|
Name |
Accession |
Description |
Interval |
E-value |
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
10-278 |
1.04e-117 |
|
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: 338.42 E-value: 1.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 10 FLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPWP 89
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 90 DQFIYLQVTRGVARRDHAFPAHAVPTVFAMSSELPPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQAAVDAG 169
Cdd:cd01558 81 EGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 170 AAECVMFR-DGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSAT 248
Cdd:cd01558 161 ADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLTSTT 240
|
250 260 270
....*....|....*....|....*....|
gi 1891747475 249 REVLAITRLDGKAVGAGRPGPVWASLHAAY 278
Cdd:cd01558 241 AEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
9-282 |
7.48e-104 |
|
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: 304.03 E-value: 7.48e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 9 VFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPW 88
Cdd:COG0115 3 IWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 89 PDQFIYLQVTRGVARRDHaFPAHAVPTVFAMSSELPPVPAALREDGVAAITLPDERW---LHCDIKSTSLLGNVLARQAA 165
Cdd:COG0115 83 EDGYIRPQVTRGVGGRGV-FAEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAapgGLGGIKTGNYLNNVLAKQEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 166 VDAGAAECVMFR-DGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLL 244
Cdd:COG0115 162 KEAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFL 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 1891747475 245 SSATREVLAITRLDGKAVGAGRPGPVWASLHAAYQAAK 282
Cdd:COG0115 242 TGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDIV 279
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
6-284 |
2.62e-89 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 267.18 E-value: 2.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 6 SQTVFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVER 85
Cdd:PRK06680 2 KRIAYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 86 HPWPDQFIYLQVTRGVARRDHAFPAHAV-PTVFAMSSEL-PPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQ 163
Cdd:PRK06680 82 NRVREGLVYLQVTRGVARRDHVFPAADVkPSVVVFAKSVdFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 164 AAVDAGAAECVMFRDGFLTEGSASNIWVV-RNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADEL 242
Cdd:PRK06680 162 AAKEAGAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1891747475 243 LLSSATREVLAITRLDGKAVGAGRPGPVWASLHAAY--QAAKSA 284
Cdd:PRK06680 242 FITAASSFVFPVVQIDGKQIGNGKPGPIAKRLREAYeeFARLTA 285
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
9-280 |
7.01e-80 |
|
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: 242.72 E-value: 7.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 9 VFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPW 88
Cdd:TIGR01121 2 VLWNGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 89 PDQFIYLQVTRGVARRDHAFPAHAVPTVFAMSSELPPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQAAVDA 168
Cdd:TIGR01121 82 NTGHVYFQVTRGVAPRNHQFPAGTVKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 169 GAAECVMFRDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSAT 248
Cdd:TIGR01121 162 GAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVSSTT 241
|
250 260 270
....*....|....*....|....*....|..
gi 1891747475 249 REVLAITRLDGKAVGAGRPGPVWASLHAAYQA 280
Cdd:TIGR01121 242 AEITPVIEIDGQQIGDGKPGPWTRQLQKAFEE 273
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
35-257 |
2.26e-50 |
|
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: 165.22 E-value: 2.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 35 AIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPWPDQFIYLQVTRGVARRDHAFPAhavP 114
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFGLPTSD---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 115 TVFAMSSELPPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQAAVDAGAAECVMF-RDGFLTEGSASNIWVVR 193
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVFLVK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1891747475 194 NGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRL 257
Cdd:pfam01063 158 GGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
10-278 |
1.04e-117 |
|
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: 338.42 E-value: 1.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 10 FLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPWP 89
