|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
68-412 |
0e+00 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 579.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 68 SADRSDEESGGEIDWDNLGFGLTPTDYMYVMRCSlEDGVFSRGELSRYGNIELSPSSGVINYGQGLFEGLKAYRaaNQQG 147
Cdd:PLN02782 58 SSSYTEVTELADIDWDNLGFGLVPTDYMYIMKCN-RDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYR--KEDG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 148 SYMLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLANRRWVPPQGKGALYIRPLLIGSGPILGLAPAPEYTFLIY 227
Cdd:PLN02782 135 NILLFRPEENAIRMRNGAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIY 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 228 AAPVGTYFKEGLAPINLVVEDSIHRAMPGGTGGVKTITNYAPVLKAQMDAKSRGFTDVLYLDAVHKTYLEEASSCNLFIV 307
Cdd:PLN02782 215 VSPVGNYFKEGVAPINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 308 KDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGTAVVVAPVSSVTYHGQRYEF-RTGHD 386
Cdd:PLN02782 295 KDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSITYKGKRVSYgEGGFG 374
|
330 340
....*....|....*....|....*.
gi 1002252950 387 TLSQTLHTTLTSIQMGLAEDKKGWTV 412
Cdd:PLN02782 375 TVSQQLYTVLTSLQMGLIEDNMNWTV 400
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
119-402 |
5.32e-115 |
|
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.
Pssm-ID: 238798 Cd Length: 279 Bit Score: 337.25 E-value: 5.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 119 ELSPSSGVINYGQGLFEGLKAYRAANQQGSymLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLANRRWVPPQGK 198
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIV--LFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 199 GALYIRPLLIGSGPILGLAPAPEYTFLIYAAPVGTYFKEGLAPINLVVEDSiHRAMPGGTGGVKTITNYAPVLKAQMDAK 278
Cdd:cd01557 79 ASLYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVSSF-RRAAPGGPGAAKAGGNYAASLLAQKEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 279 SRGFTDVLYLDAVHKtYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVF 358
Cdd:cd01557 158 EKGYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVF 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002252950 359 CTGTAVVVAPVSSVTYHGQRY-EFRTGHdtLSQTLHTTLTSIQMG 402
Cdd:cd01557 237 ATGTAAVVTPVGEIDYRGKEPgEGEVGP--VTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
110-412 |
9.21e-112 |
|
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: 330.18 E-value: 9.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 110 GELSRYGNIELSPSSGVINYGQGLFEGLKAYRAANqqGSYMLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLAN 189
Cdd:TIGR01123 4 GRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCAD--GSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 190 RRWVPPQGKGA-LYIRPLLIGSGPILGLAPAPEYTFLIYAAPVGTYFKEGLAPINLVVEDSIHRAMPGGTGGVKTITNYA 268
Cdd:TIGR01123 82 KDWVPPYGSGAsLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVTTEYDRAAPGGTGAVKVGGNYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 269 PVLKAQMDAKSRGFTDVLYLDAVHKTYLEEASSCNLF-IVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVS 347
Cdd:TIGR01123 162 ASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFfITGDGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERRID 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 348 IDDL----VGADEVFCTGTAVVVAPVSSVTYHGQRYEFRTGH-DTLSQTLHTTLTSIQMGLAEDKKGWTV 412
Cdd:TIGR01123 242 IDELkafvEAGEIVFACGTAAVITPVGEIQHGGKEVVFASGQpGEVTKALYDELTDIQYGDFEDPYGWIV 311
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
110-362 |
3.18e-81 |
|
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: 251.26 E-value: 3.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 110 GELSRYGNIELSPSSGVINYGQGLFEGLKAYraanqQGSymLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLA 188
Cdd:COG0115 7 GELVPEEEATISVLDRGLHYGDGVFEGIRAY-----DGR--LFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 189 NrrwvppqGKGALYIRPLLIGSGPILGL-APAPEYTFLIYAAPVGTYFKEGLA-PINLVVEdSIHRAMPGGTGGVKTiTN 266
Cdd:COG0115 80 N-------GLEDGYIRPQVTRGVGGRGVfAEEYEPTVIIIASPLPAYPAEAYEkGVRVITS-PYRRAAPGGLGGIKT-GN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 267 YAPVLKAQMDAKSRGFTDVLYLDAvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLV 346
Cdd:COG0115 151 YLNNVLAKQEAKEAGADEALLLDT--DGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPI 228
|
250
....*....|....*.
