|
Name |
Accession |
Description |
Interval |
E-value |
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
27-299 |
2.75e-92 |
|
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: 275.25 E-value: 2.75e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 27 YVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGMR 106
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 107 DG-AHARlmVTRGVKKTPNQDPRFIigGATVVCVAEH-KVVTPEAKRNGLKLFTStlrcsgPDVFDLRLN--SHSRLNLI 182
Cdd:cd01558 81 EGdVYIQ--VTRGVGPRGHDFPKCV--KPTVVIITQPlPLPPAELLEKGVRVITV------PDIRWLRCDikSLNLLNNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 183 QALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWTS-SGRYCFNGITRATVVRLAREAGIPVHEGDFTLAEVYA 261
Cdd:cd01558 151 LAKQEAKEAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPpLDNGILPGITRATVIELAKELGIPVEERPFSLEELYT 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
7Z79_D 262 ADEAFVTGTLAGLTPVSSVDGRALVP--LGPLTQRLDALY 299
Cdd:cd01558 231 ADEVFLTSTTAEVMPVVEIDGRPIGDgkPGPVTKRLREAY 270
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
25-302 |
7.70e-92 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 274.83 E-value: 7.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 25 LVYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNG 104
Cdd:PRK08320 4 LIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRKNN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 105 MRDgAHARLMVTRGV-------KKTPNqdprfiiggATVVCVAEHKVVTP-EAKRNGLKLFTSTLRCSGPDVFDLRLNSH 176
Cdd:PRK08320 84 LRD-AYIRLVVSRGVgdlgldpRKCPK---------PTVVCIAEPIGLYPgELYEKGLKVITVSTRRNRPDALSPQVKSL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 177 SRLNLIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWT---SSGryCFNGITRATVVRLAREAGIPVHEGD 253
Cdd:PRK08320 154 NYLNNILAKIEANLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITpptYAG--ALEGITRNAVIEIAKELGIPVREEL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
7Z79_D 254 FTLAEVYAADEAFVTGTLAGLTPVSSVDGRAL---VPlGPLTQRLDALYRAY 302
Cdd:PRK08320 232 FTLHDLYTADEVFLTGTAAEVIPVVKVDGRVIgdgKP-GPITKKLLEEFREL 282
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
25-309 |
3.70e-91 |
|
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: 272.83 E-value: 3.70e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 25 LVYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNG 104
Cdd:COG0115 2 LIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 105 MRDGaHARLMVTRGVKK----TPNQDPRFIIggatvvCVAEHKVVTPEAKRNGLKLFTSTLRCSGPDVfDLRLNSHSRLN 180
Cdd:COG0115 82 LEDG-YIRPQVTRGVGGrgvfAEEYEPTVII------IASPLPAYPAEAYEKGVRVITSPYRRAAPGG-LGGIKTGNYLN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 181 LIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLAEV 259
Cdd:COG0115 154 NVLAKQEAKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTpPLSGGILPGITRDSVIELARELGIPVEERPISLEEL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
7Z79_D 260 YAADEAFVTGTLAGLTPVSSVDGRAL--VPLGPLTQRLDALYRAYIASANEA 309
Cdd:COG0115 234 YTADEVFLTGTAAEVTPVTEIDGRPIgdGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
27-310 |
1.17e-61 |
|
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: 197.97 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 27 YVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDG----RIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLR 102
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTdkgpAIFRLKEHIQRLYDSAKIYRMEIPYSKEELMEATRETLRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 103 NGMRDgAHARLMVTRGVKKTpNQDPRfiIGGATVVCVAEH---KVVTPEAKRNGLKLFTSTLRCSGPDVFDLRLNSHSR- 178
Cdd:TIGR01122 81 NNLRS-AYIRPLVFRGDGDL-GLNPR--AGYKPDVIIAAWpwgAYLGEEALEKGIDAKVSSWRRNAPNTIPTAAKAGGNy 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 179 LNLIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLA 257
