|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
1-340 |
0e+00 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 625.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 1 MTVNLDWDNLGFAYRKLPFRYISHFKDGKWDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAE 80
Cdd:PRK13357 13 EKRAIDWANLGFGYVFTDHMVVIDYKDGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFRPDANAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 81 RLQRTADRLLMPHVPTDKFIAAVKSVVRANEEFVPPYGTGATLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGG 160
Cdd:PRK13357 93 RLQRSADRLLMPELPEELFLEAVKQLVKADRDWVPPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVGAYFKGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 161 LTPTNFIVSKEYDRAAPNGTGAAKVGGNYAASLLPGKYAHEKQFSDVIYLDPATHTKIEEVGAANFFGITKDNQFITPLS 240
Cdd:PRK13357 173 VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNFFFITKDGTVTPPLS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 241 PSILPSITKYSLLYLAKErFGMEAIEGDVFVDE------LDKFTEAGACGTAAVISPIGGIQNGDDFHVFYsETEVGPAT 314
Cdd:PRK13357 253 GSILPGITRDSLLQLAED-LGLTVEERPVSIDEwqadaaSGEFTEAFACGTAAVITPIGGIKYKDKEFVIG-DGEVGPVT 330
|
330 340
....*....|....*....|....*.
gi 446139925 315 RKLYDELVGIQFGDVEAPEGWIYKVD 340
Cdd:PRK13357 331 QKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
30-339 |
8.28e-171 |
|
branched-chain amino acid aminotransferase, group II; 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 less similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 233278 Cd Length: 313 Bit Score: 477.33 E-value: 8.28e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 30 WDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAERLQRTADRLLMPHVPTDKFIAAVKSVVRA 109
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 110 NEEFVPPYGTGATLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGGLTPTNFIVSKEYDRAAPNGTGAAKVGGNY 189
Cdd:TIGR01123 81 NKDWVPPYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVTTEYDRAAPGGTGAVKVGGNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 190 AASLLPGKYAHEKQFSDVIYLDPATHTKIEEVGAANFFGITKDNQ-FITPLSPSILPSITKYSLLYLAKERfGMEAIEGD 268
Cdd:TIGR01123 161 AASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGDGElVTPPLSGSILPGITRDSLLQLAKDL-GMEVEERR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139925 269 VFVDELDKFTEAG----ACGTAAVISPIGGIQNGDDFHVFYSEtEVGPATRKLYDELVGIQFGDVEAPEGWIYKV 339
Cdd:TIGR01123 240 IDIDELKAFVEAGeivfACGTAAVITPVGEIQHGGKEVVFASG-QPGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
42-327 |
2.69e-133 |
|
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: 380.77 E-value: 2.69e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 42 HISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAERLQRTADRLLMPHVPTDKFIAAVKSVVRANEEFvPPYGTGA 121
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADW-VPYGGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 122 TLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGGLTPTNFIVSkEYDRAAPNGTGAAKVGGNYAASLLPGKYAHE 201
Cdd:cd01557 80 SLYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 202 KQFSDVIYLDPAtHTKIEEVGAANFFGItKDNQFITP-LSPSILPSITKYSLLYLAKErFGMEAIEGDVFVDELDKFTEA 280
Cdd:cd01557 159 KGYDQALWLDGA-HGYVAEVGTMNIFFV-KDGELITPpLDGSILPGITRDSILELARD-LGIKVEERPITRDELYEADEV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446139925 281 GACGTAAVISPIGGIQNGDDfhvFYSETEVGPATRKLYDELVGIQFG 327