gi 1002252950 347 SIDDLVGADEVFCTGT 362
Cdd:COG0115 229 SLEELYTADEVFLTGT 244
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
132-362 |
1.82e-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: 145.96 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 132 GLFEGLKAYRaanqqgsYMLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLANRRWVPpqgkgalYIRPLL-IG 209
Cdd:pfam01063 1 GVFETLRVYN-------GKIFFLDEHLARLRRSAKLLGIPLPfDEEDLRKIIEELLKANGLGVG-------RLRLTVsRG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 210 SGPILGLAPAPEYTFLIYAAPVGTYFKEGLAPINLVVEDsihraMPGGTGGVKTiTNYAPVLKAQMDAKSRGFTDVLYLD 289
Cdd:pfam01063 67 PGGFGLPTSDPTLAIFVSALPPPPESKKKGVISSLVRRN-----PPSPLPGAKT-LNYLENVLARREAKAQGADDALLLD 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002252950 290 AvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGT 362
Cdd:pfam01063 141 E--DGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNS 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02782 |
PLN02782 |
Branched-chain amino acid aminotransferase |
68-412 |
0e+00 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 215418 Cd Length: 403 Bit Score: 579.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 68 SADRSDEESGGEIDWDNLGFGLTPTDYMYVMRCSlEDGVFSRGELSRYGNIELSPSSGVINYGQGLFEGLKAYRaaNQQG 147
Cdd:PLN02782 58 SSSYTEVTELADIDWDNLGFGLVPTDYMYIMKCN-RDGEFSKGELQRFGNIELSPSAGVLNYGQGLFEGLKAYR--KEDG 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 148 SYMLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLANRRWVPPQGKGALYIRPLLIGSGPILGLAPAPEYTFLIY 227
Cdd:PLN02782 135 NILLFRPEENAIRMRNGAERMCMPAPTVEQFVEAVKETVLANKRWVPPPGKGSLYIRPLLMGSGAVLGLAPAPEYTFLIY 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 228 AAPVGTYFKEGLAPINLVVEDSIHRAMPGGTGGVKTITNYAPVLKAQMDAKSRGFTDVLYLDAVHKTYLEEASSCNLFIV 307
Cdd:PLN02782 215 VSPVGNYFKEGVAPINLIVENEFHRATPGGTGGVKTIGNYAAVLKAQSIAKAKGYSDVLYLDCVHKKYLEEVSSCNIFIV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 308 KDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGTAVVVAPVSSVTYHGQRYEF-RTGHD 386
Cdd:PLN02782 295 KDNVISTPAIKGTILPGITRKSIIDVARSQGFQVEERNVTVDELLEADEVFCTGTAVVVSPVGSITYKGKRVSYgEGGFG 374
|
330 340
....*....|....*....|....*.
gi 1002252950 387 TLSQTLHTTLTSIQMGLAEDKKGWTV 412
Cdd:PLN02782 375 TVSQQLYTVLTSLQMGLIEDNMNWTV 400
|
|
| PLN03117 |
PLN03117 |
Branched-chain-amino-acid aminotransferase; Provisional |
61-415 |
2.85e-172 |
|
Branched-chain-amino-acid aminotransferase; Provisional
Pssm-ID: 178664 Cd Length: 355 Bit Score: 485.59 E-value: 2.85e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 61 SSLPQLDSadRSDEESGgEIDWDNLGFGLTPTDYMYVMRCSLEDGvFSRGELSRYGNIELSPSSGVINYGQGLFEGLKAY 140
Cdd:PLN03117 4 SSSPLPTS--KADEKYA-NVKWEELGFALVPTDYMYVAKCKQGES-FSEGKIVPYGDISISPCAGILNYGQGLFEGLKAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 141 RAanQQGSYMLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLANRRWVPPQGKGALYIRPLLIGSGPILGLAPAP 220
Cdd:PLN03117 80 RT--EDGRITLFRPDQNALRMQTGADRLCMTPPSLEQFVEAVKQTVLANKKWVPPPGKGTLYIRPLLIGSGAVLGVAPAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 221 EYTFLIYAAPVGTYFKEGlAPINLVVEDSIHRAMPGGTGGVKTITNYAPVLKAQMDAKSRGFTDVLYLDAVHKTYLEEAS 300
Cdd:PLN03117 158 EYTFLIYASPVGNYHKAS-SGLNLKVDHKHRRAHSGGTGGVKSCTNYSPVVKSLIEAKSSGFSDVLFLDAATGKNIEELS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 301 SCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGTAVVVAPVSSVTYHGQRYE 380
Cdd:PLN03117 237 ACNIFILKGNIVSTPPTSGTILPGVTRKSISELARDIGYQVEERDVSVDELLEAEEVFCTGTAVVVKAVETVTFHDKKVK 316
|
330 340 350
....*....|....*....|....*....|....*
gi 1002252950 381 FRTGHDTLSQTLHTTLTSIQMGLAEDKKGWTVAID 415
Cdd:PLN03117 317 YRTGEEALSTKLHLILTNIQMGVVEDKKGWMVEID 351
|
|
| PLN02259 |
PLN02259 |
branched-chain-amino-acid aminotransferase 2 |
79-415 |
8.85e-166 |
|
branched-chain-amino-acid aminotransferase 2
Pssm-ID: 177901 Cd Length: 388 Bit Score: 470.74 E-value: 8.85e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 79 EIDWDNLGFGLTPTDYMYVMRCSlEDGVFSRGELSRYGNIELSPSSGVINYGQGLFEGLKAYRAANqqGSYMLFRPEENA 158
Cdd:PLN02259 55 DLDWDNLGFGLNPADYMYVMKCS-KDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKEN--GKLLLFRPDHNA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 159 RRMQHGAERMCMPSPSVEQFVHAVKQTVLANRRWVPPQGKGALYIRPLLIGSGPILGLAPAPEYTFLIYAAPVGTYFKEG 238
Cdd:PLN02259 132 IRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 239 LAPINLVVEDSIHRAMPGGTGGVKTITNYAPVLKAQMDAKSRGFTDVLYLDAVHKTYLEEASSCNLFIVKDGVVATPATV 318
Cdd:PLN02259 212 MAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPATN 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 319 GTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGTAVVVAPVSSVTYHGQRYEFRTGHDTLSQTLHTTLTS 398
Cdd:PLN02259 292 GTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEKRVEYKTGDESVCQKLRSVLVG 371
|
330
....*....|....*..
