLARLEMP-EVDEEALLEGLKQLIDV 121
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAY--DGR--LFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 122 ERDwvpegegQSLYIRPFVFATEGILGVRSSH-QYKLLIILSPSGAYYGGDTLKSTKIYVEdEYVRAVRGGVGFAKvAGN 200
Cdd:COG0115 80 NGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITS-PYRRAAPGGLGGIK-TGN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 201 YAASLLAQTNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRV 280
Cdd:COG0115 151 YLNNVLAKQEAKEAGADEALLLD--TDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394256726 281 SIEELFNAydkgelTEVFGSGTAAVISPVGTLryedREIVINNNEPGKITQKLYDTYTGIQSGKLED 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 |
3.05e-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: 149.04 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 68 AVFEGLKAYkhNGEVvlFRPDQNFKRINNSLARLEMP-EVDEEALLEGLKQLIDVERDWVPegegqslYIRPFVFATEGI 146
Cdd:pfam01063 1 GVFETLRVY--NGKI--FFLDEHLARLRRSAKLLGIPlPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 147 LGVRSSHqYKLLIILSPSgaYYGGDTLKSTKIYveDEYVRAVRGGVGFAKVaGNYAASLLAQTNANKLGYDQVLWLDgvE 226
Cdd:pfam01063 70 FGLPTSD-PTLAIFVSAL--PPPPESKKKGVIS--SLVRRNPPSPLPGAKT-LNYLENVLARREAKAQGADDALLLD--E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 227 QKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAydkgelTEVFGSGTAAVI 306
Cdd:pfam01063 142 DGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEA------DEAFLTNSLRGV 215
|
...
gi 394256726 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: 609.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 1 MSEKVKFEKRESLKEKPDTANLGFGQYFTDYMLSVDYDADQgWHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYKH-N 79
Cdd:PRK13357 1 FTVTLKPNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHkD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 80 GEVVLFRPDQNFKRINNSLARLEMPEVDEEALLEGLKQLIDVERDWV-PEGEGQSLYIRPFVFATEGILGVRSSHQYKLL 158
Cdd:PRK13357 80 GSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVpPYGEGASLYLRPFMIATEPFLGVKPAEEYIFC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 159 IILSPSGAYYGGDtLKSTKIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNI 238
Cdd:PRK13357 160 VIASPVGAYFKGG-VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 239 FFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAYDKGELTEVFGSGTAAVISPVGTLRYEDRE 318
Cdd:PRK13357 239 FFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADAASGEFTEAFACGTAAVITPIGGIKYKDKE 318
|
330 340 350
....*....|....*....|....*....|....*...
gi 394256726 319 IVINNNEPGKITQKLYDTYTGIQSGKLEDKYGWRVEVP 356
Cdd:PRK13357 319 FVIGDGEVGPVTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
43-355 |
4.75e-150 |
|
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: 425.33 E-value: 4.75e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 43 WHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYKH-NGEVVLFRPDQNFKRINNSLARLEMPEVDEEALLEGLKQLIDV 121
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCaDGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 122 ERDWVP-EGEGQSLYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGGDtLKSTKIYVEDEYVRAVRGGVGFAKVAGN 200
Cdd:TIGR01123 81 NKDWVPpYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGG-LAPVSIFVTTEYDRAAPGGTGAVKVGGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 201 YAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVEN-GKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERR 279
Cdd:TIGR01123 160 YAASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGdGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394256726 280 VSIEELFNAYDKGEltEVFGSGTAAVISPVGTLRYEDREIVINNNEPGKITQKLYDTYTGIQSGKLEDKYGWRVEV 355
Cdd:TIGR01123 240 IDIDELKAFVEAGE--IVFACGTAAVITPVGEIQHGGKEVVFASGQPGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
55-343 |