Cdd:cd01557 236 FATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
30-331 |
4.88e-78 |
|
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: 240.48 E-value: 4.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 30 WDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKdgsiqLFRPDQNAERLQRTADRLLMPH-VPTDKFIAAVKSVVR 108
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGR-----LFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 109 ANEefvppygtGATLYIRPLLIGVGDIIGVKPAE-EYIFTVFAMPVGSYFKGGL-TPTNFIVSkEYDRAAPNGTGAAKvG 186
Cdd:COG0115 79 ANG--------LEDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYeKGVRVITS-PYRRAAPGGLGGIK-T 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 187 GNYAASLLPGKYAHEKQFSDVIYLDpaTHTKIEEVGAANFFGItKDNQFITP-LSPSILPSITKYSLLYLAKERfGMEAI 265
Cdd:COG0115 149 GNYLNNVLAKQEAKEAGADEALLLD--TDGYVAEGSGSNVFIV-KDGVLVTPpLSGGILPGITRDSVIELAREL-GIPVE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139925 266 EGDVFVDELDKFTEAGACGTAAVISPIGGIqngDDFHVfySETEVGPATRKLYDELVGIQFGDVEA 331
Cdd:COG0115 225 ERPISLEELYTADEVFLTGTAAEVTPVTEI---DGRPI--GDGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
55-295 |
6.98e-33 |
|
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: 121.70 E-value: 6.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 55 QAFEGLKAYrtkDGSIqlFRPDQNAERLQRTADRLLMPHVPTDKFI-AAVKSVVRANEEFVPpygtgatlYIRPLLIGVG 133
Cdd:pfam01063 1 GVFETLRVY---NGKI--FFLDEHLARLRRSAKLLGIPLPFDEEDLrKIIEELLKANGLGVG--------RLRLTVSRGP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 134 DIIGVKPAE-EYIFTVFAMPVGSYFKGGLTptnfiVSKEYDRAAPNGTGAAKVGgNYAASLLPGKYAHEKQFSDVIYLDP 212
Cdd:pfam01063 68 GGFGLPTSDpTLAIFVSALPPPPESKKKGV-----ISSLVRRNPPSPLPGAKTL-NYLENVLARREAKAQGADDALLLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 213 ATHtkIEEVGAANFFgITKDNQFITP-LSPSILPSITKYSLLYLAKERfGMEAIEGDVFVDELDKFTEAGACGTAAVISP 291
Cdd:pfam01063 142 DGN--VTEGSTSNVF-LVKGGTLYTPpLESGILPGITRQALLDLAKAL-GLEVEERPITLADLQEADEAFLTNSLRGVTP 217
|
....
gi 446139925 292 IGGI 295
Cdd:pfam01063 218 VSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
1-340 |
0e+00 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 625.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 1 MTVNLDWDNLGFAYRKLPFRYISHFKDGKWDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAE 80
Cdd:PRK13357 13 EKRAIDWANLGFGYVFTDHMVVIDYKDGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFRPDANAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 81 RLQRTADRLLMPHVPTDKFIAAVKSVVRANEEFVPPYGTGATLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGG 160
Cdd:PRK13357 93 RLQRSADRLLMPELPEELFLEAVKQLVKADRDWVPPYGEGASLYLRPFMIATEPFLGVKPAEEYIFCVIASPVGAYFKGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 161 LTPTNFIVSKEYDRAAPNGTGAAKVGGNYAASLLPGKYAHEKQFSDVIYLDPATHTKIEEVGAANFFGITKDNQFITPLS 240
Cdd:PRK13357 173 VKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNFFFITKDGTVTPPLS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 241 PSILPSITKYSLLYLAKErFGMEAIEGDVFVDE------LDKFTEAGACGTAAVISPIGGIQNGDDFHVFYsETEVGPAT 314
Cdd:PRK13357 253 GSILPGITRDSLLQLAED-LGLTVEERPVSIDEwqadaaSGEFTEAFACGTAAVITPIGGIKYKDKEFVIG-DGEVGPVT 330
|
330 340
....*....|....*....|....*.
