|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
1-268 |
2.15e-172 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 476.26 E-value: 2.15e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 1 MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQNGVLK 80
Cdd:PRK06092 1 MFWINGQPQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDWAQLEQEMKQLAAELENGVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 81 VVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNAD 160
Cdd:PRK06092 81 VIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLALCPTRLGRNPLLAGIKHLNRLEQVLIRAELEQTEAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 161 EALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMP 240
Cdd:PRK06092 161 EALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSLMP 240
|
250 260
....*....|....*....|....*...
gi 1487551604 241 VMPVCACGDVSFSSATLYEYLAPLCERP 268
Cdd:PRK06092 241 VWPVRAIGETSYSSGTLTRYLQPLCERL 268
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
3-263 |
3.34e-165 |
|
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: 457.82 E-value: 3.34e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 3 LINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQNGVLKVV 82
Cdd:TIGR03461 1 WVNGVLQTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLPDWDALREEMAQLAAGYSLGVLKVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 83 ISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEA 162
Cdd:TIGR03461 81 ISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRLGVSPVRLGRNPLLAGIKHLNRLEQVLIKAELENSEADEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 163 LVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVM 242
Cdd:TIGR03461 161 LVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSADEVFITNSLMGVV 240
|
250 260
....*....|....*....|.
gi 1487551604 243 PVCACGDVSFSSATLYEYLAP 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 |
1.72e-112 |
|
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: 323.88 E-value: 1.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 16 DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQ--NGVLKVVISRGSGGRGYS 93
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAANDidEGRIRLILSRGPGGRGYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 94 TLNSGPATRILSVTAYPAhydRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTE 173
Cdd:cd01559 81 PSVCPGPALYVSVIPLPP---AWRQDGVRLITCPVRLGEQPLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRVIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 174 CCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCACGDVSFS 253
Cdd:cd01559 158 GTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDDHDGP 237
|
250
....*....|..
gi 1487551604 254 SATLYEYLAPLC 265
Cdd:cd01559 238 PGPLTRALRELL 249
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
1-254 |
2.11e-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: 248.95 E-value: 2.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 1 MFLING----HKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDF-WPQLEQEMKTL--AAE 73
Cdd:COG0115 2 LIWLNGelvpEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYtEEELLEAIRELvaANG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 74 QQNGVLKVVISRGSGGRGYSTLNSGPaTRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSH 153
Cdd:COG0115 82 LEDGYIRPQVTRGVGGRGVFAEEYEP-TVIIIASPLPAYPAEAYEKGVRVITSPYRRAAPGGLGGIKTGNYLNNVLAKQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 154 LEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMV 233
Cdd:COG0115 161 AKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVF 240
|
250 260
....*....|....*....|.
gi 1487551604 234 ICNALMPVMPVCACGDVSFSS 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 |
1.77e-59 |
|
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: 188.34 E-value: 1.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 24 GCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDF-WPQLEQEMKTLAAEQQ--NGVLKVVISRGSGGRGYSTLNsgpA 100
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFdEEDLRKIIEELLKANGlgVGRLRLTVSRGPGGFGLPTSD---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 101 TRILSVTAYPAHYDRLRNEGITlalSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLF 180
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVIS---SLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSNVF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487551604 181 WRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCAC 247
Cdd:pfam01063 155 LVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
1-268 |
2.15e-172 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 476.26 E-value: 2.15e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 1 MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQNGVLK 80
Cdd:PRK06092 1 MFWINGQPQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDWAQLEQEMKQLAAELENGVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 81 VVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNAD 160
Cdd:PRK06092 81 VIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLALCPTRLGRNPLLAGIKHLNRLEQVLIRAELEQTEAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 161 EALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMP 240
Cdd:PRK06092 161 EALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSLMP 240
|
250 260
....*....|....*....|....*...
