|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
1-354 |
0e+00 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 717.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 1 MAPSAQPLPVSVSDEKYANVKWEELAFKFVRTDYMYVAKCNHGESFQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYR 80
Cdd:PLN03117 1 MAPSSSPLPTSKADEKYANVKWEELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 81 TEDGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGTLYIRPILFGSGPILGSFPIPETT 160
Cdd:PLN03117 81 TEDGRITLFRPDQNALRMQTGADRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 161 FTAFACPVGRYHKDNSGLNLKIEDQFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANV 240
Cdd:PLN03117 161 FLIYASPVGNYHKASSGLNLKVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 241 FMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASVTFKDKKTGFKTG 320
Cdd:PLN03117 241 FILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTG 320
|
330 340 350
....*....|....*....|....*....|....
gi 15230923 321 EETLAAKLYETLSDIQTGRVEDTKGWTVEIDRQG 354
Cdd:PLN03117 321 EEALSTKLHLILTNIQMGVVEDKKGWMVEIDRCQ 354
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
58-338 |
4.33e-105 |
|
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: 309.51 E-value: 4.33e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 58 QLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGT 137
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 138 LYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHKD-NSGLNLKIEDqFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQ 216
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGgEKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 217 GFSDILFLDAATGkNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCT 296
Cdd:cd01557 160 GYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15230923 297 GTASIVTSIASVTFKDKKTGFKTGEEtLAAKLYETLSDIQTG 338
Cdd:cd01557 239 GTAAVVTPVGEIDYRGKEPGEGEVGP-VTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
47-350 |
2.14e-103 |
|
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: 306.68 E-value: 2.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 47 QEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALAN 126
Cdd:TIGR01123 2 HNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 127 KKWIPPPGKG-TLYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHKDNSG-LNLKIEDQFRRAFPSGTGGVKSITNYC 204
Cdd:TIGR01123 82 KDWVPPYGSGaSLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLApVSIFVTTEYDRAAPGGTGAVKVGGNYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 205 PVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANVFML--KGNVVSTPtIAGTILPGVTRNCVMELCRDFGYQVEERTI 282
Cdd:TIGR01123 162 ASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFItgDGELVTPP-LSGSILPGITRDSLLQLAKDLGMEVEERRI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230923 283 pLVDFLDA-----DEAFCTGTASIVTSIASVTFKDKKTGFKTGEE-TLAAKLYETLSDIQTGRVEDTKGWTVEI 350
Cdd:TIGR01123 241 -DIDELKAfveagEIVFACGTAAVITPVGEIQHGGKEVVFASGQPgEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
46-342 |
4.13e-84 |
|
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: 256.27 E-value: 4.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 46 FQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYrteDGRIllFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVAL 124
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAY---DGRL--FRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 125 ANkkwipppGKGTLYIRPILFGSGPILGSFPI-PETTFTAFACPVGRYHKDN--SGLNLKIEDqFRRAFPSGTGGVKSiT 201
Cdd:COG0115 79 AN-------GLEDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAyeKGVRVITSP-YRRAAPGGLGGIKT-G 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 202 NYCPVWIPLAEAKKQGFSDILFLDAAtgKNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERT 281
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLLDTD--GYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230923 282 IPLVDFLDADEAFCTGTASIVTSIASV---TFKDKKTGfktgeeTLAAKLYETLSDIQTGRVED 342
Cdd:COG0115 228 ISLEELYTADEVFLTGTAAEVTPVTEIdgrPIGDGKPG------PVTRRLRELYTDIVRGEAED 285
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
71-308 |
3.55e-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: 143.65 E-value: 3.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 71 GLYEGLKAYrteDGRIllFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVALANKKWIPppgkgtlYIRPILF-GSG 148
Cdd:pfam01063 1 GVFETLRVY---NGKI--FFLDEHLARLRRSAKLLGIPLPfDEEDLRKIIEELLKANGLGVG-------RLRLTVSrGPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 149 PILGSFPIPETTFTAFACPVGRYhkdnSGLNLKIEDQFRRAFPSGTGGVKSiTNYCPVWIPLAEAKKQGFSDILFLDAAT 228
Cdd:pfam01063 69 GFGLPTSDPTLAIFVSALPPPPE----SKKKGVISSLVRRNPPSPLPGAKT-LNYLENVLARREAKAQGADDALLLDEDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 229 gkNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASV 308
Cdd:pfam01063 144 --NVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
1-354 |
0e+00 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 717.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 1 MAPSAQPLPVSVSDEKYANVKWEELAFKFVRTDYMYVAKCNHGESFQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYR 80
Cdd:PLN03117 1 MAPSSSPLPTSKADEKYANVKWEELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 81 TEDGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGTLYIRPILFGSGPILGSFPIPETT 160
Cdd:PLN03117 81 TEDGRITLFRPDQNALRMQTGADRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 161 FTAFACPVGRYHKDNSGLNLKIEDQFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANV 240
Cdd:PLN03117 161 FLIYASPVGNYHKASSGLNLKVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 241 FMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASVTFKDKKTGFKTG 320
Cdd:PLN03117 241 FILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTG 320
|
330 340 350
....*....|....*....|....*....|....