gi 446139925 315 RKLYDELVGIQFGDVEAPEGWIYKVD 340
Cdd:PRK13357 331 QKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
30-339 |
8.28e-171 |
|
branched-chain amino acid aminotransferase, group II; 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 less similar to the DAAT family. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 233278 Cd Length: 313 Bit Score: 477.33 E-value: 8.28e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 30 WDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAERLQRTADRLLMPHVPTDKFIAAVKSVVRA 109
Cdd:TIGR01123 1 WHNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 110 NEEFVPPYGTGATLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGGLTPTNFIVSKEYDRAAPNGTGAAKVGGNY 189
Cdd:TIGR01123 81 NKDWVPPYGSGASLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVTTEYDRAAPGGTGAVKVGGNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 190 AASLLPGKYAHEKQFSDVIYLDPATHTKIEEVGAANFFGITKDNQ-FITPLSPSILPSITKYSLLYLAKERfGMEAIEGD 268
Cdd:TIGR01123 161 AASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGDGElVTPPLSGSILPGITRDSLLQLAKDL-GMEVEERR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139925 269 VFVDELDKFTEAG----ACGTAAVISPIGGIQNGDDFHVFYSEtEVGPATRKLYDELVGIQFGDVEAPEGWIYKV 339
Cdd:TIGR01123 240 IDIDELKAFVEAGeivfACGTAAVITPVGEIQHGGKEVVFASG-QPGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
42-327 |
2.69e-133 |
|
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: 380.77 E-value: 2.69e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 42 HISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAERLQRTADRLLMPHVPTDKFIAAVKSVVRANEEFvPPYGTGA 121
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADW-VPYGGGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 122 TLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGGLTPTNFIVSkEYDRAAPNGTGAAKVGGNYAASLLPGKYAHE 201
Cdd:cd01557 80 SLYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVS-SFRRAAPGGPGAAKAGGNYAASLLAQKEAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 202 KQFSDVIYLDPAtHTKIEEVGAANFFGItKDNQFITP-LSPSILPSITKYSLLYLAKErFGMEAIEGDVFVDELDKFTEA 280
Cdd:cd01557 159 KGYDQALWLDGA-HGYVAEVGTMNIFFV-KDGELITPpLDGSILPGITRDSILELARD-LGIKVEERPITRDELYEADEV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446139925 281 GACGTAAVISPIGGIQNGDDfhvFYSETEVGPATRKLYDELVGIQFG 327
Cdd:cd01557 236 FATGTAAVVTPVGEIDYRGK---EPGEGEVGPVTKKLYDLLTDIQYG 279
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
4-335 |
3.40e-97 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 293.68 E-value: 3.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 4 NLDWDNLGFAYRKLPFRYISHF-KDGKWDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAERL 82
Cdd:PLN02782 69 DIDWDNLGFGLVPTDYMYIMKCnRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRM 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 83 QRTADRLLMPHVPTDKFIAAVKSVVRANEEFVPPYGTGaTLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGGLT 162
Cdd:PLN02782 149 RNGAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKG-SLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 163 PTNFIVSKEYDRAAPNGTGAAKVGGNYAASLLPGKYAHEKQFSDVIYLDpATHTK-IEEVGAANFFgITKDNQFITP-LS 240
Cdd:PLN02782 228 PINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLD-CVHKKyLEEVSSCNIF-IVKDNVISTPaIK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 241 PSILPSITKYSLLYLAKERfGMEAIEGDVFVDELDKFTEAGACGTAAVISPIGGIQNGDDfHVFYSETEVGPATRKLYDE 320
Cdd:PLN02782 306 GTILPGITRKSIIDVARSQ-GFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSITYKGK-RVSYGEGGFGTVSQQLYTV 383
|
330
....*....|....*
gi 446139925 321 LVGIQFGDVEAPEGW 335
Cdd:PLN02782 384 LTSLQMGLIEDNMNW 398
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
4-340 |
1.44e-90 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 274.89 E-value: 1.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 4 NLDWDNLGFAYRKLPFRYISHFKDGK-WDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAERL 82
Cdd:PLN03117 19 NVKWEELGFALVPTDYMYVAKCKQGEsFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 83 QRTADRLLMPHVPTDKFIAAVKSVVRANEEFVPPYGTGaTLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFK--GG 160
Cdd:PLN03117 99 QTGADRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKG-TLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKasSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 161 LtptNFIVSKEYDRAAPNGTGAAKVGGNYAASLLPGKYAHEKQFSDVIYLDPATHTKIEEVGAANFFgITKDNQFITP-L 239
Cdd:PLN03117 178 L---NLKVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNIF-ILKGNIVSTPpT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 240 SPSILPSITKYSLLYLAKErFGMEAIEGDVFVDELDKFTEAGACGTAAVISPIGGIQNGDDfHVFYSETEVGPATrKLYD 319
Cdd:PLN03117 254 SGTILPGVTRKSISELARD-IGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDK-KVKYRTGEEALST-KLHL 330
|
330 340
....*....|....*....|.
