|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
1-266 |
6.99e-159 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 441.97 E-value: 6.99e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 1 MLLINGIEQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPDIDTLRNEMRQAAQGQGSAVVK 80
Cdd:PRK06092 1 MFWINGQPQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDWAQLEQEMKQLAAELENGVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 81 VIISRGAGKRGYSIAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSAD 160
Cdd:PRK06092 81 VIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLALCPTRLGRNPLLAGIKHLNRLEQVLIRAELEQTEAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 161 EALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMP 240
Cdd:PRK06092 161 EALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSLMP 240
|
250 260
....*....|....*....|....*.
gi 495164135 241 LVPVRSIDGHAYASRELYHYLIPHCE 266
Cdd:PRK06092 241 VWPVRAIGETSYSSGTLTRYLQPLCE 266
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
3-261 |
2.31e-154 |
|
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: 430.09 E-value: 2.31e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 3 LINGIEQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPDIDTLRNEMRQAAQGQGSAVVKVI 82
Cdd:TIGR03461 1 WVNGVLQTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLPDWDALREEMAQLAAGYSLGVLKVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 83 ISRGAGKRGYSIAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSADEA 162
Cdd:TIGR03461 81 ISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRLGVSPVRLGRNPLLAGIKHLNRLEQVLIKAELENSEADEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 163 LVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLV 242
Cdd:TIGR03461 161 LVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSADEVFITNSLMGVV 240
|
250
....*....|....*....
gi 495164135 243 PVRSIDGHAYASRELYHYL 261
Cdd:TIGR03461 241 PVNAIGETSYPSRTLTRLL 259
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
16-261 |
2.96e-92 |
|
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: 272.65 E-value: 2.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 16 DRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPDIDTLRNEMRQAAQGQ--GSAVVKVIISRGAGKRGYS 93
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAANdiDEGRIRLILSRGPGGRGYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 94 IAGCSAPTRIVSRSAYPDfycEWRERGVSLATSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWVTE 173
Cdd:cd01559 81 PSVCPGPALYVSVIPLPP---AWRQDGVRLITCPVRLGEQPLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRVIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 174 CCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSIDGHAYA 253
Cdd:cd01559 158 GTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDDHDGP 237
|
....*...
gi 495164135 254 SRELYHYL 261
Cdd:cd01559 238 PGPLTRAL 245
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
1-254 |
2.67e-85 |
|
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: 255.88 E-value: 2.67e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 1 MLLING----IEQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQ--AAQG 73
Cdd:COG0115 2 LIWLNGelvpEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRElvAANG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 74 QGSAVVKVIISRGAGKRGYSiAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRLGRNPHLAGIKHLNRLEQVLIRTH 153
Cdd:COG0115 82 LEDGYIRPQVTRGVGGRGVF-AEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAAPGGLGGIKTGNYLNNVLAKQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 154 LEQTSADEALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVF 233
Cdd:COG0115 161 AKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVF 240
|
250 260
....*....|....*....|.
gi 495164135 234 ICNALMPLVPVRSIDGHAYAS 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 |
1.10e-55 |
|
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: 178.32 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 24 GCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQ--AAQGQGSAVVKVIISRGAGKRGYSiagCSAP 100
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPfDEEDLRKIIEEllKANGLGVGRLRLTVSRGPGGFGLP---TSDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 101 TRIVSRSAYPDFYCEWRERGVSlatSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWVTECCAANLF 180
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVIS---SLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSNVF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495164135 181 WRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSI 247
Cdd:pfam01063 155 LVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
1-266 |
6.99e-159 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 441.97 E-value: 6.99e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 1 MLLINGIEQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPDIDTLRNEMRQAAQGQGSAVVK 80
Cdd:PRK06092 1 MFWINGQPQESLSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLDDWAQLEQEMKQLAAELENGVLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 81 VIISRGAGKRGYSIAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSAD 160
Cdd:PRK06092 81 VIISRGSGGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLALCPTRLGRNPLLAGIKHLNRLEQVLIRAELEQTEAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 161 EALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMP 240
Cdd:PRK06092 161 EALVLDSEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSLMP 240
|
250 260
....*....|....*....|....*.