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGKPFALDEHLDRLYRSAKELRIDIPYTREELKELIRELVAKNEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 90 DQFIYLQVTRGVARRDHAFPAHAVPTVFAMSSELPPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQAAVDAG 169
Cdd:cd01558 81 EGDVYIQVTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDIRWLRCDIKSLNLLNNVLAKQEAKEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 170 AAECVMFR-DGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSAT 248
Cdd:cd01558 161 ADEAILLDaDGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLTSTT 240
|
250 260 270
....*....|....*....|....*....|
gi 1891747475 249 REVLAITRLDGKAVGAGRPGPVWASLHAAY 278
Cdd:cd01558 241 AEVMPVVEIDGRPIGDGKPGPVTKRLREAY 270
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
9-282 |
7.48e-104 |
|
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: 304.03 E-value: 7.48e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 9 VFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPW 88
Cdd:COG0115 3 IWLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPIPYTEEELLEAIRELVAANGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 89 PDQFIYLQVTRGVARRDHaFPAHAVPTVFAMSSELPPVPAALREDGVAAITLPDERW---LHCDIKSTSLLGNVLARQAA 165
Cdd:COG0115 83 EDGYIRPQVTRGVGGRGV-FAEEYEPTVIIIASPLPAYPAEAYEKGVRVITSPYRRAapgGLGGIKTGNYLNNVLAKQEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 166 VDAGAAECVMFR-DGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLL 244
Cdd:COG0115 162 KEAGADEALLLDtDGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISLEELYTADEVFL 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 1891747475 245 SSATREVLAITRLDGKAVGAGRPGPVWASLHAAYQAAK 282
Cdd:COG0115 242 TGTAAEVTPVTEIDGRPIGDGKPGPVTRRLRELYTDIV 279
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
6-284 |
2.62e-89 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 267.18 E-value: 2.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 6 SQTVFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVER 85
Cdd:PRK06680 2 KRIAYVNGRYVNHREARVHIEDRGFQFADGIYEVCAVRDGKLVDLDRHLARLFRSLGEIRIAPPMTRAELVEVLRELIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 86 HPWPDQFIYLQVTRGVARRDHAFPAHAV-PTVFAMSSEL-PPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQ 163
Cdd:PRK06680 82 NRVREGLVYLQVTRGVARRDHVFPAADVkPSVVVFAKSVdFARPAAAAETGIKVITVPDNRWKRCDIKSVGLLPNVLAKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 164 AAVDAGAAECVMFRDGFLTEGSASNIWVV-RNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADEL 242
Cdd:PRK06680 162 AAKEAGAQEAWMVDDGFVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1891747475 243 LLSSATREVLAITRLDGKAVGAGRPGPVWASLHAAY--QAAKSA 284
Cdd:PRK06680 242 FITAASSFVFPVVQIDGKQIGNGKPGPIAKRLREAYeeFARLTA 285
|
|
| D_amino_aminoT |
TIGR01121 |
D-amino acid aminotransferase; This enzyme is a homodimer. The pyridoxal phosphate attachment ... |
9-280 |
7.01e-80 |
|
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: 242.72 E-value: 7.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 9 VFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPW 88
Cdd:TIGR01121 2 VLWNGQLVEREEAKIDIEDRGYQFGDGVYEVIRVYNGKLFTVNEHIDRLYASAAKIRIDIPYTKEELHQLLHELVEKNNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 89 PDQFIYLQVTRGVARRDHAFPAHAVPTVFAMSSELPPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQAAVDA 168
Cdd:TIGR01121 82 NTGHVYFQVTRGVAPRNHQFPAGTVKPVITAYTKEVPRPEENLEKGVKAITVEDIRWLRCDIKSLNLLGNVLAKQEAHEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 169 GAAECVMFRDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSAT 248
Cdd:TIGR01121 162 GAYEAILHRGGTVTEGSSSNVYGIKDGVLYTHPANNLILNGITRMVILACAEENGIPVKEEPFTKEELLNADEVFVSSTT 241
|
250 260 270
....*....|....*....|....*....|..
gi 1891747475 249 REVLAITRLDGKAVGAGRPGPVWASLHAAYQA 280
Cdd:TIGR01121 242 AEITPVIEIDGQQIGDGKPGPWTRQLQKAFEE 273
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
27-278 |
1.27e-77 |
|
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: 236.34 E-value: 1.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 27 DRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPWPDQFIYLQVTRGVARRDH 106
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPIPYDREELREALKELVAANNGASLYIRPLLTRGVGGLGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 107 AFPAHAVPTVFAMSSELPPvPAALREDGVAAITLPDER----WLHCDIKSTSLLGNVLARQAAVDAGAAECVMFRD-GFL 181
Cdd:cd00449 81 APPPSPEPTFVVFASPVGA-YAKGGEKGVRLITSPDRRraapGGTGDAKTGGNLNSVLAKQEAAEAGADEALLLDDnGYV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 182 TEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRLDGKA 261
Cdd:cd00449 160 TEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAEVTPVTEIDGRG 239
|
250
....*....|....*..