2.98e-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: 391.56 E-value: 2.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 55 EISPAAQGLHYGQAVFEGLKAYKH-NGEVVLFRPDQNFKRINNSLARLEMPEVDEEALLEGLKQLIDVERDWVPEGEGQS 133
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTpDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 134 LYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGGdTLKSTKIYVEdEYVRAVRGGVGFAKVAGNYAASLLAQTNANK 213
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKG-GEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 214 LGYDQVLWLDGvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFnaydkgE 293
Cdd:cd01557 159 KGYDQALWLDG-AHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELY------E 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 394256726 294 LTEVFGSGTAAVISPVGtlRYEDREIVINNNEPGKITQKLYDTYTGIQSG 343
Cdd:cd01557 232 ADEVFATGTAAVVTPVG--EIDYRGKEPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
43-347 |
1.35e-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: 324.06 E-value: 1.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 43 WHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYkhNGEvvLFRPDQNFKRINNSLARLEMP-EVDEEALLEGLKQLIDV 121
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAY--DGR--LFRLDEHLARLNRSAKRLGIPiPYTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 122 ERDwvpegegQSLYIRPFVFATEGILGVRSSH-QYKLLIILSPSGAYYGGDTLKSTKIYVEdEYVRAVRGGVGFAKvAGN 200
Cdd:COG0115 80 NGL-------EDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYEKGVRVITS-PYRRAAPGGLGGIK-TGN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 201 YAASLLAQTNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRV 280
Cdd:COG0115 151 YLNNVLAKQEAKEAGADEALLLD--TDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394256726 281 SIEELFNAydkgelTEVFGSGTAAVISPVGTLryedREIVINNNEPGKITQKLYDTYTGIQSGKLED 347
Cdd:COG0115 229 SLEELYTA------DEVFLTGTAAEVTPVTEI----DGRPIGDGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
18-355 |
1.79e-97 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 294.83 E-value: 1.79e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 18 DTANLGFGQYFTDYMLSVDYDADQGWHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAY-KHNGEVVLFRPDQNFKRINN 96
Cdd:PLN02782 71 DWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYrKEDGNILLFRPEENAIRMRN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 97 SLARLEMPEVDEEALLEGLKQLIDVERDWVPEGEGQSLYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGgDTLKST 176
Cdd:PLN02782 151 GAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFK-EGVAPI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 177 KIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSIL 256
Cdd:PLN02782 230 NLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIVKDNVISTPAIKGTIL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 257 PGITRKSIIQLAEDLGYEVEERRVSIEELFNAydkgelTEVFGSGTAAVISPVGTLRYEDREIVINNNEPGKITQKLYDT 336
Cdd:PLN02782 310 PGITRKSIIDVARSQGFQVEERNVTVDELLEA------DEVFCTGTAVVVSPVGSITYKGKRVSYGEGGFGTVSQQLYTV 383
|
330
....*....|....*....
gi 394256726 337 YTGIQSGKLEDKYGWRVEV 355
Cdd:PLN02782 384 LTSLQMGLIEDNMNWTVEL 402
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
62-337 |
1.81e-93 |
|
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: 279.49 E-value: 1.81e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 62 GLHYGQAVFEGLKAYKhngeVVLFRPDQNFKRINNSLARLEMP-EVDEEALLEGLKQLIDVerdwvpeGEGQSLYIRPFV 140
Cdd:cd00449 3 GLHYGDGVFEGLRAGK----GRLFRLDEHLDRLNRSAKRLGLPiPYDREELREALKELVAA-------NNGASLYIRPLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 141 FATEGILGV--RSSHQYKLLIILSPSGAYYGGdTLKSTKIYVEDEYVRAVRGGVGFAKvAGNYAASLLAQTNANKLGYDQ 218
Cdd:cd00449 72 TRGVGGLGVapPPSPEPTFVVFASPVGAYAKG-GEKGVRLITSPDRRRAAPGGTGDAK-TGGNLNSVLAKQEAAEAGADE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 219 VLWLDGveQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAydkgelTEVF 298