Cdd:TIGR01122 157 LNSLLAKSEARRHGYDEAILLDVEGYVAEGSGENIFIVKDGVLFTpPVTSSILPGITRDTVITLAKELGIEVVEQPISRE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
7Z79_D 258 EVYAADEAFVTGTLAGLTPVSSVDGRALVP--LGPLTQRLDALYRAYIASANEAH 310
Cdd:TIGR01122 237 ELYTADEAFFTGTAAEITPIREVDGRKIGNgrRGPVTKKLQEAFFDLVTGGTEDY 291
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
52-280 |
3.66e-47 |
|
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: 158.29 E-value: 3.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 52 GVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGMRDGAhARLMVTRGVKK--TPNQDPRF 129
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGR-LRLTVSRGPGGfgLPTSDPTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 130 IIggatvvCVAEHKVVTPEAKRNGlklfTSTLRCSGPDVFDLRLNSHSRLNLIQALIQAIQAGADEALMLDPNGFVSSCN 209
Cdd:pfam01063 80 AI------FVSALPPPPESKKKGV----ISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7Z79_D 210 STNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSSV 280
Cdd:pfam01063 150 TSNVFLVKGGTLYTpPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
27-299 |
2.75e-92 |
|
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: 275.25 E-value: 2.75e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 27 YVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGMR 106
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 107 DG-AHARlmVTRGVKKTPNQDPRFIigGATVVCVAEH-KVVTPEAKRNGLKLFTStlrcsgPDVFDLRLN--SHSRLNLI 182
Cdd:cd01558 81 EGdVYIQ--VTRGVGPRGHDFPKCV--KPTVVIITQPlPLPPAELLEKGVRVITV------PDIRWLRCDikSLNLLNNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 183 QALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWTS-SGRYCFNGITRATVVRLAREAGIPVHEGDFTLAEVYA 261
Cdd:cd01558 151 LAKQEAKEAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPpLDNGILPGITRATVIELAKELGIPVEERPFSLEELYT 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
7Z79_D 262 ADEAFVTGTLAGLTPVSSVDGRALVP--LGPLTQRLDALY 299
Cdd:cd01558 231 ADEVFLTSTTAEVMPVVEIDGRPIGDgkPGPVTKRLREAY 270
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
25-302 |
7.70e-92 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 274.83 E-value: 7.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 25 LVYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNG 104
Cdd:PRK08320 4 LIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLSKEEMTEIVLETLRKNN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 105 MRDgAHARLMVTRGV-------KKTPNqdprfiiggATVVCVAEHKVVTP-EAKRNGLKLFTSTLRCSGPDVFDLRLNSH 176
Cdd:PRK08320 84 LRD-AYIRLVVSRGVgdlgldpRKCPK---------PTVVCIAEPIGLYPgELYEKGLKVITVSTRRNRPDALSPQVKSL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 177 SRLNLIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWT---SSGryCFNGITRATVVRLAREAGIPVHEGD 253
Cdd:PRK08320 154 NYLNNILAKIEANLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITpptYAG--ALEGITRNAVIEIAKELGIPVREEL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
7Z79_D 254 FTLAEVYAADEAFVTGTLAGLTPVSSVDGRAL---VPlGPLTQRLDALYRAY 302
Cdd:PRK08320 232 FTLHDLYTADEVFLTGTAAEVIPVVKVDGRVIgdgKP-GPITKKLLEEFREL 282
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
25-309 |
3.70e-91 |
|
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: 272.83 E-value: 3.70e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 25 LVYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNG 104
Cdd:COG0115 2 LIWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 105 MRDGaHARLMVTRGVKK----TPNQDPRFIIggatvvCVAEHKVVTPEAKRNGLKLFTSTLRCSGPDVfDLRLNSHSRLN 180
Cdd:COG0115 82 LEDG-YIRPQVTRGVGGrgvfAEEYEPTVII------IASPLPAYPAEAYEKGVRVITSPYRRAAPGG-LGGIKTGNYLN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 181 LIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLAEV 259
