|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
1-321 |
0e+00 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 688.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 1 MYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQ 80
Cdd:PLN03117 35 MYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGADRLCMTPPSLEQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 81 FVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSGLNLKVDHKYHRAHSGGT 160
Cdd:PLN03117 115 FVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASSGLNLKVDHKHRRAHSGGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 161 GGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIG 240
Cdd:PLN03117 195 GGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 241 YQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAALSTKLHSMLTNIQMGVVEDKKGWMVDIDPCQ 320
Cdd:PLN03117 275 YQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEALSTKLHLILTNIQMGVVEDKKGWMVEIDRCQ 354
|
.
gi 1063694220 321 G 321
Cdd:PLN03117 355 G 355
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
24-304 |
5.18e-118 |
|
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: 341.10 E-value: 5.18e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 24 SISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGT 103
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 104 LYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHK-VSSGLNLKVDHkYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSA 182
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKgGEKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 183 GFSDVLFLDAATGrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCT 262
Cdd:cd01557 160 GYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063694220 263 GTAVVVKAVETVTFHDKKVKY-RTGEaaLSTKLHSMLTNIQMG 304
Cdd:cd01557 239 GTAAVVTPVGEIDYRGKEPGEgEVGP--VTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
14-316 |
1.84e-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: 1.84e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 14 QGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANK 93
Cdd:TIGR01123 3 NGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKANK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 94 KWVPPPGKG-TLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSG-LNLKVDHKYHRAHSGGTGGVKSCTNYSP 171
Cdd:TIGR01123 83 DWVPPYGSGaSLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLApVSIFVTTEYDRAAPGGTGAVKVGGNYAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 172 VVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIV--KGNIVsTPPTSGTILPGVTRKSISELAHDIGYQVEERDVS 249
Cdd:TIGR01123 163 SLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFItgDGELV-TPPLSGSILPGITRDSLLQLAKDLGMEVEERRID 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063694220 250 VDELLEA----EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAA-LSTKLHSMLTNIQMGVVEDKKGWMVDI 316
Cdd:TIGR01123 242 IDELKAFveagEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGeVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
15-308 |
1.15e-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: 1.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 15 GKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLANk 93
Cdd:COG0115 7 GELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVAAN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 94 kwvpppGKGTLYIRPLLLGSGATLGV-APAPEYTFLIYASPVGDY--HKVSSGLNLKVdHKYHRAHSGGTGGVKSCtNYS 170
Cdd:COG0115 81 ------GLEDGYIRPQVTRGVGGRGVfAEEYEPTVIIIASPLPAYpaEAYEKGVRVIT-SPYRRAAPGGLGGIKTG-NYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 171 PVVKSLLEAKSAGFSDVLFLDAAtgRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSV 250
Cdd:COG0115 153 NNVLAKQEAKEAGADEALLLDTD--GYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694220 251 DELLEAEEVFCTGTAVVVKAVETVtfhDKKVKYRTGEAALSTKLHSMLTNIQMGVVED 308
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 ... |
37-271 |
9.37e-43 |
|
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: 9.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 37 GLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCM-TPPTLEQFVEAVKQTVLANKKWVPppgkgtlYIRPLLLGSGA 115
Cdd:pfam01063 1 GVFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIpLPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 116 TLGVaPAPEYTFLIYAS----PVGDYHKVSSGLNLKVDHKYHRAhsggtgGVKScTNYSPVVKSLLEAKSAGFSDVLFLD 191
Cdd:pfam01063 69 GFGL-PTSDPTLAIFVSalppPPESKKKGVISSLVRRNPPSPLP------GAKT-LNYLENVLARREAKAQGADDALLLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 192 AAtgRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAV 271
Cdd:pfam01063 141 ED--GNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPV 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
1-321 |
0e+00 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 688.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 1 MYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQ 80
Cdd:PLN03117 35 MYVAKCKQGESFSEGKIVPYGDISISPCAGILNYGQGLFEGLKAYRTEDGRITLFRPDQNALRMQTGADRLCMTPPSLEQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 81 FVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSGLNLKVDHKYHRAHSGGT 160
Cdd:PLN03117 115 FVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAPEYTFLIYASPVGNYHKASSGLNLKVDHKHRRAHSGGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 161 GGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIG 240
Cdd:PLN03117 195 GGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELSACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 241 YQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAALSTKLHSMLTNIQMGVVEDKKGWMVDIDPCQ 320
Cdd:PLN03117 275 YQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEEALSTKLHLILTNIQMGVVEDKKGWMVEIDRCQ 354
|
.
