|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
1-268 |
4.83e-171 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 472.79 E-value: 4.83e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 1 MFLINGYKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFWPQLEQEMKTLAAEQQNGVLK 80
Cdd:PRK06092 1 MFWINGQPQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDWAQLEQEMKQLAAELENGVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 81 VVISRGSGGRGYSTLNSGPATRILSVTVYPAHYDRLRNEGMTLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNAD 160
Cdd:PRK06092 81 VIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLALCPTRLGRNPLLAGIKHLNRLEQVLIRAELEQTEAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 161 EALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMP 240
Cdd:PRK06092 161 EALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSLMP 240
|
250 260
....*....|....*....|....*...
gi 446400848 241 VMPVRACGDVSFSSATLYEYLAPLCERP 268
Cdd:PRK06092 241 VWPVRAIGETSYSSGTLTRYLQPLCERL 268
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
3-263 |
2.96e-161 |
|
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 132501 Cd Length: 261 Bit Score: 447.80 E-value: 2.96e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 3 LINGYKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFWPQLEQEMKTLAAEQQNGVLKVV 82
Cdd:TIGR03461 1 WVNGVLQTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLPDWDALREEMAQLAAGYSLGVLKVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 83 ISRGSGGRGYSTLNSGPATRILSVTVYPAHYDRLRNEGMTLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEA 162
Cdd:TIGR03461 81 ISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRLGVSPVRLGRNPLLAGIKHLNRLEQVLIKAELENSEADEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 163 LVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVM 242
Cdd:TIGR03461 161 LVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSADEVFITNSLMGVV 240
|
250 260
....*....|....*....|.
gi 446400848 243 PVRACGDVSFSSATLYEYLAP 263
Cdd:TIGR03461 241 PVNAIGETSYPSRTLTRLLQP 261
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
16-265 |
7.13e-110 |
|
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: 317.33 E-value: 7.13e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 16 DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFWPQLEQEMKTLAAEQQ--NGVLKVVISRGSGGRGYS 93
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAANDidEGRIRLILSRGPGGRGYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 94 TLNSGPATRILSVTVYPAhydRLRNEGMTLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTE 173
Cdd:cd01559 81 PSVCPGPALYVSVIPLPP---AWRQDGVRLITCPVRLGEQPLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRVIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 174 CCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVMPVRACGDVSFS 253
Cdd:cd01559 158 GTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDDHDGP 237
|
250
....*....|..
gi 446400848 254 SATLYEYLAPLC 265
Cdd:cd01559 238 PGPLTRALRELL 249
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
1-254 |
2.54e-82 |
|
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: 248.57 E-value: 2.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 1 MFLING----YKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMI-FCDFWPQLEQEMKTL--AAE 73
Cdd:COG0115 2 LIWLNGelvpEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIpIPYTEEELLEAIRELvaANG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 74 QQNGVLKVVISRGSGGRGYSTLNSGPaTRILSVTVYPAHYDRLRNEGMTLALSPVRLGRNPHLAGIKHLNRLEQVLIRSH 153
Cdd:COG0115 82 LEDGYIRPQVTRGVGGRGVFAEEYEP-TVIIIASPLPAYPAEAYEKGVRVITSPYRRAAPGGLGGIKTGNYLNNVLAKQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 154 LEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMV 233
Cdd:COG0115 161 AKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVF 240
|
250 260
....*....|....*....|.
gi 446400848 234 ICNALMPVMPVRACGDVSFSS 254
Cdd:COG0115 241 LTGTAAEVTPVTEIDGRPIGD 261
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
24-247 |
3.20e-58 |
|
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: 184.87 E-value: 3.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 24 GCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDF-WPQLEQEMKTLAAEQQ--NGVLKVVISRGSGGRGYSTLNsgpA 100
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFdEEDLRKIIEELLKANGlgVGRLRLTVSRGPGGFGLPTSD---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 101 TRILSVTVYPAHYDRLRNEGmtlALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLF 180
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGV---ISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSNVF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446400848 181 WRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVMPVRAC 247
Cdd:pfam01063 155 LVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
1-268 |
4.83e-171 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 472.79 E-value: 4.83e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 1 MFLINGYKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFWPQLEQEMKTLAAEQQNGVLK 80
Cdd:PRK06092 1 MFWINGQPQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDWAQLEQEMKQLAAELENGVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 81 VVISRGSGGRGYSTLNSGPATRILSVTVYPAHYDRLRNEGMTLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNAD 160
Cdd:PRK06092 81 VIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLALCPTRLGRNPLLAGIKHLNRLEQVLIRAELEQTEAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 161 EALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMP 240
Cdd:PRK06092 161 EALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSLMP 240
|
250 260
....*....|....*....|....*...
