|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
5-294 |
0e+00 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 651.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 5 LAYEKFVLWNDEVIDTTKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLY 84
Cdd:PRK12400 1 MAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 85 KLIERNHFHEDGTIYLQVSRGVQARTHVFSYDNPPTIYAYITKKERPALWIEYGIRAISEPDTRWLRCDIKSLNLLPNVL 164
Cdd:PRK12400 81 KLIENNNFHEDGTIYLQVSRGVQARTHTFSYDVPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 165 AATKAERKGCKEALLVRNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQAD 244
Cdd:PRK12400 161 AATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQAD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1124301608 245 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKKLQKSFNQILLQSNMASS 294
Cdd:PRK12400 241 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKMLQRSFSQSLLQSNMSSS 290
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
11-284 |
2.22e-115 |
|
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130191 Cd Length: 276 Bit Score: 333.24 E-value: 2.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 11 VLWNDEVIDttKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERN 90
Cdd:TIGR01121 2 VLWNGQLVE--REEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 91 HFhEDGTIYLQVSRGVQARTHVFSYDN-PPTIYAYITKKERPALWIEYGIRAISEPDTRWLRCDIKSLNLLPNVLAATKA 169
Cdd:TIGR01121 80 NL-NTGHVYFQVTRGVAPRNHQFPAGTvKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 170 ERKGCKEALLVRNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFT 249
Cdd:TIGR01121 159 HEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVS 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1124301608 250 GTTIEILPMTHLDGTAIQDGQVGPITKKLQKSFNQ 284
Cdd:TIGR01121 239 STTAEITPVIEIDGQQIGDGKPGPWTRQLQKAFEE 273
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
12-282 |
1.01e-112 |
|
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: 326.48 E-value: 1.01e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 12 LWNDEVIDttKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNH 91
Cdd:cd01558 1 YLNGEYVP--REEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 92 FhEDGTIYLQVSRGVQARTHVFSYDNPPTIYAYITK-KERPALWIEYGIRAISEPDTRWLRCDIKSLNLLPNVLAATKAE 170
Cdd:cd01558 79 G-GEGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPlPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 171 RKGCKEALLVR-NGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFT 249
Cdd:cd01558 158 EAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237
|
250 260 270
....*....|....*....|....*....|...
gi 1124301608 250 GTTIEILPMTHLDGTAIQDGQVGPITKKLQKSF 282
Cdd:cd01558 238 STTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
10-285 |
3.59e-100 |
|
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: 295.17 E-value: 3.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 10 FVLWNDEVIDttKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIER 89
Cdd:COG0115 2 LIWLNGELVP--EEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 90 NHFhEDGTIYLQVSRGVQARTHvFSYDNPPTIYAYITK-KERPALWIEYGIRAISEPDTRW---LRCDIKSLNLLPNVLA 165
Cdd:COG0115 80 NGL-EDGYIRPQVTRGVGGRGV-FAEEYEPTVIIIASPlPAYPAEAYEKGVRVITSPYRRAapgGLGGIKTGNYLNNVLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 166 ATKAERKGCKEALLVR-NGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQAD 244
Cdd:COG0115 158 KQEAKEAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTAD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1124301608 245 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKKLQKSFNQI 285
Cdd:COG0115 238 EVFLTGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDI 278
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
39-257 |
1.59e-50 |
|
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: 165.99 E-value: 1.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 39 GVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFhEDGTIYLQVSRGVQARTHVFSydnP 118
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGL-GVGRLRLTVSRGPGGFGLPTS---D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 119 PTIYAYITKKERPA-LWIEYGIRAISEPDTRWLRCDIKSLNLLPNVLAATKAERKGCKEALLV-RNGIVTEGSHSNFFLI 196
Cdd:pfam01063 77 PTLAIFVSALPPPPeSKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVFLV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124301608 197 KNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGTTIEILP 257
Cdd:pfam01063 157 KGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTP 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
5-294 |
0e+00 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 651.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 5 LAYEKFVLWNDEVIDTTKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLY 84
Cdd:PRK12400 1 MAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 85 KLIERNHFHEDGTIYLQVSRGVQARTHVFSYDNPPTIYAYITKKERPALWIEYGIRAISEPDTRWLRCDIKSLNLLPNVL 164
Cdd:PRK12400 81 KLIENNNFHEDGTIYLQVSRGVQARTHTFSYDVPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 165 AATKAERKGCKEALLVRNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQAD 244
