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Conserved domains on  [gi|487987889|ref|WP_002060282|]
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MULTISPECIES: D-amino-acid transaminase [Bacillus]

Protein Classification

aminotransferase class IV( domain architecture ID 1051)

aminotransferase class IV is a pyridoxaL 5'-phosphate dependent enzyme (PLPDE), similar to Staphylococcus D-alanine aminotransferase

Gene Ontology:  GO:0030170
PubMed:  31989227

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_IV super family cl00224
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 5-294 0e+00

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.


The actual alignment was detected with superfamily member PRK12400:

Pssm-ID: 444764  Cd Length: 290  Bit Score: 638.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   5 LAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLY 84
Cdd:PRK12400   1 MAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  85 KLIESNNFYEDGTIYLQVSRGVQARTHAFSYDIPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNVL 164
Cdd:PRK12400  81 KLIENNNFHEDGTIYLQVSRGVQARTHTFSYDVPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 165 AATKAERKGCKEALLVRNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQAD 244
Cdd:PRK12400 161 AATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQAD 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 487987889 245 ECFFTGTTIEILPMTHLDGAAIQDGQVGPITKTIQKSFSQSLLKSNTPSS 294
Cdd:PRK12400 241 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKMLQRSFSQSLLQSNMSSS 290
 
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: 638.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   5 LAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLY 84
Cdd:PRK12400   1 MAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  85 KLIESNNFYEDGTIYLQVSRGVQARTHAFSYDIPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNVL 164
Cdd:PRK12400  81 KLIENNNFHEDGTIYLQVSRGVQARTHTFSYDVPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 165 AATKAERKGCKEALLVRNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQAD 244
Cdd:PRK12400 161 AATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQAD 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 487987889 245 ECFFTGTTIEILPMTHLDGAAIQDGQVGPITKTIQKSFSQSLLKSNTPSS 294
Cdd:PRK12400 241 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKMLQRSFSQSLLQSNMSSS 290
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 11-287 2.15e-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: 2.15e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   11 VLWNDAVIDTTKQKtyIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESN 90
Cdd:TIGR01121   2 VLWNGQLVEREEAK--IDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   91 NFyEDGTIYLQVSRGVQARTHAFSYD-IPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNVLAATKA 169
Cdd:TIGR01121  80 NL-NTGHVYFQVTRGVAPRNHQFPAGtVKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  170 ERKGCKEALLVRNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFT 249
Cdd:TIGR01121 159 HEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVS 238

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 487987889  250 GTTIEILPMTHLDGAAIQDGQVGPITKTIQKSFSQSLL 287
Cdd:TIGR01121 239 STTAEITPVIEIDGQQIGDGKPGPWTRQLQKAFEEKIP 276
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 12-282 3.91e-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: 324.94  E-value: 3.91e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  12 LWNDAVIDTTKQKtyIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNN 91
Cdd:cd01558    1 YLNGEYVPREEAK--VSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  92 FyEDGTIYLQVSRGVQARTHAFSYDIPPTIYAYITK-KERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNVLAATKAE 170
Cdd:cd01558   79 G-GEGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPlPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 171 RKGCKEALLVR-NGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFT 249
Cdd:cd01558  158 EAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 487987889 250 GTTIEILPMTHLDGAAIQDGQVGPITKTIQKSF 282
Cdd:cd01558  238 STTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 9-284 8.59e-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: 294.02  E-value: 8.59e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   9 RFVLWNDAVIDttkqktyieLEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIE 88
Cdd:COG0115    8 ELVPEEEATIS---------VLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  89 SNNFyEDGTIYLQVSRGVQARTHaFSYDIPPTIYAYITK-KERPALWIEYGVRAISEPDTRW---LRCDIKSLNLLPNVL 164
Cdd:COG0115   79 ANGL-EDGYIRPQVTRGVGGRGV-FAEEYEPTVIIIASPlPAYPAEAYEKGVRVITSPYRRAapgGLGGIKTGNYLNNVL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 165 AATKAERKGCKEALLVR-NGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQA 243
Cdd:COG0115  157 AKQEAKEAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTA 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 487987889 244 DECFFTGTTIEILPMTHLDGAAIQDGQVGPITKTIQKSFSQ 284
Cdd:COG0115  237 DEVFLTGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTD 277
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 39-257 1.91e-53