gi 495164135 241 LVPVRSIDGHAYASRELYHYLIPHCE 266
Cdd:PRK06092 241 VWPVRAIGETSYSSGTLTRYLQPLCE 266
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
3-261 |
2.31e-154 |
|
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: 430.09 E-value: 2.31e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 3 LINGIEQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPDIDTLRNEMRQAAQGQGSAVVKVI 82
Cdd:TIGR03461 1 WVNGVLQTQISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLPDWDALREEMAQLAAGYSLGVLKVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 83 ISRGAGKRGYSIAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSADEA 162
Cdd:TIGR03461 81 ISRGSGGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRLGVSPVRLGRNPLLAGIKHLNRLEQVLIKAELENSEADEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 163 LVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLV 242
Cdd:TIGR03461 161 LVLDTDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSADEVFITNSLMGVV 240
|
250
....*....|....*....
gi 495164135 243 PVRSIDGHAYASRELYHYL 261
Cdd:TIGR03461 241 PVNAIGETSYPSRTLTRLL 259
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
16-261 |
2.96e-92 |
|
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: 272.65 E-value: 2.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 16 DRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPDIDTLRNEMRQAAQGQ--GSAVVKVIISRGAGKRGYS 93
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAANdiDEGRIRLILSRGPGGRGYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 94 IAGCSAPTRIVSRSAYPDfycEWRERGVSLATSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWVTE 173
Cdd:cd01559 81 PSVCPGPALYVSVIPLPP---AWRQDGVRLITCPVRLGEQPLLAGLKHLNYLENVLAKREARDRGADEALFLDTDGRVIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 174 CCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSIDGHAYA 253
Cdd:cd01559 158 GTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDDHDGP 237
|
....*...
gi 495164135 254 SRELYHYL 261
Cdd:cd01559 238 PGPLTRAL 245
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
1-254 |
2.67e-85 |
|
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: 255.88 E-value: 2.67e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 1 MLLING----IEQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQ--AAQG 73
Cdd:COG0115 2 LIWLNGelvpEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRElvAANG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 74 QGSAVVKVIISRGAGKRGYSiAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRLGRNPHLAGIKHLNRLEQVLIRTH 153
Cdd:COG0115 82 LEDGYIRPQVTRGVGGRGVF-AEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAAPGGLGGIKTGNYLNNVLAKQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 154 LEQTSADEALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVF 233
Cdd:COG0115 161 AKEAGADEALLLDTDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVF 240
|
250 260
....*....|....*....|.
gi 495164135 234 ICNALMPLVPVRSIDGHAYAS 254
Cdd:COG0115 241 LTGTAAEVTPVTEIDGRPIGD 261
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
16-250 |
5.50e-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: 218.62 E-value: 5.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 16 DRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQ--AAQGQGSAVVKVIISRGAGKRGY 92
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPyDREELREALKElvAANNGASLYIRPLLTRGVGGLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 93 SIAGCSAPTRIVSRSAYPDfYCEWRERGVSLATSPVRLG-RNPHLAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWV 171
Cdd:cd00449 81 APPPSPEPTFVVFASPVGA-YAKGGEKGVRLITSPDRRRaAPGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDNGYV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164135 172 TECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSIDGH 250
Cdd:cd00449 160 TEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGR 238
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
24-247 |
1.10e-55 |
|
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: 178.32 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 24 GCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQ--AAQGQGSAVVKVIISRGAGKRGYSiagCSAP 100
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPfDEEDLRKIIEEllKANGLGVGRLRLTVSRGPGGFGLP---TSDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 101 TRIVSRSAYPDFYCEWRERGVSlatSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWVTECCAANLF 180
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVIS---SLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLDEDGNVTEGSTSNVF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495164135 181 WRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSI 247
Cdd:pfam01063 155 LVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
3-249 |
1.70e-38 |
|
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: 135.42 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 3 LING----IEQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQ--AAQGQG 75
Cdd:cd01558 1 YLNGeyvpREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPyTREELKELIRElvAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 76 SAVVKVIISRGAGKRGYSIAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRlgRNPHLAgIKHLNRLEQVLIRTHLE 155
Cdd:cd01558 81 EGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDI--RWLRCD-IKSLNLLNNVLAKQEAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 156 QTSADEALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFIC 235
Cdd:cd01558 158 EAGADEAILLDADGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLT 237
|
250
....*....|....