gi 1002252950 399 IQMGLAEDKKGWTVAID 415
Cdd:PLN02259 372 IQTGLIEDNKGWVTDIN 388
|
|
| PRK13357 |
PRK13357 |
branched-chain amino acid aminotransferase; Provisional |
65-415 |
7.36e-144 |
|
branched-chain amino acid aminotransferase; Provisional
Pssm-ID: 237363 Cd Length: 356 Bit Score: 413.39 E-value: 7.36e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 65 QLDSADRSDEESggEIDWDNLGFGLTPTDYMYVMRCSleDGVFSRGELSRYGNIELSPSSGVINYGQGLFEGLKAYRAAN 144
Cdd:PRK13357 4 TLKPNPTSDEKR--AIDWANLGFGYVFTDHMVVIDYK--DGKWHDARLVPYGPLELDPAATVLHYGQEIFEGLKAYRHKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 145 qqGSYMLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLANRRWVPPQGKGA-LYIRPLLIGSGPILGLAPAPEYT 223
Cdd:PRK13357 80 --GSIVLFRPDANAKRLQRSADRLLMPELPEELFLEAVKQLVKADRDWVPPYGEGAsLYLRPFMIATEPFLGVKPAEEYI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 224 FLIYAAPVGTYFKEGLAPINLVVEDSIHRAMPGGTGGVKTITNYAPVLKAQMDAKSRGFTDVLYLDAVHKTYLEEASSCN 303
Cdd:PRK13357 158 FCVIASPVGAYFKGGVKPVSIWVSDEYDRAAPGGTGAAKVGGNYAASLLAQAEAKEKGCDQVLYLDAVEHTYIEEVGGMN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 304 LF-IVKDGVVATPATvGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGA------DEVFCTGTAVVVAPVSSVTYHG 376
Cdd:PRK13357 238 FFfITKDGTVTPPLS-GSILPGITRDSLLQLAEDLGLTVEERPVSIDEWQADaasgefTEAFACGTAAVITPIGGIKYKD 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1002252950 377 QRYEFrtgHDT----LSQTLHTTLTSIQMGLAEDKKGWTVAID 415
Cdd:PRK13357 317 KEFVI---GDGevgpVTQKLYDELTGIQFGDVEDPHGWIVKVD 356
|
|
| PLN02883 |
PLN02883 |
Branched-chain amino acid aminotransferase |
65-414 |
5.07e-140 |
|
Branched-chain amino acid aminotransferase
Pssm-ID: 178471 Cd Length: 384 Bit Score: 404.87 E-value: 5.07e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 65 QLDSADRSDEESGgEIDWDNLGFGLTPTDYMYVMRcSLEDGVFSRGELSRYGNIELSPSSGVINYGQGLFEGLKAYRAan 144
Cdd:PLN02883 38 HVSGAEREDEEYA-DVDWDKLGFSLVRTDFMFATK-SCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRG-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 145 QQGSYMLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLANRRWVPPQGKGALYIRPLLIGSGPILGLAPAPEYTF 224
Cdd:PLN02883 114 EDGRILLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAAPEYTF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 225 LIYAAPVGTYFKEGLAPINLVVEDSIHRAMPGGTGGVKTITNYAPVLKAQMDAKSRGFTDVLYLDAVHKTYLEEASSCNL 304
Cdd:PLN02883 194 LVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 305 FIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGTAVVVAPVSSVTYHGQRYEFRTG 384
Cdd:PLN02883 274 FLVKGNIIVTPATSGTILGGITRKSIIEIALDLGYKVEERRVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVG 353
|
330 340 350
....*....|....*....|....*....|
gi 1002252950 385 HDTLSQTLHTTLTSIQMGLAEDKKGWTVAI 414
Cdd:PLN02883 354 DGIVTQQLRSILLGIQTGSIQDTKDWVLQI 383
|
|
| BCAT_beta_family |
cd01557 |
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the ... |
119-402 |
5.32e-115 |
|
BCAT_beta_family: Branched-chain aminotransferase catalyses the transamination of the branched-chain amino acids leusine, isoleucine and valine to their respective alpha-keto acids, alpha-ketoisocaproate, alpha-keto-beta-methylvalerate and alpha-ketoisovalerate. The enzyme requires pyridoxal 5'-phosphate (PLP) as a cofactor to catalyze the reaction. It has been found that mammals have two foms of the enzyme - mitochondrial and cytosolic forms while bacteria contain only one form of the enzyme. The mitochondrial form plays a significant role in skeletal muscle glutamine and alanine synthesis and in interorgan nitrogen metabolism.Members of this subgroup are widely distributed in all three forms of life.