gi 15230923 321 EETLAAKLYETLSDIQTGRVEDTKGWTVEIDRQG 354
Cdd:PLN03117 321 EEALSTKLHLILTNIQMGVVEDKKGWMVEIDRCQ 354
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
18-350 |
2.05e-144 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 414.25 E-value: 2.05e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 18 ANVKWEELAFKFVRTDYMYVAKCNHGESFQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQNGLR 97
Cdd:PLN02782 68 ADIDWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 98 LQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGTLYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHKDN-S 176
Cdd:PLN02782 148 MRNGAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGvA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 177 GLNLKIEDQFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANVFMLKGNVVSTPTIAGT 256
Cdd:PLN02782 228 PINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIVKDNVISTPAIKGT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 257 ILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASVTFKDKKtgFKTGEETLAA---KLYETLS 333
Cdd:PLN02782 308 ILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSITYKGKR--VSYGEGGFGTvsqQLYTVLT 385
|
330
....*....|....*..
gi 15230923 334 DIQTGRVEDTKGWTVEI 350
Cdd:PLN02782 386 SLQMGLIEDNMNWTVEL 402
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
14-351 |
2.12e-141 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 406.03 E-value: 2.12e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 14 DEKYANVKWEELAFKFVRTDYMYVAKCNHGESFQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQ 93
Cdd:PLN02259 50 DDVYADLDWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 94 NGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGTLYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHK 173
Cdd:PLN02259 130 NAIRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 174 DN-SGLNLKIEDQFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANVFMLKGNVVSTPT 252
Cdd:PLN02259 210 EGmAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 253 IAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASVTFKDKKTGFKTGEETLAAKLYETL 332
Cdd:PLN02259 290 TNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEKRVEYKTGDESVCQKLRSVL 369
|
330
....*....|....*....
gi 15230923 333 SDIQTGRVEDTKGWTVEID 351
Cdd:PLN02259 370 VGIQTGLIEDNKGWVTDIN 388
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
6-351 |
2.77e-134 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 386.81 E-value: 2.77e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 6 QPLPVSVSDEKyANVKWEELAFKFVRTDYMYVAKCNHGEsFQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGR 85
Cdd:PRK13357 4 TLKPNPTSDEK-RAIDWANLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 86 ILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKG-TLYIRPILFGSGPILGSFPIPETTFTAF 164
Cdd:PRK13357 82 IVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVPPYGEGaSLYLRPFMIATEPFLGVKPAEEYIFCVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 165 ACPVGRYHKDN-SGLNLKIEDQFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANVFML 243
Cdd:PRK13357 162 ASPVGAYFKGGvKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNFFFI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 244 KGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDA------DEAFCTGTASIVTSIASVTFKDKKTGF 317
Cdd:PRK13357 242 TKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADaasgefTEAFACGTAAVITPIGGIKYKDKEFVI 321
|
330 340 350
....*....|....*....|....*....|....*..