Cdd:PRK12400 161 AATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQAD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1124301608 245 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKKLQKSFNQILLQSNMASS 294
Cdd:PRK12400 241 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKMLQRSFSQSLLQSNMSSS 290
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
11-284 |
2.22e-115 |
|
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment site is the Lys at position 146 of the seed alignment, in the motif Cys-Asp-Ile-Lys-Ser-Leu-Asn. Specificity is broad for various D-amino acids, and differs among members of the family; the family is designated equivalog, but with this caveat attached. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130191 Cd Length: 276 Bit Score: 333.24 E-value: 2.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 11 VLWNDEVIDttKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERN 90
Cdd:TIGR01121 2 VLWNGQLVE--REEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 91 HFhEDGTIYLQVSRGVQARTHVFSYDN-PPTIYAYITKKERPALWIEYGIRAISEPDTRWLRCDIKSLNLLPNVLAATKA 169
Cdd:TIGR01121 80 NL-NTGHVYFQVTRGVAPRNHQFPAGTvKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 170 ERKGCKEALLVRNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFT 249
Cdd:TIGR01121 159 HEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVS 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1124301608 250 GTTIEILPMTHLDGTAIQDGQVGPITKKLQKSFNQ 284
Cdd:TIGR01121 239 STTAEITPVIEIDGQQIGDGKPGPWTRQLQKAFEE 273
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
12-282 |
1.01e-112 |
|
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: 326.48 E-value: 1.01e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 12 LWNDEVIDttKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNH 91
Cdd:cd01558 1 YLNGEYVP--REEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 92 FhEDGTIYLQVSRGVQARTHVFSYDNPPTIYAYITK-KERPALWIEYGIRAISEPDTRWLRCDIKSLNLLPNVLAATKAE 170
Cdd:cd01558 79 G-GEGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPlPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 171 RKGCKEALLVR-NGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFT 249
Cdd:cd01558 158 EAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237
|
250 260 270
....*....|....*....|....*....|...
gi 1124301608 250 GTTIEILPMTHLDGTAIQDGQVGPITKKLQKSF 282
Cdd:cd01558 238 STTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
27-282 |
1.30e-108 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 316.49 E-value: 1.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 27 IELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFHEdGTIYLQVSRGV 106
Cdd:PRK06680 19 VHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRVRE-GLVYLQVTRGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 107 QARTHVF-SYDNPPTI--YAYITKKERPALWIEYGIRAISEPDTRWLRCDIKSLNLLPNVLAATKAERKGCKEALLVRNG 183
Cdd:PRK06680 98 ARRDHVFpAADVKPSVvvFAKSVDFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKEAGAQEAWMVDDG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 184 IVTEGSHSNFFLI-KNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLD 262
Cdd:PRK06680 178 FVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITAASSFVFPVVQID 257
|
250 260
....*....|....*....|
gi 1124301608 263 GTAIQDGQVGPITKKLQKSF 282
Cdd:PRK06680 258 GKQIGNGKPGPIAKRLREAY 277
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
10-285 |
3.59e-100 |
|
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: 295.17 E-value: 3.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 10 FVLWNDEVIDttKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIER 89
Cdd:COG0115 2 LIWLNGELVP--EEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 90 NHFhEDGTIYLQVSRGVQARTHvFSYDNPPTIYAYITK-KERPALWIEYGIRAISEPDTRW---LRCDIKSLNLLPNVLA 165
Cdd:COG0115 80 NGL-EDGYIRPQVTRGVGGRGV-FAEEYEPTVIIIASPlPAYPAEAYEKGVRVITSPYRRAapgGLGGIKTGNYLNNVLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 166 ATKAERKGCKEALLVR-NGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQAD 244
Cdd:COG0115 158 KQEAKEAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTAD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1124301608 245 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKKLQKSFNQI 285
Cdd:COG0115 238 EVFLTGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDI 278
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
32-282 |
1.97e-88 |
|
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: 264.08 E-value: 1.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 32 RGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNhFHEDGTIYLQVSRGVQARTH 111
Cdd:cd00449 2 RGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAAN-NGASLYIRPLLTRGVGGLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 112 VFSYDNPPTIYAYITKKERPALWIEYGIRAISEPDTR----WLRCDIKSLNLLPNVLAATKAERKGCKEALLVR-NGIVT 186
Cdd:cd00449 81 APPPSPEPTFVVFASPVGAYAKGGEKGVRLITSPDRRraapGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDdNGYVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 187 EGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLDGTAI 266
Cdd:cd00449 161 EGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGRGI 240
|
250
....*....|....*.