gi 495164135 236 NALMPLVPVRSIDG 249
Cdd:cd01558 238 STTAEVMPVVEIDG 251
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
8-249 |
1.36e-30 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 115.35 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 8 EQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPD---------IDTLR-NEMRqaaqgqgSA 77
Cdd:PRK08320 15 EEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDSAKAIMLEIPLskeemteivLETLRkNNLR-------DA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 78 VVKVIISRGAGKRGYSIAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRlgRNPHLA---GIKHLNRLEQVLIRTHL 154
Cdd:PRK08320 88 YIRLVVSRGVGDLGLDPRKCPKPTVVCIAEPIGLYPGELYEKGLKVITVSTR--RNRPDAlspQVKSLNYLNNILAKIEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 155 EQTSADEALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFI 234
Cdd:PRK08320 166 NLAGVDEAIMLNDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTADEVFL 245
|
250
....*....|....*
gi 495164135 235 CNALMPLVPVRSIDG 249
Cdd:PRK08320 246 TGTAAEVIPVVKVDG 260
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
1-256 |
4.61e-29 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 111.21 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 1 MLLINGI----EQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIP-------VPDI-DTLRNemr 68
Cdd:PRK07650 1 LIYVNGQyveeEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIEwtmtkdeVLLIlKNLLE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 69 qaAQGQGSAVVKVIISRGAGKRGYSIAGCSAPTRIV--SRSAYPDFYCEwrERGVSLAT---SP---VRLgrnphlagiK 140
Cdd:PRK07650 78 --KNGLENAYVRFNVSAGIGEIGLQTEMYEEPTVIVymKPLAPPGLPAE--KEGVVLKQrrnTPegaFRL---------K 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 141 HLNRLEQVLIRTHLEQTSADEALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEIN 220
Cdd:PRK07650 145 SHHYLNNILGKREIGNDPNKEGIFLTEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGF 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 495164135 221 APASALEEADEVFICNALMPLVPVRSIDGHAYASRE 256
Cdd:PRK07650 225 YTKEELLSADEVFVTNSIQEIVPLTRIEERDFPGKV 260
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
8-249 |
5.37e-26 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 103.50 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 8 EQDCLSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPdidTLRNEMRQAA------QGQGSAVVKV 81
Cdd:PRK12479 16 EKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIP---LTVDEMEEAVlqtlqkNEYADAYIRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 82 IISRGAGKRGYSIAGCSAPTRIVSRSAYPDFYCEWRERGVSLATSPVRlgRNPHLA---GIKHLNRLEQVLIRTHLEQTS 158
Cdd:PRK12479 93 IVSRGKGDLGLDPRSCVKPSVIIIAEQLKLFPQEFYDNGLSVVSVASR--RNTPDAldpRIKSMNYLNNVLVKIEAAQAG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 159 ADEALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNAL 238
Cdd:PRK12479 171 VLEALMLNQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLTGTA 250
|
250
....*....|.
