|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
1-356 |
0e+00 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 753.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 1 MAPSSSPLrTTSETDEKYANVKWEELGFALTPIDYMYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAY 80
Cdd:PLN03117 1 MAPSSSPL-PTSKADEKYANVKWEELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 81 RTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEY 160
Cdd:PLN03117 80 RTEDGRITLFRPDQNALRMQTGADRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 161 TFLIYASPVGDYHKVSSGLNLKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACN 240
Cdd:PLN03117 160 TFLIYASPVGNYHKASSGLNLKVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 241 IFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRT 320
Cdd:PLN03117 240 IFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRT 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 8569092 321 GEAALSTKLHSMLTNIQMGVVEDKKGWMVDIDPCQG 356
Cdd:PLN03117 320 GEEALSTKLHLILTNIQMGVVEDKKGWMVEIDRCQG 355
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
59-339 |
1.46e-117 |
|
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: 341.48 E-value: 1.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 59 SISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGT 138
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 139 LYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHK-VSSGLNLKVDHkYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSA 217
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKgGEKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 218 GFSDVLFLDAATGrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCT 297
Cdd:cd01557 160 GYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 8569092 298 GTAVVVKAVETVTFHDKKVKY-RTGEaaLSTKLHSMLTNIQMG 339
Cdd:cd01557 239 GTAAVVTPVGEIDYRGKEPGEgEVGP--VTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
49-351 |
7.79e-110 |
|
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: 323.25 E-value: 7.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 49 QGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANK 128
Cdd:TIGR01123 3 NGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKANK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 129 KWVPPPGKG-TLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSG-LNLKVDHKYHRAHSGGTGGVKSCTNYSP 206
Cdd:TIGR01123 83 DWVPPYGSGaSLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLApVSIFVTTEYDRAAPGGTGAVKVGGNYAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 207 VVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIV--KGNIVsTPPTSGTILPGVTRKSISELAHDIGYQVEERDVS 284
Cdd:TIGR01123 163 SLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFItgDGELV-TPPLSGSILPGITRDSLLQLAKDLGMEVEERRID 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8569092 285 VDELLEA----EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAA-LSTKLHSMLTNIQMGVVEDKKGWMVDI 351
Cdd:TIGR01123 242 IDELKAFveagEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGeVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
50-343 |
3.81e-88 |
|
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: 266.67 E-value: 3.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 50 GKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLANk 128
Cdd:COG0115 7 GELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVAAN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 129 kwvpppGKGTLYIRPLLLGSGATLGV-APAPEYTFLIYASPVGDY--HKVSSGLNLKVdHKYHRAHSGGTGGVKSCtNYS 205
Cdd:COG0115 81 ------GLEDGYIRPQVTRGVGGRGVfAEEYEPTVIIIASPLPAYpaEAYEKGVRVIT-SPYRRAAPGGLGGIKTG-NYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 206 PVVKSLLEAKSAGFSDVLFLDAAtgRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSV 285
Cdd:COG0115 153 NNVLAKQEAKEAGADEALLLDTD--GYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 8569092 286 DELLEAEEVFCTGTAVVVKAVETVtfhDKKVKYRTGEAALSTKLHSMLTNIQMGVVED 343
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 ... |
72-306 |
2.28e-42 |
|
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: 146.73 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 72 GLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCM-TPPTLEQFVEAVKQTVLANKKWVPppgkgtlYIRPLLLGSGA 150
Cdd:pfam01063 1 GVFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIpLPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 151 TLGVaPAPEYTFLIYAS----PVGDYHKVSSGLNLKVDHKYHRAhsggtgGVKScTNYSPVVKSLLEAKSAGFSDVLFLD 226
Cdd:pfam01063 69 GFGL-PTSDPTLAIFVSalppPPESKKKGVISSLVRRNPPSPLP------GAKT-LNYLENVLARREAKAQGADDALLLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 227 AAtgRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAV 306
Cdd:pfam01063 141 ED--GNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPV 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
1-356 |
0e+00 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 753.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 1 MAPSSSPLrTTSETDEKYANVKWEELGFALTPIDYMYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAY 80
Cdd:PLN03117 1 MAPSSSPL-PTSKADEKYANVKWEELGFALVPTDYMYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 81 RTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEY 160
Cdd:PLN03117 80 RTEDGRITLFRPDQNALRMQTGADRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 161 TFLIYASPVGDYHKVSSGLNLKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACN 240
Cdd:PLN03117 160 TFLIYASPVGNYHKASSGLNLKVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 241 IFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRT 320
Cdd:PLN03117 240 IFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRT 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 8569092 321 GEAALSTKLHSMLTNIQMGVVEDKKGWMVDIDPCQG 356
Cdd:PLN03117 320 GEEALSTKLHLILTNIQMGVVEDKKGWMVEIDRCQG 355
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
10-351 |
1.01e-175 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 493.98 E-value: 1.01e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 10 TTSETDEkYANVKWEELGFALTPIDYMYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRI 89
Cdd:PLN02782 60 SYTEVTE-LADIDWDNLGFGLVPTDYMYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 90 FRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPV 169
Cdd:PLN02782 139 FRPEENAIRMRNGAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 170 GDYHKVS-SGLNLKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNI 248
Cdd:PLN02782 219 GNYFKEGvAPINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIVKDNV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 249 VSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKY-RTGEAALST 327
Cdd:PLN02782 299 ISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSITYKGKRVSYgEGGFGTVSQ 378
|
330 340
....*....|....*....|....