gi 1124301608 267 QDGQVGPITKKLQKSF 282
Cdd:cd00449 241 GDGKPGPVTRKLRELL 256
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
36-285 |
2.44e-63 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 201.25 E-value: 2.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 36 FGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFhEDGTIYLQVSRGVQ-------- 107
Cdd:PRK08320 28 YGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRKNNL-RDAYIRLVVSRGVGdlgldprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 108 -ARTHVFSYDNPPTIYayitkkerPALWIEYGIRAISEPdTRWLRCD-----IKSLNLLPNVLAATKAERKGCKEALLV- 180
Cdd:PRK08320 107 cPKPTVVCIAEPIGLY--------PGELYEKGLKVITVS-TRRNRPDalspqVKSLNYLNNILAKIEANLAGVDEAIMLn 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 181 RNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGTTIEILPMTH 260
Cdd:PRK08320 178 DEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTADEVFLTGTAAEVIPVVK 257
|
250 260
....*....|....*....|....*
gi 1124301608 261 LDGTAIQDGQVGPITKKLQKSFNQI 285
Cdd:PRK08320 258 VDGRVIGDGKPGPITKKLLEEFREL 282
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
36-282 |
4.23e-52 |
|
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: 172.54 E-value: 4.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 36 FGDGVYEVIRLYKGNFHL----LDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFhEDGTIYLQVSRG------ 105
Cdd:TIGR01122 23 YGTGVFEGIRAYDTDKGPaifrLKEHIQRLYDSAKIYRMEIPYSKEELMEATRETLRKNNL-RSAYIRPLVFRGdgdlgl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 106 ---VQARTHVFsydnpptIYAYITKKERPALWIEYGIRAISepdTRWLRCD-------IKSLNLLPN-VLAATKAERKGC 174
Cdd:TIGR01122 102 nprAGYKPDVI-------IAAWPWGAYLGEEALEKGIDAKV---SSWRRNApntiptaAKAGGNYLNsLLAKSEARRHGY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 175 KEALLV-RNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGTTI 253
Cdd:TIGR01122 172 DEAILLdVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELYTADEAFFTGTAA 251
|
250 260
....*....|....*....|....*....