Cdd:COG0115 154 NVLAKQEAKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTpPLSGGILPGITRDSVIELARELGIPVEERPISLEEL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
7Z79_D 260 YAADEAFVTGTLAGLTPVSSVDGRAL--VPLGPLTQRLDALYRAYIASANEA 309
Cdd:COG0115 234 YTADEVFLTGTAAEVTPVTEIDGRPIgdGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
25-301 |
5.08e-67 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 211.74 E-value: 5.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 25 LVYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNG 104
Cdd:PRK12479 5 YIYMNGEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKNE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 105 MRDgAHARLMVTRGvKKTPNQDPRFIIGGATVVCVAEHKVVTPEAKRNGLKLFTSTLRCSGPDVFDLRLNSHSRLNLIQA 184
Cdd:PRK12479 85 YAD-AYIRLIVSRG-KGDLGLDPRSCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASRRNTPDALDPRIKSMNYLNNVLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 185 LIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWTSSGRY-CFNGITRATVVRLAREAGIPVHEGDFTLAEVYAAD 263
Cdd:PRK12479 163 KIEAAQAGVLEALMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLgALEGITRNSVIELCERLSIPCEERPFTRHDVYVAD 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
7Z79_D 264 EAFVTGTLAGLTPVSSVDGRAL---VPlGPLTQRLDALYRA 301
Cdd:PRK12479 243 EVFLTGTAAELIPVVKVDSREIgdgKP-GSVTKQLTEEFKK 282
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
44-299 |
3.48e-66 |
|
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: 208.22 E-value: 3.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 44 DAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGMRDGAhARLMVTRGVKK-- 121
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASLY-IRPLLTRGVGGlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 122 -TPNQDPRFiiggaTVVCVAEHKVVTPEAKRNGLKLFTSTLRCSGPDVFDLRLNSHSRLNLIQALIQAIQAGADEALMLD 200
Cdd:cd00449 80 vAPPPSPEP-----TFVVFASPVGAYAKGGEKGVRLITSPDRRRAAPGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 201 PNGFVSSCNSTNFFAVRNGALWTSSGRYCF-NGITRATVVRLAREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSS 279
Cdd:cd00449 155 DNGYVTEGSASNVFIVKDGELVTPPLDGGIlPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTE 234
|
250 260
....*....|....*....|..
7Z79_D 280 VDGRALVPL--GPLTQRLDALY 299
Cdd:cd00449 235 IDGRGIGDGkpGPVTRKLRELL 256
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
27-310 |
1.17e-61 |
|
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: 197.97 E-value: 1.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 27 YVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDG----RIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLR 102
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTdkgpAIFRLKEHIQRLYDSAKIYRMEIPYSKEELMEATRETLRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 103 NGMRDgAHARLMVTRGVKKTpNQDPRfiIGGATVVCVAEH---KVVTPEAKRNGLKLFTSTLRCSGPDVFDLRLNSHSR- 178
Cdd:TIGR01122 81 NNLRS-AYIRPLVFRGDGDL-GLNPR--AGYKPDVIIAAWpwgAYLGEEALEKGIDAKVSSWRRNAPNTIPTAAKAGGNy 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 179 LNLIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLA 257
Cdd:TIGR01122 157 LNSLLAKSEARRHGYDEAILLDVEGYVAEGSGENIFIVKDGVLFTpPVTSSILPGITRDTVITLAKELGIEVVEQPISRE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
7Z79_D 258 EVYAADEAFVTGTLAGLTPVSSVDGRALVP--LGPLTQRLDALYRAYIASANEAH 310
Cdd:TIGR01122 237 ELYTADEAFFTGTAAEITPIREVDGRKIGNgrRGPVTKKLQEAFFDLVTGGTEDY 291
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
21-310 |
2.01e-51 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 171.87 E-value: 2.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 21 NDAVLVYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDG----RIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVV 96