gi 446139925 320 ELVGIQFGDVEAPEGWIYKVD 340
Cdd:PLN03117 331 ILTNIQMGVVEDKKGWMVEID 351
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
47-321 |
7.03e-82 |
|
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: 249.06 E-value: 7.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 47 SPALHYGQQAFEGLKAYRtkdgsIQLFRPDQNAERLQRTADRLLMP-HVPTDKFIAAVKSVVRANeefvppygTGATLYI 125
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGK-----GRLFRLDEHLDRLNRSAKRLGLPiPYDREELREALKELVAAN--------NGASLYI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 126 RPLLIGVGDIIGV--KPAEEYIFTVFAMPVGSYFKGGLTPTNFIVSKEYDRAAPNGTGAAKVGGNyAASLLPGKYAHEKQ 203
Cdd:cd00449 68 RPLLTRGVGGLGVapPPSPEPTFVVFASPVGAYAKGGEKGVRLITSPDRRRAAPGGTGDAKTGGN-LNSVLAKQEAAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 204 FSDVIYLDPATHtkIEEVGAANFFGItKDNQFITP-LSPSILPSITKYSLLYLAKERfGMEAIEGDVFVDELDKFTEAGA 282
Cdd:cd00449 147 ADEALLLDDNGY--VTEGSASNVFIV-KDGELVTPpLDGGILPGITRDSVIELAKEL-GIKVEERPISLDELYAADEVFL 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 446139925 283 CGTAAVISPIGGIQNGDdfhvfYSETEVGPATRKLYDEL 321
Cdd:cd00449 223 TGTAAEVTPVTEIDGRG-----IGDGKPGPVTRKLRELL 256
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
3-340 |
6.60e-81 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 251.18 E-value: 6.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 3 VNLDWDNLGFAYRKLPFRYISH-FKDGKWDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAER 81
Cdd:PLN02259 54 ADLDWDNLGFGLNPADYMYVMKcSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 82 LQRTADRLLMPHVPTDKFIAAVKSVVRANEEFVPPYGTGaTLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGGL 161
Cdd:PLN02259 134 MKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKG-TLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEGM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 162 TPTNFIVSKEYDRAAPNGTGAAKVGGNYAASLLPGKYAHEKQFSDVIYLDPATHTKIEEVGAANFFgITKDNQFITPLSP 241
Cdd:PLN02259 213 AALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVF-VVKGRTISTPATN 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 242 -SILPSITKYSLLYLAKERfGMEAIEGDVFVDELDKFTEAGACGTAAVISPIGGIQNGDDFHVFYSETEvgPATRKLYDE 320
Cdd:PLN02259 292 gTILEGITRKSVMEIASDQ-GYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEKRVEYKTGDE--SVCQKLRSV 368
|
330 340
....*....|....*....|
gi 446139925 321 LVGIQFGDVEAPEGWIYKVD 340
Cdd:PLN02259 369 LVGIQTGLIEDNKGWVTDIN 388
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
30-331 |
4.88e-78 |
|
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: 240.48 E-value: 4.88e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 30 WDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKdgsiqLFRPDQNAERLQRTADRLLMPH-VPTDKFIAAVKSVVR 108
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAYDGR-----LFRLDEHLARLNRSAKRLGIPIpYTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 109 ANEefvppygtGATLYIRPLLIGVGDIIGVKPAE-EYIFTVFAMPVGSYFKGGL-TPTNFIVSkEYDRAAPNGTGAAKvG 186