Pssm-ID: 238798 Cd Length: 279 Bit Score: 337.25 E-value: 5.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 119 ELSPSSGVINYGQGLFEGLKAYRAANQQGSymLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLANRRWVPPQGK 198
Cdd:cd01557 1 SLHPATHALHYGQAVFEGLKAYRTPDGKIV--LFRPDENAERLNRSARRLGLPPFSVEEFIDAIKELVKLDADWVPYGGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 199 GALYIRPLLIGSGPILGLAPAPEYTFLIYAAPVGTYFKEGLAPINLVVEDSiHRAMPGGTGGVKTITNYAPVLKAQMDAK 278
Cdd:cd01557 79 ASLYIRPFIFGTDPQLGVSPALEYLFAVFASPVGAYFKGGEKGVSALVSSF-RRAAPGGPGAAKAGGNYAASLLAQKEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 279 SRGFTDVLYLDAVHKtYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVF 358
Cdd:cd01557 158 EKGYDQALWLDGAHG-YVAEVGTMNIFFVKDGELITPPLDGSILPGITRDSILELARDLGIKVEERPITRDELYEADEVF 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002252950 359 CTGTAVVVAPVSSVTYHGQRY-EFRTGHdtLSQTLHTTLTSIQMG 402
Cdd:cd01557 237 ATGTAAVVTPVGEIDYRGKEPgEGEVGP--VTKKLYDLLTDIQYG 279
|
|
| ilvE_II |
TIGR01123 |
branched-chain amino acid aminotransferase, group II; Among the class IV aminotransferases are ... |
110-412 |
9.21e-112 |
|
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: 330.18 E-value: 9.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 110 GELSRYGNIELSPSSGVINYGQGLFEGLKAYRAANqqGSYMLFRPEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLAN 189
Cdd:TIGR01123 4 GRLTPYGPLHLDPGSTVLHYGQECFEGLKAYRCAD--GSIVLFRPDANAARLRRSARRLLMPELPDELFLEALRQLVKAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 190 RRWVPPQGKGA-LYIRPLLIGSGPILGLAPAPEYTFLIYAAPVGTYFKEGLAPINLVVEDSIHRAMPGGTGGVKTITNYA 268
Cdd:TIGR01123 82 KDWVPPYGSGAsLYLRPFVIGTEPNLGVRPAPEYLFYVFASPVGAYFKGGLAPVSIFVTTEYDRAAPGGTGAVKVGGNYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 269 PVLKAQMDAKSRGFTDVLYLDAVHKTYLEEASSCNLF-IVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVS 347
Cdd:TIGR01123 162 ASLLAQAKAAEQGCDQVVYLDPVEHTYIEEVGAMNFFfITGDGELVTPPLSGSILPGITRDSLLQLAKDLGMEVEERRID 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 348 IDDL----VGADEVFCTGTAVVVAPVSSVTYHGQRYEFRTGH-DTLSQTLHTTLTSIQMGLAEDKKGWTV 412
Cdd:TIGR01123 242 IDELkafvEAGEIVFACGTAAVITPVGEIQHGGKEVVFASGQpGEVTKALYDELTDIQYGDFEDPYGWIV 311
|
|
| PLPDE_IV |
cd00449 |
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ... |
126-362 |
8.95e-82 |
|
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.
