|
Name |
Accession |
Description |
Interval |
E-value |
| trpB_rel |
TIGR01415 |
pyridoxal-phosphate dependent TrpB-like enzyme; This model represents a family of ... |
11-424 |
0e+00 |
|
pyridoxal-phosphate dependent TrpB-like enzyme; This model represents a family of pyridoxal-phosphate dependent enzyme (pfam00291) closely related to the beta subunit of tryptophan synthase (TIGR00263). However, the only case in which a member of this family replaces a member of TIGR00263 is in Sulfolobus species which contain two sequences which hit this model, one of which is proximal to the alpha subunit. In every other case so far, either the species appears not to make tryptophan (there is no trp synthase alpha subunit), or a trp synthase beta subunit matching TIGR00263 is also found. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273609 Cd Length: 419 Bit Score: 726.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 11 MPDHWYNILPDLPEELPTPRDETGE---AFDTLKKAVPAKVLEYEFSGERYPKIPDEILERYMQVGRPTPIIRAKKLEEL 87
Cdd:TIGR01415 1 IPKHWYNILPDLPEPLPPPLDPEGEepiAIEKLKRIFPEKLLEQEVSGERWIKIPGEVLKRYAQIGRPTPLIRAKGLEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 88 LGGNLKIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVRTSFYAKPYRK 167
Cdd:TIGR01415 81 LGTPARIYYKYESVSPTGSHKINTAIAQAYYAKIEGAKRLVTETGAGQWGSALSLAGALFGLECKVFMVRVSFNQKPYRK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 168 YMMYMYGAHPHPSPSEFTEYGREVLKRMPDTPGSLGLAISEAIHYALDNG-GKYIAGSVINSDILFKTIAGMEAKKQMEM 246
Cdd:TIGR01415 161 YLMELYGAEVIPSPSEFTEFGREVLKEDPDHPGSLGIAISEAIEYALSDEdTKYSLGSVLNHVLLHQTVIGLEAKKQMEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 247 AGEDPDYIVGVVGGGSNYAALAFPFLADELsSGKIRRTYIASGSKEVPKMTEGEYRYDYPDTGKVLPLLKMYTIGYDFIP 326
Cdd:TIGR01415 241 AGEDPDVIIGCVGGGSNFAGLAFPFVADKL-SGKIDRRFIAAEPKACPTLTRGEYRYDFGDTAGLTPLLKMYTLGHDFIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 327 PAVYAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKNR--GEKKTVLV 404
Cdd:TIGR01415 320 PPIHAGGLRYHGVAPTLSLLVNLGIVEARAYDQEEAFEAAVIFAKTEGIVPAPESAHAIAAAIDEARKCRetGEEKVILF 399
|
410 420
....*....|....*....|
gi 13878841 405 SFSGHGLLDLGNYAEALHFE 424
Cdd:TIGR01415 400 NLSGHGLLDLKAYAKYLHGE 419
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
1-423 |
0e+00 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 682.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 1 MIRIDLKQDEMPDHWYNILPDLPEELPTPRD-ETGE--AFDTLKKAVPAKVLEYEFSGERYPKIPDEILERYmQVGRPTP 77
Cdd:PRK12391 1 QTKILLDEDEIPTQWYNILADLPEPLPPPLDpGTGEpvTPEDLAPIFPMELIEQEVSTERYIDIPEEVREIY-RLWRPTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 78 IIRAKKLEELLGGNLKIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVR 157
Cdd:PRK12391 80 LIRARRLEKALGTPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACALFGLECTVFMVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 158 TSFYAKPYRKYMMYMYGAHPHPSPSEFTEYGREVLKRMPDTPGSLGLAISEAIHYALDNGG-KYIAGSVINSDILFKTIA 236
Cdd:PRK12391 160 VSYEQKPYRRSLMETYGAEVIPSPSDLTEAGRKILAEDPDHPGSLGIAISEAVEDAAKRPDtKYALGSVLNHVLLHQTVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 237 GMEAKKQMEMAGEDPDYIVGVVGGGSNYAALAFPFLADELsSGKIRRTYIASGSKEVPKMTEGEYRYDYPDTGKVLPLLK 316
Cdd:PRK12391 240 GLEAKKQLELAGEYPDVVIGCVGGGSNFAGLAFPFLGDKL-EGKKDTRFIAVEPAACPTLTKGEYAYDFGDTAGLTPLLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 317 MYTIGYDFIPPAVYAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKNR 396
Cdd:PRK12391 319 MYTLGHDFVPPPIHAGGLRYHGMAPLVSLLVHEGLIEARAYPQTEVFEAAVLFARTEGIVPAPESSHAIAAAIDEALKAK 398
|
410 420
....*....|....*....|....*....