Cdd:cd00449 150 ALLLDD--NGYVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAA------DEVF 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 394256726 299 GSGTAAVISPVGTLRYEDreivINNNEPGKITQKLYDTY 337
Cdd:cd00449 222 LTGTAAEVTPVTEIDGRG----IGDGKPGPVTRKLRELL 256
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
22-355 |
8.72e-86 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 263.33 E-value: 8.72e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 22 LGFGQYFTDYMLSVDYDADQGWHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYK-HNGEVVLFRPDQNFKRINNSLAR 100
Cdd:PLN03117 25 LGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRtEDGRITLFRPDQNALRMQTGADR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 101 LEMPEVDEEALLEGLKQLIDVERDWVPEGEGQSLYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGGDTLKSTKiyV 180
Cdd:PLN03117 105 LCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASSGLNLK--V 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 181 EDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGIT 260
Cdd:PLN03117 183 DHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNIFILKGNIVSTPPTSGTILPGVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 261 RKSIIQLAEDLGYEVEERRVSIEELFNAydkgelTEVFGSGTAAVISPVGTLRYEDREIVINNNEPGkITQKLYDTYTGI 340
Cdd:PLN03117 263 RKSISELARDIGYQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEA-LSTKLHLILTNI 335
|
330
....*....|....*
gi 394256726 341 QSGKLEDKYGWRVEV 355
Cdd:PLN03117 336 QMGVVEDKKGWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
18-351 |
1.36e-80 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 251.18 E-value: 1.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 18 DTANLGFGQYFTDYMLSVDYDADQGWHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAY-KHNGEVVLFRPDQNFKRINN 96
Cdd:PLN02259 57 DWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYrKENGKLLLFRPDHNAIRMKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 97 SLARLEMPEVDEEALLEGLKQLIDVERDWVPEGEGQSLYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGgDTLKST 176
Cdd:PLN02259 137 GAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFK-EGMAAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 177 KIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSIL 256
Cdd:PLN02259 216 NLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPATNGTIL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 257 PGITRKSIIQLAEDLGYEVEERRVSIEELFNAydkgelTEVFGSGTAAVISPVGTLRYEDREIVINNNEPgKITQKLYDT 336
Cdd:PLN02259 296 EGITRKSVMEIASDQGYQVVEKAVHVDEVMDA------DEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE-SVCQKLRSV 368
|
330
....*....|....*
gi 394256726 337 YTGIQSGKLEDKYGW 351
Cdd:PLN02259 369 LVGIQTGLIEDNKGW 383
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
18-355 |
1.45e-69 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 222.67 E-value: 1.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 18 DTANLGFGQYFTDYMLSVDYDADQGWHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYK-HNGEVVLFRPDQNFKRINN 96
Cdd:PLN02883 53 DWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRgEDGRILLFRPELNAMRMKI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 97 SLARLEMPEVDEEALLEGLKQLIDVERDWVPEGEGQSLYIRPFVFATEGILGVRSSHQYKLLIILSPSGAYYGGDTlKST 176
Cdd:PLN02883 133 GAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGT-AAL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 177 KIYVEDEYVRAVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDGVEQKYVEEVGSMNIFFVENGKVVTPALNGSIL 256
Cdd:PLN02883 212 NLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNIIVTPATSGTIL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 257 PGITRKSIIQLAEDLGYEVEERRVSIEELfnaydkGELTEVFGSGTAAVISPVGTLRYEDREIVINNNEpGKITQKLYDT 336
Cdd:PLN02883 292 GGITRKSIIEIALDLGYKVEERRVPVEEL------KEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGD-GIVTQQLRSI 364
|
330
....*....|....*....