Pssm-ID: 238254 [Multi-domain] Cd Length: 256 Bit Score: 251.75 E-value: 8.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 126 VINYGQGLFEGLKAYRAAnqqgsymLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLANrrwvppqGKGALYIR 204
Cdd:cd00449 3 GLHYGDGVFEGLRAGKGR-------LFRLDEHLDRLNRSAKRLGLPIPyDREELREALKELVAAN-------NGASLYIR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 205 PLLIGSGPILGLAPAP--EYTFLIYAAPVGTYFKEGLAPINLVVEDSIHRAMPGGTGGVKTiTNYAPVLKAQMDAKSRGF 282
Cdd:cd00449 69 PLLTRGVGGLGVAPPPspEPTFVVFASPVGAYAKGGEKGVRLITSPDRRRAAPGGTGDAKT-GGNLNSVLAKQEAAEAGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 283 TDVLYLDAvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGT 362
Cdd:cd00449 148 DEALLLDD--NGYVTEGSASNVFIVKDGELVTPPLDGGILPGITRDSVIELAKELGIKVEERPISLDELYAADEVFLTGT 225
|
|
| IlvE |
COG0115 |
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ... |
110-362 |
3.18e-81 |
|
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: 251.26 E-value: 3.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 110 GELSRYGNIELSPSSGVINYGQGLFEGLKAYraanqQGSymLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLA 188
Cdd:COG0115 7 GELVPEEEATISVLDRGLHYGDGVFEGIRAY-----DGR--LFRLDEHLARLNRSAKRLGIPIPyTEEELLEAIRELVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 189 NrrwvppqGKGALYIRPLLIGSGPILGL-APAPEYTFLIYAAPVGTYFKEGLA-PINLVVEdSIHRAMPGGTGGVKTiTN 266
Cdd:COG0115 80 N-------GLEDGYIRPQVTRGVGGRGVfAEEYEPTVIIIASPLPAYPAEAYEkGVRVITS-PYRRAAPGGLGGIKT-GN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 267 YAPVLKAQMDAKSRGFTDVLYLDAvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLV 346
Cdd:COG0115 151 YLNNVLAKQEAKEAGADEALLLDT--DGYVAEGSGSNVFIVKDGVLVTPPLSGGILPGITRDSVIELARELGIPVEERPI 228
|
250
....*....|....*.
gi 1002252950 347 SIDDLVGADEVFCTGT 362
Cdd:COG0115 229 SLEELYTADEVFLTGT 244
|
|
| PRK06606 |
PRK06606 |
branched-chain amino acid transaminase; |
127-362 |
2.90e-44 |
|
branched-chain amino acid transaminase;
Pssm-ID: 235841 Cd Length: 306 Bit Score: 156.08 E-value: 2.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 127 INYGQGLFEGLKAYRaaNQQGSyMLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLANRRwvppqgKGAlYIRP 205
Cdd:PRK06606 30 LHYGTGVFEGIRAYD--TPKGP-AIFRLREHTKRLFNSAKILRMEIPySVDELMEAQREVVRKNNL------KSA-YIRP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 206 LL-IGSGpilGLAPAPEYT---FLIYAAPVGTYF-KEGLAP-INLVVEdSIHRAMPGGT-GGVKTITNYAPVLKAQMDAK 278
Cdd:PRK06606 100 LVfVGDE---GLGVRPHGLptdVAIAAWPWGAYLgEEALEKgIRVKVS-SWTRHAPNSIpTRAKASGNYLNSILAKTEAR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 279 SRGFTDVLYLDAvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVF 358
Cdd:PRK06606 176 RNGYDEALLLDV--EGYVSEGSGENIFIVRDGVLYTPPLTSSILEGITRDTVITLAKDLGIEVIERRITRDELYIADEVF 253
|
....
gi 1002252950 359 CTGT 362
Cdd:PRK06606 254 FTGT 257
|
|
| Aminotran_4 |
pfam01063 |
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ... |
132-362 |
1.82e-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: 145.96 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 132 GLFEGLKAYRaanqqgsYMLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLANRRWVPpqgkgalYIRPLL-IG 209
Cdd:pfam01063 1 GVFETLRVYN-------GKIFFLDEHLARLRRSAKLLGIPLPfDEEDLRKIIEELLKANGLGVG-------RLRLTVsRG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 210 SGPILGLAPAPEYTFLIYAAPVGTYFKEGLAPINLVVEDsihraMPGGTGGVKTiTNYAPVLKAQMDAKSRGFTDVLYLD 289
Cdd:pfam01063 67 PGGFGLPTSDPTLAIFVSALPPPPESKKKGVISSLVRRN-----PPSPLPGAKT-LNYLENVLARREAKAQGADDALLLD 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002252950 290 AvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGT 362
Cdd:pfam01063 141 E--DGNVTEGSTSNVFLVKGGTLYTPPLESGILPGITRQALLDLAKALGLEVEERPITLADLQEADEAFLTNS 211
|
|
| ilvE_I |
TIGR01122 |
branched-chain amino acid aminotransferase, group I; Among the class IV aminotransferases are ... |
110-362 |
4.51e-40 |
|
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: 144.81 E-value: 4.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 110 GELSRYGNIELSPSSGVINYGQGLFEGLKAYRaaNQQGSYmLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLA 188
Cdd:TIGR01122 4 GEFVDWEDAKVHVLTHALHYGTGVFEGIRAYD--TDKGPA-IFRLKEHIQRLYDSAKIYRMEIPySKEELMEATRETLRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 189 NrrwvppqGKGALYIRPLLIGSGPILGLAPAPEYT--FLIYAAPVGTYF-KEGLAPINLVVEDSIHRAMPGGT-GGVKTI 264
Cdd:TIGR01122 81 N-------NLRSAYIRPLVFRGDGDLGLNPRAGYKpdVIIAAWPWGAYLgEEALEKGIDAKVSSWRRNAPNTIpTAAKAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 265 TNYAPVLKAQMDAKSRGFTDVLYLDAvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEER 344
Cdd:TIGR01122 154 GNYLNSLLAKSEARRHGYDEAILLDV--EGYVAEGSGENIFIVKDGVLFTPPVTSSILPGITRDTVITLAKELGIEVVEQ 231
|
250
....*....|....*...