gi 1487551604 241 VMPVCACGDVSFSSATLYEYLAPLCERP 268
Cdd:PRK06092 241 VWPVRAIGETSYSSGTLTRYLQPLCERL 268
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
3-263 |
3.34e-165 |
|
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: 457.82 E-value: 3.34e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 3 LINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQNGVLKVV 82
Cdd:TIGR03461 1 WVNGVLQTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLPDWDALREEMAQLAAGYSLGVLKVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 83 ISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEA 162
Cdd:TIGR03461 81 ISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRLGVSPVRLGRNPLLAGIKHLNRLEQVLIKAELENSEADEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 163 LVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVM 242
Cdd:TIGR03461 161 LVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSADEVFITNSLMGVV 240
|
250 260
....*....|....*....|.
gi 1487551604 243 PVCACGDVSFSSATLYEYLAP 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 |
1.72e-112 |
|
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: 323.88 E-value: 1.72e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 16 DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQLEQEMKTLAAEQQ--NGVLKVVISRGSGGRGYS 93
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAANDidEGRIRLILSRGPGGRGYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 94 TLNSGPATRILSVTAYPAhydRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTE 173
Cdd:cd01559 81 PSVCPGPALYVSVIPLPP---AWRQDGVRLITCPVRLGEQPLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRVIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 174 CCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCACGDVSFS 253
Cdd:cd01559 158 GTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDDHDGP 237
|
250
....*....|..
gi 1487551604 254 SATLYEYLAPLC 265
Cdd:cd01559 238 PGPLTRALRELL 249
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
1-254 |
2.11e-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: 248.95 E-value: 2.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 1 MFLING----HKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDF-WPQLEQEMKTL--AAE 73
Cdd:COG0115 2 LIWLNGelvpEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYtEEELLEAIRELvaANG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 74 QQNGVLKVVISRGSGGRGYSTLNSGPaTRILSVTAYPAHYDRLRNEGITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSH 153
Cdd:COG0115 82 LEDGYIRPQVTRGVGGRGVFAEEYEP-TVIIIASPLPAYPAEAYEKGVRVITSPYRRAAPGGLGGIKTGNYLNNVLAKQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 154 LEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMV 233
Cdd:COG0115 161 AKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVF 240
|
250 260
....*....|....*....|.
gi 1487551604 234 ICNALMPVMPVCACGDVSFSS 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 |
5.02e-71 |
|
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: 219.01 E-value: 5.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 16 DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDF-WPQLEQEMKTLAAEQ--QNGVLKVVISRGSGGRGY 92
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYdREELREALKELVAANngASLYIRPLLTRGVGGLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 93 STLNSGPATRILSVTAYPAhYDRLRNEGITLALSPVRLG-RNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWV 171
Cdd:cd00449 81 APPPSPEPTFVVFASPVGA-YAKGGEKGVRLITSPDRRRaAPGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDNGYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 172 TECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCACGDVS 251
Cdd:cd00449 160 TEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGRG 239
|
.
gi 1487551604 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 |
1.77e-59 |
|
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: 188.34 E-value: 1.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 24 GCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDF-WPQLEQEMKTLAAEQQ--NGVLKVVISRGSGGRGYSTLNsgpA 100
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFdEEDLRKIIEELLKANGlgVGRLRLTVSRGPGGFGLPTSD---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 101 TRILSVTAYPAHYDRLRNEGITlalSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTECCAANLF 180
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVIS---SLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSNVF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487551604 181 WRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPVCAC 247
Cdd:pfam01063 155 LVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
3-246 |
1.01e-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: 133.49 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 3 LING----HKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIScdfWPQLEQEMKTL------AA 72
Cdd:cd01558 1 YLNGeyvpREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRID---IPYTREELKELirelvaKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 73 EQQNGVLKVVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRlgRNPHLAgIKHLNRLEQVLIRS 152
Cdd:cd01558 78 EGGEGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDI--RWLRCD-IKSLNLLNNVLAKQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 153 HLEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEM 232
Cdd:cd01558 155 EAKEAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEV 234
|
250
....*....|....