gi 15230923 318 ---KTGEetLAAKLYETLSDIQTGRVEDTKGWTVEID 351
Cdd:PRK13357 322 gdgEVGP--VTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
14-350 |
7.32e-132 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 381.76 E-value: 7.32e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 14 DEKYANVKWEELAFKFVRTDYMYVAKCNHGESFQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQ 93
Cdd:PLN02883 46 DEEYADVDWDKLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 94 NGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGTLYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHK 173
Cdd:PLN02883 126 NAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 174 D-NSGLNLKIEDQFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANVFMLKGNVVSTPT 252
Cdd:PLN02883 206 EgTAALNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNIIVTPA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 253 IAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASVTFKDKKTGFKTGEETLAAKLYETL 332
Cdd:PLN02883 286 TSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSIL 365
|
330
....*....|....*...
gi 15230923 333 SDIQTGRVEDTKGWTVEI 350
Cdd:PLN02883 366 LGIQTGSIQDTKDWVLQI 383
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
58-338 |
4.33e-105 |
|
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: 309.51 E-value: 4.33e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 58 QLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKWIPPPGKGT 137
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 138 LYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHKD-NSGLNLKIEDqFRRAFPSGTGGVKSITNYCPVWIPLAEAKKQ 216
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGgEKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 217 GFSDILFLDAATGkNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCT 296
Cdd:cd01557 160 GYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15230923 297 GTASIVTSIASVTFKDKKTGFKTGEEtLAAKLYETLSDIQTG 338
Cdd:cd01557 239 GTAAVVTPVGEIDYRGKEPGEGEVGP-VTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
47-350 |
2.14e-103 |
|
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: 306.68 E-value: 2.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 47 QEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALAN 126
Cdd:TIGR01123 2 HNGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 127 KKWIPPPGKG-TLYIRPILFGSGPILGSFPIPETTFTAFACPVGRYHKDNSG-LNLKIEDQFRRAFPSGTGGVKSITNYC 204
Cdd:TIGR01123 82 KDWVPPYGSGaSLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLApVSIFVTTEYDRAAPGGTGAVKVGGNYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 205 PVWIPLAEAKKQGFSDILFLDAATGKNIEELFAANVFML--KGNVVSTPtIAGTILPGVTRNCVMELCRDFGYQVEERTI 282
Cdd:TIGR01123 162 ASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFItgDGELVTPP-LSGSILPGITRDSLLQLAKDLGMEVEERRI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230923 283 pLVDFLDA-----DEAFCTGTASIVTSIASVTFKDKKTGFKTGEE-TLAAKLYETLSDIQTGRVEDTKGWTVEI 350
Cdd:TIGR01123 241 -DIDELKAfveagEIVFACGTAAVITPVGEIQHGGKEVVFASGQPgEVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
46-342 |
4.13e-84 |
|
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: 256.27 E-value: 4.13e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 46 FQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYrteDGRIllFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVAL 124
Cdd:COG0115 4 WLNGELVPEEEATISVLDRGLHYGDGVFEGIRAY---DGRL--FRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 125 ANkkwipppGKGTLYIRPILFGSGPILGSFPI-PETTFTAFACPVGRYHKDN--SGLNLKIEDqFRRAFPSGTGGVKSiT 201
Cdd:COG0115 79 AN-------GLEDGYIRPQVTRGVGGRGVFAEeYEPTVIIIASPLPAYPAEAyeKGVRVITSP-YRRAAPGGLGGIKT-G 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 202 NYCPVWIPLAEAKKQGFSDILFLDAAtgKNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERT 281
Cdd:COG0115 150 NYLNNVLAKQEAKEAGADEALLLDTD--GYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15230923 282 IPLVDFLDADEAFCTGTASIVTSIASV---TFKDKKTGfktgeeTLAAKLYETLSDIQTGRVED 342
Cdd:COG0115 228 ISLEELYTADEVFLTGTAAEVTPVTEIdgrPIGDGKPG------PVTRRLRELYTDIVRGEAED 285
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
65-332 |
4.96e-76 |
|
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: 234.80 E-value: 4.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 65 VLQYGQGLYEGLKAYRtedgrILLFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVALANKKwipppgkGTLYIRPI 143
Cdd:cd00449 3 GLHYGDGVFEGLRAGK-----GRLFRLDEHLDRLNRSAKRLGLPIPyDREELREALKELVAANNG-------ASLYIRPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 144 LFGSGPILGSFP--IPETTFTAFACPVGRYHKD-NSGLNLKIEDQFRRAFPSGTGGVKSiTNYCPVWIPLAEAKKQGFSD 220
Cdd:cd00449 71 LTRGVGGLGVAPppSPEPTFVVFASPVGAYAKGgEKGVRLITSPDRRRAAPGGTGDAKT-GGNLNSVLAKQEAAEAGADE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 221 ILFLDAATgkNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTAS 300
Cdd:cd00449 150 ALLLDDNG--YVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGTAA 227
|
250 260 270
....*....|....*....|....*....|..