gi 1002252950 345 LVSIDDLVGADEVFCTGT 362
Cdd:TIGR01122 232 PISREELYTADEAFFTGT 249
|
|
| D-AAT_like |
cd01558 |
D-Alanine aminotransferase (D-AAT_like): D-amino acid aminotransferase catalyzes ... |
129-362 |
9.98e-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: 9.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 129 YGQGLFEGLKAYRAanqqgsyMLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLANRrwvppQGKGALYIRpLL 207
Cdd:cd01558 23 FGDGVYEVIRVYNG-------KPFALDEHLDRLYRSAKELRIDIPyTREELKELIRELVAKNE-----GGEGDVYIQ-VT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 208 IGSGPILGLAPAPEYTFL-IYAAPVGTYFKEGLA-PINLVVEDSI---HRAmpggtggVKTItNYAPVLKAQMDAKSRGF 282
Cdd:cd01558 90 RGVGPRGHDFPKCVKPTVvIITQPLPLPPAELLEkGVRVITVPDIrwlRCD-------IKSL-NLLNNVLAKQEAKEAGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 283 TDVLYLDAvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGT 362
Cdd:cd01558 162 DEAILLDA--DGLVTEGSSSNVFIVKNGVLVTPPLDNGILPGITRATVIELAKELGIPVEERPFSLEELYTADEVFLTST 239
|
|
| PRK08320 |
PRK08320 |
branched-chain amino acid aminotransferase; Reviewed |
129-362 |
5.53e-31 |
|
branched-chain amino acid aminotransferase; Reviewed
Pssm-ID: 236238 [Multi-domain] Cd Length: 288 Bit Score: 119.98 E-value: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 129 YGQGLFEGLKAYraanqqgSYMLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLANrrwvppQGKGAlYIRPLL 207
Cdd:PRK08320 28 YGDGVFEGIRAY-------NGRVFRLKEHIDRLYDSAKAIMLEIPlSKEEMTEIVLETLRKN------NLRDA-YIRLVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 208 I-GSGPiLGLAP--APEYTFLIYAAPVGTYFKE----GLApinlVVEDSIHRAMPGGTG-GVKTItNYAPVLKAQMDAKS 279
Cdd:PRK08320 94 SrGVGD-LGLDPrkCPKPTVVCIAEPIGLYPGElyekGLK----VITVSTRRNRPDALSpQVKSL-NYLNNILAKIEANL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 280 RGFTDVLYLDavHKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFC 359
Cdd:PRK08320 168 AGVDEAIMLN--DEGYVAEGTGDNIFIVKNGKLITPPTYAGALEGITRNAVIEIAKELGIPVREELFTLHDLYTADEVFL 245
|
...