Cdd:PRK06606 4 DRAGYIWFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTpkgpAIFRLREHTKRLFNSAKILRMEIPYSVDELMEAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 97 VDTFLRNGMRDgAHARLMVTRGVKK----TPNQDPRFIIG----GAtvvcvaehkVVTPEAKRNGLKLFTSTLRCSGPDV 168
Cdd:PRK06606 84 REVVRKNNLKS-AYIRPLVFVGDEGlgvrPHGLPTDVAIAawpwGA---------YLGEEALEKGIRVKVSSWTRHAPNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 169 FDLR-------LNShsrlnlIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWT---SSGryCFNGITRATV 238
Cdd:PRK06606 154 IPTRakasgnyLNS------ILAKTEARRNGYDEALLLDVEGYVSEGSGENIFIVRDGVLYTpplTSS--ILEGITRDTV 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7Z79_D 239 VRLAREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSSVDGRALVPL--GPLTQRLDALYRAYIASANEAH 310
Cdd:PRK06606 226 ITLAKDLGIEVIERRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGNGkrGPITEKLQSAYFDIVRGRTEKY 299
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
26-303 |
1.49e-49 |
|
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: 166.07 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 26 VYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGM 105
Cdd:TIGR01121 2 VLWNGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 106 RDGaHARLMVTRGVKKTPNQDPRFIIGGatVVCVAEHKVVTPEAK-RNGLKLFTSTlrcsgpDVFDLRLNSHSrLNLIQA 184
Cdd:TIGR01121 82 NTG-HVYFQVTRGVAPRNHQFPAGTVKP--VITAYTKEVPRPEENlEKGVKAITVE------DIRWLRCDIKS-LNLLGN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 185 LI---QAIQAGADEALMLDpNGFVSSCNSTNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLAEVY 260
Cdd:TIGR01121 152 VLakqEAHEKGAYEAILHR-GGTVTEGSSSNVYGIKDGVLYThPANNLILNGITRMVILACAEENGIPVKEEPFTKEELL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
7Z79_D 261 AADEAFVTGTLAGLTPVSSVDGRAL---VPlGPLTQRLDALYRAYI 303
Cdd:TIGR01121 231 NADEVFVSSTTAEITPVIEIDGQQIgdgKP-GPWTRQLQKAFEEKI 275
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
52-280 |
3.66e-47 |
|
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: 158.29 E-value: 3.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 52 GVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGMRDGAhARLMVTRGVKK--TPNQDPRF 129
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGR-LRLTVSRGPGGfgLPTSDPTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 130 IIggatvvCVAEHKVVTPEAKRNGlklfTSTLRCSGPDVFDLRLNSHSRLNLIQALIQAIQAGADEALMLDPNGFVSSCN 209
Cdd:pfam01063 80 AI------FVSALPPPPESKKKGV----ISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7Z79_D 210 STNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSSV 280
Cdd:pfam01063 150 TSNVFLVKGGTLYTpPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
26-299 |
2.69e-43 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 150.08 E-value: 2.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 26 VYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGM 105
Cdd:PRK06680 5 AYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRRNRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 106 RDGAhARLMVTRGVKKT----PNQDPRfiiggATVVCVAEHK---VVTPEAKrNGLKLFTStlrcsgPDVFDLRLNSHSR 178
Cdd:PRK06680 85 REGL-VYLQVTRGVARRdhvfPAADVK-----PSVVVFAKSVdfaRPAAAAE-TGIKVITV------PDNRWKRCDIKSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 179 LNLIQALI--QAIQAGADEALMLDpNGFVSSCNSTNFFAV-RNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDF 254
Cdd:PRK06680 152 GLLPNVLAkqAAKEAGAQEAWMVD-DGFVTEGASSNAWIVtKDGKLVTrPADNFILPGITRHTLIDLAKELGLEVEERPF 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
7Z79_D 255 TLAEVYAADEAFVTGTLAGLTPVSSVDGRAL---VPlGPLTQRLDALY 299
Cdd:PRK06680 231 TLQEAYAAREAFITAASSFVFPVVQIDGKQIgngKP-GPIAKRLREAY 277
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
44-299 |
1.37e-41 |
|
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: 144.76 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 44 DAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMtRAQTKQVVVDTFLRNGMRDGAhARLMVTRGVkktp 123