gi 13878841 397 --GEKKTVLVSFSGHGLLDLGNYAEALHF 423
Cdd:PRK12391 399 eeGEEKVILFNLSGHGLLDLAAYDAYLAG 427
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
1-421 |
0e+00 |
|
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport and metabolism]; Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440961 Cd Length: 433 Bit Score: 556.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 1 MIRIDLKQDEMPDHWYNILPDLPEELPTPRD-ETGE--AFDTLKKAVPAKVLEYEFSGERYPKIPDEILERYmQVGRPTP 77
Cdd:COG1350 2 QTKILLDESEIPTQWYNILADLPEPLPPPLHpGTGEpvTPEDLAPIFPMELIEQEMSTERWIEIPEEVREIY-RLWRPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 78 IIRAKKLEELLGGNLKIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVR 157
Cdd:COG1350 81 LYRARRLEKALGTPAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALSFACALFGLECTVYMVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 158 TSFYAKPYRKYMMYMYGAHPHPSPSEFTEYGREVLKRMPDTPGSLGLAISEAIHYALDNGG-KYIAGSVINSDILFKTIA 236
Cdd:COG1350 161 VSYEQKPYRRSMMETYGAEVIPSPSDLTEAGRKILAEDPDTPGSLGIAISEAVEDAATRDDtKYALGSVLNHVLLHQTVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 237 GMEAKKQMEMAGEDPDYIVGVVGGGSNYAALAFPFLADELsSGKIRRTYIASGSKEVPKMTEGEYRYDYPDTGKVLPLLK 316
Cdd:COG1350 241 GLEAKKQLEKAGEYPDVVIGCAGGGSNFAGLAFPFLRDKL-RGKKDVRFIAVEPAACPTLTRGVYAYDFGDTAGLTPLLK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 317 MYTIGYDFIPPAVYAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHAL--PILKEIADK 394
Cdd:COG1350 320 MYTLGHDFIPPPIHAGGLRYHGMAPLVSQLYHDGLIEAVAYPQLEVFEAGVLFARTEGIVPAPESAHAIkaAIDEALKCK 399
|
410 420
....*....|....*....|....*..
gi 13878841 395 NRGEKKTVLVSFSGHGLLDLGNYAEAL 421
Cdd:COG1350 400 EEGEEKTILFNLSGHGHFDLAAYDAYL 426
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
45-417 |
3.12e-169 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 478.57 E-value: 3.12e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 45 PAKVLEYEFSGERY-PKIPDEILERYMQ-VGRPTPIIRAKKLEELLGGNlKIFLKMESYTYSGSHKINSALAHVFFAREE 122
Cdd:cd06446 2 ALEELEQEFSKERYdPDFPEELRELYKDyVGRPTPLYRAKRLSEYLGGA-KIYLKREDLNHTGAHKINNALGQALLAKRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 123 GAKFVSTETGAGQWGSAVALASALFHMESHIFMVRTSFYAKPYRKYMMYMYGAHPHPSPSEFteygrevlkrmpdtpGSL 202
Cdd:cd06446 81 GKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGS---------------GTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 203 GLAISEAIHYALDN--GGKYIAGSVI------NSDILFKTIAGMEAKKQM-EMAGEDPDYIVGVVGGGSNYAALAFPFLA 273
Cdd:cd06446 146 KDAISEAIRDWVTNveDTHYLLGSVVgphpypNMVRDFQSVIGEEAKKQIlEKEGELPDVVIACVGGGSNAAGLFYPFIN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 274 DElssgkiRRTYIASGSKEVPKMTEGEYRYDYPDTGKVLPLLKMYTIG---YDFIPPAVYAGGLRYHAVAPTLSLLMNKG 350
Cdd:cd06446 226 DK------DVKLIGVEAGGCGLETGGHAAYLFGGTAGVLHGLKMYTLQdedGQIVPPHSISAGLDYPGVGPEHAYLKDSG 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13878841 351 IVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKnRGEKKTVLVSFSGHGLLDLGNY 417
Cdd:cd06446 300 RVEYVAVTDEEALEAFKLLARTEGIIPALESSHAIAYAIKLAKK-LGKEKVIVVNLSGRGDKDLQTV 365
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
71-408 |
5.55e-43 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 152.46 E-value: 5.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 71 QVGRPTPIIRAKKLEELLGGNlkIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHME 150
Cdd:pfam00291 3 LGIGPTPLVRLPRLSKELGVD--VYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 151 SHIFMVRTsfyAKPYRKYMMYMYGAHPHPSPSEFTEygrevlkrmpdtpgslglAISEAIHYALDNGGKYIAGSVINSDI 230
Cdd:pfam00291 81 VTIVVPED---APPGKLLLMRALGAEVVLVGGDYDE------------------AVAAARELAAEGPGAYYINQYDNPLN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 231 L--FKTIaGMEAKKQMemaGEDPDYIVGVVGGGSNYAALAFPFLAdelSSGKIRRtyIASGSKEVPKMtegeyrYDYPDT 308
Cdd:pfam00291 140 IegYGTI-GLEILEQL---GGDPDAVVVPVGGGGLIAGIARGLKE---LGPDVRV--IGVEPEGAPAL------ARSLAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 309 GKVLPLLKMYTIgydfippavyAGGLRYHAVAPTLSL-LMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPI 387
Cdd:pfam00291 205 GRPVPVPVADTI----------ADGLGVGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAA 274
|
330 340
....*....|....*....|.