gi 446400848 241 VMPVRACGDVSFSSATLYEYLAPLCERP 268
Cdd:PRK06092 241 VWPVRAIGETSYSSGTLTRYLQPLCERL 268
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
3-263 |
2.96e-161 |
|
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC lyase), EC 4.1.3.38, the PabC protein of PABA biosynthesis. PABA (para-aminobenzoate) is a precursor of folate, needed for de novo purine biosynthesis. This enzyme is a pyridoxal-phosphate-binding protein in the class IV aminotransferase family (pfam01063). [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid]
Pssm-ID: 132501 Cd Length: 261 Bit Score: 447.80 E-value: 2.96e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 3 LINGYKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFWPQLEQEMKTLAAEQQNGVLKVV 82
Cdd:TIGR03461 1 WVNGVLQTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLPDWDALREEMAQLAAGYSLGVLKVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 83 ISRGSGGRGYSTLNSGPATRILSVTVYPAHYDRLRNEGMTLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEA 162
Cdd:TIGR03461 81 ISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRLGVSPVRLGRNPLLAGIKHLNRLEQVLIKAELENSEADEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 163 LVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVM 242
Cdd:TIGR03461 161 LVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSADEVFITNSLMGVV 240
|
250 260
....*....|....*....|.
gi 446400848 243 PVRACGDVSFSSATLYEYLAP 263
Cdd:TIGR03461 241 PVNAIGETSYPSRTLTRLLQP 261
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
16-265 |
7.13e-110 |
|
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: 317.33 E-value: 7.13e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 16 DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFWPQLEQEMKTLAAEQQ--NGVLKVVISRGSGGRGYS 93
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAANDidEGRIRLILSRGPGGRGYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 94 TLNSGPATRILSVTVYPAhydRLRNEGMTLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTE 173
Cdd:cd01559 81 PSVCPGPALYVSVIPLPP---AWRQDGVRLITCPVRLGEQPLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRVIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 174 CCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVMPVRACGDVSFS 253
Cdd:cd01559 158 GTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDDHDGP 237
|
250
....*....|..
gi 446400848 254 SATLYEYLAPLC 265
Cdd:cd01559 238 PGPLTRALRELL 249
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
1-254 |
2.54e-82 |
|
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: 248.57 E-value: 2.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 1 MFLING----YKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMI-FCDFWPQLEQEMKTL--AAE 73
Cdd:COG0115 2 LIWLNGelvpEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIpIPYTEEELLEAIRELvaANG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 74 QQNGVLKVVISRGSGGRGYSTLNSGPaTRILSVTVYPAHYDRLRNEGMTLALSPVRLGRNPHLAGIKHLNRLEQVLIRSH 153
Cdd:COG0115 82 LEDGYIRPQVTRGVGGRGVFAEEYEP-TVIIIASPLPAYPAEAYEKGVRVITSPYRRAAPGGLGGIKTGNYLNNVLAKQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 154 LEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMV 233
Cdd:COG0115 161 AKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVF 240
|
250 260
....*....|....*....|.
gi 446400848 234 ICNALMPVMPVRACGDVSFSS 254
Cdd:COG0115 241 LTGTAAEVTPVTEIDGRPIGD 261
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
16-252 |
1.05e-69 |
|
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: 215.54 E-value: 1.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 16 DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDF-WPQLEQEMKTLAAEQ--QNGVLKVVISRGSGGRGY 92
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYdREELREALKELVAANngASLYIRPLLTRGVGGLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 93 STLNSGPATRILSVTVYPAhYDRLRNEGMTLALSPVRLG-RNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWV 171
Cdd:cd00449 81 APPPSPEPTFVVFASPVGA-YAKGGEKGVRLITSPDRRRaAPGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDNGYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 172 TECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVMPVRACGDVS 251
Cdd:cd00449 160 TEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGRG 239
|
.
