|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
2-284 |
0e+00 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 552.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 2 LIYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNE 81
Cdd:PRK07650 1 LIYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 82 LEHAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPAPGDIVEKEGVVLKQVRNTPEGAFRLKSHHYLNNILGKREIGN 161
Cdd:PRK07650 81 LENAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQRRNTPEGAFRLKSHHYLNNILGKREIGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 162 VVDKEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTN 241
Cdd:PRK07650 161 DPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFVTN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1586385891 242 SIQEIVPLYHIEGRDFPGKVGMITKRFMHLYEMQREKLWSRNE 284
Cdd:PRK07650 241 SIQEIVPLTRIEERDFPGKVGMVTKRLQNLYEMQREKLWSRNE 283
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
1-273 |
8.47e-102 |
|
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: 299.03 E-value: 8.47e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 1 MLIYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKN 80
Cdd:COG0115 1 RLIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 81 ELEHAYVRFNVSAGVDEIGLQTEMYEePSVIVFIKPLPAPGDIVEKEGV---VLKQVRNTPEGAFRLKSHHYLNNILGKR 157
Cdd:COG0115 81 GLEDGYIRPQVTRGVGGRGVFAEEYE-PTVIIIASPLPAYPAEAYEKGVrviTSPYRRAAPGGLGGIKTGNYLNNVLAKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 158 E-IGNVVDkEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADE 236
Cdd:COG0115 160 EaKEAGAD-EALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADE 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 1586385891 237 VFVTNSIQEIVPLYHIEGRDFP-GKVGMITKRFMHLYE 273
Cdd:COG0115 239 VFLTGTAAEVTPVTEIDGRPIGdGKPGPVTRRLRELYT 276
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
4-272 |
2.51e-79 |
|
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: 241.35 E-value: 2.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 4 YVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNELE 83
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 84 HAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPAPGDIVEKEGVVLKQVRNTPEGAFRLKSHHYLNNILGKREIGNVV 163
Cdd:cd01558 81 EGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 164 DKEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNSI 243
Cdd:cd01558 161 ADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLTSTT 240
|
250 260 270
....*....|....*....|....*....|
gi 1586385891 244 QEIVPLYHIEGRD-FPGKVGMITKRFMHLY 272
Cdd:cd01558 241 AEVMPVVEIDGRPiGDGKPGPVTKRLREAY 270
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
29-248 |
1.58e-63 |
|
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: 199.12 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 29 GVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNELEHAYVRFNVSAGVDEIGLQTEmyeEP 108
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFGLPTS---DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 109 SVIVFIKPLPAPGDIVEKEGVVLKQVRNTPEGAFRLKSHHYLNNILGKREIGNV-VDkEGVFLTEAGYVAEGIVSNLFFV 187
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQgAD-DALLLDEDGNVTEGSTSNVFLV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586385891 188 KDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNSIQEIVP 248
Cdd:pfam01063 157 KGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTP 217
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
4-272 |
1.19e-58 |
|
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: 189.49 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 4 YVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHP----FLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVK 79
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTDKgpaiFRLKEHIQRLYDSAKIYRMEIPYSKEELMEATRETLRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 80 NELEHAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPA-PGDIVEKEGVVLKQV---RNTPEGAF-RLKS-HHYLNNI 153
Cdd:TIGR01122 81 NNLRSAYIRPLVFRGDGDLGLNPRAGYKPDVIIAAWPWGAyLGEEALEKGIDAKVSswrRNAPNTIPtAAKAgGNYLNSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 154 LGKRE-IGNVVDkEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELL 232
Cdd:TIGR01122 161 LAKSEaRRHGYD-EAILLDVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1586385891 233 SADEVFVTNSIQEIVPLYHIEGRDF-PGKVGMITKRFMHLY 272
Cdd:TIGR01122 240 TADEAFFTGTAAEITPIREVDGRKIgNGRRGPVTKKLQEAF 280