gi 1063694220 321 G 321
Cdd:PLN03117 355 G 355
|
|
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
1-316 |
1.95e-166 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 468.94 E-value: 1.95e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 1 MYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQ 80
Cdd:PLN02782 85 MYIMKCNRDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYRKEDGNILLFRPEENAIRMRNGAERMCMPAPTVEQ 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 81 FVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVS-SGLNLKVDHKYHRAHSGG 159
Cdd:PLN02782 165 FVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIYVSPVGNYFKEGvAPINLIVENEFHRATPGG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 160 TGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDI 239
Cdd:PLN02782 245 TGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIVKDNVISTPAIKGTILPGITRKSIIDVARSQ 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694220 240 GYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKY-RTGEAALSTKLHSMLTNIQMGVVEDKKGWMVDI 316
Cdd:PLN02782 325 GFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSITYKGKRVSYgEGGFGTVSQQLYTVLTSLQMGLIEDNMNWTVEL 402
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
1-317 |
1.42e-144 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 412.96 E-value: 1.42e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 1 MYVAKCRQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQ 80
Cdd:PLN02259 71 MYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 81 FVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVS-SGLNLKVDHKYHRAHSGG 159
Cdd:PLN02259 151 FVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEGmAALNLYVEEEYVRAAPGG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 160 TGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDI 239
Cdd:PLN02259 231 AGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQ 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694220 240 GYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAALSTKLHSMLTNIQMGVVEDKKGWMVDID 317
Cdd:PLN02259 311 GYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEKRVEYKTGDESVCQKLRSVLVGIQTGLIEDNKGWVTDIN 388
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
1-317 |
6.55e-139 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 397.21 E-value: 6.55e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 1 MYVAKCRQGEsFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQ 80
Cdd:PRK13357 32 MVVIDYKDGK-WHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKDGSIVLFRPDANAKRLQRSADRLLMPELPEEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 81 FVEAVKQTVLANKKWVPPPGKG-TLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKvsSGLN---LKVDHKYHRAH 156
Cdd:PRK13357 111 FLEAVKQLVKADRDWVPPYGEGaSLYLRPFMIATEPFLGVKPAEEYIFCVIASPVGAYFK--GGVKpvsIWVSDEYDRAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 157 SGGTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELA 236
Cdd:PRK13357 189 PGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMNFFFITKDGTVTPPLSGSILPGITRDSLLQLA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 237 HDIGYQVEERDVSVDELLEA------EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEA-ALSTKLHSMLTNIQMGVVEDK 309
Cdd:PRK13357 269 EDLGLTVEERPVSIDEWQADaasgefTEAFACGTAAVITPIGGIKYKDKEFVIGDGEVgPVTQKLYDELTGIQFGDVEDP 348
|
....*...
