|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
1-318 |
0e+00 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 641.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 1 MFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQ 80
Cdd:PLN02883 67 MFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKIGAERMCMHSPSVHQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 81 FIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGG 160
Cdd:PLN02883 147 FIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 161 TGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDL 240
Cdd:PLN02883 227 TGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDL 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186478315 241 GYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILVGIQTGSIQDTKDWVLQIA 318
Cdd:PLN02883 307 GYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILLGIQTGSIQDTKDWVLQIA 384
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
24-305 |
3.22e-115 |
|
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: 334.16 E-value: 3.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 24 ELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGS 103
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 104 LYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIpRAYLGGTGGVKAISNYGPVLEVMRRAKSR 183
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVSSFR-RAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 184 GFSDVLYLDADTGkNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCT 263
Cdd:cd01557 160 GYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 186478315 264 GTAAGVASVGSITFKNTRTEYkVGDGIVTQQLRSILVGIQTG 305
Cdd:cd01557 239 GTAAVVTPVGEIDYRGKEPGE-GEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
14-317 |
8.02e-105 |
|
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: 309.00 E-value: 8.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 14 QGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANR 93
Cdd:TIGR01123 3 NGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKANK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 94 RWVPPPGKG-SLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGTGGVKAISNYGP 172
Cdd:TIGR01123 83 DWVPPYGSGaSLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVTTEYDRAAPGGTGAVKVGGNYAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 173 VLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGN-TIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPV 251
Cdd:TIGR01123 163 SLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGDgELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERRIDI 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478315 252 EELKEA----EEVFCTGTAAGVASVGSITFKNTRTEYKVGD-GIVTQQLRSILVGIQTGSIQDTKDWVLQI 317
Cdd:TIGR01123 243 DELKAFveagEIVFACGTAAVITPVGEIQHGGKEVVFASGQpGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
15-309 |
1.99e-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: 1.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 15 GYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEdgrvlLFRPELNAMRMKIGAERMCMHSP-SVHQFIEGVKQTVLANr 93
Cdd:COG0115 7 GELVPEEEATISVLDRGLHYGDGVFEGIRAYDGR-----LFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVAAN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 94 rwvpppGKGSLYLRPLLFGSGASLGVAAA-SEYTFLVFGSPVQNYFKEGTAA-LNLYVEEVIpRAYLGGTGGVKAIsNYG 171
Cdd:COG0115 81 ------GLEDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKgVRVITSPYR-RAAPGGLGGIKTG-NYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 172 PVLEVMRRAKSRGFSDVLYLDADtgKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPV 251
Cdd:COG0115 153 NNVLAKQEAKEAGADEALLLDTD--GYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478315 252 EELKEAEEVFCTGTAAGVASVGSItfkntrTEYKVGD---GIVTQQLRSILVGIQTGSIQD 309
Cdd:COG0115 231 EELYTADEVFLTGTAAEVTPVTEI------DGRPIGDgkpGPVTRRLRELYTDIVRGEAED 285
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
37-275 |
5.99e-41 |
|
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: 142.11 E-value: 5.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 37 GLIEGMKAYRGEdgrvlLFRPELNAMRMKIGAERMCM-HSPSVHQFIEGVKQTVLANRRWVPppgkgslYLRPLLFGSGA 115
Cdd:pfam01063 1 GVFETLRVYNGK-----IFFLDEHLARLRRSAKLLGIpLPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 116 SLGVAAaSEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGtggVKAIsNYGPVLEVMRRAKSRGFSDVLYLDADT 195
Cdd:pfam01063 69 GFGLPT-SDPTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPG---AKTL-NYLENVLARREAKAQGADDALLLDEDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 196 gkNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSI 275
Cdd:pfam01063 144 --NVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
1-318 |
0e+00 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 641.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 1 MFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQ 80