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: 173.70  E-value: 1.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   39 GVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNNFYeDGTIYLQVSRGVQARTHAFSydiP 118
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLG-VGRLRLTVSRGPGGFGLPTS---D 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  119 PTIYAYITKKERPA-LWIEYGVRAISEPDTRWLRCDIKSLNLLPNVLAATKAERKGCKEALLV-RNGIVTEGSRSNFFLI 196
Cdd:pfam01063  77 PTLAIFVSALPPPPeSKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVFLV 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487987889  197 KNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGTTIEILP 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: 638.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   5 LAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLY 84
Cdd:PRK12400   1 MAYERFVLWNDAVIDTTKQKTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  85 KLIESNNFYEDGTIYLQVSRGVQARTHAFSYDIPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNVL 164
Cdd:PRK12400  81 KLIENNNFHEDGTIYLQVSRGVQARTHTFSYDVPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 165 AATKAERKGCKEALLVRNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQAD 244
Cdd:PRK12400 161 AATKAERKGCKEALFVRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQAD 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 487987889 245 ECFFTGTTIEILPMTHLDGAAIQDGQVGPITKTIQKSFSQSLLKSNTPSS 294
Cdd:PRK12400 241 ECFFTGTTIEILPMTHLDGTAIQDGQVGPITKMLQRSFSQSLLQSNMSSS 290
D_amino_aminoT TIGR01121
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ...
 11-287 2.15e-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: 2.15e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   11 VLWNDAVIDTTKQKtyIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESN 90
Cdd:TIGR01121   2 VLWNGQLVEREEAK--IDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   91 NFyEDGTIYLQVSRGVQARTHAFSYD-IPPTIYAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNVLAATKA 169
Cdd:TIGR01121  80 NL-NTGHVYFQVTRGVAPRNHQFPAGtVKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  170 ERKGCKEALLVRNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFT 249
Cdd:TIGR01121 159 HEKGAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVS 238

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 487987889  250 GTTIEILPMTHLDGAAIQDGQVGPITKTIQKSFSQSLL 287
Cdd:TIGR01121 239 STTAEITPVIEIDGQQIGDGKPGPWTRQLQKAFEEKIP 276
D-AAT_like cd01558
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ...
 12-282 3.91e-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: 324.94  E-value: 3.91e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  12 LWNDAVIDTTKQKtyIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNN 91
Cdd:cd01558    1 YLNGEYVPREEAK--VSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  92 FyEDGTIYLQVSRGVQARTHAFSYDIPPTIYAYITK-KERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNVLAATKAE 170
Cdd:cd01558   79 G-GEGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPlPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 171 RKGCKEALLVR-NGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFT 249
Cdd:cd01558  158 EAGADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 487987889 250 GTTIEILPMTHLDGAAIQDGQVGPITKTIQKSF 282
Cdd:cd01558  238 STTAEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
PRK06680 PRK06680
D-amino acid aminotransferase; Reviewed
 27-282 1.54e-104

D-amino acid aminotransferase; Reviewed


Pssm-ID: 180656 [Multi-domain]  Cd Length: 286  Bit Score: 306.09  E-value: 1.54e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  27 IELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNNFYEdGTIYLQVSRGV 106
Cdd:PRK06680  19 VHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRVRE-GLVYLQVTRGV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 107 QARTHAF-SYDIPPTI--YAYITKKERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNVLAATKAERKGCKEALLVRNG 183
Cdd:PRK06680  98 ARRDHVFpAADVKPSVvvFAKSVDFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQAAKEAGAQEAWMVDDG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 184 IVTEGSRSNFFLI-KNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGTTIEILPMTHLD 262
Cdd:PRK06680 178 FVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITAASSFVFPVVQID 257