gi 8569092 328 KLHSMLTNIQMGVVEDKKGWMVDI 351
Cdd:PLN02782 379 QLYTVLTSLQMGLIEDNMNWTVEL 402
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
2-352 |
8.62e-156 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 442.62 E-value: 8.62e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 2 APSSSPLRTTSET------DEKYANVKWEELGFALTPIDYMYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFE 75
Cdd:PLN02259 31 AQAASALREERKKplyqngDDVYADLDWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 76 GLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVA 155
Cdd:PLN02259 111 GTKAYRKENGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 156 PAPEYTFLIYASPVGDYHKVS-SGLNLKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIE 234
Cdd:PLN02259 191 PAPEYTFIVYASPVGNYFKEGmAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 235 ELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDK 314
Cdd:PLN02259 271 EASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEK 350
|
330 340 350
....*....|....*....|....*....|....*...
gi 8569092 315 KVKYRTGEAALSTKLHSMLTNIQMGVVEDKKGWMVDID 352
Cdd:PLN02259 351 RVEYKTGDESVCQKLRSVLVGIQTGLIEDNKGWVTDIN 388
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
15-351 |
3.08e-146 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 418.35 E-value: 3.08e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 15 DEKYANVKWEELGFALTPIDYMYVAK-CRQGeSFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPD 93
Cdd:PLN02883 46 DEEYADVDWDKLGFSLVRTDFMFATKsCRDG-NFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 94 QNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYH 173
Cdd:PLN02883 125 LNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 174 KV-SSGLNLKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTP 252
Cdd:PLN02883 205 KEgTAALNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNIIVTP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 253 PTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAALSTKLHSM 332
Cdd:PLN02883 285 ATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSI 364
|
330
....*....|....*....