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
2-284 |
0e+00 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 552.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 2 LIYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNE 81
Cdd:PRK07650 1 LIYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 82 LEHAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPAPGDIVEKEGVVLKQVRNTPEGAFRLKSHHYLNNILGKREIGN 161
Cdd:PRK07650 81 LENAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQRRNTPEGAFRLKSHHYLNNILGKREIGN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 162 VVDKEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTN 241
Cdd:PRK07650 161 DPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFVTN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1586385891 242 SIQEIVPLYHIEGRDFPGKVGMITKRFMHLYEMQREKLWSRNE 284
Cdd:PRK07650 241 SIQEIVPLTRIEERDFPGKVGMVTKRLQNLYEMQREKLWSRNE 283
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
1-273 |
8.47e-102 |
|
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: 299.03 E-value: 8.47e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 1 MLIYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKN 80
Cdd:COG0115 1 RLIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 81 ELEHAYVRFNVSAGVDEIGLQTEMYEePSVIVFIKPLPAPGDIVEKEGV---VLKQVRNTPEGAFRLKSHHYLNNILGKR 157
Cdd:COG0115 81 GLEDGYIRPQVTRGVGGRGVFAEEYE-PTVIIIASPLPAYPAEAYEKGVrviTSPYRRAAPGGLGGIKTGNYLNNVLAKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 158 E-IGNVVDkEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADE 236
Cdd:COG0115 160 EaKEAGAD-EALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADE 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 1586385891 237 VFVTNSIQEIVPLYHIEGRDFP-GKVGMITKRFMHLYE 273
Cdd:COG0115 239 VFLTGTAAEVTPVTEIDGRPIGdGKPGPVTRRLRELYT 276
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
4-272 |
2.51e-79 |
|
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: 241.35 E-value: 2.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 4 YVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNELE 83
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 84 HAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPAPGDIVEKEGVVLKQVRNTPEGAFRLKSHHYLNNILGKREIGNVV 163
Cdd:cd01558 81 EGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 164 DKEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNSI 243
Cdd:cd01558 161 ADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLTSTT 240
|
250 260 270
....*....|....*....|....*....|
gi 1586385891 244 QEIVPLYHIEGRD-FPGKVGMITKRFMHLY 272
Cdd:cd01558 241 AEVMPVVEIDGRPiGDGKPGPVTKRLREAY 270
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
21-272 |
2.92e-78 |
|
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: 237.88 E-value: 2.92e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 21 DHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNELEHAYVRFNVSAGVDEIGL 100
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASLYIRPLLTRGVGGLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 101 QTEMYEEPSVIVFIKPLPAPGDIVEKeGVVLK----QVRNTPEGAFRLKSHHYLNNILGKREIGNVVDKEGVFLTEAGYV 176
Cdd:cd00449 81 APPPSPEPTFVVFASPVGAYAKGGEK-GVRLItspdRRRAAPGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDNGYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 177 AEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNSIQEIVPLYHIEGRD 256
Cdd:cd00449 160 TEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGRG 239
|
250
....*....|....*..
gi 1586385891 257 -FPGKVGMITKRFMHLY 272
Cdd:cd00449 240 iGDGKPGPVTRKLRELL 256
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
1-269 |
3.74e-75 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 231.30 E-value: 3.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 1 MLIYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKN 80
Cdd:PRK08320 3 QLIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRKN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 81 ELEHAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPA-PGDIVEK--EGVVLKQVRNTPEG-AFRLKSHHYLNNILGK 156
Cdd:PRK08320 83 NLRDAYIRLVVSRGVGDLGLDPRKCPKPTVVCIAEPIGLyPGELYEKglKVITVSTRRNRPDAlSPQVKSLNYLNNILAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 157 REIGNVVDKEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADE 236
Cdd:PRK08320 163 IEANLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTADE 242
|
250 260 270
....*....|....*....|....*....|....