Cdd:COG0115 79 ANG--------LEDGYIRPQVTRGVGGRGVFAEEyEPTVIIIASPLPAYPAEAYeKGVRVITS-PYRRAAPGGLGGIK-T 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 187 GNYAASLLPGKYAHEKQFSDVIYLDpaTHTKIEEVGAANFFGItKDNQFITP-LSPSILPSITKYSLLYLAKERfGMEAI 265
Cdd:COG0115 149 GNYLNNVLAKQEAKEAGADEALLLD--TDGYVAEGSGSNVFIV-KDGVLVTPpLSGGILPGITRDSVIELAREL-GIPVE 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139925 266 EGDVFVDELDKFTEAGACGTAAVISPIGGIqngDDFHVfySETEVGPATRKLYDELVGIQFGDVEA 331
Cdd:COG0115 225 ERPISLEELYTADEVFLTGTAAEVTPVTEI---DGRPI--GDGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
4-339 |
4.98e-68 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 218.05 E-value: 4.98e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 4 NLDWDNLGFAYRKLPFRYISHF-KDGKWDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKDGSIQLFRPDQNAERL 82
Cdd:PLN02883 51 DVDWDKLGFSLVRTDFMFATKScRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 83 QRTADRLLMPHVPTDKFIAAVKSVVRANEEFVPPYGTGaTLYIRPLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGGLT 162
Cdd:PLN02883 131 KIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKG-SLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGTA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 163 PTNFIVSKEYDRAAPNGTGAAKVGGNYAASLLPGKYAHEKQFSDVIYLDPATHTKIEEVGAANFFgITKDNQFITP-LSP 241
Cdd:PLN02883 210 ALNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIF-LVKGNIIVTPaTSG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 242 SILPSITKYSLLYLAKErFGMEAIEGDVFVDELDKFTEAGACGTAAVISPIGGIQngddFHVFYSETEVGPA--TRKLYD 319
Cdd:PLN02883 289 TILGGITRKSIIEIALD-LGYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSIT----FKNTRTEYKVGDGivTQQLRS 363
|
330 340
....*....|....*....|
gi 446139925 320 ELVGIQFGDVEAPEGWIYKV 339
Cdd:PLN02883 364 ILLGIQTGSIQDTKDWVLQI 383
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
24-339 |
3.55e-42 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 148.37 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 24 HFKDGK-WDDGKLTD--DATLHISesSPALHYGQQAFEGLKAYRTKDGSiQLFRPDQNAERLQRTADRLLMPhVP--TDK 98
Cdd:PRK06606 3 ADRAGYiWFNGELVPweDAKVHVL--THALHYGTGVFEGIRAYDTPKGP-AIFRLREHTKRLFNSAKILRME-IPysVDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 99 FIAAVKSVVRANEEfvppygtgATLYIRPlLIGVGDI-IGVKPAEEYI-FTVFAMPVGSYfkggLTPTNF-------IVS 169
Cdd:PRK06606 79 LMEAQREVVRKNNL--------KSAYIRP-LVFVGDEgLGVRPHGLPTdVAIAAWPWGAY----LGEEALekgirvkVSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 170 keYDRAAPNGT-GAAKVGGNYAASLLPGKYAHEKQFSDVIYLDpaTHTKIEEVGAANFFgITKDNQFITP-LSPSILPSI 247
Cdd:PRK06606 146 --WTRHAPNSIpTRAKASGNYLNSILAKTEARRNGYDEALLLD--VEGYVSEGSGENIF-IVRDGVLYTPpLTSSILEGI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 248 TKYSLLYLAKErFGMEAIEGDVFVDELDKFTEAGACGTAAVISPIGGIqngDDFHVfySETEVGPATRKLYDELVGIQFG 327
Cdd:PRK06606 221 TRDTVITLAKD-LGIEVIERRITRDELYIADEVFFTGTAAEVTPIREV---DGRQI--GNGKRGPITEKLQSAYFDIVRG 294
|
330
....*....|..