gi 495164135 239 MPLVPVRSIDG 249
Cdd:PRK12479 251 AELIPVVKVDS 261
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
12-253 |
2.12e-22 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 93.48 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 12 LSATDRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPDIDTLRNEMRQAAQ----GQGSAVVKVIISRGa 87
Cdd:PRK07849 28 LHADDLAAVRGDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPEPDLDRWRRAVELAIEewraPEDEAALRLVYSRG- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 88 gkrgysIAGCSAPTRIVSRSAYPDFYCEWRERGVSLATS----PVRLG-RNP-HLAGIKHLNRLEQVLIRTHLEQTSADE 161
Cdd:PRK07849 107 ------RESGGAPTAWVTVSPVPERVARARREGVSVITLdrgyPSDAAeRAPwLLAGAKTLSYAVNMAALRYAARRGADD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 162 ALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPL 241
Cdd:PRK07849 181 VIFTSTDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWLVSSVRLA 260
|
250
....*....|..
gi 495164135 242 VPVRSIDGHAYA 253
Cdd:PRK07849 261 ARVHTLDGRPLP 272
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
16-251 |
1.70e-20 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 88.15 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 16 DRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP----DIDTLRNEMRQAAQGQGSAVVKVIISRGAGKRG 91
Cdd:PRK12400 27 ERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPfskaELITLLYKLIENNNFHEDGTIYLQVSRGVQART 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 92 YSIAGCSAPT--RIVSRSAYPDFyceWRERGVSLATSP-VRLGRnphlAGIKHLNRLEQVLIRTHLEQTSADEALVLDSe 168
Cdd:PRK12400 107 HTFSYDVPPTiyAYITKKERPAL---WIEYGVRAISEPdTRWLR----CDIKSLNLLPNILAATKAERKGCKEALFVRN- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 169 GWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSID 248
Cdd:PRK12400 179 GTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLD 258
|
...
gi 495164135 249 GHA 251
Cdd:PRK12400 259 GTA 261
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
16-251 |
2.36e-20 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 88.53 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 16 DRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQ--AAQGQGSAVVKVIISRGAGKRGY 92
Cdd:PLN02845 61 DHMVHRGHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPfDRATLRRILLQtvAASGCRNGSLRYWLSAGPGGFSL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 93 SIAGCSAPTRIVsrSAYPDFYCEWRERGVSLATSPVRLgRNPHLAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWVT 172
Cdd:PLN02845 141 SPSGCSEPAFYA--VVIEDTYAQDRPEGVKVVTSSVPI-KPPQFATVKSVNYLPNALSQMEAEERGAFAGIWLDEEGFVA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 173 ECCAANL-FWRKGKAVFTPRLDQAgVDGLMRRHIIGLLNQSVWR--LSEINAPASALEE---ADE-VFICNALmPLVPVR 245
Cdd:PLN02845 218 EGPNMNVaFLTNDGELVLPPFDKI-LSGCTARRVLELAPRLVSPgdLRGVKQRKISVEEakaADEmMLIGSGV-PVLPIV 295
|
....*.
gi 495164135 246 SIDGHA 251
Cdd:PLN02845 296 SWDGQP 301
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
16-249 |
4.14e-20 |
|
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: 87.42 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 16 DRAVQFGDGCFTTARVRDG----VVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQA--AQGQGSAVVKVIISRGAG 88
Cdd:TIGR01122 18 THALHYGTGVFEGIRAYDTdkgpAIFRLKEHIQRLYDSAKIYRMEIPySKEELMEATRETlrKNNLRSAYIRPLVFRGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 89 KRG-YSIAGCSaPTRIVSRSAYPDFY-CEWRERGVSLATSPVRlgRNPH---LAGIKHL-NRLEQVLIRTHLEQTSADEA 162
Cdd:TIGR01122 98 DLGlNPRAGYK-PDVIIAAWPWGAYLgEEALEKGIDAKVSSWR--RNAPntiPTAAKAGgNYLNSLLAKSEARRHGYDEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 163 LVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLV 242
Cdd:TIGR01122 175 ILLDVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELYTADEAFFTGTAAEIT 254
|
....*..