Cdd:PLN02883 67 MFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKIGAERMCMHSPSVHQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 81 FIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGG 160
Cdd:PLN02883 147 FIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 161 TGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDL 240
Cdd:PLN02883 227 TGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALDL 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186478315 241 GYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILVGIQTGSIQDTKDWVLQIA 318
Cdd:PLN02883 307 GYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILLGIQTGSIQDTKDWVLQIA 384
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
1-318 |
1.03e-165 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 467.02 E-value: 1.03e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 1 MFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQ 80
Cdd:PLN02782 85 MYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRNGAERMCMPAPTVEQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 81 FIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGG 160
Cdd:PLN02782 165 FVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGVAPINLIVENEFHRATPGG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 161 TGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDL 240
Cdd:PLN02782 245 TGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQ 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478315 241 GYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKV-GDGIVTQQLRSILVGIQTGSIQDTKDWVLQIA 318
Cdd:PLN02782 325 GFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSITYKGKRVSYGEgGFGTVSQQLYTVLTSLQMGLIEDNMNWTVELS 403
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
1-317 |
1.07e-156 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 442.06 E-value: 1.07e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 1 MFATKsCRDG-NFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVH 79
Cdd:PLN03117 35 MYVAK-CKQGeSFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGADRLCMTPPSLE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 80 QFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEgTAALNLYVEEVIPRAYLG 159
Cdd:PLN03117 114 QFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKA-SSGLNLKVDHKHRRAHSG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 160 GTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALD 239
Cdd:PLN03117 193 GTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARD 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186478315 240 LGYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILVGIQTGSIQDTKDWVLQI 317
Cdd:PLN03117 273 IGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEALSTKLHLILTNIQMGVVEDKKGWMVEI 350
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
1-317 |
1.25e-147 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 420.28 E-value: 1.25e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 1 MFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQ 80
Cdd:PLN02259 71 MYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 81 FIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGG 160
Cdd:PLN02259 151 FVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEGMAALNLYVEEEYVRAAPGG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 161 TGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDL 240
Cdd:PLN02259 231 AGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQ 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186478315 241 GYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILVGIQTGSIQDTKDWVLQI 317
Cdd:PLN02259 311 GYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEKRVEYKTGDESVCQKLRSVLVGIQTGLIEDNKGWVTDI 387
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
8-314 |
5.25e-134 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 384.50 E-value: 5.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 8 RDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQ 87
Cdd:PRK13357 38 KDGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 88 TVLANRRWVPPPGKG-SLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGTGGVKA 166
Cdd:PRK13357 118 LVKADRDWVPPYGEGaSLYLRPFMIATEPFLGVKPAEEYIFCVIASPVGAYFKGGVKPVSIWVSDEYDRAAPGGTGAAKV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 167 ISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEE 246
Cdd:PRK13357 198 GGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNFFFITKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEE 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186478315 247 RSVPVEELKEA------EEVFCTGTAAGVASVGSITFKNtrTEYKVGDGI---VTQQLRSILVGIQTGSIQDTKDWV 314
Cdd:PRK13357 278 RPVSIDEWQADaasgefTEAFACGTAAVITPIGGIKYKD--KEFVIGDGEvgpVTQKLYDELTGIQFGDVEDPHGWI 352
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
24-305 |