gi 446139925 328 DVEAPEGWIYKV 339
Cdd:PRK06606 295 RTEKYAHWLTPV 306
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
30-339 |
1.38e-35 |
|
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: 130.94 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 30 WDDGKLTD--DATLHISesSPALHYGQQAFEGLKAYRTKDGSIqLFRPDQNAERLQRTADRLLMPhVP--TDKFIAAVKS 105
Cdd:TIGR01122 1 WMDGEFVDweDAKVHVL--THALHYGTGVFEGIRAYDTDKGPA-IFRLKEHIQRLYDSAKIYRME-IPysKEELMEATRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 106 VVRANEEfvppygtgATLYIRPLL-IGVGDiIGVKPAEEYIFTVF--AMPVGSYFkGGLTPTNFIVSK--EYDRAAPNGT 180
Cdd:TIGR01122 77 TLRKNNL--------RSAYIRPLVfRGDGD-LGLNPRAGYKPDVIiaAWPWGAYL-GEEALEKGIDAKvsSWRRNAPNTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 181 -GAAKVGGNYAASLLPGKYAHEKQFSDVIYLDPatHTKIEEVGAANFFgITKDNQFITP-LSPSILPSITKYSLLYLAKE 258
Cdd:TIGR01122 147 pTAAKAGGNYLNSLLAKSEARRHGYDEAILLDV--EGYVAEGSGENIF-IVKDGVLFTPpVTSSILPGITRDTVITLAKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 259 RfGMEAIEGDVFVDELDKFTEAGACGTAAVISPI---GGIQNGDDfhvfysetEVGPATRKLYDELVGIQFGDVEAPEGW 335
Cdd:TIGR01122 224 L-GIEVVEQPISREELYTADEAFFTGTAAEITPIrevDGRKIGNG--------RRGPVTKKLQEAFFDLVTGGTEDYWGW 294
|
....
gi 446139925 336 IYKV 339
Cdd:TIGR01122 295 LTYV 298
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
55-295 |
6.98e-33 |
|
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: 121.70 E-value: 6.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 55 QAFEGLKAYrtkDGSIqlFRPDQNAERLQRTADRLLMPHVPTDKFI-AAVKSVVRANEEFVPpygtgatlYIRPLLIGVG 133
Cdd:pfam01063 1 GVFETLRVY---NGKI--FFLDEHLARLRRSAKLLGIPLPFDEEDLrKIIEELLKANGLGVG--------RLRLTVSRGP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 134 DIIGVKPAE-EYIFTVFAMPVGSYFKGGLTptnfiVSKEYDRAAPNGTGAAKVGgNYAASLLPGKYAHEKQFSDVIYLDP 212
Cdd:pfam01063 68 GGFGLPTSDpTLAIFVSALPPPPESKKKGV-----ISSLVRRNPPSPLPGAKTL-NYLENVLARREAKAQGADDALLLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 213 ATHtkIEEVGAANFFgITKDNQFITP-LSPSILPSITKYSLLYLAKERfGMEAIEGDVFVDELDKFTEAGACGTAAVISP 291
Cdd:pfam01063 142 DGN--VTEGSTSNVF-LVKGGTLYTPpLESGILPGITRQALLDLAKAL-GLEVEERPITLADLQEADEAFLTNSLRGVTP 217
|
....