gi 1891747475 262 VGAGRPGPVWASLHAAY 278
Cdd:cd00449 240 IGDGKPGPVTRKLRELL 256
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
27-278 |
2.01e-55 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 180.60 E-value: 2.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 27 DRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVER-HPWPDQFIYLQVTRGVARRD 105
Cdd:PRK12400 27 ERGLQFGDGVYEVIRLYKGNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENnNFHEDGTIYLQVSRGVQART 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 106 HAFPAHAVPTVFAMSSElPPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQAAVDAGAAECVMFRDGFLTEGS 185
Cdd:PRK12400 107 HTFSYDVPPTIYAYITK-KERPALWIEYGVRAISEPDTRWLRCDIKSLNLLPNILAATKAERKGCKEALFVRNGTVTEGS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 186 ASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRLDGKAVGAG 265
Cdd:PRK12400 186 HSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADECFFTGTTIEILPMTHLDGTAIQDG 265
|
250
....*....|...
gi 1891747475 266 RPGPVWASLHAAY 278
Cdd:PRK12400 266 QVGPITKMLQRSF 278
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
6-279 |
1.17e-51 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 170.82 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 6 SQTVFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSlAKT---RIPNPRDSTgwTALITEI 82
Cdd:PRK08320 2 EQLIYLNGEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNGRVFRLKEHIDRLYDS-AKAimlEIPLSKEEM--TEIVLET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 83 VERHPWPDQFIYLQVTRGVArrDHAF-PAH-AVPTVFAMSSELPPVPAALREDGVAAITLPDERwLHCD-----IKSTSL 155
Cdd:PRK08320 79 LRKNNLRDAYIRLVVSRGVG--DLGLdPRKcPKPTVVCIAEPIGLYPGELYEKGLKVITVSTRR-NRPDalspqVKSLNY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 156 LGNVLARQAAVDAGAAECVMF-RDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITRE 234
Cdd:PRK08320 156 LNNILAKIEANLAGVDEAIMLnDEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLH 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1891747475 235 EVLSADELLLSSATREVLAITRLDGKAVGAGRPGPVWASLHAAYQ 279
Cdd:PRK08320 236 DLYTADEVFLTGTAAEVIPVVKVDGRVIGDGKPGPITKKLLEEFR 280
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
35-257 |
2.26e-50 |
|
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: 165.22 E-value: 2.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 35 AIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHPWPDQFIYLQVTRGVARRDHAFPAhavP 114
Cdd:pfam01063 1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGIPLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRGPGGFGLPTSD---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 115 TVFAMSSELPPVPAALREDGVAAITLPDERWLHCDIKSTSLLGNVLARQAAVDAGAAECVMF-RDGFLTEGSASNIWVVR 193
Cdd:pfam01063 78 TLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPGAKTLNYLENVLARREAKAQGADDALLLdEDGNVTEGSTSNVFLVK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1891747475 194 NGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRL 257
Cdd:pfam01063 158 GGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
27-278 |
2.85e-47 |
|
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: 158.24 E-value: 2.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 27 DRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITeIVERHPWPDQFIYLQVTRGVARRDH 106
Cdd:cd01559 1 DRGFAYGDGVFETMRALDGRLFLLDAHLARLERSARRLGIPEPDLPRLRAALES-LLAANDIDEGRIRLILSRGPGGRGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 107 AFPAHAVPTVFAMSSELPPvpaALREDGVAAITLP---DERWLHCDIKSTSLLGNVLARQAAVDAGAAECVMFR-DGFLT 182
Cdd:cd01559 80 APSVCPGPALYVSVIPLPP---AWRQDGVRLITCPvrlGEQPLLAGLKHLNYLENVLAKREARDRGADEALFLDtDGRVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 183 EGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRLDGkav 262
Cdd:cd01559 157 EGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVAPVTAIDD--- 233
|
250
....*....|....*.