gi 1586385891 237 VFVTNSIQEIVPLYHIEGRDF-PGKVGMITKRFM 269
Cdd:PRK08320 243 VFLTGTAAEVIPVVKVDGRVIgDGKPGPITKKLL 276
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
21-272 |
1.93e-72 |
|
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: 222.95 E-value: 1.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 21 DHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMtKDDVMLILKNLLVKNELEHAYVRFNVSAGVDEIGL 100
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPD-LPRLRAALESLLAANDIDEGRIRLILSRGPGGRGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 101 QTEMYEEPSVIVFIKPLPAPGDIvekEGVVLK--QVRNT-PEGAFRLKSHHYLNNILGKREIGNVVDKEGVFLTEAGYVA 177
Cdd:cd01559 80 APSVCPGPALYVSVIPLPPAWRQ---DGVRLItcPVRLGeQPLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 178 EGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNSIQEIVPLYHIEGRDF 257
Cdd:cd01559 157 EGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDDHDG 236
|
250
....*....|....*
gi 1586385891 258 PgkVGMITKRFMHLY 272
Cdd:cd01559 237 P--PGPLTRALRELL 249
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
29-248 |
1.58e-63 |
|
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: 199.12 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 29 GVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNELEHAYVRFNVSAGVDEIGLQTEmyeEP 108
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFGLPTS---DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 109 SVIVFIKPLPAPGDIVEKEGVVLKQVRNTPEGAFRLKSHHYLNNILGKREIGNV-VDkEGVFLTEAGYVAEGIVSNLFFV 187
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQgAD-DALLLDEDGNVTEGSTSNVFLV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586385891 188 KDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNSIQEIVP 248
Cdd:pfam01063 157 KGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTP 217
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
4-272 |
1.19e-58 |
|
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: 189.49 E-value: 1.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 4 YVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHP----FLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVK 79
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTDKgpaiFRLKEHIQRLYDSAKIYRMEIPYSKEELMEATRETLRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 80 NELEHAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPA-PGDIVEKEGVVLKQV---RNTPEGAF-RLKS-HHYLNNI 153
Cdd:TIGR01122 81 NNLRSAYIRPLVFRGDGDLGLNPRAGYKPDVIIAAWPWGAyLGEEALEKGIDAKVSswrRNAPNTIPtAAKAgGNYLNSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 154 LGKRE-IGNVVDkEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELL 232
Cdd:TIGR01122 161 LAKSEaRRHGYD-EAILLDVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1586385891 233 SADEVFVTNSIQEIVPLYHIEGRDF-PGKVGMITKRFMHLY 272
Cdd:TIGR01122 240 TADEAFFTGTAAEITPIREVDGRKIgNGRRGPVTKKLQEAF 280
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
2-278 |
7.61e-58 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 187.47 E-value: 7.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 2 LIYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNE 81
Cdd:PRK12479 5 YIYMNGEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKNE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 82 LEHAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPAPGDIVEKEGVVLKQV---RNTPEGAF-RLKSHHYLNNILGKR 157
Cdd:PRK12479 85 YADAYIRLIVSRGKGDLGLDPRSCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVasrRNTPDALDpRIKSMNYLNNVLVKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 158 EIGNVVDKEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEV 237
Cdd:PRK12479 165 EAAQAGVLEALMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEV 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1586385891 238 FVTNSIQEIVPLYHIEGRDF-PGKVGMITKRFM-HLYEMQREK 278
Cdd:PRK12479 245 FLTGTAAELIPVVKVDSREIgDGKPGSVTKQLTeEFKKLTRER 287
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
2-272 |
1.04e-52 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 174.18 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 2 LIYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHP----FLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLL 77