gi 13878841 388 LKEIADKNRGEKKTVLVSFSG 408
Cdd:pfam00291 275 LKLALAGELKGGDRVVVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| trpB_rel |
TIGR01415 |
pyridoxal-phosphate dependent TrpB-like enzyme; This model represents a family of ... |
11-424 |
0e+00 |
|
pyridoxal-phosphate dependent TrpB-like enzyme; This model represents a family of pyridoxal-phosphate dependent enzyme (pfam00291) closely related to the beta subunit of tryptophan synthase (TIGR00263). However, the only case in which a member of this family replaces a member of TIGR00263 is in Sulfolobus species which contain two sequences which hit this model, one of which is proximal to the alpha subunit. In every other case so far, either the species appears not to make tryptophan (there is no trp synthase alpha subunit), or a trp synthase beta subunit matching TIGR00263 is also found. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273609 Cd Length: 419 Bit Score: 726.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 11 MPDHWYNILPDLPEELPTPRDETGE---AFDTLKKAVPAKVLEYEFSGERYPKIPDEILERYMQVGRPTPIIRAKKLEEL 87
Cdd:TIGR01415 1 IPKHWYNILPDLPEPLPPPLDPEGEepiAIEKLKRIFPEKLLEQEVSGERWIKIPGEVLKRYAQIGRPTPLIRAKGLEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 88 LGGNLKIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVRTSFYAKPYRK 167
Cdd:TIGR01415 81 LGTPARIYYKYESVSPTGSHKINTAIAQAYYAKIEGAKRLVTETGAGQWGSALSLAGALFGLECKVFMVRVSFNQKPYRK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 168 YMMYMYGAHPHPSPSEFTEYGREVLKRMPDTPGSLGLAISEAIHYALDNG-GKYIAGSVINSDILFKTIAGMEAKKQMEM 246
Cdd:TIGR01415 161 YLMELYGAEVIPSPSEFTEFGREVLKEDPDHPGSLGIAISEAIEYALSDEdTKYSLGSVLNHVLLHQTVIGLEAKKQMEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 247 AGEDPDYIVGVVGGGSNYAALAFPFLADELsSGKIRRTYIASGSKEVPKMTEGEYRYDYPDTGKVLPLLKMYTIGYDFIP 326
Cdd:TIGR01415 241 AGEDPDVIIGCVGGGSNFAGLAFPFVADKL-SGKIDRRFIAAEPKACPTLTRGEYRYDFGDTAGLTPLLKMYTLGHDFIP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 327 PAVYAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKNR--GEKKTVLV 404
Cdd:TIGR01415 320 PPIHAGGLRYHGVAPTLSLLVNLGIVEARAYDQEEAFEAAVIFAKTEGIVPAPESAHAIAAAIDEARKCRetGEEKVILF 399
|
410 420
....*....|....*....|
gi 13878841 405 SFSGHGLLDLGNYAEALHFE 424
Cdd:TIGR01415 400 NLSGHGLLDLKAYAKYLHGE 419
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
1-423 |
0e+00 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 682.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 1 MIRIDLKQDEMPDHWYNILPDLPEELPTPRD-ETGE--AFDTLKKAVPAKVLEYEFSGERYPKIPDEILERYmQVGRPTP 77
Cdd:PRK12391 1 QTKILLDEDEIPTQWYNILADLPEPLPPPLDpGTGEpvTPEDLAPIFPMELIEQEVSTERYIDIPEEVREIY-RLWRPTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 78 IIRAKKLEELLGGNLKIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVR 157
Cdd:PRK12391 80 LIRARRLEKALGTPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACALFGLECTVFMVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 158 TSFYAKPYRKYMMYMYGAHPHPSPSEFTEYGREVLKRMPDTPGSLGLAISEAIHYALDNGG-KYIAGSVINSDILFKTIA 236
Cdd:PRK12391 160 VSYEQKPYRRSLMETYGAEVIPSPSDLTEAGRKILAEDPDHPGSLGIAISEAVEDAAKRPDtKYALGSVLNHVLLHQTVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 237 GMEAKKQMEMAGEDPDYIVGVVGGGSNYAALAFPFLADELsSGKIRRTYIASGSKEVPKMTEGEYRYDYPDTGKVLPLLK 316
Cdd:PRK12391 240 GLEAKKQLELAGEYPDVVIGCVGGGSNFAGLAFPFLGDKL-EGKKDTRFIAVEPAACPTLTKGEYAYDFGDTAGLTPLLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 317 MYTIGYDFIPPAVYAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKNR 396
Cdd:PRK12391 319 MYTLGHDFVPPPIHAGGLRYHGMAPLVSLLVHEGLIEARAYPQTEVFEAAVLFARTEGIVPAPESSHAIAAAIDEALKAK 398
|
410 420
....*....|....*....|....*....
gi 13878841 397 --GEKKTVLVSFSGHGLLDLGNYAEALHF 423
Cdd:PRK12391 399 eeGEEKVILFNLSGHGLLDLAAYDAYLAG 427
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
1-421 |
0e+00 |
|
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport and metabolism]; Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440961 Cd Length: 433 Bit Score: 556.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 1 MIRIDLKQDEMPDHWYNILPDLPEELPTPRD-ETGE--AFDTLKKAVPAKVLEYEFSGERYPKIPDEILERYmQVGRPTP 77
Cdd:COG1350 2 QTKILLDESEIPTQWYNILADLPEPLPPPLHpGTGEpvTPEDLAPIFPMELIEQEMSTERWIEIPEEVREIY-RLWRPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 78 IIRAKKLEELLGGNLKIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVR 157
Cdd:COG1350 81 LYRARRLEKALGTPAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALSFACALFGLECTVYMVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 158 TSFYAKPYRKYMMYMYGAHPHPSPSEFTEYGREVLKRMPDTPGSLGLAISEAIHYALDNGG-KYIAGSVINSDILFKTIA 236
Cdd:COG1350 161 VSYEQKPYRRSMMETYGAEVIPSPSDLTEAGRKILAEDPDTPGSLGIAISEAVEDAATRDDtKYALGSVLNHVLLHQTVI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 237 GMEAKKQMEMAGEDPDYIVGVVGGGSNYAALAFPFLADELsSGKIRRTYIASGSKEVPKMTEGEYRYDYPDTGKVLPLLK 316
Cdd:COG1350 241 GLEAKKQLEKAGEYPDVVIGCAGGGSNFAGLAFPFLRDKL-RGKKDVRFIAVEPAACPTLTRGVYAYDFGDTAGLTPLLK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 317 MYTIGYDFIPPAVYAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHAL--PILKEIADK 394
Cdd:COG1350 320 MYTLGHDFIPPPIHAGGLRYHGMAPLVSQLYHDGLIEAVAYPQLEVFEAGVLFARTEGIVPAPESAHAIkaAIDEALKCK 399
|
410 420
....*....|....*....|....*..