gi 1063694220 310 KGWMVDID 317
Cdd:PRK13357 349 HGWIVKVD 356
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
1-316 |
2.32e-136 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 391.77 E-value: 2.32e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 1 MYVAK-CRQGeSFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLE 79
Cdd:PLN02883 67 MFATKsCRDG-NFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRILLFRPELNAMRMKIGAERMCMHSPSVH 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 80 QFVEAVKQTVLANKKWVPPPGKGTLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKV-SSGLNLKVDHKYHRAHSG 158
Cdd:PLN02883 146 QFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTFLVFGSPVQNYFKEgTAALNLYVEEVIPRAYLG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 159 GTGGVKSCTNYSPVVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHD 238
Cdd:PLN02883 226 GTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNIIVTPATSGTILGGITRKSIIEIALD 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694220 239 IGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAALSTKLHSMLTNIQMGVVEDKKGWMVDI 316
Cdd:PLN02883 306 LGYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILLGIQTGSIQDTKDWVLQI 383
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
24-304 |
5.18e-118 |
|
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: 341.10 E-value: 5.18e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 24 SISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANKKWVPPPGKGT 103
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIVLFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 104 LYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHK-VSSGLNLKVDHkYHRAHSGGTGGVKSCTNYSPVVKSLLEAKSA 182
Cdd:cd01557 81 LYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKgGEKGVSALVSS-FRRAAPGGPGAAKAGGNYAASLLAQKEAAEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 183 GFSDVLFLDAATGrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCT 262
Cdd:cd01557 160 GYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVFAT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063694220 263 GTAVVVKAVETVTFHDKKVKY-RTGEaaLSTKLHSMLTNIQMG 304
Cdd:cd01557 239 GTAAVVTPVGEIDYRGKEPGEgEVGP--VTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
14-316 |
1.84e-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: 1.84e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 14 QGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANK 93
Cdd:TIGR01123 3 NGRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCADGSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKANK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 94 KWVPPPGKG-TLYIRPLLLGSGATLGVAPAPEYTFLIYASPVGDYHKVSSG-LNLKVDHKYHRAHSGGTGGVKSCTNYSP 171
Cdd:TIGR01123 83 DWVPPYGSGaSLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLApVSIFVTTEYDRAAPGGTGAVKVGGNYAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 172 VVKSLLEAKSAGFSDVLFLDAATGRNIEELTACNIFIV--KGNIVsTPPTSGTILPGVTRKSISELAHDIGYQVEERDVS 249
Cdd:TIGR01123 163 SLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFFItgDGELV-TPPLSGSILPGITRDSLLQLAKDLGMEVEERRID 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063694220 250 VDELLEA----EEVFCTGTAVVVKAVETVTFHDKKVKYRTGEAA-LSTKLHSMLTNIQMGVVEDKKGWMVDI 316
Cdd:TIGR01123 242 IDELKAFveagEIVFACGTAAVITPVGEIQHGGKEVVFASGQPGeVTKALYDELTDIQYGDFEDPYGWIVEV 313
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
15-308 |
1.15e-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: 1.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 15 GKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLANk 93
Cdd:COG0115 7 GELVPEEEATISVLDRGLHYGDGVFEGIRAYDG-----RLFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVAAN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 94 kwvpppGKGTLYIRPLLLGSGATLGV-APAPEYTFLIYASPVGDY--HKVSSGLNLKVdHKYHRAHSGGTGGVKSCtNYS 170