                        250       260
                 ....*....|....*....|
gi 487987889 263 GAAIQDGQVGPITKTIQKSF 282
Cdd:PRK06680 258 GKQIGNGKPGPIAKRLREAY 277
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
 9-284 8.59e-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: 294.02  E-value: 8.59e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   9 RFVLWNDAVIDttkqktyieLEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIE 88
Cdd:COG0115    8 ELVPEEEATIS---------VLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  89 SNNFyEDGTIYLQVSRGVQARTHaFSYDIPPTIYAYITK-KERPALWIEYGVRAISEPDTRW---LRCDIKSLNLLPNVL 164
Cdd:COG0115   79 ANGL-EDGYIRPQVTRGVGGRGV-FAEEYEPTVIIIASPlPAYPAEAYEKGVRVITSPYRRAapgGLGGIKTGNYLNNVL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 165 AATKAERKGCKEALLVR-NGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQA 243
Cdd:COG0115  157 AKQEAKEAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTA 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 487987889 244 DECFFTGTTIEILPMTHLDGAAIQDGQVGPITKTIQKSFSQ 284
Cdd:COG0115  237 DEVFLTGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTD 277
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
 32-282 3.09e-89

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: 266.00  E-value: 3.09e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  32 RGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNNFyEDGTIYLQVSRGVQARTH 111
Cdd:cd00449    2 RGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNG-ASLYIRPLLTRGVGGLGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 112 AFSYDIPPTIYAYITKKERPALWIEYGVRAISEPDTR----WLRCDIKSLNLLPNVLAATKAERKGCKEALLVR-NGIVT 186
Cdd:cd00449   81 APPPSPEPTFVVFASPVGAYAKGGEKGVRLITSPDRRraapGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDdNGYVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 187 EGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGTTIEILPMTHLDGAAI 266
Cdd:cd00449  161 EGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGRGI 240

                        250
                 ....*....|....*.
gi 487987889 267 QDGQVGPITKTIQKSF 282
Cdd:cd00449  241 GDGKPGPVTRKLRELL 256
PRK08320 PRK08320
branched-chain amino acid aminotransferase; Reviewed
 33-282 2.81e-62

branched-chain amino acid aminotransferase; Reviewed


Pssm-ID: 236238 [Multi-domain]  Cd Length: 288  Bit Score: 198.56  E-value: 2.81e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  33 GLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNNfYEDGTIYLQVSRGVQ----- 107
Cdd:PRK08320  25 GFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRKNN-LRDAYIRLVVSRGVGdlgld 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 108 ----ARTHAFSydIPPTIYAYitkkerPALWIEYGVRAISEPdTRWLRCD-----IKSLNLLPNVLAATKAERKGCKEAL 178
Cdd:PRK08320 104 prkcPKPTVVC--IAEPIGLY------PGELYEKGLKVITVS-TRRNRPDalspqVKSLNYLNNILAKIEANLAGVDEAI 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 179 LV-RNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGTTIEILP 257
Cdd:PRK08320 175 MLnDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTADEVFLTGTAAEVIP 254

                        250       260
                 ....*....|....*....|....*
gi 487987889 258 MTHLDGAAIQDGQVGPITKTIQKSF 282
Cdd:PRK08320 255 VVKVDGRVIGDGKPGPITKKLLEEF 279
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
 39-257 1.91e-53

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: 173.70  E-value: 1.91e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   39 GVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNNFYeDGTIYLQVSRGVQARTHAFSydiP 118
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLG-VGRLRLTVSRGPGGFGLPTS---D 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  119 PTIYAYITKKERPA-LWIEYGVRAISEPDTRWLRCDIKSLNLLPNVLAATKAERKGCKEALLV-RNGIVTEGSRSNFFLI 196
Cdd:pfam01063  77 PTLAIFVSALPPPPeSKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVFLV 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487987889  197 KNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGTTIEILP 257
Cdd:pfam01063 157 KGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTP 217
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-52