gi 15230923 301 IVTSIASVTFKDkKTGFKTGEETlaAKLYETL 332
Cdd:cd00449 228 EVTPVTEIDGRG-IGDGKPGPVT--RKLRELL 256
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
46-346 |
8.19e-42 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 147.99 E-value: 8.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 46 FQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGrillfrpdQNGLRLQAGADRLY---------MPYpSVDQFV 116
Cdd:PRK06606 10 WFNGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTPKG--------PAIFRLREHTKRLFnsakilrmeIPY-SVDELM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 117 SAIKQVALANKkwiPPPGkgtlYIRPILFGSGPILGSFPIP-ETTFTAFACPVGRYHKDNS---GLNLKIEdQFRRAFPS 192
Cdd:PRK06606 81 EAQREVVRKNN---LKSA----YIRPLVFVGDEGLGVRPHGlPTDVAIAAWPWGAYLGEEAlekGIRVKVS-SWTRHAPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 193 GT-GGVKSITNYcpVWIPLA--EAKKQGFSDILFLDAAtGKnIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMEL 269
Cdd:PRK06606 153 SIpTRAKASGNY--LNSILAktEARRNGYDEALLLDVE-GY-VSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 270 CRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASVtfkDkktGFKTGEET---LAAKLYETLSDIQTGRVEDTKGW 346
Cdd:PRK06606 229 AKDLGIEVIERRITRDELYIADEVFFTGTAAEVTPIREV---D---GRQIGNGKrgpITEKLQSAYFDIVRGRTEKYAHW 302
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
71-308 |
3.55e-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: 143.65 E-value: 3.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 71 GLYEGLKAYrteDGRIllFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVALANKKWIPppgkgtlYIRPILF-GSG 148
Cdd:pfam01063 1 GVFETLRVY---NGKI--FFLDEHLARLRRSAKLLGIPLPfDEEDLRKIIEELLKANGLGVG-------RLRLTVSrGPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 149 PILGSFPIPETTFTAFACPVGRYhkdnSGLNLKIEDQFRRAFPSGTGGVKSiTNYCPVWIPLAEAKKQGFSDILFLDAAT 228
Cdd:pfam01063 69 GFGLPTSDPTLAIFVSALPPPPE----SKKKGVISSLVRRNPPSPLPGAKT-LNYLENVLARREAKAQGADDALLLDEDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 229 gkNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASV 308
Cdd:pfam01063 144 --NVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPVSSI 221
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
46-346 |
6.33e-39 |
|
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: 140.19 E-value: 6.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 46 FQEGKILPFADLQLNPCAAVLQYGQGLYEGLKAYRTEDGRILlFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVAL 124
Cdd:TIGR01122 1 WMDGEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDTDKGPAI-FRLKEHIQRLYDSAKIYRMEIPySKEELMEATRETLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 125 ANkkwipppGKGTLYIRPILFGSGPILGSFPIPETTFTAF--ACPVGRYHKDNS---GLNLKIEDQFRRAFPSGTGGVKS 199
Cdd:TIGR01122 80 KN-------NLRSAYIRPLVFRGDGDLGLNPRAGYKPDVIiaAWPWGAYLGEEAlekGIDAKVSSWRRNAPNTIPTAAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 200 ITNYCPVWIPLAEAKKQGFSDILFLDaaTGKNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEE 279