gi 446400848 252 F 252
Cdd:cd00449 240 I 240
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
24-247 |
3.20e-58 |
|
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: 184.87 E-value: 3.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 24 GCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDF-WPQLEQEMKTLAAEQQ--NGVLKVVISRGSGGRGYSTLNsgpA 100
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFdEEDLRKIIEELLKANGlgVGRLRLTVSRGPGGFGLPTSD---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 101 TRILSVTVYPAHYDRLRNEGmtlALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLF 180
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGV---ISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSNVF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446400848 181 WRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVMPVRAC 247
Cdd:pfam01063 155 LVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
14-246 |
5.34e-37 |
|
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: 131.57 E-value: 5.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 14 VSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFcdfWPQLEQEMKTL------AAEQQNGVLKVVISRGS 87
Cdd:cd01558 16 VFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRID---IPYTREELKELirelvaKNEGGEGDVYIQVTRGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 88 GGRGYSTLNSGPATRILSVTVYPAHYDRLRNEGMTLALSPVRlgRNPHLAgIKHLNRLEQVLIRSHLEQTNADEALVLDS 167
Cdd:cd01558 93 GPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDI--RWLRCD-IKSLNLLNNVLAKQEAKEAGADEAILLDA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446400848 168 EGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVMPVRA 246
Cdd:cd01558 170 DGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLTSTTAEVMPVVE 248
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
1-254 |
4.82e-27 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 105.82 E-value: 4.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 1 MFLINGY----KQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFWPQ--LEQEMKTLAAEQ 74
Cdd:PRK07650 1 LIYVNGQyveeEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDevLLILKNLLEKNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 75 -QNGVLKVVISRGSGGRGYSTLNSGPATRILSVTVYPAHYDRLRNEGMTLAL---SP---VRLgrnphlagiKHLNRLEQ 147
Cdd:PRK07650 81 lENAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQrrnTPegaFRL---------KSHHYLNN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 148 VLIRSHLEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEAL 227
Cdd:PRK07650 152 ILGKREIGNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELL 231
|
250 260
....*....|....*....|....*..
gi 446400848 228 QADEMVICNALMPVMPVRACGDVSFSS 254
Cdd:PRK07650 232 SADEVFVTNSIQEIVPLTRIEERDFPG 258
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
4-231 |
6.93e-24 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 97.63 E-value: 6.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 4 ING--YKQESLAVS--DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCdfwPQLEQEMK-----TLAA-E 73
Cdd:PRK08320 7 LNGefVPKEEAKVSvfDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEI---PLSKEEMTeivleTLRKnN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 74 QQNGVLKVVISRGSGGRGYSTLNSGPATRILSVTVYPAHYDRLRNEGMTLALSPVRlgRNPHLA---GIKHLNRLEQVLI 150
Cdd:PRK08320 84 LRDAYIRLVVSRGVGDLGLDPRKCPKPTVVCIAEPIGLYPGELYEKGLKVITVSTR--RNRPDAlspQVKSLNYLNNILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 151 RSHLEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQAD 230
Cdd:PRK08320 162 KIEANLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTAD 241
|
.
gi 446400848 231 E 231
Cdd:PRK08320 242 E 242
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
3-244 |
2.88e-23 |
|
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: 95.57 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 3 LINGY--KQESLAVS--DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFW-PQLEQEMKTLAAEQQ-- 75
Cdd:TIGR01121 3 LWNGQlvEREEAKIDieDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTkEELHQLLHELVEKNNln 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 76 NGVLKVVISRGSGGRGYS-TLNSGPATRILSVTVYPAHYDRLRNEGMTLALSPVRLGRnphlAGIKHLNRLEQVLIRSHL 154
Cdd:TIGR01121 83 TGHVYFQVTRGVAPRNHQfPAGTVKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLR----CDIKSLNLLGNVLAKQEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 155 EQTNADEAlVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVI 234
Cdd:TIGR01121 159 HEKGAYEA-ILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFV 237
|
250
....*....|
gi 446400848 235 CNALMPVMPV 244
Cdd:TIGR01121 238 SSTTAEITPV 247
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