gi 13878841 395 NRGEKKTVLVSFSGHGLLDLGNYAEAL 421
Cdd:COG1350 400 EEGEEKTILFNLSGHGHFDLAAYDAYL 426
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
45-417 |
3.12e-169 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 478.57 E-value: 3.12e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 45 PAKVLEYEFSGERY-PKIPDEILERYMQ-VGRPTPIIRAKKLEELLGGNlKIFLKMESYTYSGSHKINSALAHVFFAREE 122
Cdd:cd06446 2 ALEELEQEFSKERYdPDFPEELRELYKDyVGRPTPLYRAKRLSEYLGGA-KIYLKREDLNHTGAHKINNALGQALLAKRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 123 GAKFVSTETGAGQWGSAVALASALFHMESHIFMVRTSFYAKPYRKYMMYMYGAHPHPSPSEFteygrevlkrmpdtpGSL 202
Cdd:cd06446 81 GKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGS---------------GTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 203 GLAISEAIHYALDN--GGKYIAGSVI------NSDILFKTIAGMEAKKQM-EMAGEDPDYIVGVVGGGSNYAALAFPFLA 273
Cdd:cd06446 146 KDAISEAIRDWVTNveDTHYLLGSVVgphpypNMVRDFQSVIGEEAKKQIlEKEGELPDVVIACVGGGSNAAGLFYPFIN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 274 DElssgkiRRTYIASGSKEVPKMTEGEYRYDYPDTGKVLPLLKMYTIG---YDFIPPAVYAGGLRYHAVAPTLSLLMNKG 350
Cdd:cd06446 226 DK------DVKLIGVEAGGCGLETGGHAAYLFGGTAGVLHGLKMYTLQdedGQIVPPHSISAGLDYPGVGPEHAYLKDSG 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13878841 351 IVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKnRGEKKTVLVSFSGHGLLDLGNY 417
Cdd:cd06446 300 RVEYVAVTDEEALEAFKLLARTEGIIPALESSHAIAYAIKLAKK-LGKEKVIVVNLSGRGDKDLQTV 365
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
22-424 |
4.52e-49 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 176.15 E-value: 4.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 22 LPEELPTPRDETGEAFdtlKKAVPAKVLEYEFSgerypkipdEILERYmqVGRPTPIIRAKKLEELLGGnlKIFLKMESY 101
Cdd:PRK13803 232 VPETLMANLQELQESY---TKIIKSNEFQKTFK---------RLLQNY--AGRPTPLTEAKRLSDIYGA--RIYLKREDL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 102 TYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVRTSFYAKPYRKYMMYMYGAHPHPSP 181
Cdd:PRK13803 296 NHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIPVL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 182 SefteyGREVLKRmpdtpgslglAISEAIHY--ALDNGGKYIAGSVINSD------ILFKTIAGMEAKKQM-EMAGEDPD 252
Cdd:PRK13803 376 S-----GSKTLKD----------AVNEAIRDwvASVPDTHYLIGSAVGPHpypemvAYFQSVIGEEAKEQLkEQTGKLPD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 253 YIVGVVGGGSNYAALAFPFLADEL-------SSGKIRRT--YIASGSKEVPKMTEGEYRYDYPDT-GKVLPllkMYTIgy 322
Cdd:PRK13803 441 AIIACVGGGSNAIGIFYHFLDDPSvkligveAGGKGVNTgeHAATIKKGRKGVLHGSMTYLMQDEnGQILE---PHSI-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 323 dfippavyAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKNRgEKKTV 402
Cdd:PRK13803 516 --------SAGLDYPGIGPMHANLFETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFK-KKDIV 586
|
410 420
....*....|....*....|..
gi 13878841 403 LVSFSGHGLLDLGNYAEalHFE 424
Cdd:PRK13803 587 IVNLSGRGDKDIPTLKE--YFE 606
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
22-423 |
1.61e-45 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 161.96 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 22 LPEELPTPRDETGEAFDTLKKAVpakvleyEFSGERypkipDEILERYmqVGRPTPIIRAKKLEELLGGnLKIFLKMESY 101
Cdd:PRK13028 23 VPPELKPALDELEAAYEEIKKDP-------DFIAEL-----RYLLKHY--VGRPTPLYHAKRLSEELGG-AQIYLKREDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 102 TYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFM----VRtsfyakpyRKYM----MYMY 173
Cdd:PRK13028 88 NHTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMgevdIE--------RQHPnvfrMKLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 174 GAHPHPSPSefteyGREVLKRmpdtpgslglAISEAI----------HYALdnggkyiaGSVINSDIL------FKTIAG 237
Cdd:PRK13028 160 GAEVVPVTR-----GGRTLKE----------AVDSAFedylkdpdntHYAI--------GSVVGPHPFpmmvrdFQSVIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 238 MEAKKQM-EMAGEDPDYIVGVVGGGSNYAALAFPFLADE-------------LSSGKirrtYIASGSKEVPKMTEGEYRY 303
Cdd:PRK13028 217 EEAREQFlEMTGRLPDAVVACVGGGSNAIGLFSAFLDDEsvrlvgvepagrgLDLGE----HAATLTLGKPGVIHGFKSY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 304 ---DypDTGKVLPllkMYTIgydfippavyAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPE 380
Cdd:PRK13028 293 vlqD--EDGEPAP---VHSI----------AAGLDYPGVGPEHAYLKDIGRVEYVTATDEEALDAFFLLSRTEGIIPALE 357
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 13878841 381 TSHALPILKEIAdKNRGEKKTVLVSFSGHGLLDLGNYAEALHF 423
Cdd:PRK13028 358 SSHAVAYAIKLA-PELSKDETILVNLSGRGDKDIDYVAEMLGL 399
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
22-421 |
2.09e-45 |
|
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. the beta chain contains the functional domain for or the synthesis of tryptophan from indole and serine. The enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-P attachment site is contained within the conserved region [LIVM]-x-H-x-G-[STA]-H-K-x-N] [K is the pyridoxal-P attachment site] which is present between residues 90-100 of the model. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 272987 Cd Length: 385 Bit Score: 161.38 E-value: 2.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 22 LPEELPTPRDETGEAFDTLKKAvPAKVLEYefsgerypkipDEILERYmqVGRPTPIIRAKKLEELLGGNlKIFLKMESY 101