Cdd:COG0115 81 ------GLEDGYIRPQVTRGVGGRGVfAEEYEPTVIIIASPLPAYpaEAYEKGVRVIT-SPYRRAAPGGLGGIKTG-NYL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 171 PVVKSLLEAKSAGFSDVLFLDAAtgRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSV 250
Cdd:COG0115 153 NNVLAKQEAKEAGADEALLLDTD--GYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPISL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694220 251 DELLEAEEVFCTGTAVVVKAVETVtfhDKKVKYRTGEAALSTKLHSMLTNIQMGVVED 308
Cdd:COG0115 231 EELYTADEVFLTGTAAEVTPVTEI---DGRPIGDGKPGPVTRRLRELYTDIVRGEAED 285
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
29-279 |
1.99e-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: 252.52 E-value: 1.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 29 SPILNYGQGLFEGLKAYRteddrIRIFRPDQNALRMQTGAERLCM-TPPTLEQFVEAVKQTVLANKKwvpppgkGTLYIR 107
Cdd:cd00449 1 DRGLHYGDGVFEGLRAGK-----GRLFRLDEHLDRLNRSAKRLGLpIPYDREELREALKELVAANNG-------ASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 108 PLLLGSGATLGVAPAP--EYTFLIYASPVGDYHKV-SSGLNLKVDHKYHRAHSGGTGGVKsCTNYSPVVKSLLEAKSAGF 184
Cdd:cd00449 69 PLLTRGVGGLGVAPPPspEPTFVVFASPVGAYAKGgEKGVRLITSPDRRRAAPGGTGDAK-TGGNLNSVLAKQEAAEAGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 185 SDVLFLDAATgrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGT 264
Cdd:cd00449 148 DEALLLDDNG--YVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGT 225
|
250
....*....|....*
gi 1063694220 265 AVVVKAVETVTFHDK 279
Cdd:cd00449 226 AAEVTPVTEIDGRGI 240
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
14-312 |
2.39e-50 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 169.17 E-value: 2.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 14 QGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTEDDRIrIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLAN 92
Cdd:PRK06606 12 NGELVPWEDAKVHVLTHALHYGTGVFEGIRAYDTPKGPA-IFRLREHTKRLFNSAKILRMEIPySVDELMEAQREVVRKN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 93 KkwvPPPGkgtlYIRPLL-LGSGAtLGVAPaPEYT--FLIYASPVGDY---HKVSSGLNLKVDhKYHRAHSGGT-GGVKS 165
Cdd:PRK06606 91 N---LKSA----YIRPLVfVGDEG-LGVRP-HGLPtdVAIAAWPWGAYlgeEALEKGIRVKVS-SWTRHAPNSIpTRAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 166 CTNYspvVKSLL---EAKSAGFSDVLFLDAAtGrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQ 242
Cdd:PRK06606 161 SGNY---LNSILaktEARRNGYDEALLLDVE-G-YVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIE 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063694220 243 VEERDVSVDELLEAEEVFCTGTAVVVKAVETVtfhDkkvKYRTGEAA---LSTKLHSMLTNIQMGVVEDKKGW 312
Cdd:PRK06606 236 VIERRITRDELYIADEVFFTGTAAEVTPIREV---D---GRQIGNGKrgpITEKLQSAYFDIVRGRTEKYAHW 302
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
15-313 |
2.02e-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: 153.67 E-value: 2.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 15 GKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeDDRIRIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLANk 93
Cdd:TIGR01122 4 GEFVDWEDAKVHVLTHALHYGTGVFEGIRAYDT-DKGPAIFRLKEHIQRLYDSAKIYRMEIPySKEELMEATRETLRKN- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 94 kwvpppGKGTLYIRPLLLGSGATLGVAPAPEYT--FLIYASPVGDY---HKVSSGLNLKVDhKYHRAHSGGT-GGVKSCT 167
Cdd:TIGR01122 82 ------NLRSAYIRPLVFRGDGDLGLNPRAGYKpdVIIAAWPWGAYlgeEALEKGIDAKVS-SWRRNAPNTIpTAAKAGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 168 NYspvVKSLL---EAKSAGFSDVLFLDaaTGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVE 244
Cdd:TIGR01122 155 NY---LNSLLaksEARRHGYDEAILLD--VEGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 245 ERDVSVDELLEAEEVFCTGTAVVVKAVETVtfhdKKVKYRTGEAALSTK-LHSMLTNIQMGVVEDKKGWM 313