gi 1891747475 263 GAGRPGPVWASLHAAY 278
Cdd:cd01559 234 HDGPPGPLTRALRELL 249
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
7-280 |
6.00e-47 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 158.96 E-value: 6.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 7 QTVFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERH 86
Cdd:PRK12479 4 QYIYMNGEFVEKEKAVVSVYDHGFLYGDGVFEGIRSYGGNVFCLKEHVKRLYESAKSILLTIPLTVDEMEEAVLQTLQKN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 87 PWPDQFIYLQVTRGvaRRDHAFPAHAV--PTVFAMSSELPPVPAALREDGVAAITLPDER----WLHCDIKSTSLLGNVL 160
Cdd:PRK12479 84 EYADAYIRLIVSRG--KGDLGLDPRSCvkPSVIIIAEQLKLFPQEFYDNGLSVVSVASRRntpdALDPRIKSMNYLNNVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 161 ARQAAVDAGAAECVMF-RDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSA 239
Cdd:PRK12479 162 VKIEAAQAGVLEALMLnQQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1891747475 240 DELLLSSATREVLAITRLDGKAVGAGRPGPVWASLHAAYQA 280
Cdd:PRK12479 242 DEVFLTGTAAELIPVVKVDSREIGDGKPGSVTKQLTEEFKK 282
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
10-278 |
1.07e-37 |
|
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: 134.79 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 10 FLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVY----GRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVER 85
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYdtdkGPAIFRLKEHIQRLYDSAKIYRMEIPYSKEELMEATRETLRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 86 HPWPDQFIYLQVTRGVARRDHAFPAHAVPTVFAMSSELPPVPAALR-EDGVAAITLPDERwLHCD-----IKSTSL-LGN 158
Cdd:TIGR01122 81 NNLRSAYIRPLVFRGDGDLGLNPRAGYKPDVIIAAWPWGAYLGEEAlEKGIDAKVSSWRR-NAPNtiptaAKAGGNyLNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 159 VLARQAAVDAGAAECVMF-RDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVL 237
Cdd:TIGR01122 160 LLAKSEARRHGYDEAILLdVEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1891747475 238 SADELLLSSATREVLAITRLDGKAVGAGRPGPVWASLHAAY 278
Cdd:TIGR01122 240 TADEAFFTGTAAEITPIREVDGRKIGNGRRGPVTKKLQEAF 280
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
23-257 |
1.17e-29 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 113.01 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 23 VPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPrdstGWTALITEIVE-RHPWPDQFIYLQVTRGV 101
Cdd:PRK06092 12 LSVSDRSTQYGDGCFTTARVRDGQVSLLSRHLQRLQDACERLAIPLD----DWAQLEQEMKQlAAELENGVLKVIISRGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 102 ARRDHAFPAHAVPTVFAMSSELPPVPAALREDGVAA----ITLPDERWLhCDIKSTSLLGNVLARQAAVDAGAAECVMF- 176
Cdd:PRK06092 88 GGRGYSPAGCAAPTRILSVSPYPAHYSRWREQGITLalcpTRLGRNPLL-AGIKHLNRLEQVLIRAELEQTEADEALVLd 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 177 RDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITR 256
Cdd:PRK06092 167 SEGWVIECCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFICNSLMPVWPVRA 246
|
.
gi 1891747475 257 L 257
Cdd:PRK06092 247 I 247
|
|
| pabC_Proteo |
TIGR03461 |
aminodeoxychorismate lyase; Members of this protein family are aminodeoxychorismate lyase (ADC ... |
23-258 |
1.20e-28 |
|
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: 109.98 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 23 VPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPrdstGWTALITEIVER-HPWPDQFIYLQVTRGV 101
Cdd:TIGR03461 10 ISVSDRGLQYGDGCFTTAKVRNGKIELLDLHLERLQDAAARLGIPLP----DWDALREEMAQLaAGYSLGVLKVIISRGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 102 ARRDHAFPAHAVPTVFAMSSELPPVPAALREDGVA----AITLPDERWLhCDIKSTSLLGNVLARQAAVDAGAAECVMF- 176
Cdd:TIGR03461 86 GGRGYSPPGCSDPTRIISVSPYPAHYSAWQQQGIRlgvsPVRLGRNPLL-AGIKHLNRLEQVLIKAELENSEADEALVLd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 177 RDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITR 256
Cdd:TIGR03461 165 TDGNVVECTAANIFWRKGNQVFTPDLSYCGVAGVMRQHVLALLPALGYEIEEVKAGLEELLSADEVFITNSLMGVVPVNA 244
|
..