Cdd:TIGR00263 11 VPETLMPALEELEAAFEDAKAD-PAFWAEL-----------NELLRNY--AGRPTPLTFAPNLTEALGGA-KIYLKREDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 102 TYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVRTSFYAKPYRKYMMYMYGAHPHPSP 181
Cdd:TIGR00263 76 NHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 182 SefteyGREVLKRmpdtpgslglAISEAIHYALDN--GGKYIAGSVINSDIL------FKTIAGMEAKKQM-EMAGEDPD 252
Cdd:TIGR00263 156 S-----GSGTLKD----------AVNEALRDWVTSvdDTHYVLGSAVGPHPFptmvrdFQSVIGEEAKEQIlEQEGRLPD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 253 YIVGVVGGGSNYAALAFPFLADE-------------LSSGKIRRTyIASGSkevPKMTEGEYRYDYPD-TGKVLPllkMY 318
Cdd:TIGR00263 221 AVIACVGGGSNAIGIFYAFIDDPsvqligveagglgIDTHKHAAT-LSKGS---PGVLHGMKTYLLQDeDGQILE---AH 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 319 TIgydfippavyAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKNRgE 398
Cdd:TIGR00263 294 SV----------SAGLDYPGVGPEHAYLHETGRATYEAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLP-K 362
|
410 420
....*....|....*....|...
gi 13878841 399 KKTVLVSFSGHGLLDLGNYAEAL 421
Cdd:TIGR00263 363 DQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
76-409 |
1.57e-44 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 154.98 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 76 TPIIRAKKLEELLGGNlkIFLKMESYTYSGSHKINSALAHVFFAREEG---AKFVSTETGaGQWGSAVALASALFHMESH 152
Cdd:cd00640 1 TPLVRLKRLSKLGGAN--IYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTG-GNTGIALAAAAARLGLKCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 153 IFMVRTsfyAKPYRKYMMYMYGAHPHPSPSEFTEygrevlkrmpdtpgslglAISEAIHYALDNGGKYIAGSVINSD-IL 231
Cdd:cd00640 78 IVMPEG---ASPEKVAQMRALGAEVVLVPGDFDD------------------AIALAKELAEEDPGAYYVNQFDNPAnIA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 232 FKTIAGMEAKKQMEmaGEDPDYIVGVVGGGSNYAALAFPFLADelssgkirrtyiasgskevpkmtegeyrydypdtgkv 311
Cdd:cd00640 137 GQGTIGLEILEQLG--GQKPDAVVVPVGGGGNIAGIARALKEL------------------------------------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 312 LPLLKMYtigydfippavyagglryhAVAPTlsllmnkgivsARDYDQEEAFKWARIFSETEGYIPAPETSHALPILKEI 391
Cdd:cd00640 178 LPNVKVI-------------------GVEPE-----------VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKL 227
|
330
....*....|....*...
gi 13878841 392 ADKNrGEKKTVLVSFSGH 409
Cdd:cd00640 228 AKKL-GKGKTVVVILTGG 244
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
23-424 |
8.74e-44 |
|
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439903 Cd Length: 400 Bit Score: 157.51 E-value: 8.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 23 PEELPTPRDETGEAFDTLKKavpakvlEYEFSGERypkipDEILERYmqVGRPTPIIRAKKLEELLGGnLKIFLKMESYT 102
Cdd:COG0133 23 PETLMPALDELEEAYEKAKN-------DPEFQAEL-----DYLLKDY--VGRPTPLYFAERLSEKLGG-AKIYLKREDLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 103 YSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFM----VRtsfyakpyRKYM----MYMYG 174
Cdd:COG0133 88 HTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMgeedIE--------RQALnvfrMKLLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 175 AHPHPSPSefteyGREVLKrmpDtpgslglAISEAIHYALDNGGK--YIAGSV--------INSDilFKTIAGMEAKKQM 244
Cdd:COG0133 160 AEVVPVTS-----GSRTLK---D-------AVNEALRDWVTNVDDthYLIGSVvgphpypmMVRD--FQSVIGREAREQI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 245 -EMAGEDPDYIVGVVGGGSNYAALAFPFLADE-------------LSSGKirrtYIASGSKEVPKMTEGEYRY---DypD 307
Cdd:COG0133 223 lEKEGRLPDAVVACVGGGSNAIGIFYPFLDDEsvrligveaggkgLETGE----HAATLTKGRPGVLHGARTYllqD--E 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 308 TGKVLPllkMYTIgydfippavyAGGLRYHAVAPTLSLLMNKG---IVSARDydqEEAFKWARIFSETEGYIPAPETSHA 384
Cdd:COG0133 297 DGQILE---THSI----------SAGLDYPGVGPEHAYLKDTGraeYVSVTD---DEALEAFQLLSRTEGIIPALESAHA 360
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 13878841 385 LPILKEIAdKNRGEKKTVLVSFSGHGLLDLGNYAEALHFE 424
Cdd:COG0133 361 LAYALKLA-PELSKDQIIVVNLSGRGDKDVDTVAKYLGLE 399
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
71-408 |
5.55e-43 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 152.46 E-value: 5.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 71 QVGRPTPIIRAKKLEELLGGNlkIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHME 150
Cdd:pfam00291 3 LGIGPTPLVRLPRLSKELGVD--VYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 151 SHIFMVRTsfyAKPYRKYMMYMYGAHPHPSPSEFTEygrevlkrmpdtpgslglAISEAIHYALDNGGKYIAGSVINSDI 230
Cdd:pfam00291 81 VTIVVPED---APPGKLLLMRALGAEVVLVGGDYDE------------------AVAAARELAAEGPGAYYINQYDNPLN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 231 L--FKTIaGMEAKKQMemaGEDPDYIVGVVGGGSNYAALAFPFLAdelSSGKIRRtyIASGSKEVPKMtegeyrYDYPDT 308
Cdd:pfam00291 140 IegYGTI-GLEILEQL---GGDPDAVVVPVGGGGLIAGIARGLKE---LGPDVRV--IGVEPEGAPAL------ARSLAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 309 GKVLPLLKMYTIgydfippavyAGGLRYHAVAPTLSL-LMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALPI 387
Cdd:pfam00291 205 GRPVPVPVADTI----------ADGLGVGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAA 274
|
330 340
....*....|....*....|.