gi 446139925 292 IGGI 295
Cdd:pfam01063 218 VSSI 221
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
26-323 |
3.48e-23 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 97.35 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 26 KDGK-WDDGKLTD--DATLHISesSPALHYGQQAFEGLKAYrtkDGSIqlFRPDQNAERLQRTADRLLMPhVP--TDKFI 100
Cdd:PRK07544 7 RDGFiWMDGELVPwrDAKVHVL--THGLHYASSVFEGERAY---GGKI--FKLREHSERLRRSAELLDFE-IPysVAEID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 101 AAVKSVVRANeefvppygtGAT-LYIRPLLIGVGDIIGVKPAEEYI-FTVFAMPVGSYF-----KGGLTPTnfivSKEYD 173
Cdd:PRK07544 79 AAKKETLAAN---------GLTdAYVRPVAWRGSEMMGVSAQQNKIhLAIAAWEWPSYFdpeakMKGIRLD----IAKWR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 174 RAAPNGT-GAAKVGGNYAASLLPGKYAHEKQFSDVIYLDPATHtkIEEVGAANFFGItKDNQFITPLSPSILPSITKYSL 252
Cdd:PRK07544 146 RPDPETApSAAKAAGLYMICTISKHAAEAKGYADALMLDYRGY--VAEATGANIFFV-KDGVIHTPTPDCFLDGITRQTV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139925 253 LYLAKERfGMEAIEGDVFVDELDKFTEAGACGTAAVISPIGGIqnGDdfHVFysetEVGPATRKL---YDELVG 323
Cdd:PRK07544 223 IELAKRR-GIEVVERHIMPEELAGFSECFLTGTAAEVTPVSEI--GE--YRF----TPGAITRDLmddYEALVR 287
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
30-321 |
6.76e-14 |
|
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: 70.71 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 30 WDDGKLTDDATLHISESSPALHYGQQAFEGLKAYRTKdgsiqLFRPDQNAERLQRTADRLLMPH-VPTDKFIAAVKSVVR 108
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNGK-----PFALDEHLDRLYRSAKELRIDIpYTREELKELIRELVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 109 ANEefvppyGTGATLYIRpLLIGVGDIIGVKPAEEYIFTVFAMPVGSYFKGGLTPTNFIVSKEYDRAapNGTGAAKVGgN 188
Cdd:cd01558 76 KNE------GGEGDVYIQ-VTRGVGPRGHDFPKCVKPTVVIITQPLPLPPAELLEKGVRVITVPDIR--WLRCDIKSL-N 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 189 YAASLLPGKYAHEKQFSDVIYLDPatHTKIEEVGAANFFGITKDNQFITPLSPSILPSITKYSLLYLAKErFGMEAIEGD 268
Cdd:cd01558 146 LLNNVLAKQEAKEAGADEAILLDA--DGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKE-LGIPVEERP 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446139925 269 VFVDELDKFTEAGACGTAAVISPIGGIqNGDDFHvfysETEVGPATRKLYDEL 321
Cdd:cd01558 223 FSLEELYTADEVFLTSTTAEVMPVVEI-DGRPIG----DGKPGPVTKRLREAY 270
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
49-321 |
3.34e-09 |
|
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: 56.55 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 49 ALHYGQQAFEGLKAYrtkDGSIQLFrpDQNAERLQRTADRLLMPHVPTDKFIAAVKSVVRANeefvpPYGTGAtlyIRpL 128
Cdd:cd01559 3 GFAYGDGVFETMRAL---DGRLFLL--DAHLARLERSARRLGIPEPDLPRLRAALESLLAAN-----DIDEGR---IR-L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 129 LI--GVGD---IIGVKPAEEYIFTVFAMPVGSYFKGGLTPTNFIVSKEYdraaPNGTGAAKVggNYAASLLPGKYAHEKQ 203
Cdd:cd01559 69 ILsrGPGGrgyAPSVCPGPALYVSVIPLPPAWRQDGVRLITCPVRLGEQ----PLLAGLKHL--NYLENVLAKREARDRG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 204 FSDVIYLDPATHtkIEEVGAANFFgITKDNQFITP-LSPSILPSITKYSLLYLAKERfGMEAIEGDVFVDELDKFTEAGA 282