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 ... |
37-271 |
9.37e-43 |
|
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: 9.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 37 GLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCM-TPPTLEQFVEAVKQTVLANKKWVPppgkgtlYIRPLLLGSGA 115
Cdd:pfam01063 1 GVFETLRVYNG-----KIFFLDEHLARLRRSAKLLGIpLPFDEEDLRKIIEELLKANGLGVG-------RLRLTVSRGPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 116 TLGVaPAPEYTFLIYAS----PVGDYHKVSSGLNLKVDHKYHRAhsggtgGVKScTNYSPVVKSLLEAKSAGFSDVLFLD 191
Cdd:pfam01063 69 GFGL-PTSDPTLAIFVSalppPPESKKKGVISSLVRRNPPSPLP------GAKT-LNYLENVLARREAKAQGADDALLLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 192 AAtgRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAV 271
Cdd:pfam01063 141 ED--GNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNSLRGVTPV 218
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
12-265 |
4.65e-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: 130.80 E-value: 4.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 12 FTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMT-PPTLEQFVEAVKQTVL 90
Cdd:cd01558 1 YLNGEYVPREEAKVSVFDRGFLFGDGVYEVIRVYNG-----KPFALDEHLDRLYRSAKELRIDiPYTREELKELIRELVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 91 ANKKwvpppGKGTLYIRPlllgsgaTLGVAP---------APEYTFLIYASPVGDYHKVSSGL---------NLKVDhky 152
Cdd:cd01558 76 KNEG-----GEGDVYIQV-------TRGVGPrghdfpkcvKPTVVIITQPLPLPPAELLEKGVrvitvpdirWLRCD--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 153 hrahsggtggVKScTNYSPVVKSLLEAKSAGFSDVLFLDAatGRNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSI 232
Cdd:cd01558 141 ----------IKS-LNLLNNVLAKQEAKEAGADEAILLDA--DGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATV 207
|
250 260 270
....*....|....*....|....*....|...
gi 1063694220 233 SELAHDIGYQVEERDVSVDELLEAEEVFCTGTA 265
Cdd:cd01558 208 IELAKELGIPVEERPFSLEELYTADEVFLTSTT 240
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
15-274 |
7.37e-31 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 117.66 E-value: 7.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 15 GKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPP-TLEQFVEAVKQTVLANK 93
Cdd:PRK08320 9 GEFVPKEEAKVSVFDHGFLYGDGVFEGIRAYNG-----RVFRLKEHIDRLYDSAKAIMLEIPlSKEEMTEIVLETLRKNN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 94 kwvpppgkgtL---YIRPLLLGSGATLGVAP--APEYTFLIYASPVGDYHKvssglnlkvdHKYHRahsgGTGGVKSCTN 168
Cdd:PRK08320 84 ----------LrdaYIRLVVSRGVGDLGLDPrkCPKPTVVCIAEPIGLYPG----------ELYEK----GLKVITVSTR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 169 ------YSPVVKSL---------LEAKSAGFSDVLFLDaATGrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSIS 233
Cdd:PRK08320 140 rnrpdaLSPQVKSLnylnnilakIEANLAGVDEAIMLN-DEG-YVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVI 217
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1063694220 234 ELAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETV 274
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 ... |
34-264 |
5.26e-28 |
|
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: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 34 YGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVKQTVLANkkwvpPPGKGtlYIRpLLL-- 111
Cdd:cd01559 6 YGDGVFETMRALDG-----RLFLLDAHLARLERSARRLGIPEPDLPRLRAALESLLAAN-----DIDEG--RIR-LILsr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 112 ---GSGATLGVAPAPeyTFLIYASPVgDYHKVSSGLNLKVDhKYHRAHSGGTGGVKSCtNYSPVVKSLLEAKSAGFSDVL 188
Cdd:cd01559 73 gpgGRGYAPSVCPGP--ALYVSVIPL-PPAWRQDGVRLITC-PVRLGEQPLLAGLKHL-NYLENVLAKREARDRGADEAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063694220 189 FLDAAtGRNIEElTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGT 264