gi 13878841 388 LKEIADKNRGEKKTVLVSFSG 408
Cdd:pfam00291 275 LKLALAGELKGGDRVVVVLTG 295
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
23-424 |
2.03e-42 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 153.68 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 23 PEELPTPRDETGEAFDTLKKavpakvlEYEFSGERypkipDEILERYmqVGRPTPIIRAKKLEELLGGNlKIFLKMESYT 102
Cdd:PRK04346 20 PETLMPALEELEEAYEKAKN-------DPEFQAEL-----DYLLKNY--VGRPTPLYFAERLSEHLGGA-KIYLKREDLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 103 YSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFM----VRtsfyakpyRKYM----MYMYG 174
Cdd:PRK04346 85 HTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMgaedVE--------RQALnvfrMKLLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 175 AHPHPSPSefteyGREVLKrmpDtpgslglAISEAIHYALDNGGK--YIAGSV--------INSDilFKTIAGMEAKKQM 244
Cdd:PRK04346 157 AEVVPVTS-----GSRTLK---D-------AVNEALRDWVTNVEDthYLIGSVagphpyptMVRD--FQSVIGEEAKAQI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 245 -EMAGEDPDYIVGVVGGGSNYAALAFPFLADE-------------LSSGKirrtYIASGSKEVPKMTEGEYRY---DypD 307
Cdd:PRK04346 220 lEKEGRLPDAVVACVGGGSNAIGIFHPFIDDEsvrligveaagkgLETGK----HAATLTKGRPGVLHGAKTYllqD--E 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 308 TGKVLPllkMYTIgydfippavyAGGLRYHAVAPTLSLLMNKG---IVSARDydqEEAFKWARIFSETEGYIPAPETSHA 384
Cdd:PRK04346 294 DGQILE---THSI----------SAGLDYPGVGPEHAYLKDIGraeYVSITD---DEALEAFQLLSRLEGIIPALESSHA 357
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 13878841 385 LPILKEIAdKNRGEKKTVLVSFSGHGLLDLGNYAEALHFE 424
Cdd:PRK04346 358 LAYALKLA-PTLGKDQIIVVNLSGRGDKDVFTVAKLLGVI 396
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
63-424 |
1.25e-33 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 130.26 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 63 DEILERYmqVGRPTPIIRAKKLEELL----GGNLKIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGS 138
Cdd:PLN02618 56 AGILKDY--VGRETPLYFAERLTEHYkradGEGPEIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 139 AVALASALFHMESHIFMVRTSFYAKPYRKYMMYMYGAHPHPSPSefteygrevlkrmpdTPGSLGLAISEAIHYALDN-- 216
Cdd:PLN02618 134 ATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEVRPVHS---------------GTATLKDATSEAIRDWVTNve 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 217 GGKYIAGSVINSDIL------FKTIAGMEAKKQ-MEMAGEDPDYIVGVVGGGSNYAALAFPFLADE-------------L 276
Cdd:PLN02618 199 TTHYILGSVAGPHPYpmmvrdFHSVIGKETRRQaMEKWGGKPDVLVACVGGGSNAMGLFHEFIDDEdvrligveaagfgL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 277 SSGKirrtYIASGSKEVPKMTEGEYRYDYPDT-GKVlpllkmytigydfIPPAVYAGGLRYHAVAPTLSLLMNKGIVSAR 355
Cdd:PLN02618 279 DSGK----HAATLTKGEVGVLHGAMSYLLQDEdGQI-------------IEPHSISAGLDYPGVGPEHSFLKDTGRAEYY 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13878841 356 DYDQEEAFKWARIFSETEGYIPAPETSHALPILKEIADKNRGEKKtVLVSFSGHGLLDLGNYAEALHFE 424
Cdd:PLN02618 342 SVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTK-VVVNCSGRGDKDVNTAIKYLQVS 409
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
22-414 |
2.07e-32 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 129.76 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 22 LPEELPTPRDETGEAFDTlKKAVPAKVLEYEFSGERYpkipdeilerymqVGRPTPIIRAKKLEELL----GGNLKIFLK 97
Cdd:PRK13802 287 VPEALITALDELERVYTQ-AKADPEFHKELATLNQRY-------------VGRPSPLTEAPRFAERVkektGLDARVFLK 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 98 MESYTYSGSHKINSALAHVFFAREEGAKFVSTETGAGQWGSAVALASALFHMESHIFMVRTSFYAKPYRKYMMYMYGAhp 177
Cdd:PRK13802 353 REDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGA-- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 178 hpspsEFTE--YGREVLKRmpdtpgslglAISEAIHYALDN--GGKYIAGSVINSDIL------FKTIAGMEAKKQM-EM 246
Cdd:PRK13802 431 -----EVVEvtLGDRILKD----------AINEALRDWVTNvkDTHYLLGTVAGPHPFpamvrdFQKIIGEEAKQQLqDW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 247 AGED-PDYIVGVVGGGSNYAALAFPFLADEL-------------SSGK--IRrtyIASGSKEVpKMTEGEYRYDYP-DTG 309
Cdd:PRK13802 496 YGIDhPDAICACVGGGSNAIGVMNAFLDDERvnlygyeaggngpESGKhaIR---FAPGTGEL-GMFQGAKSYLLEnDEG 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 310 KVlplLKMYTIgydfippavyAGGLRYHAVAPTLSLLMNKGIVSARDYDQEEAFKWARIFSETEGYIPAPETSHALP-IL 388
Cdd:PRK13802 572 QT---LDTYSI----------SAGLDYASVGPEHAWLKDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAgAY 638
|
410 420
....*....|....*....|....*...