Cdd:cd01559 143 ADEALFLDTDGR--VIEGTASNLF-FVKDGELVTPsLDRGGLAGITRQRVIELAAAK-GYAVDERPLRLEDLLAADEAFL 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 446139925 283 CGTAAVISPIGGIqNGDDFhvfysetEVGPATRKLYDEL 321
Cdd:cd01559 219 TNSLLGVAPVTAI-DDHDG-------PPGPLTRALRELL 249
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
52-320 |
7.72e-08 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 52.95 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 52 YGQQAFEGLKAYrtkDGSIqlFRPDQNAERLQRTADRLLM-PHVPTDKFIAAVKSVVRANEefvppygtgatL---YIRP 127
Cdd:PRK08320 28 YGDGVFEGIRAY---NGRV--FRLKEHIDRLYDSAKAIMLeIPLSKEEMTEIVLETLRKNN-----------LrdaYIRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 128 LLI-GVGDiIGVKPAEEYIFTVF-------AMPvGSYFKGGLTptnfIVSKEYDRAAPNGTGAAKVGGNYAASLLPGKYA 199
Cdd:PRK08320 92 VVSrGVGD-LGLDPRKCPKPTVVciaepigLYP-GELYEKGLK----VITVSTRRNRPDALSPQVKSLNYLNNILAKIEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 200 HEKQFSDVIYLDpaTHTKIEEVGAANFFgITKDNQFITP-LSPSILPSITKYSLLYLAKERfGMEAIEG-----DVFV-D 272
Cdd:PRK08320 166 NLAGVDEAIMLN--DEGYVAEGTGDNIF-IVKNGKLITPpTYAGALEGITRNAVIEIAKEL-GIPVREElftlhDLYTaD 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 446139925 273 ELdkFTeagaCGTAAVISP---IGG--IQNGddfhvfysetEVGPATRKLYDE 320
Cdd:PRK08320 242 EV--FL----TGTAAEVIPvvkVDGrvIGDG----------KPGPITKKLLEE 278
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
199-317 |
8.47e-05 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 43.77 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 199 AHEKQFSDVIYLDPATHTkieEVGAANFFGITKDNQFIT-PLSPSILPSITKYSLLYLAKERfGMEAIEGDVFVDELDKF 277
Cdd:PRK06680 163 AKEAGAQEAWMVDDGFVT---EGASSNAWIVTKDGKLVTrPADNFILPGITRHTLIDLAKEL-GLEVEERPFTLQEAYAA 238
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446139925 278 TEAGACGTAAVISP---IGGIQNGDDfhvfysetEVGPATRKL 317
Cdd:PRK06680 239 REAFITAASSFVFPvvqIDGKQIGNG--------KPGPIAKRL 273
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
18-319 |
4.13e-04 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 41.48 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 18 PFRYISHFKDGKWDDGkltdDATLhISESSPALHYGQQAFEGLKAYrtkDGsiqlFRPDQNA--ERLQRTADRLLM-PHV 94
Cdd:PRK13356 3 PGSNTWTFFDGEWHEG----NVPI-MGPADHAAWLGSTVFDGARAF---EG----VTPDLDLhcARVNRSAEALGLkPTV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 95 PTDKFIAAVKSVVRAneefvppYGTGATLYIRPLLIGV-GDIIGVKPAEEYifTVFA-------MPVGSYFKGGLTPtnf 166
Cdd:PRK13356 71 SAEEIEALAREGLKR-------FDPDTALYIRPMYWAEdGFASGVAPDPES--TRFAlcleeapMPEPTGFSLTLSP--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 167 ivskeYDRAAPNGTGA-AKvggnyAASLLPG-----KYAHEKQFSDVIYLDPATHtkIEEVGAANFFgITKDNQFITPL- 239
Cdd:PRK13356 139 -----FRRPTLEMAPTdAK-----AGCLYPNnaralREARSRGFDNALVLDMLGN--VAETATSNVF-MVKDGVVFTPVp 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139925 240 SPSILPSITKYSLLYLAKERfGMEAIEGDVFVDELDKFTEAGACGTAAVISPIGGIqngDDfhvfySETEVGPATRKLYD 319
Cdd:PRK13356 206 NGTFLNGITRQRVIALLRED-GVTVVETTLTYEDFLEADEVFSTGNYSKVVPVTRF---DD-----RSLQPGPVTRRARE 276
|
|
| |