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPD-LPRLRAALESLLAANDIDEGR-IRLILSRGP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 124 nQDPRFIIGGA---TVVCVAehKVVTPEAKRNGLKLFTSTLRCSGPDVFdLRLNSHSRLNLIQALIQAIQAGADEALMLD 200
Cdd:cd01559 75 -GGRGYAPSVCpgpALYVSV--IPLPPAWRQDGVRLITCPVRLGEQPLL-AGLKHLNYLENVLAKREARDRGADEALFLD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 201 PNGFVSSCNSTNFFAVRNGALWTSSGRYC-FNGITRATVVRLAREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSS 279
Cdd:cd01559 151 TDGRVIEGTASNLFFVKDGELVTPSLDRGgLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTA 230
|
250 260
....*....|....*....|
7Z79_D 280 VDGRALVPlGPLTQRLDALY 299
Cdd:cd01559 231 IDDHDGPP-GPLTRALRELL 249
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
25-303 |
2.58e-38 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 137.02 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 25 LVYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNG 104
Cdd:PRK07650 1 LIYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDEVLLILKNLLEKNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 105 MRDgAHARLMVTRGVKktpnqDPRFIIG---GATVVC---------VAEHK--VV------TPEAKRnglklftstlrcs 164
Cdd:PRK07650 81 LEN-AYVRFNVSAGIG-----EIGLQTEmyeEPTVIVymkplappgLPAEKegVVlkqrrnTPEGAF------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 165 gpdvfdlRLNSHSRLNLIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWTSS---GryCFNGITRATVVRL 241
Cdd:PRK07650 142 -------RLKSHHYLNNILGKREIGNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSletG--ILNGITRAFVIKV 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
7Z79_D 242 AREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSSVDGRALV-PLGPLTQRLDALYRAYI 303
Cdd:PRK07650 213 LEELGIEVKEGFYTKEELLSADEVFVTNSIQEIVPLTRIEERDFPgKVGMVTKRLQNLYEMQR 275
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
50-299 |
6.35e-32 |
|
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: 119.99 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 50 GDGVWEGV---RLVDGRIVSF--DAHIDRMYEGAKSIALDigmtrAQTKQVVVDtflrngmrdgAHARLmVTRGVKKTPN 124
Cdd:cd01557 12 GQAVFEGLkayRTPDGKIVLFrpDENAERLNRSARRLGLP-----PFSVEEFID----------AIKEL-VKLDADWVPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 125 QDP-----R-FIIGGATVVCVAEHkvvtPEAKrngLKLFTS---TLRCSGPDVFDLRLNSHSR---------------LN 180
Cdd:cd01557 76 GGGaslyiRpFIFGTDPQLGVSPA----LEYL---FAVFASpvgAYFKGGEKGVSALVSSFRRaapggpgaakaggnyAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 181 LIQALIQAIQAGADEALMLDP-NGFVSSCNSTNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLAE 258
Cdd:cd01557 149 SLLAQKEAAEKGYDQALWLDGaHGYVAEVGTMNIFFVKDGELITpPLDGSILPGITRDSILELARDLGIKVEERPITRDE 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
7Z79_D 259 VYAADEAFVTGTLAGLTPVSSVDGRALVPL----GPLTQRLDALY 299
Cdd:cd01557 229 LYEADEVFATGTAAVVTPVGEIDYRGKEPGegevGPVTKKLYDLL 273
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
35-307 |
1.24e-30 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 117.04 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 35 RHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGMRDGAHARLM 114
Cdd:PRK12400 18 KQKTYIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENNNFHEDGTIYLQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 115 VTRGVKKTPNQDPRFIigGATVVCVAEHKvvtpeaKRNGLKLFTSTLRCSGPDVFDLRLNSHSrLNLIQALIQAIQA--- 191
Cdd:PRK12400 98 VSRGVQARTHTFSYDV--PPTIYAYITKK------ERPALWIEYGVRAISEPDTRWLRCDIKS-LNLLPNILAATKAerk 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 192 GADEALMLDpNGFVSSCNSTNFFAVRNGALWTSSGRY-CFNGITRATVVRLAREAGIPVHEGDFTLAEVYAADEAFVTGT 270
Cdd:PRK12400 169 GCKEALFVR-NGTVTEGSHSNFFLIKNGTLYTHPANHlILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADECFFTGT 247
|
250 260 270
....*....|....*....|....*....|....*....