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: 170.95  E-value: 3.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  32 RGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSlPFSKAELITLLYKLIESNNFyEDGTIYLQVSRGVQARTH 111
Cdd:cd01559    2 RGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIP-EPDLPRLRAALESLLAANDI-DEGRIRLILSRGPGGRGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 112 AFSYDIPPTiyAYITKKERPALWIEYGVRAISEPDT---RWLRCDIKSLNLLPNVLAATKAERKGCKEALLVR-NGIVTE 187
Cdd:cd01559   80 APSVCPGPA--LYVSVIPLPPAWRQDGVRLITCPVRlgeQPLLAGLKHLNYLENVLAKREARDRGADEALFLDtDGRVIE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 188 GSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGTTIEILPMTHLDGAaiq 267
Cdd:cd01559  158 GTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDDH--- 234

                        250
                 ....*....|....*
gi 487987889 268 DGQVGPITKTIQKSF 282
Cdd:cd01559  235 DGPPGPLTRALRELL 249
ilvE_I TIGR01122
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ...
 10-283 1.60e-51

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: 171.00  E-value: 1.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   10 FVLWNDAVIdttkqktyiELEERGLQFGDGVYEVMRLYNGNFHL----LDPHITRLYRSLEEIELSLPFSKAELITLLYK 85
Cdd:TIGR01122   6 FVDWEDAKV---------HVLTHALHYGTGVFEGIRAYDTDKGPaifrLKEHIQRLYDSAKIYRMEIPYSKEELMEATRE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   86 LIESNNFyEDGTIYLQVSRGVQARTHAFSYDIPPT--IYAYITKKERPALWIEYGVRAISepdTRWLRCD-------IKS 156
Cdd:TIGR01122  77 TLRKNNL-RSAYIRPLVFRGDGDLGLNPRAGYKPDviIAAWPWGAYLGEEALEKGIDAKV---SSWRRNApntiptaAKA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  157 LNLLPN-VLAATKAERKGCKEALLV-RNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEEL 234
Cdd:TIGR01122 153 GGNYLNsLLAKSEARRHGYDEAILLdVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQP 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 487987889  235 FSIRDVYQADECFFTGTTIEILPMTHLDGAAIQDGQVGPITKTIQKSFS 283
Cdd:TIGR01122 233 ISREELYTADEAFFTGTAAEITPIREVDGRKIGNGRRGPVTKKLQEAFF 281
PRK12479 PRK12479
branched-chain-amino-acid transaminase;
22-282 1.88e-48

branched-chain-amino-acid transaminase;


Pssm-ID: 183549 [Multi-domain]  Cd Length: 299  Bit Score: 163.20  E-value: 1.88e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  22 KQKTYIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNNfYEDGTIYLQ 101
Cdd:PRK12479  15 KEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKNE-YADAYIRLI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 102 VSRG-----VQARthafSYDIPPTIYAYITKKERPALWIEYGVRAISEPDTR----WLRCDIKSLNLLPNVLAATKAERK 172
Cdd:PRK12479  94 VSRGkgdlgLDPR----SCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASRRntpdALDPRIKSMNYLNNVLVKIEAAQA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 173 GCKEALLV-RNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGT 251
Cdd:PRK12479 170 GVLEALMLnQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLTGT 249

                        250       260       270
                 ....*....|....*....|....*....|.
gi 487987889 252 TIEILPMTHLDGAAIQDGQVGPITKTIQKSF 282
Cdd:PRK12479 250 AAELIPVVKVDSREIGDGKPGSVTKQLTEEF 280
PRK06606 PRK06606
branched-chain amino acid transaminase;
34-282 2.61e-41

branched-chain amino acid transaminase;