3-252 |
9.87e-19 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 83.44 E-value: 9.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 3 LING----YKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFcdfWP----QLEQEMKTLAAEQ 74
Cdd:PRK06680 6 YVNGryvnHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIA---PPmtraELVEVLRELIRRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 75 Q--NGVLKVVISRGSGGR--GYSTLNSGPatrilSVTVYPAHYDRLRNE-----GMTLALSP-VRLGRnphlAGIKHLNR 144
Cdd:PRK06680 83 RvrEGLVYLQVTRGVARRdhVFPAADVKP-----SVVVFAKSVDFARPAaaaetGIKVITVPdNRWKR----CDIKSVGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 145 LEQVLIRSHLEQTNADEALVLDsEGWVTECCAANlFW--RKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQAS 222
Cdd:PRK06680 154 LPNVLAKQAAKEAGAQEAWMVD-DGFVTEGASSN-AWivTKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFT 231
|
250 260 270
....*....|....*....|....*....|
gi 446400848 223 LEEALQADEMVICNALMPVMPVRACGDVSF 252
Cdd:PRK06680 232 LQEAYAAREAFITAASSFVFPVVQIDGKQI 261
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
8-249 |
1.02e-18 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 83.46 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 8 KQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCdfwPQLEQEMKTLAAE--QQNGV----LKV 81
Cdd:PRK12479 16 EKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTI---PLTVDEMEEAVLQtlQKNEYadayIRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 82 VISRGSGGRGYSTLN-SGPATRILS--VTVYPAHYdrlRNEGMTLALSPVRlgRNPHLA---GIKHLNRLEQVLIRSHLE 155
Cdd:PRK12479 93 IVSRGKGDLGLDPRScVKPSVIIIAeqLKLFPQEF---YDNGLSVVSVASR--RNTPDAldpRIKSMNYLNNVLVKIEAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 156 QTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVIC 235
Cdd:PRK12479 168 QAGVLEALMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLT 247
|
250
....*....|....*....
gi 446400848 236 NA---LMPVMPV--RACGD 249
Cdd:PRK12479 248 GTaaeLIPVVKVdsREIGD 266
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
22-244 |
4.09e-16 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 76.59 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 22 GDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFwpqlEQE------MKTLAAEQ-QNGVLKVVISRGSGgrGYST 94
Cdd:PLN02845 67 GHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPF----DRAtlrrilLQTVAASGcRNGSLRYWLSAGPG--GFSL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 95 LNSGPATRILSVTVYPAHYDRLRNEGMTLALSPVRLgRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTEC 174
Cdd:PLN02845 141 SPSGCSEPAFYAVVIEDTYAQDRPEGVKVVTSSVPI-KPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLDEEGFVAEG 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446400848 175 CAANL-FWRKGNVVYTPRLDQAgVNGI----MRQFCIRLLAQSSYQLVEVQ-ASLEEALQADEMVICNALMPVMPV 244
Cdd:PLN02845 220 PNMNVaFLTNDGELVLPPFDKI-LSGCtarrVLELAPRLVSPGDLRGVKQRkISVEEAKAADEMMLIGSGVPVLPI 294
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
14-245 |
6.87e-15 |
|
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: 72.78 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 14 VSDRATQFGDGCFTTARVIDGKVSL----LSAHIQRLQDACQRLMIFCDFWPQlEQEMKTLAAEQQNGV----LKVVISR 85
Cdd:TIGR01122 16 VLTHALHYGTGVFEGIRAYDTDKGPaifrLKEHIQRLYDSAKIYRMEIPYSKE-ELMEATRETLRKNNLrsayIRPLVFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 86 GSGGRGYSTLNSGPATRILSVTVYPAHYDRLRNE-GMTLALSPVRlgRNPH---LAGIKHL-NRLEQVLIRSHLEQTNAD 160
Cdd:TIGR01122 95 GDGDLGLNPRAGYKPDVIIAAWPWGAYLGEEALEkGIDAKVSSWR--RNAPntiPTAAKAGgNYLNSLLAKSEARRHGYD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 161 EALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMP 240
Cdd:TIGR01122 173 EAILLDVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELYTADEAFFTGTAAE 252
|
....*
gi 446400848 241 VMPVR 245
Cdd:TIGR01122 253 ITPIR 257
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
3-244 |
6.95e-15 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 72.74 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 3 LINGYKQES-LAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFCDFwpqLEQEMKTLAAE-------Q 74
Cdd:PRK12400 13 VIDTTKQKTyIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPF---SKAELITLLYKliennnfH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 75 QNGVLKVVISRGSGGRGYSTLNSGPATrilsVTVYPAHYDR--LRNEGMTLALSP--VRLGRnphlAGIKHLNRLEQVLI 150
Cdd:PRK12400 90 EDGTIYLQVSRGVQARTHTFSYDVPPT----IYAYITKKERpaLWIEYGVRAISEpdTRWLR----CDIKSLNLLPNILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 151 RSHLEQTNADEALVLDSeGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQAD 230
Cdd:PRK12400 162 ATKAERKGCKEALFVRN-GTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQAD 240
|
250
....*....|....