gi 1487551604 233 VICNALMPVMPVCA 246
Cdd:cd01558 235 FLTSTTAEVMPVVE 248
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
1-254 |
1.17e-28 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 110.06 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 1 MFLINGH----KQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWPQ--LEQEMKTLAAEQ 74
Cdd:PRK07650 1 LIYVNGQyveeEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEWTMTKDevLLILKNLLEKNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 75 -QNGVLKVVISRGSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNEGITLAL---SP---VRLgrnphlagiKHLNRLEQ 147
Cdd:PRK07650 81 lENAYVRFNVSAGIGEIGLQTEMYEEPTVIVYMKPLAPPGLPAEKEGVVLKQrrnTPegaFRL---------KSHHYLNN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 148 VLIRSHLEQTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESL 227
Cdd:PRK07650 152 ILGKREIGNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELL 231
|
250 260
....*....|....*....|....*..
gi 1487551604 228 QADEMVICNALMPVMPVCACGDVSFSS 254
Cdd:PRK07650 232 SADEVFVTNSIQEIVPLTRIEERDFPG 258
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
3-244 |
1.11e-24 |
|
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: 99.43 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 3 LINGH--KQESLAVS--DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFW-PQLEQEMKTLAAEQQ-- 75
Cdd:TIGR01121 3 LWNGQlvEREEAKIDieDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTkEELHQLLHELVEKNNln 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 76 NGVLKVVISRGSGGRGYSTlnsgPATRILSV-TAYPAHYDR-LRN--EGITLALSP-VRLGRnphlAGIKHLNRLEQVLI 150
Cdd:TIGR01121 83 TGHVYFQVTRGVAPRNHQF----PAGTVKPViTAYTKEVPRpEENleKGVKAITVEdIRWLR----CDIKSLNLLGNVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 151 RSHLEQTNADEAlVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQAD 230
Cdd:TIGR01121 155 KQEAHEKGAYEA-ILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNAD 233
|
250
....*....|....
gi 1487551604 231 EMVICNALMPVMPV 244
Cdd:TIGR01121 234 EVFVSSTTAEITPV 247
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
21-231 |
3.07e-24 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 98.40 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 21 FGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCdfwPQLEQEMK-----TLAA-EQQNGVLKVVISRGSGGRGYST 94
Cdd:PRK08320 28 YGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEI---PLSKEEMTeivleTLRKnNLRDAYIRLVVSRGVGDLGLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 95 LNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRlgRNPHLA---GIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWV 171
Cdd:PRK08320 105 RKCPKPTVVCIAEPIGLYPGELYEKGLKVITVSTR--RNRPDAlspQVKSLNYLNNILAKIEANLAGVDEAIMLNDEGYV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 172 TECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADE 231
Cdd:PRK08320 183 AEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTADE 242
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
3-252 |
4.29e-21 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 89.99 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 3 LING----HKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIScdfWP----QLEQEMKTLAAEQ 74
Cdd:PRK06680 6 YVNGryvnHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIA---PPmtraELVEVLRELIRRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 75 Q--NGVLKVVISRGSGGR--GYSTLNSGPAtriLSVTAYPAhyDRLRNE-----GITLALSP-VRLGRnphlAGIKHLNR 144
Cdd:PRK06680 83 RvrEGLVYLQVTRGVARRdhVFPAADVKPS---VVVFAKSV--DFARPAaaaetGIKVITVPdNRWKR----CDIKSVGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 145 LEQVLIRSHLEQTNADEALVLDsEGWVTECCAANlFW--RKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQAS 222
Cdd:PRK06680 154 LPNVLAKQAAKEAGAQEAWMVD-DGFVTEGASSN-AWivTKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFT 231
|
250 260 270
....*....|....*....|....*....|
gi 1487551604 223 LEESLQADEMVICNALMPVMPVCACGDVSF 252
Cdd:PRK06680 232 LQEAYAAREAFITAASSFVFPVVQIDGKQI 261
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
8-244 |
2.17e-18 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 82.69 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 8 KQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCdfwPQLEQEMKTLAAE--QQNGV----LKV 81
Cdd:PRK12479 16 EKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTI---PLTVDEMEEAVLQtlQKNEYadayIRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 82 VISRGSGGRGYSTLN-SGPATRILS--VTAYPAHYdrlRNEGITLALSPVRlgRNPHLA---GIKHLNRLEQVLIRSHLE 155
Cdd:PRK12479 93 IVSRGKGDLGLDPRScVKPSVIIIAeqLKLFPQEF---YDNGLSVVSVASR--RNTPDAldpRIKSMNYLNNVLVKIEAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 156 QTNADEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVIC 235
Cdd:PRK12479 168 QAGVLEALMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLT 247
|
....*....