3.22e-115 |
|
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: 334.16 E-value: 3.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 24 ELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGS 103
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 104 LYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIpRAYLGGTGGVKAISNYGPVLEVMRRAKSR 183
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVSSFR-RAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 184 GFSDVLYLDADTGkNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCT 263
Cdd:cd01557 160 GYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 186478315 264 GTAAGVASVGSITFKNTRTEYkVGDGIVTQQLRSILVGIQTG 305
Cdd:cd01557 239 GTAAVVTPVGEIDYRGKEPGE-GEVGPVTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
14-317 |
8.02e-105 |
|
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: 309.00 E-value: 8.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 14 QGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANR 93
Cdd:TIGR01123 3 NGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKANK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 94 RWVPPPGKG-SLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGTGGVKAISNYGP 172
Cdd:TIGR01123 83 DWVPPYGSGaSLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVTTEYDRAAPGGTGAVKVGGNYAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 173 VLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGN-TIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPV 251
Cdd:TIGR01123 163 SLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFITGDgELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERRIDI 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478315 252 EELKEA----EEVFCTGTAAGVASVGSITFKNTRTEYKVGD-GIVTQQLRSILVGIQTGSIQDTKDWVLQI 317
Cdd:TIGR01123 243 DELKAFveagEIVFACGTAAVITPVGEIQHGGKEVVFASGQpGEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
15-309 |
1.99e-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: 1.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 15 GYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEdgrvlLFRPELNAMRMKIGAERMCMHSP-SVHQFIEGVKQTVLANr 93
Cdd:COG0115 7 GELVPEEEATISVLDRGLHYGDGVFEGIRAYDGR-----LFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVAAN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 94 rwvpppGKGSLYLRPLLFGSGASLGVAAA-SEYTFLVFGSPVQNYFKEGTAA-LNLYVEEVIpRAYLGGTGGVKAIsNYG 171
Cdd:COG0115 81 ------GLEDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAYEKgVRVITSPYR-RAAPGGLGGIKTG-NYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 172 PVLEVMRRAKSRGFSDVLYLDADtgKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPV 251
Cdd:COG0115 153 NNVLAKQEAKEAGADEALLLDTD--GYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478315 252 EELKEAEEVFCTGTAAGVASVGSItfkntrTEYKVGD---GIVTQQLRSILVGIQTGSIQD 309
Cdd:COG0115 231 EELYTADEVFLTGTAAEVTPVTEI------DGRPIGDgkpGPVTRRLRELYTDIVRGEAED 285
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
32-299 |
2.00e-78 |
|
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: 239.43 E-value: 2.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 32 LNYGQGLIEGMKAYRGedgrvLLFRPELNAMRMKIGAERMCM-HSPSVHQFIEGVKQTVLANrrwvpppGKGSLYLRPLL 110
Cdd:cd00449 4 LHYGDGVFEGLRAGKG-----RLFRLDEHLDRLNRSAKRLGLpIPYDREELREALKELVAAN-------NGASLYIRPLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 111 FGSGASLGVA--AASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGTGGVKAISNYGPVLeVMRRAKSRGFSDV 188
Cdd:cd00449 72 TRGVGGLGVAppPSPEPTFVVFASPVGAYAKGGEKGVRLITSPDRRRAAPGGTGDAKTGGNLNSVL-AKQEAAEAGADEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 189 LYLDADTgkNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTAAG 268
Cdd:cd00449 151 LLLDDNG--YVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAAE 228
|
250 260 270
....*....|....*....|....*....|.
gi 186478315 269 VASVGSITFKNTrTEYKVGDgiVTQQLRSIL 299
Cdd:cd00449 229 VTPVTEIDGRGI-GDGKPGP--VTRKLRELL 256
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
37-275 |
5.99e-41 |
|
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: 142.11 E-value: 5.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 37 GLIEGMKAYRGEdgrvlLFRPELNAMRMKIGAERMCM-HSPSVHQFIEGVKQTVLANRRWVPppgkgslYLRPLLFGSGA 115
Cdd:pfam01063 1 GVFETLRVYNGK-----IFFLDEHLARLRRSAKLLGIpLPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 116 SLGVAAaSEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGtggVKAIsNYGPVLEVMRRAKSRGFSDVLYLDADT 195
Cdd:pfam01063 69 GFGLPT-SDPTLAIFVSALPPPPESKKKGVISSLVRRNPPSPLPG---AKTL-NYLENVLARREAKAQGADDALLLDEDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 196 gkNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSI 275
Cdd:pfam01063 144 --NVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
32-314 |
1.68e-38 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 137.97 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 32 LNYGQGLIEGMKAYRGEDGRVLlFRPELNAMRMKIGAERMCMHSP-SVHQFIEGVKQTVLANrrwvpppGKGSLYLRPLL 110