gi 1002252950 360 TGT 362
Cdd:PRK08320 246 TGT 248
|
|
| PRK13356 |
PRK13356 |
branched-chain amino acid aminotransferase; |
159-361 |
2.50e-27 |
|
branched-chain amino acid aminotransferase;
Pssm-ID: 237362 Cd Length: 286 Bit Score: 110.04 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 159 RRMQHGAERMCM-PSPSVEQFVHAVKQTVlanRRWvppQGKGALYIRPLLIG-SGPILGLAPAPEYT---FLIYAAPvgt 233
Cdd:PRK13356 55 ARVNRSAEALGLkPTVSAEEIEALAREGL---KRF---DPDTALYIRPMYWAeDGFASGVAPDPESTrfaLCLEEAP--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 234 yfkeglapinlvvedsihraMPGGTGGVKTITNYA-PVL-----------------KAQMDAKSRGFTDVLYLDAVHKty 295
Cdd:PRK13356 126 --------------------MPEPTGFSLTLSPFRrPTLemaptdakagclypnnaRALREARSRGFDNALVLDMLGN-- 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002252950 296 LEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTG 361
Cdd:PRK13356 184 VAETATSNVFMVKDGVVFTPVPNGTFLNGITRQRVIALLREDGVTVVETTLTYEDFLEADEVFSTG 249
|
|
| ADCL_like |
cd01559 |
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ... |
129-362 |
1.76e-26 |
|
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: 106.62 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 129 YGQGLFEGLKAYraanqQGSYMLFrpEENARRMQHGAERMCMPSPSVEQFVHAVKQTVLANrrwvpPQGKGAlyIRpLLI 208
Cdd:cd01559 6 YGDGVFETMRAL-----DGRLFLL--DAHLARLERSARRLGIPEPDLPRLRAALESLLAAN-----DIDEGR--IR-LIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 209 GSGPILGLAPAPEYTFLIYAAPVGTYFKEGLAPINLVVEDSIHRAMPGGTGGVKTiTNYAPVLKAQMDAKSRGFTDVLYL 288
Cdd:cd01559 71 SRGPGGRGYAPSVCPGPALYVSVIPLPPAWRQDGVRLITCPVRLGEQPLLAGLKH-LNYLENVLAKREARDRGADEALFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002252950 289 DAvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCTGT 362
Cdd:cd01559 150 DT--DGRVIEGTASNLFFVKDGELVTPSLDRGGLAGITRQRVIELAAAKGYAVDERPLRLEDLLAADEAFLTNS 221
|
|
| PRK12479 |
PRK12479 |
branched-chain-amino-acid transaminase; |
129-362 |
2.50e-23 |
|
branched-chain-amino-acid transaminase;
Pssm-ID: 183549 [Multi-domain] Cd Length: 299 Bit Score: 99.26 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 129 YGQGLFEGLKAYrAANqqgsymLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLANrrwvppqGKGALYIRpLL 207
Cdd:PRK12479 29 YGDGVFEGIRSY-GGN------VFCLKEHVKRLYESAKSILLTIPlTVDEMEEAVLQTLQKN-------EYADAYIR-LI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 208 IGSGP-ILGLAP--APEYTFLIYAAPVGTYFKE----GLApinlVVEDSIHRAMPGGTGGVKTITNYAPVLKAQMDAKSR 280
Cdd:PRK12479 94 VSRGKgDLGLDPrsCVKPSVIIIAEQLKLFPQEfydnGLS----VVSVASRRNTPDALDPRIKSMNYLNNVLVKIEAAQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 281 GFTDVLYLDavHKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCT 360
Cdd:PRK12479 170 GVLEALMLN--QQGYVCEGSGDNVFVVKDGKVLTPPSYLGALEGITRNSVIELCERLSIPCEERPFTRHDVYVADEVFLT 247
|
..
gi 1002252950 361 GT 362
Cdd:PRK12479 248 GT 249
|
|
| PRK07544 |
PRK07544 |
branched-chain amino acid aminotransferase; Validated |
129-362 |
1.18e-22 |
|
branched-chain amino acid aminotransferase; Validated
Pssm-ID: 181025 Cd Length: 292 Bit Score: 96.97 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 129 YGQGLFEGLKAYraanqqgSYMLFRPEENARRMQHGAERMCMPSP-SVEQFVHAVKQTVLANrrwvppqGKGALYIRPLL 207
Cdd:PRK07544 34 YASSVFEGERAY-------GGKIFKLREHSERLRRSAELLDFEIPySVAEIDAAKKETLAAN-------GLTDAYVRPVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 208 IGSGPILGLAPAPEYTFLIYAA-PVGTYF--KEGLAPINLVV--------EDSIHRAMPGGTGGVKTITNYApvlkaqmd 276
Cdd:PRK07544 100 WRGSEMMGVSAQQNKIHLAIAAwEWPSYFdpEAKMKGIRLDIakwrrpdpETAPSAAKAAGLYMICTISKHA-------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 277 AKSRGFTDVLYLDavHKTYLEEASSCNLFIVKDGVVATPaTVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADE 356
Cdd:PRK07544 172 AEAKGYADALMLD--YRGYVAEATGANIFFVKDGVIHTP-TPDCFLDGITRQTVIELAKRRGIEVVERHIMPEELAGFSE 248
|
....*.