Cdd:TIGR01122 153 GGNYLNSLLAKSEARRHGYDEAILLD--VEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15230923 280 RTIPLVDFLDADEAFCTGTASIVTSIASVtfKDKKTGFKT-GEETlaAKLYETLSDIQTGRVEDTKGW 346
Cdd:TIGR01122 231 QPISREELYTADEAFFTGTAAEITPIREV--DGRKIGNGRrGPVT--KKLQEAFFDLVTGGTEDYWGW 294
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
49-308 |
3.51e-32 |
|
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: 121.55 E-value: 3.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 49 GKILPFADLQLNPCAAVLQYGQGLYEGLKAYrteDGRIllFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVALANK 127
Cdd:cd01558 4 GEYVPREEAKVSVFDRGFLFGDGVYEVIRVY---NGKP--FALDEHLDRLYRSAKELRIDIPyTREELKELIRELVAKNE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 128 KwipppGKGTLYIRpILFGSGPILGSFPIPET-TFTAFACPVGRYHKDN--SGLNLKIEDQFRRAFPSgtggVKSItNYC 204
Cdd:cd01558 79 G-----GEGDVYIQ-VTRGVGPRGHDFPKCVKpTVVIITQPLPLPPAELleKGVRVITVPDIRWLRCD----IKSL-NLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 205 PVWIPLAEAKKQGFSDILFLDAatGKNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPL 284
Cdd:cd01558 148 NNVLAKQEAKEAGADEAILLDA--DGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSL 225
|
250 260
....*....|....*....|....
gi 15230923 285 VDFLDADEAFCTGTASIVTSIASV 308
Cdd:cd01558 226 EELYTADEVFLTSTTAEVMPVVEI 249
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
66-332 |
4.02e-31 |
|
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: 118.18 E-value: 4.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 66 LQYGQGLYEGLKAYrteDGRILLFRPDQNglRLQAGADRLYMPYPSVDQFVSAIKQVALANkkwipPPGKGtlYIRpILF 145
Cdd:cd01559 4 FAYGDGVFETMRAL---DGRLFLLDAHLA--RLERSARRLGIPEPDLPRLRAALESLLAAN-----DIDEG--RIR-LIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 146 GSGPILGSFPIPETTFTAFACPVGRYHK--DNSGLNLKIEDQfRRAFPSGTGGVKSiTNYCPVWIPLAEAKKQGFSDILF 223
Cdd:cd01559 71 SRGPGGRGYAPSVCPGPALYVSVIPLPPawRQDGVRLITCPV-RLGEQPLLAGLKH-LNYLENVLAKREARDRGADEALF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 224 LDAAtGKNIEELfAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVT 303
Cdd:cd01559 149 LDTD-GRVIEGT-ASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNSLLGVA 226
|
250 260
....*....|....*....|....*....
gi 15230923 304 SIASVTFKDKKTGfktgeeTLAAKLYETL 332
Cdd:cd01559 227 PVTAIDDHDGPPG------PLTRALRELL 249
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
133-305 |
1.47e-23 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 98.49 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 133 PGKGTLYIRPILFG-SGPILGSFPIPETTFTA---FACPVGryhkDNSGLNLKIEdQFRRAFPSgtggvKSITN------ 202
Cdd:PRK13356 87 DPDTALYIRPMYWAeDGFASGVAPDPESTRFAlclEEAPMP----EPTGFSLTLS-PFRRPTLE-----MAPTDakagcl 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 203 YCPVWIPLAEAKKQGFSDILFLDAAtgKNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTI 282
Cdd:PRK13356 157 YPNNARALREARSRGFDNALVLDML--GNVAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTVVETTL 234
|
170 180
....*....|....*....|...