gi 1487551604 236 NALMPVMPV 244
Cdd:PRK12479 248 GTAAELIPV 256
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
3-244 |
5.49e-17 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 78.52 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 3 LINGHKQES-LAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFwpqLEQEMKTLAAE-------Q 74
Cdd:PRK12400 13 VIDTTKQKTyIELEERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPF---SKAELITLLYKliennnfH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 75 QNGVLKVVISRGSGGRGYSTLNSGPATrilsVTAYPAHYDR--LRNE-GITLALSP-VRLGRnphlAGIKHLNRLEQVLI 150
Cdd:PRK12400 90 EDGTIYLQVSRGVQARTHTFSYDVPPT----IYAYITKKERpaLWIEyGVRAISEPdTRWLR----CDIKSLNLLPNILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 151 RSHLEQTNADEALVLDSeGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQAD 230
Cdd:PRK12400 162 ATKAERKGCKEALFVRN-GTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQAD 240
|
250
....*....|....
gi 1487551604 231 EMVICNALMPVMPV 244
Cdd:PRK12400 241 ECFFTGTTIEILPM 254
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
22-245 |
2.52e-16 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 77.36 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 22 GDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFwpqlEQE------MKTLAAEQ-QNGVLKVVISRGSGgrGYST 94
Cdd:PLN02845 67 GHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPF----DRAtlrrilLQTVAASGcRNGSLRYWLSAGPG--GFSL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 95 LNSGPATRILSVTAYPAHYDRLRNEGITLALSPVRLgRNPHLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVTEC 174
Cdd:PLN02845 141 SPSGCSEPAFYAVVIEDTYAQDRPEGVKVVTSSVPI-KPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLDEEGFVAEG 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487551604 175 CAANL-FWRKGNVVYTPRLDQAgVNGI----MRQFCIRLLAQSSYQLVEVQ-ASLEESLQADEMVICNALMPVMPVC 245
Cdd:PLN02845 220 PNMNVaFLTNDGELVLPPFDKI-LSGCtarrVLELAPRLVSPGDLRGVKQRkISVEEAKAADEMMLIGSGVPVLPIV 295
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
14-244 |
8.86e-16 |
|
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: 75.47 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 14 VSDRATQFGDGCFTTARVIDGKVSL----LSAHIQRLQDACQRLMISCDFWPQlEQEMKTLAAEQQNGV----LKVVISR 85
Cdd:TIGR01122 16 VLTHALHYGTGVFEGIRAYDTDKGPaifrLKEHIQRLYDSAKIYRMEIPYSKE-ELMEATRETLRKNNLrsayIRPLVFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 86 GSGGRGYSTLNSGPATRILSVTAYPAHYDRLRNE-GITLALSPVRlgRNPH---LAGIKHL-NRLEQVLIRSHLEQTNAD 160
Cdd:TIGR01122 95 GDGDLGLNPRAGYKPDVIIAAWPWGAYLGEEALEkGIDAKVSSWR--RNAPntiPTAAKAGgNYLNSLLAKSEARRHGYD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 161 EALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMP 240
Cdd:TIGR01122 173 EAILLDVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELYTADEAFFTGTAAE 252
|
....