gi 8569092 333 LTNIQMGVVEDKKGWMVDI 351
Cdd:PLN02883 365 LLGIQTGSIQDTKDWVLQI 383
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
9-352 |
7.13e-144 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 411.08 E-value: 7.13e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 9 RTTSETDEKYANVKWEELGFALTPIDYMYVAKCRQGEsFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIR 88
Cdd:PRK13357 5 LKPNPTSDEKRAIDWANLGFGYVFTDHMVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 89 IFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKG-TLYIRPLLLGSGATLGVAPAPEYTFLIYAS 167
Cdd:PRK13357 84 LFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVPPYGEGaSLYLRPFMIATEPFLGVKPAEEYIFCVIAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 168 PVGDYHKvsSGLN---LKVDHKYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIV 244
Cdd:PRK13357 164 PVGAYFK--GGVKpvsIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNFFFI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 245 KGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKY 318
Cdd:PRK13357 242 TKDGTVTPPLSGSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADaasgefTEAFACGTAAVITPIGGIKYKDKEFVI 321
|
330 340 350
....*....|....*....|....*....|....*
gi 8569092 319 RTGEA-ALSTKLHSMLTNIQMGVVEDKKGWMVDID 352
Cdd:PRK13357 322 GDGEVgPVTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
59-339 |
1.46e-117 |
|
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: 341.48 E-value: 1.46e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 59 SISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGT 138
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 139 LYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHK-VSSGLNLKVDHkYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSA 217
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKgGEKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 218 GFSDVLFLDAATGrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCT 297
Cdd:cd01557 160 GYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 8569092 298 GTAVVVKAVETVTFHDKKVKY-RTGEaaLSTKLHSMLTNIQMG 339
Cdd:cd01557 239 GTAAVVTPVGEIDYRGKEPGEgEVGP--VTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
49-351 |
7.79e-110 |
|
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: 323.25 E-value: 7.79e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 49 QGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANK 128
Cdd:TIGR01123 3 NGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKANK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 129 KWVPPPGKG-TLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSG-LNLKVDHKYHRAHSGGTGGVKSCTNYSP 206
Cdd:TIGR01123 83 DWVPPYGSGaSLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLApVSIFVTTEYDRAAPGGTGAVKVGGNYAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 207 VVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIV--KGNIVsTPPTSGTILPGVTRKSISELAHDIGYQVEERDVS 284
Cdd:TIGR01123 163 SLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFItgDGELV-TPPLSGSILPGITRDSLLQLAKDLGMEVEERRID 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8569092 285 VDELLEA----EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAA-LSTKLHSMLTNIQMGVVEDKKGWMVDI 351
Cdd:TIGR01123 242 IDELKAFveagEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGeVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
50-343 |
3.81e-88 |
|
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: 266.67 E-value: 3.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 50 GKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLANk 128
Cdd:COG0115 7 GELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVAAN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 129 kwvpppGKGTLYIRPLLLGSGATLGV-APAPEYTFLIYASPVGDY--HKVSSGLNLKVdHKYHRAHSGGTGGVKSCtNYS 205
Cdd:COG0115 81 ------GLEDGYIRPQVTRGVGGRGVfAEEYEPTVIIIASPLPAYpaEAYEKGVRVIT-SPYRRAAPGGLGGIKTG-NYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 206 PVVKSLLEAKSAGFSDVLFLDAAtgRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSV 285
Cdd:COG0115 153 NNVLAKQEAKEAGADEALLLDTD--GYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 8569092 286 DELLEAEEVFCTGTAVVVKAVETVtfhDKKVKYRTGEAALSTKLHSMLTNIQMGVVED 343
Cdd:COG0115 231 EELYTADEVFLTGTAAEVTPVTEI---DGRPIGDGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
64-314 |
3.43e-83 |
|
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: 253.29 E-value: 3.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 64 SPILNYGQGLFEGLKAYRteddrIRIFRPDQNALRMQTGAERLCM-TPPTLEQFVEAVKQTVLANKKwvpppgkGTLYIR 142