7Z79_D 271 LAGLTPVSSVDGRALV--PLGPLTQRLDALYRAYIASAN 307
Cdd:PRK12400 248 TIEILPMTHLDGTAIQdgQVGPITKMLQRSFSQSLLQSN 286
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
25-295 |
2.82e-30 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 115.32 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 25 LVYVNGQfvprHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIgmtraqtkqvVVDTFLRNG 104
Cdd:PRK06092 1 MFWINGQ----PQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPL----------DDWAQLEQE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 105 MRDGAHAR------LMVTRGV-----KKTPNQDPRFIIGGATVvcvAEHKVvtpEAKRNGLKLFTSTLRCS-GPdvfdlR 172
Cdd:PRK06092 67 MKQLAAELengvlkVIISRGSggrgySPAGCAAPTRILSVSPY---PAHYS---RWREQGITLALCPTRLGrNP-----L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 173 LNSHSRLN-LIQALIQAI--QAGADEALMLDPNGFVSSCNSTNFFAVRNGALWTSSGRYC-FNGITRATVVRLAREAGIP 248
Cdd:PRK06092 136 LAGIKHLNrLEQVLIRAEleQTEADEALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCgVAGVMRQFILELLAQSGYP 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
7Z79_D 249 VHEGDFTLAEVYAADEAFVTGTLAGLTPVSSVDGRALvPLGPLTQRL 295
Cdd:PRK06092 216 VVEVDASLEELLQADEVFICNSLMPVWPVRAIGETSY-SSGTLTRYL 261
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
26-309 |
3.09e-28 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 110.45 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 26 VYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGM 105
Cdd:PRK07544 11 IWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVAEIDAAKKETLAANGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 106 RDgAHARLMVTRGVK----KTPNQDPRFIIGgatvvCVAEHKVVTPEAKRNGLKLFTSTLRCSGPDVfdlrLNSHSR--- 178
Cdd:PRK07544 91 TD-AYVRPVAWRGSEmmgvSAQQNKIHLAIA-----AWEWPSYFDPEAKMKGIRLDIAKWRRPDPET----APSAAKaag 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 179 LNLIQALI--QAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWTSSGRyCF-NGITRATVVRLAREAGIPVHEGDFT 255
Cdd:PRK07544 161 LYMICTISkhAAEAKGYADALMLDYRGYVAEATGANIFFVKDGVIHTPTPD-CFlDGITRQTVIELAKRRGIEVVERHIM 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
7Z79_D 256 LAEVYAADEAFVTGTLAGLTPVSSVDGRALVPlGPLTQRLDALYRAYIASANEA 309
Cdd:PRK07544 240 PEELAGFSECFLTGTAAEVTPVSEIGEYRFTP-GAITRDLMDDYEALVRPRAAA 292
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
25-307 |
1.27e-26 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 106.19 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 25 LVYVNGQFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDtflrng 104
Cdd:PRK13356 8 WTFFDGEWHEGNVPIMGPADHAAWLGSTVFDGARAFEGVTPDLDLHCARVNRSAEALGLKPTVSAEEIEALARE------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 105 mrdgaharlmvtrGVKKTPNQDPRFI-------IGGATVVcvaehkVVTPEAKRNGLKLFTSTLrcSGPDVFDLRLNSHS 177
Cdd:PRK13356 82 -------------GLKRFDPDTALYIrpmywaeDGFASGV------APDPESTRFALCLEEAPM--PEPTGFSLTLSPFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 178 RL----------------NLIQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWTSSGRYCF-NGITRATVVR 240