gi 1124301608 254 EILPMTHLDGTAIQDGQVGPITKKLQKSF 282
Cdd:TIGR01122 252 EITPIREVDGRKIGNGRRGPVTKKLQEAF 280
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
32-282 |
3.95e-51 |
|
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: 168.64 E-value: 3.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 32 RGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSlPFSKAELITLLYKLIERNHFhEDGTIYLQVSRGVQARTH 111
Cdd:cd01559 2 RGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIP-EPDLPRLRAALESLLAANDI-DEGRIRLILSRGPGGRGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 112 VFSYDNPPTiyAYITKKERPALWIEYGIRAISEPDT---RWLRCDIKSLNLLPNVLAATKAERKGCKEALLVR-NGIVTE 187
Cdd:cd01559 80 APSVCPGPA--LYVSVIPLPPAWRQDGVRLITCPVRlgeQPLLAGLKHLNYLENVLAKREARDRGADEALFLDtDGRVIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 188 GSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLDGtaiQ 267
Cdd:cd01559 158 GTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDD---H 234
|
250
....*....|....*
gi 1124301608 268 DGQVGPITKKLQKSF 282
Cdd:cd01559 235 DGPPGPLTRALRELL 249
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
39-257 |
1.59e-50 |
|
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: 165.99 E-value: 1.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 39 GVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFhEDGTIYLQVSRGVQARTHVFSydnP 118
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGL-GVGRLRLTVSRGPGGFGLPTS---D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 119 PTIYAYITKKERPA-LWIEYGIRAISEPDTRWLRCDIKSLNLLPNVLAATKAERKGCKEALLV-RNGIVTEGSHSNFFLI 196
Cdd:pfam01063 77 PTLAIFVSALPPPPeSKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVFLV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124301608 197 KNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGTTIEILP 257
Cdd:pfam01063 157 KGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTP 217
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
9-285 |
1.69e-50 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 168.59 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 9 KFVLWNDEVIDttKQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIE 88
Cdd:PRK12479 4 QYIYMNGEFVE--KEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 89 RNHFhEDGTIYLQVSRG-----VQARthvfSYDNPPTIYAYITKKERPALWIEYGIRAISEPDTR----WLRCDIKSLNL 159
Cdd:PRK12479 82 KNEY-ADAYIRLIVSRGkgdlgLDPR----SCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASRRntpdALDPRIKSMNY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 160 LPNVLAATKAERKGCKEALLV-RNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVR 238
Cdd:PRK12479 157 LNNVLVKIEAAQAGVLEALMLnQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRH 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1124301608 239 DVYQADECFFTGTTIEILPMTHLDGTAIQDGQVGPITKKLQKSFNQI 285
Cdd:PRK12479 237 DVYVADEVFLTGTAAELIPVVKVDSREIGDGKPGSVTKQLTEEFKKL 283
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
36-282 |
2.97e-44 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 152.61 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 36 FGDGVYEVIRLYKGN-----FHLlDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFHEdgtIYL-------QVS 103
Cdd:PRK06606 32 YGTGVFEGIRAYDTPkgpaiFRL-REHTKRLFNSAKILRMEIPYSVDELMEAQREVVRKNNLKS---AYIrplvfvgDEG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 104 RGVQAR---THVFsydnpptIYAYitkkerPalW--------IEYGIRA-ISepdtRWLRCDIKSL--------NLLPNV 163
Cdd:PRK06606 108 LGVRPHglpTDVA-------IAAW------P--WgaylgeeaLEKGIRVkVS----SWTRHAPNSIptrakasgNYLNSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 164 LAATKAERKGCKEALLV-RNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQ 242
Cdd:PRK06606 169 LAKTEARRNGYDEALLLdVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVIERRITRDELYI 248
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1124301608 243 ADECFFTGTTIEILPMTHLDGTAIQDGQVGPITKKLQKSF 282
Cdd:PRK06606 249 ADEVFFTGTAAEVTPIREVDGRQIGNGKRGPITEKLQSAY 288
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
26-282 |
2.78e-39 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 138.95 E-value: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 26 YIELEE-------RGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFhEDGTI 98
Cdd:PRK07650 8 YVEEEEarispfdHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNGL-ENAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 99 YLQVSRGV-----QARThvfsYDNPpTIYAYITKKERPALWIE------YGIRAISEPDTRwlrcdIKSLNLLPNVLAAT 167