gi 495164135 243 PVRSIDG 249
Cdd:TIGR01122 255 PIREVDG 261
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
16-259 |
3.20e-19 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 84.60 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 16 DRAVQFGDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVP-DIDTLRNEMRQAAQ--GQGSAVVKVIISRGAGKRGY 92
Cdd:PRK06680 23 DRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPmTRAELVEVLRELIRrnRVREGLVYLQVTRGVARRDH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 93 SIAGCSAPTRIV--SRSAYPDFYCEWRERGVSLATSP-VRLGRnphlAGIKHLNRLEQVLIRTHLEQTSADEALVLDsEG 169
Cdd:PRK06680 103 VFPAADVKPSVVvfAKSVDFARPAAAAETGIKVITVPdNRWKR----CDIKSVGLLPNVLAKQAAKEAGAQEAWMVD-DG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 170 WVTECCAANlFW---RKGKAVFTPrLDQAGVDGLMRRHIIGLLNQSVWRLSEIN-APASALeEADEVFICNALMPLVPVR 245
Cdd:PRK06680 178 FVTEGASSN-AWivtKDGKLVTRP-ADNFILPGITRHTLIDLAKELGLEVEERPfTLQEAY-AAREAFITAASSFVFPVV 254
|
250 260
....*....|....*....|....
gi 495164135 246 SIDGHAYAS----------RELYH 259
Cdd:PRK06680 255 QIDGKQIGNgkpgpiakrlREAYE 278
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
22-254 |
4.41e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 81.18 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 22 GDGCFTTARVRDGVVHLLEAHLARLHEGCERLMIPVPDIDTLRNEMRQA-AQGQGSAVVKVIISRGAGKRGYSIAGcsAP 100
Cdd:PRK09266 24 NYGHFTSMQVRDGRVRGLDLHLQRLRRASRELFGAALDDDRVRAQLRAAlAAGPADASVRVTVFAPDFDFRNPLAD--VA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 101 TRIVSRSAYPdfycewrergVSLATSPVRLGRNPH---LAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWVTECCAA 177
Cdd:PRK09266 102 PDVLVATSPP----------ADGPAGPLRLQSVPYereLPHIKHVGTFGQLHLRRLAQRAGFDDALFVDPDGRVSEGATW 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 178 NL-FWRkGKAVFTPRLDQ-AGVD-GLMRRHIIGLlnqsvwRLSEINAPAsALEEADEV---FICNALMPLVPVRSIDGHA 251
Cdd:PRK09266 172 NLgFWD-GGAVVWPQAPAlPGVTmALLQRGLERL------GIPQRTRPV-TLADLGRFagaFACNAWRGQRAVSAIDDVA 243
|
...
gi 495164135 252 YAS 254
Cdd:PRK09266 244 LPD 246
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
18-250 |
7.65e-14 |
|
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: 69.53 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 18 AVQFGDGCFTTARVR---DGVVHL--LEAHLARLHEGCERLMIPVPDIDTLRNEMRQA---------AQGQGSAVVK-VI 82
Cdd:cd01557 8 ALHYGQAVFEGLKAYrtpDGKIVLfrPDENAERLNRSARRLGLPPFSVEEFIDAIKELvkldadwvpYGGGASLYIRpFI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 83 ISRGAGkrgYSIAGCSAPTRIVSRSAYPDFYCEwRERGVSL-ATSPVRlgRNPHLAGIKHL--NRLEQVLIRTHLEQTSA 159
Cdd:cd01557 88 FGTDPQ---LGVSPALEYLFAVFASPVGAYFKG-GEKGVSAlVSSFRR--AAPGGPGAAKAggNYAASLLAQKEAAEKGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 160 DEALVLDSE-GWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNAL 238
Cdd:cd01557 162 DQALWLDGAhGYVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFATGTA 241
|
250
....*....|..