Cdd:PRK06606 30 LHYGTGVFEGIRAYDTPKGPAI-FRLREHTKRLFNSAKILRMEIPySVDELMEAQREVVRKN-------NLKSAYIRPLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 111 FGSGASLGVAAAS-EYTFLVFGSPVQNYFkeGTAALNLYVE-----------EVIP-RAylggtggvKAISNYgpVLEVM 177
Cdd:PRK06606 102 FVGDEGLGVRPHGlPTDVAIAAWPWGAYL--GEEALEKGIRvkvsswtrhapNSIPtRA--------KASGNY--LNSIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 178 --RRAKSRGFSDVLYLDADtGKnIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELK 255
Cdd:PRK06606 170 akTEARRNGYDEALLLDVE-GY-VSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVIERRITRDELY 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186478315 256 EAEEVFCTGTAAGVASVGSItfkntrTEYKVGDGI---VTQQLRSILVGIQTGSIQDTKDWV 314
Cdd:PRK06606 248 IADEVFFTGTAAEVTPIREV------DGRQIGNGKrgpITEKLQSAYFDIVRGRTEKYAHWL 303
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
32-317 |
3.51e-34 |
|
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: 126.71 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 32 LNYGQGLIEGMKAYRGEDGRVLlFRPELNAMRMKIGAERMCMHSP-SVHQFIEGVKQTVLANrrwvpppGKGSLYLRPLL 110
Cdd:TIGR01122 21 LHYGTGVFEGIRAYDTDKGPAI-FRLKEHIQRLYDSAKIYRMEIPySKEELMEATRETLRKN-------NLRSAYIRPLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 111 FGSGASLGVAAASEYTFLVF-----------GSPVQNYFKEGTAALNLYVEEVIPRAylggtggVKAISNYGPVLEVMRR 179
Cdd:TIGR01122 93 FRGDGDLGLNPRAGYKPDVIiaawpwgaylgEEALEKGIDAKVSSWRRNAPNTIPTA-------AKAGGNYLNSLLAKSE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 180 AKSRGFSDVLYLDADtgKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEE 259
Cdd:TIGR01122 166 ARRHGYDEAILLDVE--GYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQPISREELYTADE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186478315 260 VFCTGTAAGVASVGSITFKntrteyKVGDGI---VTQQLRSILVGIQTGSIQDTKDWVLQI 317
Cdd:TIGR01122 244 AFFTGTAAEITPIREVDGR------KIGNGRrgpVTKKLQEAFFDLVTGGTEDYWGWLTYV 298
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
34-296 |
3.70e-28 |
|
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: 109.61 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 34 YGQGLIEGMKAYRGEdgrvlLFRPELNAMRMKIGAERMCMHSP-SVHQFIEGVKQTVLANRRwvpppGKGSLYLRPllfg 112
Cdd:cd01558 23 FGDGVYEVIRVYNGK-----PFALDEHLDRLYRSAKELRIDIPyTREELKELIRELVAKNEG-----GEGDVYIQV---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 113 sgaSLGVAAaseyTFLVFGSPVQNYFKEGTAALNLYVEEVIPRaylggtgGVKAIS--------------NY-GPVLeVM 177
Cdd:cd01558 89 ---TRGVGP----RGHDFPKCVKPTVVIITQPLPLPPAELLEK-------GVRVITvpdirwlrcdikslNLlNNVL-AK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 178 RRAKSRGFSDVLYLDADtgKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEA 257
Cdd:cd01558 154 QEAKEAGADEAILLDAD--GLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 186478315 258 EEVFCTGTAAGVASVGSItfkNTRT--EYKVGDgiVTQQLR 296
Cdd:cd01558 232 DEVFLTSTTAEVMPVVEI---DGRPigDGKPGP--VTKRLR 267
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
32-295 |
1.39e-24 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 100.82 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 32 LNYGQGLIEGMKAYRGEdgrvlLFRPELNAMRMKIGAERMCMHSP-SVHQfIEGVKQTVLANRRWVpppgkgSLYLRPLL 110
Cdd:PRK07544 32 LHYASSVFEGERAYGGK-----IFKLREHSERLRRSAELLDFEIPySVAE-IDAAKKETLAANGLT------DAYVRPVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 111 FGSGASLGVAAASEYTFLVFGS-PVQNYF----KEGTAALNLYV-----EEVIPRAylggtggVKAISNYgpvlevM--- 177
Cdd:PRK07544 100 WRGSEMMGVSAQQNKIHLAIAAwEWPSYFdpeaKMKGIRLDIAKwrrpdPETAPSA-------AKAAGLY------Mict 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 178 ---RRAKSRGFSDVLYLDADtgKNIEEVSAANIFLVKGNTIVTPaTSGTILGGITRKSIIEIALDLGYKVEERSVPVEEL 254
Cdd:PRK07544 167 iskHAAEAKGYADALMLDYR--GYVAEATGANIFFVKDGVIHTP-TPDCFLDGITRQTVIELAKRRGIEVVERHIMPEEL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 186478315 255 KEAEEVFCTGTAAGVASVGSItfkntrTEYKVGDGIVTQQL 295
Cdd:PRK07544 244 AGFSECFLTGTAAEVTPVSEI------GEYRFTPGAITRDL 278
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
34-275 |
1.60e-23 |
|
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: 96.99 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 34 YGQGLIEGMKAYrgeDGRVLLFRPELNamRMKIGAERMCMHSPSVHQFIEGVKQTVLANrrwvpPPGKGslYLRpLLFGS 113
Cdd:cd01559 6 YGDGVFETMRAL---DGRLFLLDAHLA--RLERSARRLGIPEPDLPRLRAALESLLAAN-----DIDEG--RIR-LILSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 114 GASLGVAAASeytflVFGSPVqnyfkegtaalnLYVEeVIPRAYLGGTGGVKAIS-----------------NYGPVLEV 176
Cdd:cd01559 73 GPGGRGYAPS-----VCPGPA------------LYVS-VIPLPPAWRQDGVRLITcpvrlgeqpllaglkhlNYLENVLA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 177 MRRAKSRGFSDVLYLDADtgKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKE 256
Cdd:cd01559 135 KREARDRGADEALFLDTD--GRVIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLA 212
|
250
....*....|....*....