gi 15230923 283 PLVDFLDADEAFCTGTASIVTSI 305
Cdd:PRK13356 235 TYEDFLEADEVFSTGNYSKVVPV 257
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
49-311 |
6.18e-22 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 94.27 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 49 GKILPFADLQLNPCAAVLQYGQGLYEGLKAYrteDGRIllFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVALANk 127
Cdd:PRK07544 15 GELVPWRDAKVHVLTHGLHYASSVFEGERAY---GGKI--FKLREHSERLRRSAELLDFEIPySVAEIDAAKKETLAAN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 128 kwipppGKGTLYIRPILFGSGPILGSFPIPETTFTAFAC-PVGRYHKDNS---GLNLKIEdQFRRAFPSgTGGVKSITN- 202
Cdd:PRK07544 89 ------GLTDAYVRPVAWRGSEMMGVSAQQNKIHLAIAAwEWPSYFDPEAkmkGIRLDIA-KWRRPDPE-TAPSAAKAAg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 203 -YCPVWIPLAEAKKQGFSDILFLDAAtgKNIEELFAANVFMLKGNVVSTPTiAGTILPGVTRNCVMELCRDFGYQVEERT 281
Cdd:PRK07544 161 lYMICTISKHAAEAKGYADALMLDYR--GYVAEATGANIFFVKDGVIHTPT-PDCFLDGITRQTVIELAKRRGIEVVERH 237
|
250 260 270
....*....|....*....|....*....|...
gi 15230923 282 IPLVDFLDADEAFCTGTASIVT---SIASVTFK 311
Cdd:PRK07544 238 IMPEELAGFSECFLTGTAAEVTpvsEIGEYRFT 270
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
68-308 |
6.58e-21 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 91.09 E-value: 6.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 68 YGQGLYEGLKAYrteDGRIllFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVALANKkwipppgkgtL---YIRPI 143
Cdd:PRK08320 28 YGDGVFEGIRAY---NGRV--FRLKEHIDRLYDSAKAIMLEIPlSKEEMTEIVLETLRKNN----------LrdaYIRLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 144 LF-GSGPiLGSFP--IPETTFTAFACPVGRYHKD--NSGLNLkIEDQFRRAFPSGTG-GVKSItNYCPVWIPLAEAKKQG 217
Cdd:PRK08320 93 VSrGVGD-LGLDPrkCPKPTVVCIAEPIGLYPGElyEKGLKV-ITVSTRRNRPDALSpQVKSL-NYLNNILAKIEANLAG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 218 FSDILFLDA------ATGKNIeelfaanvFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDAD 291
Cdd:PRK08320 170 VDEAIMLNDegyvaeGTGDNI--------FIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTAD 241
|
250
....*....|....*..
gi 15230923 292 EAFCTGTASIVTSIASV 308
Cdd:PRK08320 242 EVFLTGTAAEVIPVVKV 258
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
66-294 |
7.83e-15 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 73.34 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 66 LQYGQGLYEGLkayRTEDGRILLFrpDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANkkwipppGKGTLYIRpILF 145
Cdd:PRK06092 19 TQYGDGCFTTA---RVRDGQVSLL--SRHLQRLQDACERLAIPLDDWAQLEQEMKQLAAEL-------ENGVLKVI-ISR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 146 GSG-----------P--ILGSFPIP-------ETTFTAFACPV---------GRYHkdnsgLNlKIEDQFRRAfpsgtgg 196
Cdd:PRK06092 86 GSGgrgyspagcaaPtrILSVSPYPahysrwrEQGITLALCPTrlgrnpllaGIKH-----LN-RLEQVLIRA------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 197 vksitnycpvwiplaEAKKQGFSDILFLDAAtGKNIEELfAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQ 276
Cdd:PRK06092 153 ---------------ELEQTEADEALVLDSE-GWVIECC-AANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYP 215
|
250
....*....|....*...