Cdd:PRK13356 141 RPtlemaptdakagclypNNARALREARSRGFDNALVLDMLGNVAETATSNVFMVKDGVVFTPVPNGTFlNGITRQRVIA 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
7Z79_D 241 LAREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSSVDGRALVPlGPLTQRLDALYRAYIASAN 307
Cdd:PRK13356 221 LLREDGVTVVETTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSLQP-GPVTRRARELYWDWAHGGR 286
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
22-307 |
3.45e-22 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 94.26 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 22 DAVLVYVNG-----QFVPRHQAVVSVFDAGYVCGDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIAL---DIGMTRAQTk 93
Cdd:PRK07849 5 PPVVVTLDPyggseRVHDPSAPLLHADDLAAVRGDGVFETLLVRDGRPCNLEAHLERLARSAALLDLpepDLDRWRRAV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 94 QVVVDTFLRNGmrDGAHARLMVTRGVKKTpnqdprfiiGGATV-VCVAEHKVVTPEAKRNGLKLFTSTlRCSGPDVFDL- 171
Cdd:PRK07849 84 ELAIEEWRAPE--DEAALRLVYSRGRESG---------GAPTAwVTVSPVPERVARARREGVSVITLD-RGYPSDAAERa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 172 --RLNSHSRLNL---IQALIQAIQAGADEALMLDPNGFVSSCNSTNFFAVRNGALWTSSGRY-CFNGITRATVVRLAREA 245
Cdd:PRK07849 152 pwLLAGAKTLSYavnMAALRYAARRGADDVIFTSTDGYVLEGPTSTVVIATDDRLLTPPPWYgILPGTTQAALFEVAREK 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
7Z79_D 246 GIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSSVDGRALvPLGPLTQRLDALYRAYIASAN 307
Cdd:PRK07849 232 GWDCEYRALRPADLFAADGVWLVSSVRLAARVHTLDGRPL-PRDPLADELTELVDAAIVSDR 292
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
183-298 |
6.31e-13 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 68.25 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 183 QALIQAIQAGADEALMLDP--NGFVSSCNSTNFFAVRNGALWTSSgrycFN-----GITRATVVRLAREAGIPVHEGDFT 255
Cdd:PRK13357 206 LAQAEAKEKGCDQVLYLDAveHTYIEEVGGMNFFFITKDGTVTPP----LSgsilpGITRDSLLQLAEDLGLTVEERPVS 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
7Z79_D 256 LAEVYAA------DEAFVTGTLAGLTPVSSV---DGRALVP---LGPLTQRL-DAL 298
Cdd:PRK13357 282 IDEWQADaasgefTEAFACGTAAVITPIGGIkykDKEFVIGdgeVGPVTQKLyDEL 337
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
38-298 |
9.93e-13 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 67.73 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 38 AVVSVFDAGYVC-GDGVWEGVRLVDGRIVSFDAHIDRMYEGAKSIALDIGMTRAQTKQVVVDTFLRNGMRDGAhARLMVT 116
Cdd:PLN02845 54 AMVIPLDDHMVHrGHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAASGCRNGS-LRYWLS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 117 RG-----VKKTPNQDPRFIiggatVVCVAEhkvvTPEAKRN-GLKLFTSTLRCSGPDVFDLRLNSHsrlnLIQALIQ--A 188
Cdd:PLN02845 133 AGpggfsLSPSGCSEPAFY-----AVVIED----TYAQDRPeGVKVVTSSVPIKPPQFATVKSVNY----LPNALSQmeA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 189 IQAGADEALMLDPNGFVSSCNSTNF-FAVRNGALWTSSGRYCFNGITRATVVRLA---REAGI--PVHEGDFTLAEVYAA 262
Cdd:PLN02845 200 EERGAFAGIWLDEEGFVAEGPNMNVaFLTNDGELVLPPFDKILSGCTARRVLELAprlVSPGDlrGVKQRKISVEEAKAA 279
|
250 260 270
....*....|....*....|....*....|....*...