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGK-----GRLFRLDEHLDRLNRSAKRLGLpIPYDREELREALKELVAANNG-------ASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 143 PLLLGSGATLGVAPAP--EYTFLIYASPVGDYHKV-SSGLNLKVDHKYHRAHSGGTGGVKsCTNYSPVVKSLLEAKSAGF 219
Cdd:cd00449 69 PLLTRGVGGLGVAPPPspEPTFVVFASPVGAYAKGgEKGVRLITSPDRRRAAPGGTGDAK-TGGNLNSVLAKQEAAEAGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 220 SDVLFLDAATgrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGT 299
Cdd:cd00449 148 DEALLLDDNG--YVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGT 225
|
250
....*....|....*
gi 8569092 300 AVVVKAVETVTFHDK 314
Cdd:cd00449 226 AAEVTPVTEIDGRGI 240
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
49-347 |
8.06e-50 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 168.79 E-value: 8.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 49 QGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIrIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLAN 127
Cdd:PRK06606 12 NGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAKILRMEIPySVDELMEAQREVVRKN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 128 KkwvPPPGkgtlYIRPLL-LGSGAtLGVAPaPEYT--FLIYASPVGDY---HKVSSGLNLKVDhKYHRAHSGGT-GGVKS 200
Cdd:PRK06606 91 N---LKSA----YIRPLVfVGDEG-LGVRP-HGLPtdVAIAAWPWGAYlgeEALEKGIRVKVS-SWTRHAPNSIpTRAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 201 CTNYspvVKSLL---EAKSAGFSDVLFLDAAtGrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQ 277
Cdd:PRK06606 161 SGNY---LNSILaktEARRNGYDEALLLDVE-G-YVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIE 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8569092 278 VEERDVSVDELLEAEEVFCTGTAVVVKAVETVtfhDkkvKYRTGEAA---LSTKLHSMLTNIQMGVVEDKKGW 347
Cdd:PRK06606 236 VIERRITRDELYIADEVFFTGTAAEVTPIREV---D---GRQIGNGKrgpITEKLQSAYFDIVRGRTEKYAHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
50-348 |
6.37e-44 |
|
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: 153.28 E-value: 6.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 50 GKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeDDRIRIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLANk 128
Cdd:TIGR01122 4 GEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEIPySKEELMEATRETLRKN- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 129 kwvpppGKGTLYIRPLLLGSGATLGVAPAPEYT--FLIYASPVGDY---HKVSSGLNLKVDhKYHRAHSGGT-GGVKSCT 202
Cdd:TIGR01122 82 ------NLRSAYIRPLVFRGDGDLGLNPRAGYKpdVIIAAWPWGAYlgeEALEKGIDAKVS-SWRRNAPNTIpTAAKAGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 203 NYspvVKSLL---EAKSAGFSDVLFLDaaTGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVE 279
Cdd:TIGR01122 155 NY---LNSLLaksEARRHGYDEAILLD--VEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 280 ERDVSVDELLEAEEVFCTGTAVVVKAVETVtfhdKKVKYRTGEAALSTK-LHSMLTNIQMGVVEDKKGWM 348
Cdd:TIGR01122 230 EQPISREELYTADEAFFTGTAAEITPIREV----DGRKIGNGRRGPVTKkLQEAFFDLVTGGTEDYWGWL 295
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
72-306 |
2.28e-42 |
|
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: 146.73 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 72 GLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCM-TPPTLEQFVEAVKQTVLANKKWVPppgkgtlYIRPLLLGSGA 150
Cdd:pfam01063 1 GVFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIpLPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 151 TLGVaPAPEYTFLIYAS----PVGDYHKVSSGLNLKVDHKYHRAhsggtgGVKScTNYSPVVKSLLEAKSAGFSDVLFLD 226
Cdd:pfam01063 69 GFGL-PTSDPTLAIFVSalppPPESKKKGVISSLVRRNPPSPLP------GAKT-LNYLENVLARREAKAQGADDALLLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 227 AAtgRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAV 306
Cdd:pfam01063 141 ED--GNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPV 218
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
47-300 |
7.32e-36 |
|
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: 131.18 E-value: 7.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 47 FTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMT-PPTLEQFVEAVKQTVL 125
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNG-----KPFALDEHLDRLYRSAKELRIDiPYTREELKELIRELVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 126 ANKKwvpppGKGTLYIRPlllgsgaTLGVAP---------APEYTFLIYASPVGDYHKVSSGL---------NLKVDhky 187
Cdd:cd01558 76 KNEG-----GEGDVYIQV-------TRGVGPrghdfpkcvKPTVVIITQPLPLPPAELLEKGVrvitvpdirWLRCD--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 188 hrahsggtggVKScTNYSPVVKSLLEAKSAGFSDVLFLDAatGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSI 267
Cdd:cd01558 141 ----------IKS-LNLLNNVLAKQEAKEAGADEAILLDA--DGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATV 207
|
250 260 270
....*....|....*....|....*....|...