gi 394256726 337 YTGIQSGKLEDKYGWRVEV 355
Cdd:PLN02883 365 LLGIQTGSIQDTKDWVLQI 383
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
43-351 |
6.14e-68 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 215.78 E-value: 6.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 43 WHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYK-HNGEVVlFRPDQNFKRINNS--LARLEMPEVDEEalleglkqLI 119
Cdd:PRK06606 10 WFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDtPKGPAI-FRLREHTKRLFNSakILRMEIPYSVDE--------LM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 120 DVERDWVPEGEGQSLYIRPFVFATEGILGVRSsHQYK--LLIILSPSGAYYGGDTLK---STKIyveDEYVR-AVRGGVG 193
Cdd:PRK06606 81 EAQREVVRKNNLKSAYIRPLVFVGDEGLGVRP-HGLPtdVAIAAWPWGAYLGEEALEkgiRVKV---SSWTRhAPNSIPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 194 FAKVAGNYAASLLAQTNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGY 273
Cdd:PRK06606 157 RAKASGNYLNSILAKTEARRNGYDEALLLD--VEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 394256726 274 EVEERRVSIEELFNAydkgelTEVFGSGTAAVISPVgtlRYEDReIVINNNEPGKITQKLYDTYTGIQSGKLEDKYGW 351
Cdd:PRK06606 235 EVIERRITRDELYIA------DEVFFTGTAAEVTPI---REVDG-RQIGNGKRGPITEKLQSAYFDIVRGRTEKYAHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
43-355 |
1.28e-62 |
|
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: 201.82 E-value: 1.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 43 WHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYKHNGEVVLFRPDQNFKRINNS--LARLEMPEVDEEalleglkqLID 120
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTDKGPAIFRLKEHIQRLYDSakIYRMEIPYSKEE--------LME 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 121 VERDWVPEGEGQSLYIRPFVFATEGILGVRSSHQYK--LLIILSPSGAYYGGDTL-KSTKIYVEDEYVRAVRGGVGFAKV 197
Cdd:TIGR01122 73 ATRETLRKNNLRSAYIRPLVFRGDGDLGLNPRAGYKpdVIIAAWPWGAYLGEEALeKGIDAKVSSWRRNAPNTIPTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 198 AGNYAASLLAQTNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEE 277
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILLD--VEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 278 RRVSIEELFNAydkgelTEVFGSGTAAVISPVgtlryedREI---VINNNEPGKITQKLYDTYTGIQSGKLEDKYGWRVE 354
Cdd:TIGR01122 231 QPISREELYTA------DEAFFTGTAAEITPI-------REVdgrKIGNGRRGPVTKKLQEAFFDLVTGGTEDYWGWLTY 297
|
.
gi 394256726 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 |
3.05e-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: 149.04 E-value: 3.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 68 AVFEGLKAYkhNGEVvlFRPDQNFKRINNSLARLEMP-EVDEEALLEGLKQLIDVERDWVPegegqslYIRPFVFATEGI 146
Cdd:pfam01063 1 GVFETLRVY--NGKI--FFLDEHLARLRRSAKLLGIPlPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 147 LGVRSSHqYKLLIILSPSgaYYGGDTLKSTKIYveDEYVRAVRGGVGFAKVaGNYAASLLAQTNANKLGYDQVLWLDgvE 226
Cdd:pfam01063 70 FGLPTSD-PTLAIFVSAL--PPPPESKKKGVIS--SLVRRNPPSPLPGAKT-LNYLENVLARREAKAQGADDALLLD--E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 227 QKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAydkgelTEVFGSGTAAVI 306
Cdd:pfam01063 142 DGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEA------DEAFLTNSLRGV 215
|
...