gi 495164135 239 MPLVPVRSIDGH 250
Cdd:cd01557 242 AVVTPVGEIDYR 253
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
26-262 |
1.84e-13 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 68.46 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 26 FTTARVRDGVVHLLEAHLARLHEGCERLMIPVP----DIDTLRNEMrQAAQGQGSAVVKVIISRGAGKRGYSiagcSAPT 101
Cdd:PRK07544 39 FEGERAYGGKIFKLREHSERLRRSAELLDFEIPysvaEIDAAKKET-LAANGLTDAYVRPVAWRGSEMMGVS----AQQN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 102 RI---VSRSAYPDFY-CEWRERGVSLATSPVRlgrNPH---------LAGI-------KHlnrleqvlirtHLEQTSADE 161
Cdd:PRK07544 114 KIhlaIAAWEWPSYFdPEAKMKGIRLDIAKWR---RPDpetapsaakAAGLymictisKH-----------AAEAKGYAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 162 ALVLDSEGWVTECCAANLFWRKGKAVFTPRLDqAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPL 241
Cdd:PRK07544 180 ALMLDYRGYVAEATGANIFFVKDGVIHTPTPD-CFLDGITRQTVIELAKRRGIEVVERHIMPEELAGFSECFLTGTAAEV 258
|
250 260
....*....|....*....|.
gi 495164135 242 VPVRSIDGHAYASRELYHYLI 262
Cdd:PRK07544 259 TPVSEIGEYRFTPGAITRDLM 279
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
39-251 |
3.33e-13 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 67.86 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 39 LEAHLARLHEGCERLMIPVP-DIDTLRNEMRQA--AQGQGSAVVKVIISRGAGKRGYSIAGCSAPTRIvsrSAYPdfyce 115
Cdd:PRK06606 54 LREHTKRLFNSAKILRMEIPySVDELMEAQREVvrKNNLKSAYIRPLVFVGDEGLGVRPHGLPTDVAI---AAWP----- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 116 W--------RERGVSLATS----------PVRLgrnpHLAGikhlNRLEQVLIRTHLEQTSADEALVLDSEGWVTECCAA 177
Cdd:PRK06606 126 WgaylgeeaLEKGIRVKVSswtrhapnsiPTRA----KASG----NYLNSILAKTEARRNGYDEALLLDVEGYVSEGSGE 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164135 178 NLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSIDGHA 251
Cdd:PRK06606 198 NIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVIERRITRDELYIADEVFFTGTAAEVTPIREVDGRQ 271
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
160-258 |
3.78e-08 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 53.03 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 160 DEALVLDSEGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALM 239
Cdd:PRK13356 173 DNALVLDMLGNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTGNYS 252
|
90 100
....*....|....*....|....*.
gi 495164135 240 PLVPVRSIDGHAYA-------SRELY 258
Cdd:PRK13356 253 KVVPVTRFDDRSLQpgpvtrrARELY 278
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
45-247 |
2.45e-07 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 51.26 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 45 RLHEGCERLMIPVPDIDTLRNEMRQAA---------QGQGSAVVKVIIsRGAGkrgySIAGCS-AP--TRIVSRSAYPDF 112
Cdd:PLN02259 133 RMKLGAERMLMPSPSVDQFVNAVKQTAlankrwvppAGKGTLYIRPLL-MGSG----PILGLGpAPeyTFIVYASPVGNY 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 113 YCEWRErGVSLATSPVRLGRNPHLAG-IKHLNRLEQVL-IRTHLEQTSADEALVLDS--EGWVTECCAANLFWRKGKAVF 188
Cdd:PLN02259 208 FKEGMA-ALNLYVEEEYVRAAPGGAGgVKSITNYAPVLkALSRAKSRGFSDVLYLDSvkKKYLEEASSCNVFVVKGRTIS 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164135 189 TPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSI 247
Cdd:PLN02259 287 TPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTI 345
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
30-247 |