Cdd:cd01559 148 FLDTD-GRVIEG-TASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNS 221
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
7-271 |
7.21e-23 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 96.20 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 7 RQGESFTQGKIVPYGDISISPCSPILNYGQGLFEGLKAYRTeddriRIFRPDQNALRMQTGAERLCMTPPTLEQFVEAVK 86
Cdd:PRK07544 7 RDGFIWMDGELVPWRDAKVHVLTHGLHYASSVFEGERAYGG-----KIFKLREHSERLRRSAELLDFEIPYSVAEIDAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 87 QTVLANKKWVpppgkgTLYIRPLL-LGSgATLGVApAPEYT--FLIYASPVGDYHKVSSGLN-LKVDH-KYHR------- 154
Cdd:PRK07544 82 KETLAANGLT------DAYVRPVAwRGS-EMMGVS-AQQNKihLAIAAWEWPSYFDPEAKMKgIRLDIaKWRRpdpetap 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 155 AHSGGTGGVKSCTnyspvvKSLLEAKSAGFSDVLFLDAATgrNIEELTACNIFIVKGNIVSTpPTSGTILPGVTRKSISE 234
Cdd:PRK07544 154 SAAKAAGLYMICT------ISKHAAEAKGYADALMLDYRG--YVAEATGANIFFVKDGVIHT-PTPDCFLDGITRQTVIE 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063694220 235 LAHDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAV 271
Cdd:PRK07544 225 LAKRRGIEVVERHIMPEELAGFSECFLTGTAAEVTPV 261
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
68-263 |
3.50e-22 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 93.87 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 68 AERLCMTPP-TLEQFVEAVKQTVlanKKWvppPGKGTLYIRPLLLG-SGATLGVAPAPEYT---FLIYASPVGdyhkVSS 142
Cdd:PRK13356 61 AEALGLKPTvSAEEIEALAREGL---KRF---DPDTALYIRPMYWAeDGFASGVAPDPESTrfaLCLEEAPMP----EPT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 143 GLNLKVDhKYHR--AHSGGTGGVKSCTnYSPVVKSLLEAKSAGFSDVLFLDAATgrNIEELTACNIFIVKGNIVSTPPTS 220
Cdd:PRK13356 131 GFSLTLS-PFRRptLEMAPTDAKAGCL-YPNNARALREARSRGFDNALVLDMLG--NVAETATSNVFMVKDGVVFTPVPN 206
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063694220 221 GTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTG 263
Cdd:PRK13356 207 GTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTG 249
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
34-265 |
7.83e-18 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 82.31 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 34 YGQGLFEGLKAYRTEddrirIFRPDQNALRMQTGAERLCMT-PPTLEQFVEAVKQTVLANkkwvpppGKGTLYIRPLLLG 112
Cdd:PRK12479 29 YGDGVFEGIRSYGGN-----VFCLKEHVKRLYESAKSILLTiPLTVDEMEEAVLQTLQKN-------EYADAYIRLIVSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 113 SGATLGVAP--APEYTFLIYASPVGDYHK--VSSGLNLKVDHKYHRAHSGGTGGVKScTNYSPVVKSLLEAKSAGFSDVL 188
Cdd:PRK12479 97 GKGDLGLDPrsCVKPSVIIIAEQLKLFPQefYDNGLSVVSVASRRNTPDALDPRIKS-MNYLNNVLVKIEAAQAGVLEAL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063694220 189 FLDAATgrNIEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCTGTA 265
Cdd:PRK12479 176 MLNQQG--YVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLTGTA 250
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
26-259 |
6.43e-13 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 68.06 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 26 SPCSPILNY-------GQGLFEGLKAYrteDDRIRIFRPdqNALRMQTGAERLCMTPPTLEQFVEAVKqtvLANKKWVPP 98
Cdd:PRK07849 22 DPSAPLLHAddlaavrGDGVFETLLVR---DGRPCNLEA--HLERLARSAALLDLPEPDLDRWRRAVE---LAIEEWRAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 99 PGKGTL---YIRplllgsgatlGVAPAPEYTFLIYASPVGDYHKVSSGLNLKV---DHKYHraHSGGT------GGVKSc 166
Cdd:PRK07849 94 EDEAALrlvYSR----------GRESGGAPTAWVTVSPVPERVARARREGVSVitlDRGYP--SDAAErapwllAGAKT- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 167 TNYSPVVKSLLEAKSAGFSDVLFLDAaTGRNIEELTAcNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEER 246
Cdd:PRK07849 161 LSYAVNMAALRYAARRGADDVIFTST-DGYVLEGPTS-TVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYR 238
|
250
....*....|...