gi 394256726 307 SPV 309
Cdd:pfam01063 216 TPV 218
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
47-337 |
4.40e-39 |
|
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: 139.66 E-value: 4.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 47 KIVPYAPFEISPAAQGLHYGQAVFEGLKAYKHNgevvLFRPDQNFKRINNSLA--RLEMPeVDEEALLEGLKQLIdvERD 124
Cdd:cd01558 5 EYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGK----PFALDEHLDRLYRSAKelRIDIP-YTREELKELIRELV--AKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 125 WVPEGEGqslYIRPfvfaTEGIlGVRSSHQYK-----LLIILSPSGAYYGGDTLKSTK-IYVEDeyvraVRGGVGFAKvA 198
Cdd:cd01558 78 EGGEGDV---YIQV----TRGV-GPRGHDFPKcvkptVVIITQPLPLPPAELLEKGVRvITVPD-----IRWLRCDIK-S 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 199 GNYAASLLAQTNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEER 278
Cdd:cd01558 144 LNLLNNVLAKQEAKEAGADEAILLD--ADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEER 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 394256726 279 RVSIEELFNAydkgelTEVFGSGTAAVISPVGTLryEDReiVINNNEPGKITQKLYDTY 337
Cdd:cd01558 222 PFSLEELYTA------DEVFLTSTTAEVMPVVEI--DGR--PIGDGKPGPVTKRLREAY 270
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
37-338 |
4.88e-34 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 127.01 E-value: 4.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 37 YDADQG--WHDMKIVPYAPFEISPAAQGLHYGQAVFEGLKAYkhNGEVvlFRPDQNFKRINNSlARL---EMP-EVDEea 110
Cdd:PRK07544 4 FDDRDGfiWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAY--GGKI--FKLREHSERLRRS-AELldfEIPySVAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 111 lleglkqlIDVERDWVPEGEG-QSLYIRPFVFATEGILGVRSSH-QYKLLIILSPSGAYYGGDT-LKSTKIYVEdEYVR- 186
Cdd:PRK07544 77 --------IDAAKKETLAANGlTDAYVRPVAWRGSEMMGVSAQQnKIHLAIAAWEWPSYFDPEAkMKGIRLDIA-KWRRp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 187 AVRGGVGFAKVAGNYAASLLAQTNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNgSILPGITRKSIIQ 266
Cdd:PRK07544 148 DPETAPSAAKAAGLYMICTISKHAAEAKGYADALMLD--YRGYVAEATGANIFFVKDGVIHTPTPD-CFLDGITRQTVIE 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394256726 267 LAEDLGYEVEERRVSIEELfnaydkGELTEVFGSGTAAVISPVGtlryedrEIVINNNEPGKITQKLYDTYT 338
Cdd:PRK07544 225 LAKRRGIEVVERHIMPEEL------AGFSECFLTGTAAEVTPVS-------EIGEYRFTPGAITRDLMDDYE 283
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
62-333 |
4.91e-33 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 124.21 E-value: 4.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 62 GLHYGQAVFEGLKAYkhNGEVvlFRPDQNFKRINNSlAR---LEMP---EVDEEALLEGLKQlidverdwvpeGEGQSLY 135
Cdd:PRK08320 25 GFLYGDGVFEGIRAY--NGRV--FRLKEHIDRLYDS-AKaimLEIPlskEEMTEIVLETLRK-----------NNLRDAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 136 IRPFVFATEGILGV--RSSHQYKLLIILSPSGAYYGgdTLKSTKIYVEDEYVRAVRGGVGFAKVAG-NYAASLLAQTNAN 212
Cdd:PRK08320 89 IRLVVSRGVGDLGLdpRKCPKPTVVCIAEPIGLYPG--ELYEKGLKVITVSTRRNRPDALSPQVKSlNYLNNILAKIEAN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 213 KLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAydkg 292
Cdd:PRK08320 167 LAGVDEAIMLN--DEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTA---- 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 394256726 293 elTEVFGSGTAAVISPVGTLryEDReiVINNNEPGKITQKL 333
Cdd:PRK08320 241 --DEVFLTGTAAEVIPVVKV--DGR--VIGDGKPGPITKKL 275
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
62-337 |
2.96e-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: 96.99 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 62 GLHYGQAVFEGLKAYKhnGEVVLFrpDQNFKRINNSLARLEMPEVDEEALLEGLKQLIdvERDWVPEG----------EG 131
Cdd:cd01559 3 GFAYGDGVFETMRALD--GRLFLL--DAHLARLERSARRLGIPEPDLPRLRAALESLL--AANDIDEGrirlilsrgpGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 132 QSLYIRPFVFATEGIlgvrSSHQYklliilsPSGAYYGGDTLKSTKIYVEDeyvravRGGVGFAKVAgNYAASLLAQTNA 211