Cdd:PRK06606 8 YIWFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTPKgpaiFRLREHTKRLFNSAKILRMEIPYSVDELMEAQREVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 78 VKNELEHAYVR---F--NVSAGVDEIGLQTEmyeepsVIVFIKPLPAP-GDIVEKEGVVLK-------QVRNTPEGAfrl 144
Cdd:PRK06606 88 RKNNLKSAYIRplvFvgDEGLGVRPHGLPTD------VAIAAWPWGAYlGEEALEKGIRVKvsswtrhAPNSIPTRA--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 145 K-SHHYLNNILGKRE-IGNVVDkEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIK 222
Cdd:PRK06606 159 KaSGNYLNSILAKTEaRRNGYD-EALLLDVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1586385891 223 EGFFTKDELLSADEVFVTNSIQEIVPLYHIEGRDFP-GKVGMITKRFMHLY 272
Cdd:PRK06606 238 ERRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGnGKRGPITEKLQSAY 288
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
3-273 |
5.25e-49 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 163.95 E-value: 5.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 3 IYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNEL 82
Cdd:PRK06680 5 AYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 83 EHAYVRFNVSAGVD-------EIGLQtemyeePSVIVFIKPLPAPGDI-VEKEGVVLKQVRNTPEGAFRLKSHHYLNNIL 154
Cdd:PRK06680 85 REGLVYLQVTRGVArrdhvfpAADVK------PSVVVFAKSVDFARPAaAAETGIKVITVPDNRWKRCDIKSVGLLPNVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 155 GKREIGNVVDKEGVFLtEAGYVAEGIVSNLFFV-KDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLS 233
Cdd:PRK06680 159 AKQAAKEAGAQEAWMV-DDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1586385891 234 ADEVFVTNSIQEIVPLYHIEGRDF-PGKVGMITKRFMHLYE 273
Cdd:PRK06680 238 AREAFITAASSFVFPVVQIDGKQIgNGKPGPIAKRLREAYE 278
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
5-258 |
3.31e-38 |
|
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 132501 Cd Length: 261 Bit Score: 135.41 E-value: 3.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 5 VNGeyVEANEakISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKW----TMTKDDVMLILknllvkn 80
Cdd:TIGR03461 2 VNG--VLQTQ--ISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLpdwdALREEMAQLAA------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 81 ELEHAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPAPGDIVEKEGVVLK--QVR---NTpegafRLKSHHYLN---N 152
Cdd:TIGR03461 71 GYSLGVLKVIISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRLGvsPVRlgrNP-----LLAGIKHLNrleQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 153 ILGKREIGNVVDKEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELL 232
Cdd:TIGR03461 146 VLIKAELENSEADEALVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELL 225
|
250 260
....*....|....*....|....*.
gi 1586385891 233 SADEVFVTNSIQEIVPLYHIEGRDFP 258
Cdd:TIGR03461 226 SADEVFITNSLMGVVPVNAIGETSYP 251
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
5-258 |
4.88e-35 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 127.26 E-value: 4.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 5 VNGeyVEANEakISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIkwtmTKDDVMLILKNLL-VKNELE 83
Cdd:PRK06092 4 ING--QPQES--LSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAI----PLDDWAQLEQEMKqLAAELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 84 HAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPAPGDIVEKEGV--VLKQVR---NTpegafRLKSHHYLN---NILG 155
Cdd:PRK06092 76 NGVLKVIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGItlALCPTRlgrNP-----LLAGIKHLNrleQVLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 156 KREIGNVVDKEGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSAD 235
Cdd:PRK06092 151 RAELEQTEADEALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQAD 230
|
250 260
....*....|....*....|...
gi 1586385891 236 EVFVTNSIQEIVPLYHIEGRDFP 258
Cdd:PRK06092 231 EVFICNSLMPVWPVRAIGETSYS 253
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
16-272 |
1.16e-33 |
|
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: 123.85 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 16 KISPYDHGYLYGLGVFETFRIYNGHP-----FLLDDHYKRLIDALDTLQIKwTMTKDDVMLILKNLL-------VKNELE 83
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDgkivlFRPDENAERLNRSARRLGLP-PFSVEEFIDAIKELVkldadwvPYGGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 84 HAYVRFNVSAGVDEIGLQTEmyEEPSVIVFIKPLPAPGDIVEKeGV---VLKQVRNTPEGAFRLK-SHHYLNNILGKREi 159