Pssm-ID: 235841  Cd Length: 306  Bit Score: 144.90  E-value: 2.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  34 LQFGDGVYEVMRLYNGN-----FHLlDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNN----------FYEDGTI 98
Cdd:PRK06606  30 LHYGTGVFEGIRAYDTPkgpaiFRL-REHTKRLFNSAKILRMEIPYSVDELMEAQREVVRKNNlksayirplvFVGDEGL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  99 ylqvsrGVqaRTHAFSYDIppTIYAYitkkerPalW--------IEYGVRA-ISepdtRWLRCDIKSL--------NLLP 161
Cdd:PRK06606 109 ------GV--RPHGLPTDV--AIAAW------P--WgaylgeeaLEKGIRVkVS----SWTRHAPNSIptrakasgNYLN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 162 NVLAATKAERKGCKEALLV-RNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDV 240
Cdd:PRK06606 167 SILAKTEARRNGYDEALLLdVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVIERRITRDEL 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 487987889 241 YQADECFFTGTTIEILPMTHLDGAAIQDGQVGPITKTIQKSF 282
Cdd:PRK06606 247 YIADEVFFTGTAAEVTPIREVDGRQIGNGKRGPITEKLQSAY 288
PRK07650 PRK07650
4-amino-4-deoxychorismate lyase; Provisional
 26-284 5.32e-40

4-amino-4-deoxychorismate lyase; Provisional


Pssm-ID: 181067  Cd Length: 283  Bit Score: 140.87  E-value: 5.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  26 YIELEE-------RGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNNfYEDGTI 98
Cdd:PRK07650   8 YVEEEEarispfdHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNG-LENAYV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  99 YLQVSRGV-----QARThafsYDiPPTIYAYITKKERPALWIE-YGV-----RAISEPDTRwlrcdIKSLNLLPNVLAAT 167
Cdd:PRK07650  87 RFNVSAGIgeiglQTEM----YE-EPTVIVYMKPLAPPGLPAEkEGVvlkqrRNTPEGAFR-----LKSHHYLNNILGKR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 168 KAERKGCKEAL-LVRNGIVTEGSRSNFFLIKNGTLYThPANHL-ILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADE 245
Cdd:PRK07650 157 EIGNDPNKEGIfLTEEGYVAEGIVSNLFWVKGDIVYT-PSLETgILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADE 235

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 487987889 246 CFFTGTTIEILPMTHLDGAAIqDGQVGPITKTIQKSFSQ 284
Cdd:PRK07650 236 VFVTNSIQEIVPLTRIEERDF-PGKVGMVTKRLQNLYEM 273
BCAT_beta_family cd01557
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ...
 33-282 6.05e-36

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: 130.01  E-value: 6.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  33 GLQFGDGVYEVMRLY---NGNFHLLDP--HITRLYRSLEEieLSLP-FSKAELITLLYKLIESNNFY----EDGTIYL-- 100
Cdd:cd01557    8 ALHYGQAVFEGLKAYrtpDGKIVLFRPdeNAERLNRSARR--LGLPpFSVEEFIDAIKELVKLDADWvpygGGASLYIrp 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 101 -----QVSRGVQARTHA-FSYDIPPTIyAYITKKERPalwieygVRAISEPdtrWLRCDIK-------SLNLLPNVLAAT 167
Cdd:cd01557   86 fifgtDPQLGVSPALEYlFAVFASPVG-AYFKGGEKG-------VSALVSS---FRRAAPGgpgaakaGGNYAASLLAQK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 168 KAERKGCKEALLV--RNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADE 245
Cdd:cd01557  155 EAAEKGYDQALWLdgAHGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADE 234

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 487987889 246 CFFTGTTIEILPMTHLD--GAAIQDGQVGPITKTIQKSF 282
Cdd:cd01557  235 VFATGTAAVVTPVGEIDyrGKEPGEGEVGPVTKKLYDLL 273
PLN02845 PLN02845
Branched-chain-amino-acid aminotransferase-like protein
 37-275 5.28e-34

Branched-chain-amino-acid aminotransferase-like protein


Pssm-ID: 215454 [Multi-domain]  Cd Length: 336  Bit Score: 126.28  E-value: 5.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  37 GDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIESNNFyEDGTI--YLQVSRGVQARTHafS 114
Cdd:PLN02845  67 GHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAASGC-RNGSLryWLSAGPGGFSLSP--S 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 115 YDIPPTIYAyITKKERPALWIEYGVRAI--SEPDTRWLRCDIKSLNLLPNVLAATKAERKGCKEALLV-RNGIVTEGSRS 191
Cdd:PLN02845 144 GCSEPAFYA-VVIEDTYAQDRPEGVKVVtsSVPIKPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLdEEGFVAEGPNM 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 192 NF-FLIKNGTLYTHPANHlILNGIIRQYVLSLANTLHIP-----VQEELFSIRDVYQADECFFTGTTIEILPMTHLDGAA 265
Cdd:PLN02845 223 NVaFLTNDGELVLPPFDK-ILSGCTARRVLELAPRLVSPgdlrgVKQRKISVEEAKAADEMMLIGSGVPVLPIVSWDGQP 301