gi 186478315 257 AEEVFCTGTAAGVASVGSI 275
Cdd:cd01559 213 ADEAFLTNSLLGVAPVTAI 231
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
99-272 |
2.25e-21 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 91.55 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 99 PGKGSLYLRPLLFG-SGASLGVAAASEYTflvfgspvqnyfkegTAALNLYveevipRAYLGGTGGVKA-ISNYG-PVLE 175
Cdd:PRK13356 87 DPDTALYIRPMYWAeDGFASGVAPDPEST---------------RFALCLE------EAPMPEPTGFSLtLSPFRrPTLE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 176 VM-----------------RRAKSRGFSDVLYLDADtgKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIAL 238
Cdd:PRK13356 146 MAptdakagclypnnaralREARSRGFDNALVLDML--GNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLR 223
|
170 180 190
....*....|....*....|....*....|....
gi 186478315 239 DLGYKVEERSVPVEELKEAEEVFCTGTAAGVASV 272
Cdd:PRK13356 224 EDGVTVVETTLTYEDFLEADEVFSTGNYSKVVPV 257
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
34-272 |
7.42e-19 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 84.92 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 34 YGQGLIEGMKAYrgeDGRVllFRPELNAMRMKIGAERMCMHSP-SVHQFIEGVKQTVLANR------RWVPPPGKGSLYL 106
Cdd:PRK08320 28 YGDGVFEGIRAY---NGRV--FRLKEHIDRLYDSAKAIMLEIPlSKEEMTEIVLETLRKNNlrdayiRLVVSRGVGDLGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 107 RPllfgsgaslgvAAASEYTFLVFGSPVQNYFKEgtaalnLYveevipraylggTGGVKAIS------------------ 168
Cdd:PRK08320 103 DP-----------RKCPKPTVVCIAEPIGLYPGE------LY------------EKGLKVITvstrrnrpdalspqvksl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 169 NYGPVLEVMRRAKSRGFSDVLYLDaDTGkNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERS 248
Cdd:PRK08320 154 NYLNNILAKIEANLAGVDEAIMLN-DEG-YVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREEL 231
|
250 260
....*....|....*....|....
gi 186478315 249 VPVEELKEAEEVFCTGTAAGVASV 272
Cdd:PRK08320 232 FTLHDLYTADEVFLTGTAAEVIPV 255
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
34-295 |
1.60e-16 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 78.46 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 34 YGQGLIEGMKAYRGEdgrvlLFRPELNAMRMKIGAERMCMHSP-SVHQFIEGVKQTVLANR------RWVPPPGKGSLYL 106
Cdd:PRK12479 29 YGDGVFEGIRSYGGN-----VFCLKEHVKRLYESAKSILLTIPlTVDEMEEAVLQTLQKNEyadayiRLIVSRGKGDLGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 107 RPLlFGSGASLGVAAASEYTFlvfgsPvQNYFKEGTAALNLYVEEVIPRAYlggTGGVKAISNYGPVLEVMRRAKSrGFS 186
Cdd:PRK12479 104 DPR-SCVKPSVIIIAEQLKLF-----P-QEFYDNGLSVVSVASRRNTPDAL---DPRIKSMNYLNNVLVKIEAAQA-GVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 187 DVLYLDADtgKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTA 266
Cdd:PRK12479 173 EALMLNQQ--GYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLTGTA 250
|
250 260 270
....*....|....*....|....*....|..
gi 186478315 267 AGVASVGSITFKntrteyKVGDGI---VTQQL 295
Cdd:PRK12479 251 AELIPVVKVDSR------EIGDGKpgsVTKQL 276
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
206-296 |
5.03e-15 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 73.85 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 206 NIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSItfknTRTEYK 285
Cdd:PRK07650 182 NLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFVTNSIQEIVPLTRI----EERDFP 257
|
90
....*....|.