gi 13878841 389 KEIAD-KNRG-EKKTVLVSFSGHGLLDL 414
Cdd:PRK13802 639 KAAADlKAKGyEHPVMIVNISGRGDKDM 666
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
76-404 |
4.11e-16 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 78.59 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 76 TPIIRAKKLEELLGGNlKIFLKMESYTYSGSHKINSALAHVFFAREEGAKFVSTETgAGQWGSAVALASALFHMESHIFM 155
Cdd:PRK06381 16 TPLLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGT-CGNYGASIAYFARLYGLKAVIFI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 156 VRtsfyakpyrkymmymygAHPHPSPSEFTEYGREVLKrmpdTPGSLGLAISEAIHYALDNgGKYIA--GSViNSDILFK 233
Cdd:PRK06381 94 PR-----------------SYSNSRVKEMEKYGAEIIY----VDGKYEEAVERSRKFAKEN-GIYDAnpGSV-NSVVDIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 234 TIAGMeAKKQMEMAGEDPDYIVGVVGGGSNYAALAFPFladelssgkiRRTYIASGSKEVPKMTEGEyrydypdTGKVLP 313
Cdd:PRK06381 151 AYSAI-AYEIYEALGDVPDAVAVPVGNGTTLAGIYHGF----------RRLYDRGKTSRMPRMIGVS-------TSGGNQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 314 LLKMYTIGYDFIPPavyaggLRYHAVAPTlslLMNKGIVSARDYD-------------------QEEAFKWARIFSETEG 374
Cdd:PRK06381 213 IVESFKRGSSEVVD------LEVDEIRET---AVNEPLVSYRSFDgdnaleaiydshgyafgfsDDEMVKYAELLRRMEG 283
|
330 340 350
....*....|....*....|....*....|
gi 13878841 375 YIPAPETSHALPILKEIADKNRGEKKTVLV 404
Cdd:PRK06381 284 LNALPASASALAALVKYLKKNGVNDNVVAV 313
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
12-421 |
3.85e-09 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 57.90 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 12 PDHWYNILPD----LPEELPTPRDETGEAFDTLKkavpakvleyefsgeRYPKI--PDEILERY-MQVGrPTPIIRAKKL 84
Cdd:COG0498 12 SDALLYLCPDcgglLPDSYPALSREDLASRRGLW---------------RYRELlpFDDEEKAVsLGEG-GTPLVKAPRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 85 EELLGGNLkiFLKMESYTYSGSHK-INSALAhVFFAREEGAKFV---STETGAgqwgSAVALASALFHMESHIFMvrtsf 160
Cdd:COG0498 76 ADELGKNL--YVKEEGHNPTGSFKdRAMQVA-VSLALERGAKTIvcaSSGNGS----AALAAYAARAGIEVFVFV----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 161 yakPYRK------YMMYMYGAHPHPSPSEFTEYGREVLKRMpdtpGSLGLAISEAIHYAldnggkYIAGSvinsdilfKT 234
Cdd:COG0498 144 ---PEGKvspgqlAQMLTYGAHVIAVDGNFDDAQRLVKELA----ADEGLYAVNSINPA------RLEGQ--------KT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 235 IAgMEAkkqMEMAGEDPDYIVGVVGGGSNYAALafpfladelssGKIRRTYIASG-SKEVPKMT----EGEyrydypdtg 309
Cdd:COG0498 203 YA-FEI---AEQLGRVPDWVVVPTGNGGNILAG-----------YKAFKELKELGlIDRLPRLIavqaTGC--------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 310 kvLPLLKMYTIG---YDFIPPAVYAGGLR----------YHAVAPTlsllmNKGIVSARDydqEEAFKWARIFSETEGYI 376
Cdd:COG0498 259 --NPILTAFETGrdeYEPERPETIAPSMDignpsngeraLFALRES-----GGTAVAVSD---EEILEAIRLLARREGIF 328
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 13878841 377 PAPETSHALPILKEIADKNRGEK--KTVLVSfSGHGLLDLGNYAEAL 421
Cdd:COG0498 329 VEPATAVAVAGLRKLREEGEIDPdePVVVLS-TGHGLKFPDAVREAL 374
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
74-268 |
6.68e-09 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 56.73 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 74 RPTPIIRAKKLEELLGGNlkIFLKMESYTYSGSHKINSALAHVF-FAREEGAKFVSTETgAGQWGSAVALASALFHMESH 152
Cdd:cd01562 16 RRTPLLTSPTLSELLGAE--VYLKCENLQKTGSFKIRGAYNKLLsLSEEERAKGVVAAS-AGNHAQGVAYAAKLLGIPAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 153 IFMVRTsfyAKPYRKYMMYMYGAhphpspsEFTEYGRevlkrmpdtpgSLGLAISEAIHYALDNGGKYIAGsvinsdilF 232
Cdd:cd01562 93 IVMPET---APAAKVDATRAYGA-------EVVLYGE-----------DFDEAEAKARELAEEEGLTFIHP--------F 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13878841 233 ---KTIAG-----MEAKKQMemagEDPDYIVGVVGGGSNYAALA 268
Cdd:cd01562 144 ddpDVIAGqgtigLEILEQV----PDLDAVFVPVGGGGLIAGIA 183
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
67-261 |