gi 1487551604 241 VMPV 244
Cdd:TIGR01122 253 ITPI 256
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
26-262 |
6.13e-14 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 70.00 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 26 FTTARVIDGKVSLLSAHIQRLQDACQRLMISCDFWP-QLEQEMKTLAAEQ--QNGVLKVVISRGSGGRGYSTLNsgpaTR 102
Cdd:PRK07544 39 FEGERAYGGKIFKLREHSERLRRSAELLDFEIPYSVaEIDAAKKETLAANglTDAYVRPVAWRGSEMMGVSAQQ----NK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 103 I-LSVTAY--PAHYDR-LRNEGITLALSPVRlgrNPH---------LAGI-------KHlnrleqvlirsHLEQTNADEA 162
Cdd:PRK07544 115 IhLAIAAWewPSYFDPeAKMKGIRLDIAKWR---RPDpetapsaakAAGLymictisKH-----------AAEAKGYADA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 163 LVLDSEGWVTECCAANLFWRKGNVVYTPRLDqAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVM 242
Cdd:PRK07544 181 LMLDYRGYVAEATGANIFFVKDGVIHTPTPD-CFLDGITRQTVIELAKRRGIEVVERHIMPEELAGFSECFLTGTAAEVT 259
|
250 260
....*....|....*....|
gi 1487551604 243 PVCACGDVSFSSATLYEYLA 262
Cdd:PRK07544 260 PVSEIGEYRFTPGAITRDLM 279
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
22-256 |
1.08e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 66.16 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 22 GDGCFTTARVIDGKVSLLSAHIQRLQDACQRLmiscdFWPQLEQEM------KTLAAEQQNGVLKVVISRGSGGRGYSTl 95
Cdd:PRK09266 24 NYGHFTSMQVRDGRVRGLDLHLQRLRRASREL-----FGAALDDDRvraqlrAALAAGPADASVRVTVFAPDFDFRNPL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 96 nSGPATRILSVTAYPAhydrlrnegiTLALSPVRLGRNPH---LAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWVT 172
Cdd:PRK09266 98 -ADVAPDVLVATSPPA----------DGPAGPLRLQSVPYereLPHIKHVGTFGQLHLRRLAQRAGFDDALFVDPDGRVS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 173 ECCAANL-FWRKGNVVYtPrldQAGVNGIMRQfciRLLAQSSYQLVEVQAS----LEESLQADEMVICNALMPVMPVCAC 247
Cdd:PRK09266 167 EGATWNLgFWDGGAVVW-P---QAPALPGVTM---ALLQRGLERLGIPQRTrpvtLADLGRFAGAFACNAWRGQRAVSAI 239
|
....*....
gi 1487551604 248 GDVSFSSAT 256
Cdd:PRK09266 240 DDVALPDSH 248
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
160-231 |
2.90e-12 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 65.55 E-value: 2.90e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1487551604 160 DEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADE 231
Cdd:PRK06606 180 DEALLLDVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVIERRITRDELYIADE 251
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
16-252 |
4.28e-11 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 61.89 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 16 DRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMIScdfwPQL-EQEMKTLAAEqqnGVLK------VVISR--- 85
Cdd:PRK13356 27 DHAAWLGSTVFDGARAFEGVTPDLDLHCARVNRSAEALGLK----PTVsAEEIEALARE---GLKRfdpdtaLYIRPmyw 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 86 GSGGRGYSTLNSGPATR-ILSVTAYPAHYDRlrneGITLALSPVRlgrnphlagikhlnrleqvliRSHLEQ--TNA--- 159
Cdd:PRK13356 100 AEDGFASGVAPDPESTRfALCLEEAPMPEPT----GFSLTLSPFR---------------------RPTLEMapTDAkag 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 160 ------------------DEALVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQA 221
Cdd:PRK13356 155 clypnnaralrearsrgfDNALVLDMLGNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTVVETTL 234
|
250 260 270
....*....|....*....|....*....|.