                        250
                 ....*....|
gi 487987889 266 IQDGQVGPIT 275
Cdd:PLN02845 302 IGDGKVGPIT 311
PRK06092 PRK06092
4-amino-4-deoxychorismate lyase; Reviewed
 25-279 7.86e-29

4-amino-4-deoxychorismate lyase; Reviewed


Pssm-ID: 235696  Cd Length: 268  Bit Score: 111.09  E-value: 7.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  25 TYIELEERGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSkAELITLLYKLIESNnfyEDGTIYLQVSR 104
Cdd:PRK06092  10 ESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDW-AQLEQEMKQLAAEL---ENGVLKVIISR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 105 GVQARTHAFSYDIPPTI----YAYitkKERPALWIEYGVR-AISEpdTR-----WLrCDIKSLNLLPNVLAATKAERKGC 174
Cdd:PRK06092  86 GSGGRGYSPAGCAAPTRilsvSPY---PAHYSRWREQGITlALCP--TRlgrnpLL-AGIKHLNRLEQVLIRAELEQTEA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 175 KEAL-LVRNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGTTI 253
Cdd:PRK06092 160 DEALvLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSLM 239

                        250       260
                 ....*....|....*....|....*.
gi 487987889 254 EILPMThldGAAIQDGQVGPITKTIQ 279
Cdd:PRK06092 240 PVWPVR---AIGETSYSSGTLTRYLQ 262
PRK07544 PRK07544
branched-chain amino acid aminotransferase; Validated
 9-283 5.80e-23

branched-chain amino acid aminotransferase; Validated


Pssm-ID: 181025  Cd Length: 292  Bit Score: 95.81  E-value: 5.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889   9 RFVLWNDAVIDTTKQktyieleerGLQFGDGVYEVMRLYNGNFHLLDPHITRLYRSLEEIELSLPFSKAELITLLYKLIE 88
Cdd:PRK07544  16 ELVPWRDAKVHVLTH---------GLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  89 SNNFyEDGTIYLQVSRG-----VQARTHafsydippTIYAYITKKERPALWIE----YGVR-AISE---PDTRWLRCDIK 155
Cdd:PRK07544  87 ANGL-TDAYVRPVAWRGsemmgVSAQQN--------KIHLAIAAWEWPSYFDPeakmKGIRlDIAKwrrPDPETAPSAAK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 156 SLNL-LPNVLAATKAERKGCKEAL-LVRNGIVTEGSRSNFFLIKNGTLYThPANHLILNGIIRQYVLSLANTLHIPVQEE 233
Cdd:PRK07544 158 AAGLyMICTISKHAAEAKGYADALmLDYRGYVAEATGANIFFVKDGVIHT-PTPDCFLDGITRQTVIELAKRRGIEVVER 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 487987889 234 LFSIRDVYQADECFFTGTTIEILPMTHLDGAAIqdgQVGPITKTIQKSFS 283
Cdd:PRK07544 237 HIMPEELAGFSECFLTGTAAEVTPVSEIGEYRF---TPGAITRDLMDDYE 283
PRK13356 PRK13356
branched-chain amino acid aminotransferase;
152-276 4.31e-15

branched-chain amino acid aminotransferase;


Pssm-ID: 237362  Cd Length: 286  Bit Score: 73.84  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 152 CDIKSLNLLPNV-LAATKAERKGCKEALlVR--NGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHI 228
Cdd:PRK13356 149 TDAKAGCLYPNNaRALREARSRGFDNAL-VLdmLGNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGV 227