gi 446400848 231 EMVICNALMPVMPV 244
Cdd:PRK12400 241 ECFFTGTTIEILPM 254
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
26-262 |
2.27e-13 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 68.46 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 26 FTTARVIDGKVSLLSAHIQRLQDACQRLmifcDF-WP----QLEQEMKTLAAEQ--QNGVLKVVISRGSGGRGYSTLNsg 98
Cdd:PRK07544 39 FEGERAYGGKIFKLREHSERLRRSAELL----DFeIPysvaEIDAAKKETLAANglTDAYVRPVAWRGSEMMGVSAQQ-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 99 paTRI-LSVTVY--PAHYDR-LRNEGMTLALSPVRlgrNPH---------LAGI-------KHlnrleqvlirsHLEQTN 158
Cdd:PRK07544 113 --NKIhLAIAAWewPSYFDPeAKMKGIRLDIAKWR---RPDpetapsaakAAGLymictisKH-----------AAEAKG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 159 ADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDqAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNAL 238
Cdd:PRK07544 177 YADALMLDYRGYVAEATGANIFFVKDGVIHTPTPD-CFLDGITRQTVIELAKRRGIEVVERHIMPEELAGFSECFLTGTA 255
|
250 260
....*....|....*....|....
gi 446400848 239 MPVMPVRACGDVSFSSATLYEYLA 262
Cdd:PRK07544 256 AEVTPVSEIGEYRFTPGAITRDLM 279
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
160-245 |
9.83e-13 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 66.71 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 160 DEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALM 239
Cdd:PRK06606 180 DEALLLDVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVIERRITRDELYIADEVFFTGTAA 259
|
....*.
gi 446400848 240 PVMPVR 245
Cdd:PRK06606 260 EVTPIR 265
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
22-256 |
1.13e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 66.16 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 22 GDGCFTTARVIDGKVSLLSAHIQRLQDACQRLmifcdFWPQLEQEM------KTLAAEQQNGVLKVVISRGSGGRGYSTl 95
Cdd:PRK09266 24 NYGHFTSMQVRDGRVRGLDLHLQRLRRASREL-----FGAALDDDRvraqlrAALAAGPADASVRVTVFAPDFDFRNPL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 96 nSGPATRILsVTVYPAhydrlrnegMTLALSPVRLGRNPH---LAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVT 172
Cdd:PRK09266 98 -ADVAPDVL-VATSPP---------ADGPAGPLRLQSVPYereLPHIKHVGTFGQLHLRRLAQRAGFDDALFVDPDGRVS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 173 ECCAANL-FWRKGNVVYtPrldQAGVNGIMRQfciRLLAQSSYQLVEVQAS----LEEALQADEMVICNALMPVMPVRAC 247
Cdd:PRK09266 167 EGATWNLgFWDGGAVVW-P---QAPALPGVTM---ALLQRGLERLGIPQRTrpvtLADLGRFAGAFACNAWRGQRAVSAI 239
|
....*....
gi 446400848 248 GDVSFSSAT 256
Cdd:PRK09266 240 DDVALPDSH 248
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
160-252 |
7.57e-11 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 61.12 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 160 DEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALM 239
Cdd:PRK13356 173 DNALVLDMLGNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTGNYS 252
|
90
....*....|...