gi 1891747475 257 LD 258
Cdd:TIGR03461 245 IG 246
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
1-278 |
1.98e-26 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 105.23 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 1 MSTEISQTVFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVY----GRRPFRWPAHLARLQRSlAK-TRIPNPRDSTGW 75
Cdd:PRK06606 1 SMADRAGYIWFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYdtpkGPAIFRLREHTKRLFNS-AKiLRMEIPYSVDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 76 TALITEIVERHPWPDQFI-----YLQVTRGVarRDHAFPAHAVPTVFAMSSELPPvpAALrEDGVAAITlpdERWLHCDI 150
Cdd:PRK06606 80 MEAQREVVRKNNLKSAYIrplvfVGDEGLGV--RPHGLPTDVAIAAWPWGAYLGE--EAL-EKGIRVKV---SSWTRHAP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 151 KSTSLL----GN----VLARQAAVDAGAAECVMF-RDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGI-RCGLLdELCA 220
Cdd:PRK06606 152 NSIPTRakasGNylnsILAKTEARRNGYDEALLLdVEGYVSEGSGENIFIVRDGVLYTPPLTSSILEGItRDTVI-TLAK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1891747475 221 AQGIPMDIRRITREEVLSADELLLSSATREVLAITRLDGKAVGAGRPGPVWASLHAAY 278
Cdd:PRK06606 231 DLGIEVIERRITRDELYIADEVFFTGTAAEVTPIREVDGRQIGNGKRGPITEKLQSAY 288
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
9-279 |
3.05e-23 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 96.19 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 9 VFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPnprdstgWT-------ALITE 81
Cdd:PRK07650 2 IYVNGQYVEEEEARISPFDHGYLYGLGVFETFRIYNGHPFLLDDHYDRLNDALDTLQIE-------WTmtkdevlLILKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 82 IVERHPWPDQFIYLQVTRGVarRDHAFPA--HAVPTVFAMSSELPPVPAALREDGVAAITL---P--DERwlhcdIKSTS 154
Cdd:PRK07650 75 LLEKNGLENAYVRFNVSAGI--GEIGLQTemYEEPTVIVYMKPLAPPGLPAEKEGVVLKQRrntPegAFR-----LKSHH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 155 LLGNVLARQAAVDAGAAECVMF-RDGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITR 233
Cdd:PRK07650 148 YLNNILGKREIGNDPNKEGIFLtEEGYVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTK 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1891747475 234 EEVLSADELLLSSATREVLAITRLDGKaVGAGRPGPVWASLHAAYQ 279
Cdd:PRK07650 228 EELLSADEVFVTNSIQEIVPLTRIEER-DFPGKVGMVTKRLQNLYE 272
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
33-264 |
4.92e-21 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 90.02 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 33 GDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPrDSTGWTALITEIVERH--PWPDQFIYLQVTRGvarRDHAfpa 110
Cdd:PRK07849 38 GDGVFETLLVRDGRPCNLEAHLERLARSAALLDLPEP-DLDRWRRAVELAIEEWraPEDEAALRLVYSRG---RESG--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 111 hAVPTVFAMSSELPPVPAALREDGVAAITLPdeRWLHCDIKSTS---LLG--------NVLARQAAVDAGAAEcVMF--R 177
Cdd:PRK07849 111 -GAPTAWVTVSPVPERVARARREGVSVITLD--RGYPSDAAERApwlLAGaktlsyavNMAALRYAARRGADD-VIFtsT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 178 DGFLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRL 257
Cdd:PRK07849 187 DGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWLVSSVRLAARVHTL 266
|
....*..