1.49e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 55.93 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 67 ERYMQVGRPTPIIRAKKLEELLGGnlKIFLKMESYTYSGSHKINSALAHVFFAREEG---AKFVSTETgaGQWGSAVALA 143
Cdd:PRK06608 15 NRIKQYLHLTPIVHSESLNEMLGH--EIFFKVESLQKTGAFKVRGVLNHLLELKEQGklpDKIVAYST--GNHGQAVAYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 144 SALFHMESHIFMvrtSFYAKPYRKYMMYMYGAHphpspSEFTEYGREVlkrmpdtpgslglaiSEAIHYALDNGGKYIAG 223
Cdd:PRK06608 91 SKLFGIKTRIYL---PLNTSKVKQQAALYYGGE-----VILTNTRQEA---------------EEKAKEDEEQGFYYIHP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13878841 224 SviNSDilfKTIAG-----MEAKKQMemaGEDPDYIVGVVGGG 261
Cdd:PRK06608 148 S--DSD---STIAGagtlcYEALQQL---GFSPDAIFASCGGG 182
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
76-374 |
1.63e-07 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 52.52 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 76 TPIIRAKKLEELLGGNlkIFLKMESYTYSGSHKINSALAHVFFAREEGA-KFVST--ETGAGQWGSAVALASALFHMESH 152
Cdd:cd01561 3 TPLVRLNRLSPGTGAE--IYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlKPGTTiiEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 153 IFMVRTsfyAKPYRKYMMYMYGAHPHPSPsefteygrevlkrmPDTPGSLGLAISEAIHYALDNGGKYIA---GSVINSD 229
Cdd:cd01561 81 IVMPET---MSEEKRKLLRALGAEVILTP--------------EAEADGMKGAIAKARELAAETPNAFWLnqfENPANPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 230 ILFKTIaGMEAKKQMemaGEDPDYIVGVVGGGSNYAALA------FP----FLADELSSGkirrtyIASGSKEVPKMTEG 299
Cdd:cd01561 144 AHYETT-APEIWEQL---DGKVDAFVAGVGTGGTITGVArylkekNPnvriVGVDPVGSV------LFSGGPPGPHKIEG 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13878841 300 eyrydypdtgkvlpllkmytIGYDFIPPavyagglryhavaptlslLMNKGIV-SARDYDQEEAFKWARIFSETEG 374
Cdd:cd01561 214 --------------------IGAGFIPE------------------NLDRSLIdEVVRVSDEEAFAMARRLAREEG 251
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
74-155 |
1.23e-06 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 50.03 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 74 RPTPIIRAKKLEELLGGNlkIFLKMESYTYSGSHKINSALAHVF-FAREEGAKFVSTETgAGQWGSAVALASALFHMESH 152
Cdd:COG1171 23 RRTPLLRSPTLSERLGAE--VYLKLENLQPTGSFKLRGAYNALAsLSEEERARGVVAAS-AGNHAQGVAYAARLLGIPAT 99
|
...
gi 13878841 153 IFM 155
Cdd:COG1171 100 IVM 102
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
60-261 |
1.30e-05 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 46.61 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 60 KIPDEILERYMQVG---RPTPIIRAKKLEELLGGNlkIFLKMESYTYSGSHKINSALAHVFF----AREEGAKFVSTetg 132
Cdd:PRK06815 2 TLFDAILEAHQRLRpqvRVTPLEHSPLLSQHTGCE--VYLKCEHLQHTGSFKFRGASNKLRLlneaQRQQGVITASS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 133 aGQWGSAVALASALFHMESHIFmvrTSFYAKPYRKYMMYMYGAhphpspsEFTEYGREVLKrmpdtpgslglAISEAIHY 212
Cdd:PRK06815 77 -GNHGQGVALAAKLAGIPVTVY---APEQASAIKLDAIRALGA-------EVRLYGGDALN-----------AELAARRA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13878841 213 ALDNGGKYIagSVINSdilFKTIAG-----MEAKKQMemagEDPDYIVGVVGGG 261
Cdd:PRK06815 135 AEQQGKVYI--SPYND---PQVIAGqgtigMELVEQQ----PDLDAVFVAVGGG 179
|
|
| PLN02970 |
PLN02970 |
serine racemase |
76-159 |
2.06e-03 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 40.05 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13878841 76 TPIIRAKKLEELLGgnLKIFLKMESYTYSGSHKINSALAHVFFAREEGAKF-VSTETgAGQWGSAVALASALFHMESHIF 154
Cdd:PLN02970 28 TPVLTSSSLDALAG--RSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKgVVTHS-SGNHAAALALAAKLRGIPAYIV 104
|
....*
gi 13878841 155 MVRTS 159
Cdd:PLN02970 105 VPKNA 109
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
60-124 |
2.67e-03 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 39.65 E-value: 2.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13878841 60 KIPDEILERymqVGRpTPIIRAKKLEELLGGNlkIFLKMESYTYSGSHKINSALAHVFFAREEGA 124
Cdd:COG0031 2 RIYDSILEL---IGN-TPLVRLNRLSPGPGAE--IYAKLESFNPGGSVKDRIALSMIEDAEKRGL 60
|
|
| |