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 487987889 229 PVQEELFSIRDVYQADECFFTGTTIEILPMTHLDGAAIqdgQVGPITK 276
Cdd:PRK13356 228 TVVETTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSL---QPGPVTR 272
PRK07849 PRK07849
aminodeoxychorismate lyase;
37-266 2.45e-13

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 68.83  E-value: 2.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889  37 GDGVYEVMRLYNGNFHLLDPHITRLYRS-----LEEIELSlpfSKAELITLLYKLIESNNfyEDGTIYLQVSRGVQARTH 111
Cdd:PRK07849  38 GDGVFETLLVRDGRPCNLEAHLERLARSaalldLPEPDLD---RWRRAVELAIEEWRAPE--DEAALRLVYSRGRESGGA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 112 afsydipPTIYAYIT-KKERPALWIEYGVRAI-------SEPDTR--WLRCDIKSLNLLPNVLAATKAERKGCKEALLVR 181
Cdd:PRK07849 113 -------PTAWVTVSpVPERVARARREGVSVItldrgypSDAAERapWLLAGAKTLSYAVNMAALRYAARRGADDVIFTS 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 182 -NGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGTTIEILPMTH 260
Cdd:PRK07849 186 tDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWLVSSVRLAARVHT 265


                 ....*.
gi 487987889 261 LDGAAI 266
Cdd:PRK07849 266 LDGRPL 271
PLN02259 PLN02259
branched-chain-amino-acid aminotransferase 2
 154-286 4.05e-09

branched-chain-amino-acid aminotransferase 2


Pssm-ID: 177901  Cd Length: 388  Bit Score: 57.04  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 154 IKSL-NLLPNVLAATKAERKGCKEALL---VRNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIP 229
Cdd:PLN02259 234 VKSItNYAPVLKALSRAKSRGFSDVLYldsVKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQ 313

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487987889 230 VQEELFSIRDVYQADECFFTGTTIEILPMTHLdgaAIQDGQVGpiTKTIQKSFSQSL 286
Cdd:PLN02259 314 VVEKAVHVDEVMDADEVFCTGTAVVVAPVGTI---TYQEKRVE--YKTGDESVCQKL 365
PLN03117 PLN03117
Branched-chain-amino-acid aminotransferase; Provisional
 154-286 3.53e-07

Branched-chain-amino-acid aminotransferase; Provisional


Pssm-ID: 178664  Cd Length: 355  Bit Score: 50.70  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 154 IKSL-NLLPNVLAATKAERKGCKEALLV-----RNgiVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLH 227
Cdd:PLN03117 197 VKSCtNYSPVVKSLIEAKSSGFSDVLFLdaatgKN--IEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIG 274

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 487987889 228 IPVQEELFSIRDVYQADECFFTGTTIEIlpmTHLDGAAIQDGQVGpiTKTIQKSFSQSL 286
Cdd:PLN03117 275 YQVEERDVSVDELLEAEEVFCTGTAVVV---KAVETVTFHDKKVK--YRTGEEALSTKL 328
PLN02782 PLN02782
Branched-chain amino acid aminotransferase
 154-258 6.25e-06

Branched-chain amino acid aminotransferase


Pssm-ID: 215418  Cd Length: 403  Bit Score: 47.15  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487987889 154 IKSLNLLPNVLAATK-AERKGCKEALL---VRNGIVTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIP 229
Cdd:PLN02782 248 VKTIGNYAAVLKAQSiAKAKGYSDVLYldcVHKKYLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQ 327

                         90       100
                 ....*....|....*....|....*....
gi 487987889 230 VQEELFSIRDVYQADECFFTGTTIEILPM 258
Cdd:PLN02782 328 VEERNVTVDELLEADEVFCTGTAVVVSPV 356
PLN02883 PLN02883
Branched-chain amino acid aminotransferase
 185-251 2.16e-05

Branched-chain amino acid aminotransferase


Pssm-ID: 178471  Cd Length: 384  Bit Score: 45.48  E-value: 2.16e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487987889 185 VTEGSRSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLANTLHIPVQEELFSIRDVYQADECFFTGT 251
Cdd:PLN02883 265 IEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGT 331
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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