gi 8569092 268 SELAHDIGYQVEERDVSVDELLEAEEVFCTGTA 300
Cdd:cd01558 208 IELAKELGIPVEERPFSLEELYTADEVFLTSTT 240
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
50-309 |
1.12e-30 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 118.05 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 50 GKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLANK 128
Cdd:PRK08320 9 GEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNG-----RVFRLKEHIDRLYDSAKAIMLEIPlSKEEMTEIVLETLRKNN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 129 kwvpppgkgtL---YIRPLLLGSGATLGVAP--APEYTFLIYASPVGDYHKvssglnlkvdHKYHRahsgGTGGVKSCTN 203
Cdd:PRK08320 84 ----------LrdaYIRLVVSRGVGDLGLDPrkCPKPTVVCIAEPIGLYPG----------ELYEK----GLKVITVSTR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 204 ------YSPVVKSL---------LEAKSAGFSDVLFLDaATGrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSIS 268
Cdd:PRK08320 140 rnrpdaLSPQVKSLnylnnilakIEANLAGVDEAIMLN-DEG-YVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVI 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 8569092 269 ELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETV 309
Cdd:PRK08320 218 EIAKELGIPVREELFTLHDLYTADEVFLTGTAAEVIPVVKV 258
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
69-299 |
1.02e-27 |
|
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: 108.94 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 69 YGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANkkwvpPPGKGtlYIRpLLL-- 146
Cdd:cd01559 6 YGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAAN-----DIDEG--RIR-LILsr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 147 ---GSGATLGVAPAPeyTFLIYASPVgDYHKVSSGLNLKVDhKYHRAHSGGTGGVKSCtNYSPVVKSLLEAKSAGFSDVL 223
Cdd:cd01559 73 gpgGRGYAPSVCPGP--ALYVSVIPL-PPAWRQDGVRLITC-PVRLGEQPLLAGLKHL-NYLENVLAKREARDRGADEAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8569092 224 FLDAAtGRNIEElTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGT 299
Cdd:cd01559 148 FLDTD-GRVIEG-TASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNS 221
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
42-306 |
1.26e-22 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 96.20 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 42 RQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVK 121
Cdd:PRK07544 7 RDGFIWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGG-----KIFKLREHSERLRRSAELLDFEIPYSVAEIDAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 122 QTVLANKKWVpppgkgTLYIRPLL-LGSgATLGVApAPEYT--FLIYASPVGDYHKVSSGLN-LKVDH-KYHR------- 189
Cdd:PRK07544 82 KETLAANGLT------DAYVRPVAwRGS-EMMGVS-AQQNKihLAIAAWEWPSYFDPEAKMKgIRLDIaKWRRpdpetap 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 190 AHSGGTGGVKSCTnyspvvKSLLEAKSAGFSDVLFLDAATgrNIEELTACNIFIVKGNIVSTpPTSGTILPGVTRKSISE 269
Cdd:PRK07544 154 SAAKAAGLYMICT------ISKHAAEAKGYADALMLDYRG--YVAEATGANIFFVKDGVIHT-PTPDCFLDGITRQTVIE 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 8569092 270 LAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAV 306
Cdd:PRK07544 225 LAKRRGIEVVERHIMPEELAGFSECFLTGTAAEVTPV 261
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
103-298 |
6.02e-22 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 93.87 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 103 AERLCMTPP-TLEQFVEAVKQTVlanKKWvppPGKGTLYIRPLLLG-SGATLGVAPAPEYT---FLIYASPVGdyhkVSS 177
Cdd:PRK13356 61 AEALGLKPTvSAEEIEALAREGL---KRF---DPDTALYIRPMYWAeDGFASGVAPDPESTrfaLCLEEAPMP----EPT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 178 GLNLKVDhKYHR--AHSGGTGGVKSCTnYSPVVKSLLEAKSAGFSDVLFLDAATgrNIEELTACNIFIVKGNIVSTPPTS 255
Cdd:PRK13356 131 GFSLTLS-PFRRptLEMAPTDAKAGCL-YPNNARALREARSRGFDNALVLDMLG--NVAETATSNVFMVKDGVVFTPVPN 206
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 8569092 256 GTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTG 298
Cdd:PRK13356 207 GTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTG 249
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
69-300 |
1.20e-17 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 82.31 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 69 YGQGLFEGLKAYRTEddrirIFRPDQNALRMQTGAERLCMT-PPTLEQFVEAVKQTVLANkkwvpppGKGTLYIRPLLLG 147
Cdd:PRK12479 29 YGDGVFEGIRSYGGN-----VFCLKEHVKRLYESAKSILLTiPLTVDEMEEAVLQTLQKN-------EYADAYIRLIVSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 148 SGATLGVAP--APEYTFLIYASPVGDYHK--VSSGLNLKVDHKYHRAHSGGTGGVKScTNYSPVVKSLLEAKSAGFSDVL 223