Cdd:cd01557 80 SLYIRPFIFGTDPQLGVSPA--LEYLFAVFASPVGAYFKGGEK-GVsalVSSFRRAAPGGPGAAKaGGNYAASLLAQKE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 160 gnVVDK---EGVFL-TEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSAD 235
Cdd:cd01557 156 --AAEKgydQALWLdGAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEAD 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1586385891 236 EVFVTNSIQEIVPLYHIEGRD---FPGKVGMITKRFMHLY 272
Cdd:cd01557 234 EVFATGTAAVVTPVGEIDYRGkepGEGEVGPVTKKLYDLL 273
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
6-266 |
3.25e-31 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 117.81 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 6 NGEYVEANEAK--ISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNEL- 82
Cdd:PRK12400 10 NDAVIDTTKQKtyIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENNNFh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 83 EHAYVRFNVSAGVDEIGLQTEMYEEPSVIVFIKPLPAPGDIVEKegvvlkQVRNTPEGAFR-----LKSHHYLNNILGKR 157
Cdd:PRK12400 90 EDGTIYLQVSRGVQARTHTFSYDVPPTIYAYITKKERPALWIEY------GVRAISEPDTRwlrcdIKSLNLLPNILAAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 158 EIGNVVDKEGVFLTEaGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEV 237
Cdd:PRK12400 164 KAERKGCKEALFVRN-GTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADEC 242
|
250 260 270
....*....|....*....|....*....|
gi 1586385891 238 FVTNSIQEIVPLYHIEGRDFP-GKVGMITK 266
Cdd:PRK12400 243 FFTGTTIEILPMTHLDGTAIQdGQVGPITK 272
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
3-273 |
1.65e-30 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 115.84 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 3 IYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNEL 82
Cdd:PRK07544 11 IWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLAANGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 83 EHAYVR---------FNVSAGVDEIGLQTEMYEEPSVIvfikplpapGDIVEKEGVVL---KQVRNTPEGA-FRLK-SHH 148
Cdd:PRK07544 91 TDAYVRpvawrgsemMGVSAQQNKIHLAIAAWEWPSYF---------DPEAKMKGIRLdiaKWRRPDPETApSAAKaAGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 149 YLNNILGKREignvVDKEG----VFLTEAGYVAEGIVSNLFFVKDNVLYTPsLKTGILNGITRAFIIKVAEELRIEIKEG 224
Cdd:PRK07544 162 YMICTISKHA----AEAKGyadaLMLDYRGYVAEATGANIFFVKDGVIHTP-TPDCFLDGITRQTVIELAKRRGIEVVER 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1586385891 225 FFTKDELLSADEVFVTNSIQEIVPLYHIEGRDFpgKVGMITKRFMHLYE 273
Cdd:PRK07544 237 HIMPEELAGFSECFLTGTAAEVTPVSEIGEYRF--TPGAITRDLMDDYE 283
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
17-274 |
4.62e-21 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 91.23 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 17 ISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLILKNLLVKNELEHAYVRFNVSAGVD 96
Cdd:PLN02845 57 IPLDDHMVHRGHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAASGCRNGSLRYWLSAGPG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 97 EIGLQTEMYEEPSVIVFIKPLPAPGDIVEKEGVVLKQVRNTPEGAFRLKSHHYLNNILGKREIGNVVDKEGVFLTEAGYV 176
Cdd:PLN02845 137 GFSLSPSGCSEPAFYAVVIEDTYAQDRPEGVKVVTSSVPIKPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLDEEGFV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 177 AEGIVSNLFFV-KDNVLYTPSLkTGILNGITRAFIIKVAEELRIE-----IKEGFFTKDELLSADEVFVTNSIQEIVPLY 250
Cdd:PLN02845 217 AEGPNMNVAFLtNDGELVLPPF-DKILSGCTARRVLELAPRLVSPgdlrgVKQRKISVEEAKAADEMMLIGSGVPVLPIV 295
|
250 260
....*....|....*....|....*..
gi 1586385891 251 HIEGR---DfpGKVGMITkrfMHLYEM 274
Cdd:PLN02845 296 SWDGQpigD--GKVGPIT---LALHDL 317
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
27-258 |
1.67e-18 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 83.47 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 27 GLGVFETFRIYNGHPFLLDDHYKRL-------------ID----ALDTLQIKWTMTKDDVMLilknllvknelehayvRF 89
Cdd:PRK07849 38 GDGVFETLLVRDGRPCNLEAHLERLarsaalldlpepdLDrwrrAVELAIEEWRAPEDEAAL----------------RL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 90 NVSAGVDEIGlqtemyeEPSVIVFIKPLPAPGDIVEKEGV-VLKQVRNTPEGAFRL--------KSHHYLNNILGKRE-- 158
Cdd:PRK07849 102 VYSRGRESGG-------APTAWVTVSPVPERVARARREGVsVITLDRGYPSDAAERapwllagaKTLSYAVNMAALRYaa 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 159 ---IGNVVdkegvFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSAD 235
Cdd:PRK07849 175 rrgADDVI-----FTSTDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAAD 249
|
250 260
....*....|....*....|...