gi 1063694220 247 DVSVDELLEAEEV 259
Cdd:PRK07849 239 ALRPADLFAADGV 251
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
182-260 |
1.60e-12 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 66.40 E-value: 1.60e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063694220 182 AGFSDVLFLDAAtGRNIEeLTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVF 260
Cdd:PRK06092 157 TEADEALVLDSE-GWVIE-CCAANLFWRKGGVVYTPDLDQCGVAGVMRQFILELLAQSGYPVVEVDASLEELLQADEVF 233
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
179-281 |
8.54e-12 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 64.57 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 179 AKSAGFSDVLFLDAAtgrNIEELTACNIFIV-KGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAE 257
Cdd:PRK06680 163 AKEAGAQEAWMVDDG---FVTEGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAR 239
|
90 100
....*....|....*....|....
gi 1063694220 258 EVFCTGTAVVVKAVetVTFHDKKV 281
Cdd:PRK06680 240 EAFITAASSFVFPV--VQIDGKQI 261
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
205-262 |
5.03e-11 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 62.29 E-value: 5.03e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694220 205 NIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEEVFCT 262
Cdd:PRK07650 182 NLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFVT 239
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
163-300 |
1.81e-08 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 55.02 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 163 VKScTNYSPVVKSLLEAKSAGFSDVLFLDA----ATGRNieeLTACniFIVKGNIVSTPPTSgTILPGVTRKSISELA-- 236
Cdd:PLN02845 184 VKS-VNYLPNALSQMEAEERGAFAGIWLDEegfvAEGPN---MNVA--FLTNDGELVLPPFD-KILSGCTARRVLELApr 256
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063694220 237 ---HDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVetVTFHDKKV-KYRTGEAALStkLHSMLTN 300
Cdd:PLN02845 257 lvsPGDLRGVKQRKISVEEAKAADEMMLIGSGVPVLPI--VSWDGQPIgDGKVGPITLA--LHDLLLD 320
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
168-266 |
2.80e-06 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 48.09 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 168 NYSPVVKSLLEAKSAGFSDVLFLdaatgRN--IEELTACNIFIVKGNIVSTPPTSGTILPGVTRKSISELAHDIGYQVEE 245
Cdd:PRK12400 154 NLLPNILAATKAERKGCKEALFV-----RNgtVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQE 228
|
90 100
....*....|....*....|.
gi 1063694220 246 RDVSVDELLEAEEVFCTGTAV 266
Cdd:PRK12400 229 ELFSVRDVYQADECFFTGTTI 249
|
|
| PRK09266 |
PRK09266 |
hypothetical protein; Provisional |
179-298 |
2.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236438 Cd Length: 266 Bit Score: 38.81 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063694220 179 AKSAGFSDVLFLDaATGRnIEELTACNIFIVKGNIVSTPptSGTILPGVTRKSISELAHDIGYQVEERDVSVDELLEAEE 258
Cdd:PRK09266 148 AQRAGFDDALFVD-PDGR-VSEGATWNLGFWDGGAVVWP--QAPALPGVTMALLQRGLERLGIPQRTRPVTLADLGRFAG 223
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1063694220 259 VFCTGTAVVVKAVETVTFHDkkvkyRTGEAALSTKLHSML 298
Cdd:PRK09266 224 AFACNAWRGQRAVSAIDDVA-----LPDSHALLELLRRAY 258
|
|
| |