gi 1891747475 258 DGKAVGA 264
Cdd:PRK07849 267 DGRPLPR 273
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
48-270 |
5.21e-18 |
|
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: 81.47 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 48 FRWPAHLARLQRSLAKTRIPNPrDSTGWTALITEIV--ERHPWPDQF---IYLqvtRGVARRDHAF--PAHAVPTVFAMs 120
Cdd:cd01557 32 FRPDENAERLNRSARRLGLPPF-SVEEFIDAIKELVklDADWVPYGGgasLYI---RPFIFGTDPQlgVSPALEYLFAV- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 121 sELPPVPA--ALREDGVAAITlpdERWLHCDIKSTS---LLGN----VLARQAAVDAGAAECVMF--RDGFLTEGSASNI 189
Cdd:cd01557 107 -FASPVGAyfKGGEKGVSALV---SSFRRAAPGGPGaakAGGNyaasLLAQKEAAEKGYDQALWLdgAHGYVAEVGTMNI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 190 WVVRNGTIFGPPRDHLILEGI-RCGLLdELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRLD--GKAVGAGR 266
Cdd:cd01557 183 FFVKDGELITPPLDGSILPGItRDSIL-ELARDLGIKVEERPITRDELYEADEVFATGTAAVVTPVGEIDyrGKEPGEGE 261
|
....
gi 1891747475 267 PGPV 270
Cdd:cd01557 262 VGPV 265
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
23-277 |
1.37e-15 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 75.44 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 23 VPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRSLAKTRIPNPRDSTGWTALITEIVERHpwpdqfiylQVTRGVA 102
Cdd:PLN02845 57 IPLDDHMVHRGHGVFDTATIRDGHLYELDAHLDRFLRSAAKAKIPLPFDRATLRRILLQTVAAS---------GCRNGSL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 103 RrdhaFPAHAVPTVFAMSSE--LPPV---------PAALREDGVAAIT--LPDERWLHCDIKSTSLLGNVLARQAAVDAG 169
Cdd:PLN02845 128 R----YWLSAGPGGFSLSPSgcSEPAfyavviedtYAQDRPEGVKVVTssVPIKPPQFATVKSVNYLPNALSQMEAEERG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 170 A-AECVMFRDGFLTEGSASNI-WVVRNGTIFGPPRDHlILEGIRCGLLDELCAAQGIPMD-----IRRITREEVLSADEL 242
Cdd:PLN02845 204 AfAGIWLDEEGFVAEGPNMNVaFLTNDGELVLPPFDK-ILSGCTARRVLELAPRLVSPGDlrgvkQRKISVEEAKAADEM 282
|
250 260 270
....*....|....*....|....*....|....*
gi 1891747475 243 LLSSATREVLAITRLDGKAVGAGRPGPVWASLHAA 277
Cdd:PLN02845 283 MLIGSGVPVLPIVSWDGQPIGDGKVGPITLALHDL 317
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
52-278 |
2.90e-08 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 53.81 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 52 AHLARLQRSlAKTRIPNPRDSTG-WTALITEIVERHPwPDQFIYLqvtRGVARRDHAFPAHAVP----TVFAMSSELPPV 126
Cdd:PRK13356 52 LHCARVNRS-AEALGLKPTVSAEeIEALAREGLKRFD-PDTALYI---RPMYWAEDGFASGVAPdpesTRFALCLEEAPM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 127 PAAlreDGVAAITLPDER-WLHC---DIKSTSLLGNVlAR--QAAVDAGAAECVMfRD--GFLTEGSASNIWVVRNGTIF 198
Cdd:PRK13356 127 PEP---TGFSLTLSPFRRpTLEMaptDAKAGCLYPNN-ARalREARSRGFDNALV-LDmlGNVAETATSNVFMVKDGVVF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 199 GPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRLDGKAVgagRPGPVWASLHAAY 278
Cdd:PRK13356 202 TPVPNGTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTGNYSKVVPVTRFDDRSL---QPGPVTRRARELY 278
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
9-280 |
1.18e-07 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 51.90 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 9 VFLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVYGRRPFRWPAHLARLQRS--LAKTRIPnprdstgWT-----ALITE 81