3.50e-06 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 47.40 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 30 RVRDGVVHLLEAHL--ARLHEGCERLMIPVPDIDTLRNEMRQAA---------QGQGSAVVKVIISRGAGKRGysIAGCS 98
Cdd:PLN02883 112 RGEDGRILLFRPELnaMRMKIGAERMCMHSPSVHQFIEGVKQTVlanrrwvppPGKGSLYLRPLLFGSGASLG--VAAAP 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 99 APTRIVSRSAYPDFYCEWRErGVSLATSPV----RLGRNPHLAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWVTEC 174
Cdd:PLN02883 190 EYTFLVFGSPVQNYFKEGTA-ALNLYVEEVipraYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEV 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164135 175 CAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPASALEEADEVFICNALMPLVPVRSI 247
Cdd:PLN02883 269 SAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSI 341
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
12-261 |
4.21e-04 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 41.37 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 12 LSATDRAVQFGDGCF---TTARVRDGVVHLL--EAHLARLHEGCERLMIPVPDID---------TLRNEMRQAAQGQGSA 77
Cdd:PLN02782 109 LSPSAGVLNYGQGLFeglKAYRKEDGNILLFrpEENAIRMRNGAERMCMPAPTVEqfveavketVLANKRWVPPPGKGSL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 78 VVKVIIsRGAGkrgySIAGCS-AP--TRIVSRSAYPDFYCEwrerGVSlatsPVRL--GRNPHLA------GIKHLNRLE 146
Cdd:PLN02782 189 YIRPLL-MGSG----AVLGLApAPeyTFLIYVSPVGNYFKE----GVA----PINLivENEFHRAtpggtgGVKTIGNYA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 147 QVLIRTHL-EQTSADEALVLDS--EGWVTECCAANLFWRKGKAVFTPRLDQAGVDGLMRRHIIGLLNQSVWRLSEINAPA 223
Cdd:PLN02782 256 AVLKAQSIaKAKGYSDVLYLDCvhKKYLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTV 335
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 495164135 224 SALEEADEVFICNALMPLVPVRSI-----------DGHAYASRELYHYL 261
Cdd:PLN02782 336 DELLEADEVFCTGTAVVVSPVGSItykgkrvsygeGGFGTVSQQLYTVL 384
|
|
| PRK07546 |
PRK07546 |
hypothetical protein; Provisional |
38-245 |
8.48e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 169002 [Multi-domain] Cd Length: 209 Bit Score: 36.49 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 38 LLEAHLARLHEGCERLMIPVPDIDTLRNEMRQAAQGQGSAVVKVIISRgagkRGySIAGCSAPTRIVSRSAypdfycEWR 117
Cdd:PRK07546 20 RLDRHLARLERSARALGFPCDPAAVRAKLAEAVAGAQGPLRLRLTLAR----DG-RLTVETAPLPPLPPDT------VWR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 118 ergvsLATSPVRLGRNPHLAGIKHLNRLEQVLIRTHLEQTSADEALVLDSEGWVTECCAANLFW-RKGKAVFTPRLDQAG 196
Cdd:PRK07546 89 -----VAIARTRLDSADPLLRYKTTRRAAYDAARAELPPAEADEVILLNERGEVCEGTITNVFLdRGGGMLTTPPLSCGL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164135 197 VDGLMRRHiigLLNQSvwRLSEINAPASALEEADEVFICNALMPLVPVR 245
Cdd:PRK07546 164 LPGVLRAE---LLDAG--RAREAVLTVDDLKSARAIWVGNSLRGLIRAE 207
|
|
| PRK07101 |
PRK07101 |
hypothetical protein; Provisional |
140-241 |
8.78e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235934 Cd Length: 187 Bit Score: 36.46 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164135 140 KHLNR--LEQVLIRthleQTSADEALVLdSEGWVTECCAANLFWRKGKAVFTPrlDQAGVDGLMRRHiigLLNQSVWRLS 217
Cdd:PRK07101 96 KYTDRsaLNELFAQ----KGECDEIIII-KNGLVTDTSIGNLAFFDGKQWFTP--KKPLLKGTQRAR---LLDEGKIKEK 165
|
90 100
....*....|....*....|....
gi 495164135 218 EInaPASALEEADEVFICNALMPL 241
Cdd:PRK07101 166 DI--TVEDLLQYEEIRLINAMNGF 187
|
|
| |