gi 15230923 277 VEERTIPLVDFLDADEAF 294
Cdd:PRK06092 216 VVEVDASLEELLQADEVF 233
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
68-323 |
1.05e-12 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 67.67 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 68 YGQGLYEGLKAYrteDGRIllFRPDQNGLRLQAGADRLYMPYP-SVDQFVSAIKQVALANkkwipppGKGTLYIRPILFG 146
Cdd:PRK12479 29 YGDGVFEGIRSY---GGNV--FCLKEHVKRLYESAKSILLTIPlTVDEMEEAVLQTLQKN-------EYADAYIRLIVSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 147 SGPILGSFP--IPETTFTAFACPVGRYHKD--NSGLNLkIEDQFRRAFPSGTG-GVKSItNYCPVWIPLAEAKKQGFSDI 221
Cdd:PRK12479 97 GKGDLGLDPrsCVKPSVIIIAEQLKLFPQEfyDNGLSV-VSVASRRNTPDALDpRIKSM-NYLNNVLVKIEAAQAGVLEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 222 LFLDAAtgKNIEELFAANVFMLK-GNVVSTPTIAGTiLPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTAS 300
Cdd:PRK12479 175 LMLNQQ--GYVCEGSGDNVFVVKdGKVLTPPSYLGA-LEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLTGTAA 251
|
250 260
....*....|....*....|...
gi 15230923 301 IVTSIASVTFKDKKTGfKTGEET 323
Cdd:PRK12479 252 ELIPVVKVDSREIGDG-KPGSVT 273
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
239-313 |
3.66e-11 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 63.06 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 239 NVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGtaSI-----VTSIASVTFKDK 313
Cdd:PRK07650 182 NLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFVTN--SIqeivpLTRIEERDFPGK 259
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
237-316 |
8.75e-10 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 58.79 E-value: 8.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 237 AANVFMLK--GNVVSTPTIAGtILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFCTGTASIVTSIASV---TFK 311
Cdd:PRK06680 184 SSNAWIVTkdGKLVTRPADNF-ILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAREAFITAASSFVFPVVQIdgkQIG 262
|
....*
gi 15230923 312 DKKTG 316
Cdd:PRK06680 263 NGKPG 267
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
69-309 |
6.28e-09 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 56.51 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 69 GQGLYEGLKAYrteDGRILLFRPDQNglRLQAGADRLYMPYPSVDQFVSAIKQVAlanKKWIPPPGKGTL---YIRPILF 145
Cdd:PRK07849 38 GDGVFETLLVR---DGRPCNLEAHLE--RLARSAALLDLPEPDLDRWRRAVELAI---EEWRAPEDEAALrlvYSRGRES 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 146 GSGP---ILGSfPIPETTFTAFACPV-------GRYHkdnsglnlkieDQFRRAfPSGTGGVKSItNYCPVWIPLAEAKK 215
Cdd:PRK07849 110 GGAPtawVTVS-PVPERVARARREGVsvitldrGYPS-----------DAAERA-PWLLAGAKTL-SYAVNMAALRYAAR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 216 QGFSDILFLDaaTGKNIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEAFC 295
Cdd:PRK07849 176 RGADDVIFTS--TDGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGVWL 253
|
250
....*....|....
gi 15230923 296 TgtaSIVTSIASVT 309
Cdd:PRK07849 254 V---SSVRLAARVH 264
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
66-298 |
2.44e-04 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 42.31 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 66 LQYGQGLYEGLKAYRtedGRILLFRPDQNGLRLQAGADRLYMPYPSVDQFVSAIKQVALANKKwipppGKGTLYI----- 140
Cdd:PRK12400 30 LQFGDGVYEVIRLYK---GNFHLLDPHITRLYRSMEEIELTLPFSKAELITLLYKLIENNNFH-----EDGTIYLqvsrg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 141 ---RPILFgsgpilgSFPIPETTFTafacpvgrYHKDNSGLNLKIEDQFRRAFPSGTG----GVKSItNYCPVWIPLAEA 213
Cdd:PRK12400 102 vqaRTHTF-------SYDVPPTIYA--------YITKKERPALWIEYGVRAISEPDTRwlrcDIKSL-NLLPNILAATKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15230923 214 KKQGFSDILFLDAATgknIEELFAANVFMLKGNVVSTPTIAGTILPGVTRNCVMELCRDFGYQVEERTIPLVDFLDADEA 293
Cdd:PRK12400 166 ERKGCKEALFVRNGT---VTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEELFSVRDVYQADEC 242
|
....*
gi 15230923 294 FCTGT 298
Cdd:PRK12400 243 FFTGT 247
|
|
| |