gi 1586385891 236 EVFVTNSIQEIVPLYHIEGRDFP 258
Cdd:PRK07849 250 GVWLVSSVRLAARVHTLDGRPLP 272
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
1-272 |
3.14e-18 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 82.31 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 1 MLIYVNGEYVEANEAKISPYDHGYLYGLGVFETFRIYNGHPFLLDDHYKRLIDALDTLQIKWTMTKDDVMLI----LKNL 76
Cdd:PRK13356 7 TWTFFDGEWHEGNVPIMGPADHAAWLGSTVFDGARAFEGVTPDLDLHCARVNRSAEALGLKPTVSAEEIEALaregLKRF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 77 LVKNELehaYVRFNVSAgvdEIGLQTEMYEEPS-----VIVFIKPLPAPGdivekeGVVL---KQVRNTPEGA-FRLK-S 146
Cdd:PRK13356 87 DPDTAL---YIRPMYWA---EDGFASGVAPDPEstrfaLCLEEAPMPEPT------GFSLtlsPFRRPTLEMApTDAKaG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 147 HHYLNNILGKRE-----IGNvvdkeGVFLTEAGYVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEI 221
Cdd:PRK13356 155 CLYPNNARALREarsrgFDN-----ALVLDMLGNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1586385891 222 KEGFFTKDELLSADEVFVTNSIQEIVPLYHIEGRDFPgkVGMITKRFMHLY 272
Cdd:PRK13356 230 VETTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSLQ--PGPVTRRARELY 278
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
175-240 |
4.87e-13 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 68.72 E-value: 4.87e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586385891 175 YVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVT 240
Cdd:PLN02782 282 YLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCT 347
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
183-273 |
6.71e-09 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 55.92 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 183 NLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSA------DEVF------VTNSIQEIvply 250
Cdd:PRK13357 237 NFFFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADaasgefTEAFacgtaaVITPIGGI---- 312
|
90 100
....*....|....*....|....*.
gi 1586385891 251 HIEGRDF---PGKVGMITKRfmhLYE 273
Cdd:PRK13357 313 KYKDKEFvigDGEVGPVTQK---LYD 335
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
176-242 |
9.38e-08 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 52.63 E-value: 9.38e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586385891 176 VAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNS 242
Cdd:PLN03117 232 IEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGT 298
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
175-256 |
2.15e-07 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 51.65 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 175 YVAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNSIQEIVPLYHIEG 254
Cdd:PLN02259 268 YLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITY 347
|
..
gi 1586385891 255 RD 256
Cdd:PLN02259 348 QE 349
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
176-242 |
8.88e-07 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 49.71 E-value: 8.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586385891 176 VAEGIVSNLFFVKDNVLYTPSLKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNS 242
Cdd:PLN02883 265 IEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGT 331
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
166-249 |
3.27e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 46.90 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 166 EGVFLTEAGYVAEGIVSNLFF-VKDNVLYTPSLKTGILNGITRAFIIKvAEELRieikEGFFTKDELLSADEVFVTNSIQ 244
Cdd:PRK07546 127 EVILLNERGEVCEGTITNVFLdRGGGMLTTPPLSCGLLPGVLRAELLD-AGRAR----EAVLTVDDLKSARAIWVGNSLR 201
|
....*
gi 1586385891 245 EIVPL 249
Cdd:PRK07546 202 GLIRA 206
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
168-259 |
4.69e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 40.73 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586385891 168 VFLTEAGYVAEGIVSNLFFVKDNVLYTPslKTGILNGITRAFIIKVAEELRIEIKEGFFTKDELLSADEVFVTNSIQEIV 247
Cdd:PRK09266 157 LFVDPDGRVSEGATWNLGFWDGGAVVWP--QAPALPGVTMALLQRGLERLGIPQRTRPVTLADLGRFAGAFACNAWRGQR 234
|
90
....*....|..
gi 1586385891 248 PLYHIEGRDFPG 259
Cdd:PRK09266 235 AVSAIDDVALPD 246
|
|
| |