gi 186478315 286 VGDGIVTQQLR 296
Cdd:PRK07650 258 GKVGMVTKRLQ 268
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
184-299 |
1.85e-14 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 72.18 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 184 GFSDVLYLDADtGKNIEEVsAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCT 263
Cdd:PRK06092 158 EADEALVLDSE-GWVIECC-AANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVFIC 235
|
90 100 110
....*....|....*....|....*....|....*.
gi 186478315 264 GTAAGVASVGSItfknTRTEYKVgdGIVTQQLRSIL 299
Cdd:PRK06092 236 NSLMPVWPVRAI----GETSYSS--GTLTRYLQPLC 265
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
49-275 |
4.41e-14 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 71.14 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 49 DGRVLLFRPELNamRMKIGAERMCMHSPSVHQFIEGVKqtvLANRRWVPPPGKGSL---YLRpllfgsgaslGVAAASEY 125
Cdd:PRK07849 49 DGRPCNLEAHLE--RLARSAALLDLPEPDLDRWRRAVE---LAIEEWRAPEDEAALrlvYSR----------GRESGGAP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 126 TFLVFGSPVQNYFK----EGTAALNLyveeviPRAYLGGTG--------GVKAISnYGPVLEVMRRAKSRGFSDVLYLDA 193
Cdd:PRK07849 114 TAWVTVSPVPERVArarrEGVSVITL------DRGYPSDAAerapwllaGAKTLS-YAVNMAALRYAARRGADDVIFTST 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 194 DtgKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTAAGVASVG 273
Cdd:PRK07849 187 D--GYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWLVSSVRLAARVH 264
|
..
gi 186478315 274 SI 275
Cdd:PRK07849 265 TL 266
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
201-298 |
2.56e-13 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 68.80 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 201 EVSAANIFLV-KGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSITFKn 279
Cdd:PRK06680 181 EGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITAASSFVFPVVQIDGK- 259
|
90 100
....*....|....*....|..
gi 186478315 280 trteyKVGDGI---VTQQLRSI 298
Cdd:PRK06680 260 -----QIGNGKpgpIAKRLREA 276
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
147-272 |
2.00e-07 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 51.94 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 147 LYVEEVIPRAYLGGTGGVKAIS----------------NYGPVLEVMRRAKSRGFSDVLYLDADtgKNIEEVSAANI-FL 209
Cdd:PLN02845 150 FYAVVIEDTYAQDRPEGVKVVTssvpikppqfatvksvNYLPNALSQMEAEERGAFAGIWLDEE--GFVAEGPNMNVaFL 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186478315 210 VKGNTIVTPATSgTILGGITRKSIIEIA-----LDLGYKVEERSVPVEELKEAEEVFCTGTAAGVASV 272
Cdd:PLN02845 228 TNDGELVLPPFD-KILSGCTARRVLELAprlvsPGDLRGVKQRKISVEEAKAADEMMLIGSGVPVLPI 294
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
163-265 |
1.20e-06 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 49.25 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 163 GVKAIS--------------NYGPVLEVMRRAKSRGFSDVLYLDADTgknIEEVSAANIFLVKGNTIVTPATSGTILGGI 228
Cdd:PRK12400 134 GVRAISepdtrwlrcdikslNLLPNILAATKAERKGCKEALFVRNGT---VTEGSHSNFFLIKNGTLYTHPANHLILNGI 210
|
90 100 110
....*....|....*....|....*....|....*..
gi 186478315 229 TRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGT 265
Cdd:PRK12400 211 IRQYVLSLAKTLRIPVQEELFSVRDVYQADECFFTGT 247
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
178-275 |
6.46e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 46.90 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478315 178 RRAKSRGFSDVLYLDADtGKnIEEVSAANIFLVKGNTIVTPatSGTILGGITrKSIIEIALD-LGYKVEERSVPVEELKE 256
Cdd:PRK09266 146 RLAQRAGFDDALFVDPD-GR-VSEGATWNLGFWDGGAVVWP--QAPALPGVT-MALLQRGLErLGIPQRTRPVTLADLGR 220
|
90
....*....|....*....
gi 186478315 257 AEEVFCTGTAAGVASVGSI 275
Cdd:PRK09266 221 FAGAFACNAWRGQRAVSAI 239
|
|
| |