7Z79_D 263 DEAFVTGTLAGLTPVSSVDGRALV--PLGPLTQRLDAL 298
Cdd:PLN02845 280 DEMMLIGSGVPVLPIVSWDGQPIGdgKVGPITLALHDL 317
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
61-304 |
4.36e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 59.22 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 61 DGRIVSFDAHIDRMYEGAKSI---ALDIGMTRAQTKQVVVDT---------------FLRNGMRDGAHARLMVTRGVKKT 122
Cdd:PRK09266 35 DGRVRGLDLHLQRLRRASRELfgaALDDDRVRAQLRAALAAGpadasvrvtvfapdfDFRNPLADVAPDVLVATSPPADG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 123 PnqdprfiiGGATVVCVAEHKVVTPEAKRNGLklftstlrcsgpdvfdlrlnshsrLNLIQALIQAIQAGADEALMLDPN 202
Cdd:PRK09266 115 P--------AGPLRLQSVPYERELPHIKHVGT------------------------FGQLHLRRLAQRAGFDDALFVDPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 203 GFVSSCNSTNF-FAVRNGALWTSSGryCFNGITRATVVRLAREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSSVD 281
Cdd:PRK09266 163 GRVSEGATWNLgFWDGGAVVWPQAP--ALPGVTMALLQRGLERLGIPQRTRPVTLADLGRFAGAFACNAWRGQRAVSAID 240
|
250 260
....*....|....*....|...
7Z79_D 282 GralVPLGPLTQRLDALYRAYIA 304
Cdd:PRK09266 241 D---VALPDSHALLELLRRAYEA 260
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
205-280 |
2.77e-07 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 51.39 E-value: 2.77e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7Z79_D 205 VSSCNstnFFAVRNGALWTSSGR-YCFNGITRATVVRLAREAGIPVHEGDFTLAEVYAADEAFVTGTLAGLTPVSSV 280
Cdd:PLN02782 286 VSSCN---IFIVKDNVISTPAIKgTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSI 359
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
181-280 |
6.36e-07 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 50.31 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 181 LIQALIQAIQAGADEALMLDP--NGFVSSCNSTNFFAVRNGALWT--SSGRyCFNGITRATVVRLAREAGIPVHEGDFTL 256
Cdd:PLN03117 206 VVKSLIEAKSSGFSDVLFLDAatGKNIEELSACNIFILKGNIVSTppTSGT-ILPGVTRKSISELARDIGYQVEERDVSV 284
|
90 100
....*....|....*....|....
7Z79_D 257 AEVYAADEAFVTGTLAGLTPVSSV 280
Cdd:PLN03117 285 DELLEAEEVFCTGTAVVVKAVETV 308
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
181-280 |
1.81e-06 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 48.95 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 181 LIQALIQAIQAGADEALMLDP--NGFVSSCNSTNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLA 257
Cdd:PLN02259 243 VLKALSRAKSRGFSDVLYLDSvkKKYLEEASSCNVFVVKGRTISTpATNGTILEGITRKSVMEIASDQGYQVVEKAVHVD 322
|
90 100
....*....|....*....|...
7Z79_D 258 EVYAADEAFVTGTLAGLTPVSSV 280
Cdd:PLN02259 323 EVMDADEVFCTGTAVVVAPVGTI 345
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
181-280 |
2.97e-05 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 45.09 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7Z79_D 181 LIQALIQAIQAGADEALMLDPN--GFVSSCNSTNFFAVRNGALWT-SSGRYCFNGITRATVVRLAREAGIPVHEGDFTLA 257
Cdd:PLN02883 239 VLEVMRRAKSRGFSDVLYLDADtgKNIEEVSAANIFLVKGNIIVTpATSGTILGGITRKSIIEIALDLGYKVEERRVPVE 318
|
90 100
....*....|....*....|...
7Z79_D 258 EVYAADEAFVTGTLAGLTPVSSV 280
Cdd:PLN02883 319 ELKEAEEVFCTGTAAGVASVGSI 341
|
|
|