Cdd:PRK07650 87 RFNVSAGIgeiglQTEM----YEEP-TVIVYMKPLAPPGLPAEkegvvlKQRRNTPEGAFR-----LKSHHYLNNILGKR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 168 KAERKGCKEAL-LVRNGIVTEGSHSNFFLIKNGTLYThPANHL-ILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADE 245
Cdd:PRK07650 157 EIGNDPNKEGIfLTEEGYVAEGIVSNLFWVKGDIVYT-PSLETgILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADE 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1124301608 246 CFFTGTTIEILPMTHLDGTAIqDGQVGPITKKLQKSF 282
Cdd:PRK07650 236 VFVTNSIQEIVPLTRIEERDF-PGKVGMVTKRLQNLY 271
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
35-285 |
1.65e-37 |
|
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: 134.25 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 35 QFGDGVYEVIRLYK---GNFHLLDP--HITRLYRSMEEveLSLP-FSKAELITLLYKLIERNHF---HEDGT-IYL---- 100
Cdd:cd01557 10 HYGQAVFEGLKAYRtpdGKIVLFRPdeNAERLNRSARR--LGLPpFSVEEFIDAIKELVKLDADwvpYGGGAsLYIrpfi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 101 ---QVSRGVQARTH----VFSYdnpPTIyAYITKKERPalwieygIRAISEPdtrWLRCDIK-------SLNLLPNVLAA 166
Cdd:cd01557 88 fgtDPQLGVSPALEylfaVFAS---PVG-AYFKGGEKG-------VSALVSS---FRRAAPGgpgaakaGGNYAASLLAQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 167 TKAERKGCKEALLV--RNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQAD 244
Cdd:cd01557 154 KEAAEKGYDQALWLdgAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEAD 233
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1124301608 245 ECFFTGTTIEILPMTHLD--GTAIQDGQVGPITKKLQKSFNQI 285
Cdd:cd01557 234 EVFATGTAAVVTPVGEIDyrGKEPGEGEVGPVTKKLYDLLTDI 276
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
37-278 |
4.66e-34 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 126.28 E-value: 4.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 37 GDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFhEDGTI--YLQVSRGVQARTHvfS 114
Cdd:PLN02845 67 GHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAASGC-RNGSLryWLSAGPGGFSLSP--S 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 115 YDNPPTIYAyITKKERPALWIEYGIRAI--SEPDTRWLRCDIKSLNLLPNVLAATKAERKGCKEALLV-RNGIVTEGSHS 191
Cdd:PLN02845 144 GCSEPAFYA-VVIEDTYAQDRPEGVKVVtsSVPIKPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLdEEGFVAEGPNM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 192 NF-FLIKNGTLYTHPANHlILNGIIRQYVLSLANTLHIP-----VQEELFSVRDVYQADECFFTGTTIEILPMTHLDGTA 265
Cdd:PLN02845 223 NVaFLTNDGELVLPPFDK-ILSGCTARRVLELAPRLVSPgdlrgVKQRKISVEEAKAADEMMLIGSGVPVLPIVSWDGQP 301
|
250
....*....|...
gi 1124301608 266 IQDGQVGPITKKL 278
Cdd:PLN02845 302 IGDGKVGPITLAL 314
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
22-285 |
8.78e-30 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 113.40 E-value: 8.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 22 KQQTYIELEERGSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSkAELITLLYKLIernHFHEDGTIYLQ 101
Cdd:PRK06092 7 QPQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDW-AQLEQEMKQLA---AELENGVLKVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 102 VSRGVQARTHVFSYDNPPTI----YAYitkKERPALWIEYGIR-AISEpdTR-----WLrCDIKSLNLLPNVLAATKAER 171
Cdd:PRK06092 83 ISRGSGGRGYSPAGCAAPTRilsvSPY---PAHYSRWREQGITlALCP--TRlgrnpLL-AGIKHLNRLEQVLIRAELEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 172 KGCKEAL-LVRNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTG 250
Cdd:PRK06092 157 TEADEALvLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICN 236
|
250 260 270
....*....|....*....|....*....|....*
gi 1124301608 251 TTIEILPMTHLDGTAIqdgQVGPITKKLQKSFNQI 285
Cdd:PRK06092 237 SLMPVWPVRAIGETSY---SSGTLTRYLQPLCERL 268
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
33-282 |
1.16e-20 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 89.26 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 33 GSQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKAELITLLYKLIERNHFhEDGTIYLQVSRG------- 105
Cdd:PRK07544 31 GLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLAANGL-TDAYVRPVAWRGsemmgvs 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 106 -VQARTHVF-------SYDNPPTiyayitKKErpalwieyGIR-AISE---PDTRWLRCDIKSLNL-LPNVLAATKAERK 172
Cdd:PRK07544 110 aQQNKIHLAiaawewpSYFDPEA------KMK--------GIRlDIAKwrrPDPETAPSAAKAAGLyMICTISKHAAEAK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 173 GCKEAL-LVRNGIVTEGSHSNFFLIKNGTLYThPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGT 251
Cdd:PRK07544 176 GYADALmLDYRGYVAEATGANIFFVKDGVIHT-PTPDCFLDGITRQTVIELAKRRGIEVVERHIMPEELAGFSECFLTGT 254
|
250 260 270
....*....|....*....|....*....|.