Cdd:cd01559 77 RGYAPSVCPGPALYV----SVIPL-------PPAWRQDGVRLITCPVRLGE------QPLLAGLKHL-NYLENVLAKREA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 212 NKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAydk 291
Cdd:cd01559 139 RDRGADEALFLD--TDGRVIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAA--- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 394256726 292 gelTEVFGSGTAAVISPVgtLRYEDREIvinnnEPGKITQKLYDTY 337
Cdd:cd01559 214 ---DEAFLTNSLLGVAPV--TAIDDHDG-----PPGPLTRALRELL 249
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
56-337 |
3.06e-23 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 97.72 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 56 ISPAAQGLHYGQAVFEGLKAYkhngEVVLFRPDQNFKRINNSLARLEM-PEVDEEAL----LEGLKQLidverdwvpeGE 130
Cdd:PRK13356 23 MGPADHAAWLGSTVFDGARAF----EGVTPDLDLHCARVNRSAEALGLkPTVSAEEIealaREGLKRF----------DP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 131 GQSLYIRPFVFATEGILGVR----SSHQYKLLIILSPSGAYyGGDTLKSTkiyvedEYVRAVRG-GVGFAKVAGNYAASL 205
Cdd:PRK13356 89 DTALYIRPMYWAEDGFASGVapdpESTRFALCLEEAPMPEP-TGFSLTLS------PFRRPTLEmAPTDAKAGCLYPNNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 206 LAQTNANKLGYDQVLWLDGVEQkyVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEEl 285
Cdd:PRK13356 162 RALREARSRGFDNALVLDMLGN--VAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTVVETTLTYED- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 394256726 286 FNAYDkgeltEVFGSGTAAVISPVgtLRYEDREIvinnnEPGKITQKLYDTY 337
Cdd:PRK13356 239 FLEAD-----EVFSTGNYSKVVPV--TRFDDRSL-----QPGPVTRRARELY 278
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
56-353 |
6.47e-22 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 94.25 E-value: 6.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 56 ISPAAQGLHYGQAVFEGLKAYKHNgevvLFRPDQNFKRINNSLAR--LEMP---EVDEEALLEGLKQlidverdwvpeGE 130
Cdd:PRK12479 20 VSVYDHGFLYGDGVFEGIRSYGGN----VFCLKEHVKRLYESAKSilLTIPltvDEMEEAVLQTLQK-----------NE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 131 GQSLYIRPFVFATEGILGV--RSSHQYKLLII-----LSPSGAYYGGDTLKS--TKIYVEDEYVRAVRggvgfakvAGNY 201
Cdd:PRK12479 85 YADAYIRLIVSRGKGDLGLdpRSCVKPSVIIIaeqlkLFPQEFYDNGLSVVSvaSRRNTPDALDPRIK--------SMNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 202 AASLLAQTNANKLGYDQVLWLDgvEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVS 281
Cdd:PRK12479 157 LNNVLVKIEAAQAGVLEALMLN--QQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFT 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 394256726 282 IEELFNAydkgelTEVFGSGTAAVISPVgtLRYEDREivINNNEPGKITQKLYDTYTgiqsgKLEDKYGWRV 353
Cdd:PRK12479 235 RHDVYVA------DEVFLTGTAAELIPV--VKVDSRE--IGDGKPGSVTKQLTEEFK-----KLTRERGVRV 291
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
206-337 |
3.05e-17 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 80.74 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 206 LAQTNANKLGYDQVlWLdgVEQKYVEEVGSMNIFFV-ENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEE 284
Cdd:PRK06680 158 LAKQAAKEAGAQEA-WM--VDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQE 234
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 394256726 285 LFNAydkgelTEVFGSGTAAVISPVGTLryeDREiVINNNEPGKITQKLYDTY 337
Cdd:PRK06680 235 AYAA------REAFITAASSFVFPVVQI---DGK-QIGNGKPGPIAKRLREAY 277
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
226-338 |
5.05e-12 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 65.76 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 226 EQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNAydkgelTEVFGSGTAAV 305
Cdd:PRK07650 171 EEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSA------DEVFVTNSIQE 244
|
90 100 110
....*....|....*....|....*....|...