gi 1002252950 357 VFCTGT 362
Cdd:PRK07544 249 CFLTGT 254
|
|
| PRK07849 |
PRK07849 |
aminodeoxychorismate lyase; |
130-357 |
7.82e-20 |
|
aminodeoxychorismate lyase;
Pssm-ID: 236114 [Multi-domain] Cd Length: 292 Bit Score: 88.86 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 130 GQGLFEGLKAYRAanqqgsymlfRP---EENARRMQHGAERMCMPSPSVEQFVHAVKqtvLANRRWVPPQGKGAL---YI 203
Cdd:PRK07849 38 GDGVFETLLVRDG----------RPcnlEAHLERLARSAALLDLPEPDLDRWRRAVE---LAIEEWRAPEDEAALrlvYS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 204 RplligsgpilGLAPAPEYTFLIYAAPV-GTYFKEGLAPINLVVED-----SIHRAMPGGTGGVKTItNYAPVLKAQMDA 277
Cdd:PRK07849 105 R----------GRESGGAPTAWVTVSPVpERVARARREGVSVITLDrgypsDAAERAPWLLAGAKTL-SYAVNMAALRYA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 278 KSRGFTDVLYLDAvhKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEV 357
Cdd:PRK07849 174 ARRGADDVIFTST--DGYVLEGPTSTVVIATDDRLLTPPPWYGILPGTTQAALFEVAREKGWDCEYRALRPADLFAADGV 251
|
|
| PRK06680 |
PRK06680 |
D-amino acid aminotransferase; Reviewed |
277-362 |
1.55e-13 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 180656 [Multi-domain] Cd Length: 286 Bit Score: 70.34 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 277 AKSRGFTDVLYLDAVHKTyleEASSCNLFIV-KDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGAD 355
Cdd:PRK06680 163 AKEAGAQEAWMVDDGFVT---EGASSNAWIVtKDGKLVTRPADNFILPGITRHTLIDLAKELGLEVEERPFTLQEAYAAR 239
|
....*..
gi 1002252950 356 EVFCTGT 362
Cdd:PRK06680 240 EAFITAA 246
|
|
| PRK07650 |
PRK07650 |
4-amino-4-deoxychorismate lyase; Provisional |
295-360 |
2.21e-11 |
|
4-amino-4-deoxychorismate lyase; Provisional
Pssm-ID: 181067 Cd Length: 283 Bit Score: 64.22 E-value: 2.21e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002252950 295 YLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERLVSIDDLVGADEVFCT 360
Cdd:PRK07650 174 YVAEGIVSNLFWVKGDIVYTPSLETGILNGITRAFVIKVLEELGIEVKEGFYTKEELLSADEVFVT 239
|
|
| PRK12400 |
PRK12400 |
D-amino acid aminotransferase; Reviewed |
266-362 |
5.75e-09 |
|
D-amino acid aminotransferase; Reviewed
Pssm-ID: 171470 Cd Length: 290 Bit Score: 56.95 E-value: 5.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 266 NYAPVLKAQMDAKSRGFTDVLYldaVHKTYLEEASSCNLFIVKDGVVATPATVGTILPGITRKSVIELARDRGYQVEERL 345
Cdd:PRK12400 154 NLLPNILAATKAERKGCKEALF---VRNGTVTEGSHSNFFLIKNGTLYTHPANHLILNGIIRQYVLSLAKTLRIPVQEEL 230
|
90
....*....|....*..
gi 1002252950 346 VSIDDLVGADEVFCTGT 362
Cdd:PRK12400 231 FSVRDVYQADECFFTGT 247
|
|
| PRK06092 |
PRK06092 |
4-amino-4-deoxychorismate lyase; Reviewed |
298-358 |
3.14e-08 |
|
4-amino-4-deoxychorismate lyase; Reviewed
Pssm-ID: 235696 Cd Length: 268 Bit Score: 54.46 E-value: 3.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002252950 298 EASSCNLFIVKDGVVATP----ATVGtilpGITRKSVIELARDRGYQVEERLVSIDDLVGADEVF 358
Cdd:PRK06092 173 ECCAANLFWRKGGVVYTPdldqCGVA----GVMRQFILELLAQSGYPVVEVDASLEELLQADEVF 233
|
|
| PLN02845 |
PLN02845 |
Branched-chain-amino-acid aminotransferase-like protein |
255-366 |
4.95e-06 |
|
Branched-chain-amino-acid aminotransferase-like protein
Pssm-ID: 215454 [Multi-domain] Cd Length: 336 Bit Score: 48.09 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252950 255 PGGTGGVKTiTNYAPVLKAQMDAKSRGFTDVLYLDAvhKTYLEEASSCNL-FIVKDGVVATPATvGTILPGITRKSVIEL 333
Cdd:PLN02845 178 PPQFATVKS-VNYLPNALSQMEAEERGAFAGIWLDE--EGFVAEGPNMNVaFLTNDGELVLPPF-DKILSGCTARRVLEL 253
|
90 100 110
....*....|....*....|....*....|....*...
gi 1002252950 334 A-----RDRGYQVEERLVSIDDLVGADEVFCTGTAVVV 366
Cdd:PLN02845 254 AprlvsPGDLRGVKQRKISVEEAKAADEMMLIGSGVPV 291
|
|
| |