gi 1124301608 252 TIEILPMTHLDGTAIqdgQVGPITKKLQKSF 282
Cdd:PRK07544 255 AAEVTPVSEIGEYRF---TPGAITRDLMDDY 282
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
152-277 |
8.79e-17 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 78.46 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 152 CDIKSLNLLPNV-LAATKAERKGCKEALlVR--NGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHI 228
Cdd:PRK13356 149 TDAKAGCLYPNNaRALREARSRGFDNAL-VLdmLGNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGV 227
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1124301608 229 PVQEELFSVRDVYQADECFFTGTTIEILPMTHLDGTAIqdgQVGPITKK 277
Cdd:PRK13356 228 TVVETTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSL---QPGPVTRR 273
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
37-266 |
7.97e-13 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 67.29 E-value: 7.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 37 GDGVYEVIRLYKGNFHLLDPHITRLYRSMEEVELSLPFSKA--ELITLLYKLIERNhfHEDGTIYLQVSRGVQArthvfs 114
Cdd:PRK07849 38 GDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPEPDLDRwrRAVELAIEEWRAP--EDEAALRLVYSRGRES------ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 115 yDNPPTIYAYIT-KKERPALWIEYGIRAI-------SEPDTR--WLRCDIKSLNLLPNVLAATKAERKGCKEALLVR-NG 183
Cdd:PRK07849 110 -GGAPTAWVTVSpVPERVARARREGVSVItldrgypSDAAERapWLLAGAKTLSYAVNMAALRYAARRGADDVIFTStDG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 184 IVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLDG 263
Cdd:PRK07849 189 YVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWLVSSVRLAARVHTLDG 268
|
...
gi 1124301608 264 TAI 266
Cdd:PRK07849 269 RPL 271
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
154-258 |
3.40e-09 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 57.04 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 154 IKSL-NLLPNVLAATKAERKGCKEALL---VRNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIP 229
Cdd:PLN02259 234 VKSItNYAPVLKALSRAKSRGFSDVLYldsVKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQ 313
|
90 100
....*....|....*....|....*....
gi 1124301608 230 VQEELFSVRDVYQADECFFTGTTIEILPM 258
Cdd:PLN02259 314 VVEKAVHVDEVMDADEVFCTGTAVVVAPV 342
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
154-255 |
1.11e-06 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 49.16 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 154 IKSL-NLLPNVLAATKAERKGCKEALLV-----RNgiVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLH 227
Cdd:PLN03117 197 VKSCtNYSPVVKSLIEAKSSGFSDVLFLdaatgKN--IEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIG 274
|
90 100
....*....|....*....|....*...
gi 1124301608 228 IPVQEELFSVRDVYQADECFFTGTTIEI 255
Cdd:PLN03117 275 YQVEERDVSVDELLEAEEVFCTGTAVVV 302
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
154-280 |
1.34e-06 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 49.08 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124301608 154 IKSLNLLPNVLAATK-AERKGCKEALL---VRNGIVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIP 229
Cdd:PLN02782 248 VKTIGNYAAVLKAQSiAKAKGYSDVLYldcVHKKYLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQ 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1124301608 230 VQEELFSVRDVYQADECFFTGTTIEILPmthldgtaiqdgqVGPITKKLQK 280
Cdd:PLN02782 328 VEERNVTVDELLEADEVFCTGTAVVVSP-------------VGSITYKGKR 365
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
185-251 |
1.57e-05 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 45.86 E-value: 1.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124301608 185 VTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSVRDVYQADECFFTGT 251
Cdd:PLN02883 265 IEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGT 331
|
|
| |