Cdd:PRK07544 11 IWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGGKIFKLREHSERLRRSaeLLDFEIP-------YSvaeidAAKKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 82 IVERHPWPDQFIylqvtRGVARR---DHAFPAHAVPTVFAMSSElpPVPAAL-REDGVAAITL-------PDERWLHCDI 150
Cdd:PRK07544 84 TLAANGLTDAYV-----RPVAWRgseMMGVSAQQNKIHLAIAAW--EWPSYFdPEAKMKGIRLdiakwrrPDPETAPSAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 151 KSTSL-LGNVLARQAAVDAGAAECVMFR-DGFLTEGSASNIWVVRNGTIFGPPRDHlILEGIRCGLLDELCAAQGIPMDI 228
Cdd:PRK07544 157 KAAGLyMICTISKHAAEAKGYADALMLDyRGYVAEATGANIFFVKDGVIHTPTPDC-FLDGITRQTVIELAKRRGIEVVE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1891747475 229 RRITREEVLSADELLLSSATREVLAITRLDGKAVGagrPGPVWASLHAAYQA 280
Cdd:PRK07544 236 RHIMPEELAGFSECFLTGTAAEVTPVSEIGEYRFT---PGAITRDLMDDYEA 284
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
121-280 |
1.47e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 45.36 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 121 SELPPVPAALRedgvaaiTLPDERWLHcDIKSTSLLGNVLARQAAVDAGAAEcVMF--RDGFLTEGSASNIWVVRNGTIF 198
Cdd:PRK09266 112 ADGPAGPLRLQ-------SVPYERELP-HIKHVGTFGQLHLRRLAQRAGFDD-ALFvdPDGRVSEGATWNLGFWDGGAVV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 199 GPPRDhlILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADELLLSSATREVLAITRLDGKAVGAGRpgPVWASLHAAY 278
Cdd:PRK09266 183 WPQAP--ALPGVTMALLQRGLERLGIPQRTRPVTLADLGRFAGAFACNAWRGQRAVSAIDDVALPDSH--ALLELLRRAY 258
|
..
gi 1891747475 279 QA 280
Cdd:PRK09266 259 EA 260
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
125-242 |
7.35e-05 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 43.68 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 125 PVPAALREdGVAAITLPDERWLH-------CDIKSTSLLGNVLARQAAVDAGAAECVMFRDG----FLTEGSASNIWVVR 193
Cdd:PLN02782 217 PVGNYFKE-GVAPINLIVENEFHratpggtGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCvhkkYLEEVSSCNIFIVK 295
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1891747475 194 NGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDIRRITREEVLSADEL 242
Cdd:PLN02782 296 DNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEV 344
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
10-245 |
3.55e-04 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 41.63 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 10 FLNGEFLPIGEARVPVLDRGFIFGDAIYEVVPVY----GRRPFRWPAHLA-RLQRSLAKTRIPNPRDSTGWTALITEIVE 84
Cdd:PLN02259 82 FTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYrkenGKLLLFRPDHNAiRMKLGAERMLMPSPSVDQFVNAVKQTALA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 85 RHPW-PDQ---FIYLQ-VTRGVARRDHAFPAHAVPTVFAMSselpPVPAALREdGVAAITL-PDERWLHC------DIKS 152
Cdd:PLN02259 162 NKRWvPPAgkgTLYIRpLLMGSGPILGLGPAPEYTFIVYAS----PVGNYFKE-GMAALNLyVEEEYVRAapggagGVKS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891747475 153 TSLLGNVLARQAAVDAGAAECVMFRDG----FLTEGSASNIWVVRNGTIFGPPRDHLILEGIRCGLLDELCAAQGIPMDI 228
Cdd:PLN02259 237 ITNYAPVLKALSRAKSRGFSDVLYLDSvkkkYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVE 316
|
250
....*....|....*..
gi 1891747475 229 RRITREEVLSADELLLS 245
Cdd:PLN02259 317 KAVHVDEVMDADEVFCT 333
|
|
| |