gi 1487551604 222 SLEESLQADEMVICNALMPVMPVCACGDVSF 252
Cdd:PRK13356 235 TYEDFLEADEVFSTGNYSKVVPVTRFDDRSL 265
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
22-230 |
1.66e-10 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 59.97 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 22 GDGCFTTARVIDGKVSLLSAHIQRLQDACQRLMISC---DFWPQL-EQEMKTLAAEQQNGVLKVVISRGSGGrgystlnS 97
Cdd:PRK07849 38 GDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPEpdlDRWRRAvELAIEEWRAPEDEAALRLVYSRGRES-------G 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 98 GPATRILSVTAYPAHYDRLRNEGITLALS----PVRLG-RNP-HLAGIKHLNRLEQVLIRSHLEQTNADEALVLDSEGWV 171
Cdd:PRK07849 111 GAPTAWVTVSPVPERVARARREGVSVITLdrgyPSDAAeRAPwLLAGAKTLSYAVNMAALRYAARRGADDVIFTSTDGYV 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1487551604 172 TECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQAD 230
Cdd:PRK07849 191 LEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAAD 249
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
11-232 |
2.02e-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: 56.82 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 11 SLAVSDRATQFGDGCFTTARVI---DGKVSL--LSAHIQRLQDACQRLMIscdfwPQLEQEMKTLAAEQqngVLKVVISR 85
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYrtpDGKIVLfrPDENAERLNRSARRLGL-----PPFSVEEFIDAIKE---LVKLDADW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 86 GSGGRGYS------------TLNSGPATR-ILSVTAYPA-HYDRLRNEGI-TLALSPVRlgRNPHLAGIKHL--NRLEQV 148
Cdd:cd01557 73 VPYGGGASlyirpfifgtdpQLGVSPALEyLFAVFASPVgAYFKGGEKGVsALVSSFRR--AAPGGPGAAKAggNYAASL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 149 LIRSHLEQTNADEALVLDSE-GWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESL 227
Cdd:cd01557 151 LAQKEAAEKGYDQALWLDGAhGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELY 230
|
....*
gi 1487551604 228 QADEM 232
Cdd:cd01557 231 EADEV 235
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
137-244 |
1.34e-05 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 45.87 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 137 AGIKHLNRLEQVL-IRSHLEQTNADEALVLDS--EGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSS 213
Cdd:PLN02259 232 GGVKSITNYAPVLkALSRAKSRGFSDVLYLDSvkKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQG 311
|
90 100 110
....*....|....*....|....*....|.
gi 1487551604 214 YQLVEVQASLEESLQADEMVICNALMPVMPV 244
Cdd:PLN02259 312 YQVVEKAVHVDEVMDADEVFCTGTAVVVAPV 342
|
|
| PRK07101 |
PRK07101 |
hypothetical protein; Provisional |
140-240 |
1.64e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235934 Cd Length: 187 Bit Score: 44.55 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 140 KHLNRleqVLIRSHLEQT-NADEALVLdSEGWVTECCAANLFWRKGNVVYTPrlDQAGVNGIMRQfciRLLAQSsyQLVE 218
Cdd:PRK07101 96 KYTDR---SALNELFAQKgECDEIIII-KNGLVTDTSIGNLAFFDGKQWFTP--KKPLLKGTQRA---RLLDEG--KIKE 164
|
90 100
....*....|....*....|..
gi 1487551604 219 VQASLEESLQADEMVICNALMP 240
Cdd:PRK07101 165 KDITVEDLLQYEEIRLINAMNG 186
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
171-252 |
1.76e-04 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 42.23 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 171 VTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEmVICNALMPVmpVCACGDV 250
Cdd:PLN03117 232 IEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEE-VFCTGTAVV--VKAVETV 308
|
..
gi 1487551604 251 SF 252
Cdd:PLN03117 309 TF 310
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
137-260 |
5.16e-04 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 40.85 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551604 137 AGIKHLNRLEQVL-IRSHLEQTNADEALVLDSEGW--VTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSS 213
Cdd:PLN02883 228 GGVKAISNYGPVLeVMRRAKSRGFSDVLYLDADTGknIEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLG 307
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1487551604 214 YQLVEVQASLEESLQADEmVICNAlmPVMPVCACGDVSFSSaTLYEY 260
Cdd:PLN02883 308 YKVEERRVPVEELKEAEE-VFCTG--TAAGVASVGSITFKN-TRTEY 350
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
170-244 |
2.28e-03 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 39.06 E-value: 2.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487551604 170 WVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQSSYQLVEVQASLEESLQADEMVICNALMPVMPV 244
Cdd:PLN02782 282 YLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPV 356
|
|
| |