gi 446400848 240 PVMPVRACGDVSF 252
Cdd:PRK13356 253 KVVPVTRFDDRSL 265
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
11-232 |
3.97e-09 |
|
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: 56.05 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 11 SLAVSDRATQFGDGCFTTARVI---DGKVSL--LSAHIQRLQDACQRLMIfcdfwPQLEQEMKTLAAEQqngVLKVVISR 85
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYrtpDGKIVLfrPDENAERLNRSARRLGL-----PPFSVEEFIDAIKE---LVKLDADW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 86 GSGGRGYS------------TLNSGPATR-ILSVTVYP--AHYDRLRNEGMTLALSPVRlgRNPHLAGIKHL--NRLEQV 148
Cdd:cd01557 73 VPYGGGASlyirpfifgtdpQLGVSPALEyLFAVFASPvgAYFKGGEKGVSALVSSFRR--AAPGGPGAAKAggNYAASL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 149 LIRSHLEQTNADEALVLDSE-GWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEAL 227
Cdd:cd01557 151 LAQKEAAEKGYDQALWLDGAhGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELY 230
|
....*
gi 446400848 228 QADEM 232
Cdd:cd01557 231 EADEV 235
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
22-230 |
1.05e-08 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 54.96 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 22 GDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIFC---DFWPQL-EQEMKTLAAEQQNGVLKVVISRGSGGrgystlnS 97
Cdd:PRK07849 38 GDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPEpdlDRWRRAvELAIEEWRAPEDEAALRLVYSRGRES-------G 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 98 GPATRILSVTVYPAHYDRLRNEGMTLALS----PVRLG-RNP-HLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWV 171
Cdd:PRK07849 111 GAPTAWVTVSPVPERVARARREGVSVITLdrgyPSDAAeRAPwLLAGAKTLSYAVNMAALRYAARRGADDVIFTSTDGYV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446400848 172 TECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQAD 230
Cdd:PRK07849 191 LEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAAD 249
|
|
| PRK07101 |
PRK07101 |
hypothetical protein; Provisional |
26-240 |
5.79e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235934 Cd Length: 187 Bit Score: 45.70 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 26 FTTARVIDGKVSLLSAHIQRLQDAcqrlmiFCDFWPQLE----QEMKTLAAEQQNGVLKVVISRGSG----------GRG 91
Cdd:PRK07101 6 FETIAIEDGEIQNLSYHQQRYERT------LAEFYGKEApfdlAEIIQPPTELQEGLVRCRIDYNAEiyqvqyfpyqRRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 92 YSTLnsgpatRIlsvtVYPAHYDRlrnegmtlalspvrlgrnphlaGIKHLNRleqVLIRSHLEQT-NADEALVLdSEGW 170
Cdd:PRK07101 80 IRSF------QP----VYCDDIDY----------------------SLKYTDR---SALNELFAQKgECDEIIII-KNGL 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 171 VTECCAANLFWRKGNVVYTPrlDQAGVNGIMRQfciRLLAQSsyQLVEVQASLEEALQADEMVICNALMP 240
Cdd:PRK07101 124 VTDTSIGNLAFFDGKQWFTP--KKPLLKGTQRA---RLLDEG--KIKEKDITVEDLLQYEEIRLINAMNG 186
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
137-244 |
8.45e-06 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 46.25 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 137 AGIKHLNRLEQVL-IRSHLEQTNADEALVLDS--EGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSS 213
Cdd:PLN02259 232 GGVKSITNYAPVLkALSRAKSRGFSDVLYLDSvkKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQG 311
|
90 100 110
....*....|....*....|....*....|.
gi 446400848 214 YQLVEVQASLEEALQADEMVICNALMPVMPV 244
Cdd:PLN02259 312 YQVVEKAVHVDEVMDADEVFCTGTAVVVAPV 342
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
171-252 |
4.37e-05 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 44.15 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 171 VTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEmVICNALMPVmpVRACGDV 250
Cdd:PLN03117 232 IEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEE-VFCTGTAVV--VKAVETV 308
|
..
gi 446400848 251 SF 252
Cdd:PLN03117 309 TF 310
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
137-260 |
5.25e-04 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 40.85 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446400848 137 AGIKHLNRLEQVL-IRSHLEQTNADEALVLDSEGW--VTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSS 213
Cdd:PLN02883 228 GGVKAISNYGPVLeVMRRAKSRGFSDVLYLDADTGknIEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLG 307
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446400848 214 YQLVEVQASLEEALQADEmVICNAlmPVMPVRACGDVSFSSaTLYEY 260
Cdd:PLN02883 308 YKVEERRVPVEELKEAEE-VFCTG--TAAGVASVGSITFKN-TRTEY 350
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
170-244 |
1.67e-03 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 39.45 E-value: 1.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446400848 170 WVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEEALQADEMVICNALMPVMPV 244
Cdd:PLN02782 282 YLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPV 356
|
|
| |