Cdd:PRK12479 97 GKGDLGLDPrsCVKPSVIIIAEQLKLFPQefYDNGLSVVSVASRRNTPDALDPRIKS-MNYLNNVLVKIEAAQAGVLEAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8569092 224 FLDAATgrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTA 300
Cdd:PRK12479 176 MLNQQG--YVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLTGTA 250
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
61-294 |
8.69e-13 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 68.06 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 61 SPCSPILNY-------GQGLFEGLKAYrteDDRIRIFRPdqNALRMQTGAERLCMTPPTLEQFVEAVKqtvLANKKWVPP 133
Cdd:PRK07849 22 DPSAPLLHAddlaavrGDGVFETLLVR---DGRPCNLEA--HLERLARSAALLDLPEPDLDRWRRAVE---LAIEEWRAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 134 PGKGTL---YIRplllgsgatlGVAPAPEYTFLIYASPVGDYHKVSSGLNLKV---DHKYHraHSGGT------GGVKSc 201
Cdd:PRK07849 94 EDEAALrlvYSR----------GRESGGAPTAWVTVSPVPERVARARREGVSVitlDRGYP--SDAAErapwllAGAKT- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 202 TNYSPVVKSLLEAKSAGFSDVLFLDAaTGRNIEELTAcNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEER 281
Cdd:PRK07849 161 LSYAVNMAALRYAARRGADDVIFTST-DGYVLEGPTS-TVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYR 238
|
250
....*....|...
gi 8569092 282 DVSVDELLEAEEV 294
Cdd:PRK07849 239 ALRPADLFAADGV 251
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
217-295 |
2.12e-12 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 66.40 E-value: 2.12e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8569092 217 AGFSDVLFLDAAtGRNIEeLTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVF 295
Cdd:PRK06092 157 TEADEALVLDSE-GWVIE-CCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVF 233
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
214-316 |
1.07e-11 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 64.57 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 214 AKSAGFSDVLFLDAAtgrNIEELTACNIFIV-KGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAE 292
Cdd:PRK06680 163 AKEAGAQEAWMVDDG---FVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAR 239
|
90 100
....*....|....*....|....
gi 8569092 293 EVFCTGTAVVVKAVetVTFHDKKV 316
Cdd:PRK06680 240 EAFITAASSFVFPV--VQIDGKQI 261
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
240-297 |
6.48e-11 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 62.29 E-value: 6.48e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 8569092 240 NIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCT 297
Cdd:PRK07650 182 NLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFVT 239
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
198-335 |
2.23e-08 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 55.02 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 198 VKScTNYSPVVKSLLEAKSAGFSDVLFLDA----ATGRNieeLTACniFIVKGNIVSTPPTSgTILPGVTRKSISELA-- 271
Cdd:PLN02845 184 VKS-VNYLPNALSQMEAEERGAFAGIWLDEegfvAEGPN---MNVA--FLTNDGELVLPPFD-KILSGCTARRVLELApr 256
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8569092 272 ---HDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVetVTFHDKKV-KYRTGEAALStkLHSMLTN 335
Cdd:PLN02845 257 lvsPGDLRGVKQRKISVEEAKAADEMMLIGSGVPVLPI--VSWDGQPIgDGKVGPITLA--LHDLLLD 320
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
203-301 |
3.39e-06 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 48.09 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 203 NYSPVVKSLLEAKSAGFSDVLFLdaatgRN--IEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEE 280
Cdd:PRK12400 154 NLLPNILAATKAERKGCKEALFV-----RNgtVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQE 228
|
90 100
....*....|....*....|.
gi 8569092 281 RDVSVDELLEAEEVFCTGTAV 301
Cdd:PRK12400 229 ELFSVRDVYQADECFFTGTTI 249
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
214-333 |
2.83e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 38.81 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8569092 214 AKSAGFSDVLFLDaATGRnIEELTACNIFIVKGNIVSTPptSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEE 293
Cdd:PRK09266 148 AQRAGFDDALFVD-PDGR-VSEGATWNLGFWDGGAVVWP--QAPALPGVTMALLQRGLERLGIPQRTRPVTLADLGRFAG 223
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 8569092 294 VFCTGTAVVVKAVETVTFHDkkvkyRTGEAALSTKLHSML 333
Cdd:PRK09266 224 AFACNAWRGQRAVSAIDDVA-----LPDSHALLELLRRAY 258
|
|
| |