gi 394256726 306 ISPVgtLRYEDREIvinNNEPGKITQKLYDTYT 338
Cdd:PRK07650 245 IVPL--TRIEERDF---PGKVGMVTKRLQNLYE 272
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
161-335 |
3.28e-11 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 63.50 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 161 LSPSG----AYYGgDTLKSTKIYVEDEYVRAVRGGV-----GFAKVAG-NYAASLLAQTNANKLGYDQVLWLDgvEQKYV 230
Cdd:PLN02845 140 LSPSGcsepAFYA-VVIEDTYAQDRPEGVKVVTSSVpikppQFATVKSvNYLPNALSQMEAEERGAFAGIWLD--EEGFV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 231 EEVGSMNIFFVENGKV-VTPAlNGSILPGITRKSIIQLAEDLGYE-----VEERRVSIEELFNAydkgelTEVFGSGTAA 304
Cdd:PLN02845 217 AEGPNMNVAFLTNDGElVLPP-FDKILSGCTARRVLELAPRLVSPgdlrgVKQRKISVEEAKAA------DEMMLIGSGV 289
|
170 180 190
....*....|....*....|....*....|.
gi 394256726 305 VISPVgtLRYEDReiVINNNEPGKITQKLYD 335
Cdd:PLN02845 290 PVLPI--VSWDGQ--PIGDGKVGPITLALHD 316
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
66-288 |
7.58e-11 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 62.28 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 66 GQAVFEGLKAYkhNGEVVLFRPdqNFKRINNSLARLEMPEVDEEALLEGLKQLIDVERDWVPEGEGQSLYIR-------P 138
Cdd:PRK07849 38 GDGVFETLLVR--DGRPCNLEA--HLERLARSAALLDLPEPDLDRWRRAVELAIEEWRAPEDEAALRLVYSRgresggaP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 139 FVFATEGILGVRSSHQYKLliilspsgayyGGDTLKSTKIYVEDEYVRA--VRGGvgfAKVAgNYAASLLAQTNANKLGY 216
Cdd:PRK07849 114 TAWVTVSPVPERVARARRE-----------GVSVITLDRGYPSDAAERApwLLAG---AKTL-SYAVNMAALRYAARRGA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 394256726 217 DQVLWL--DGveqkYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFNA 288
Cdd:PRK07849 179 DDVIFTstDG----YVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAA 248
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
62-298 |
2.24e-10 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 60.63 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 62 GLHYGQAVFEGLKAykHNGEVVLFrpDQNFKRINNSLARLEMPEVDEEALLEGLKQLIDVERDWV-----PEGEGQSLYi 136
Cdd:PRK06092 18 STQYGDGCFTTARV--RDGQVSLL--SRHLQRLQDACERLAIPLDDWAQLEQEMKQLAAELENGVlkviiSRGSGGRGY- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 137 rpfvfATEGIlgvrssHQYKLLIILSPSGAYYG-----GDTLkstkiyvedeYVRAVRGGVGfAKVAG----NYAASLLA 207
Cdd:PRK06092 93 -----SPAGC------AAPTRILSVSPYPAHYSrwreqGITL----------ALCPTRLGRN-PLLAGikhlNRLEQVLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 208 QTNANKLGYDQVLWLDgVEQKYVEEVGSmNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEERRVSIEELFN 287
Cdd:PRK06092 151 RAELEQTEADEALVLD-SEGWVIECCAA-NLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQ 228
|
250
....*....|.
gi 394256726 288 AyDkgeltEVF 298
Cdd:PRK06092 229 A-D-----EVF 233
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
200-338 |
1.68e-08 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 55.02 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394256726 200 NYAASLLAQTNANKLGYDQVLWldgVEQKYVEEVGSMNIFFVENGKVVTPALNGSILPGITRKSIIQLAEDLGYEVEerr 279
Cdd:PRK12400 154 NLLPNILAATKAERKGCKEALF---VRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQ--- 227
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 394256726 280 vsiEELFNAYDKGELTEVFGSGTAAVISPVGTLryedREIVINNNEPGKITQKLYDTYT 338
Cdd:PRK12400 228 ---EELFSVRDVYQADECFFTGTTIEILPMTHL----DGTAIQDGQVGPITKMLQRSFS 279
|
|
| |
