|
Name |
Accession |
Description |
Interval |
E-value |
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
4-395 |
0e+00 |
|
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: 731.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 4 ENQQGYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLN 83
Cdd:COG0133 8 PDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLGGAKIYLKREDLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 84 HTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSS 163
Cdd:COG0133 88 HTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAEVVPVTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 164 GTATLKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMF 243
Cdd:COG0133 168 GSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGSNAIGIF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 244 YGFIQDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGR 323
Cdd:COG0133 248 YPFLDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDTGR 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523630390 324 VSYVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEVSRLRKGE 395
Cdd:COG0133 328 AEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGLE 399
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
5-396 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 727.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 5 NQQGYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLNH 84
Cdd:PRK04346 6 DENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLGGAKIYLKREDLNH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 85 TGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSSG 164
Cdd:PRK04346 86 TGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVVPVTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 165 TATLKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMFY 244
Cdd:PRK04346 166 SRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNAIGIFH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 245 GFIQDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGRV 324
Cdd:PRK04346 246 PFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDIGRA 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523630390 325 SYVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEVSRLRKGEF 396
Cdd:PRK04346 326 EYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLLGVIL 397
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
25-388 |
0e+00 |
|
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: 626.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 25 ALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLNHTGAHKINNTIGQVLIAKAMG 104
Cdd:cd06446 2 ALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLGGAKIYLKREDLNHTGAHKINNALGQALLAKRMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 105 KTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSSGTATLKDATSEAMRDWALNVS 184
Cdd:cd06446 82 KKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 185 NTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMFYGFIQDKKVKLFGIEAGGYSS 264
Cdd:cd06446 162 DTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 265 NPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGRVSYVSVDDEGALDAFIEVCRI 344
Cdd:cd06446 242 ETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLART 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 523630390 345 EGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEV 388
Cdd:cd06446 322 EGIIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
8-391 |
0e+00 |
|
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: 591.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 8 GYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLNHTGA 87
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGGAKIYLKREDLNHTGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 88 HKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSSGTAT 167
Cdd:TIGR00263 81 HKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 168 LKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMFYGFI 247
Cdd:TIGR00263 161 LKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 248 QDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGRVSYV 327
Cdd:TIGR00263 241 DDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATYE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523630390 328 SVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEVSRL 391
Cdd:TIGR00263 321 AITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKY 384
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
56-379 |
1.11e-34 |
|
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: 129.74 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 56 RPSPLTYAERLSKVWGGaKIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVY 135
Cdd:pfam00291 6 GPTPLVRLPRLSKELGV-DVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 136 MGEEDLRRqelNAIRMRMLGAKVVGVSSGTATLKDATSEAMRDWalnvSNTHYIVGSSigpHPFptiVRDFQSVIGIESR 215
Cdd:pfam00291 85 VPEDAPPG---KLLLMRALGAEVVLVGGDYDEAVAAARELAAEG----PGAYYINQYD---NPL---NIEGYGTIGLEIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 216 KQFkkinDKLPNAVIACVGGGSNAIGMFYGFIQDK-KVKLFGIEAGGYSSNPGSHSAtiqfGRTGFLHGTKTLviqddfg 294
Cdd:pfam00291 152 EQL----GGDPDAVVVPVGGGGLIAGIARGLKELGpDVRVIGVEPEGAPALARSLAA----GRPVPVPVADTI------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 295 qivpAHSVSAGlDYPGVGPEHAYFHKSGRVsyVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKD-LAKSMSKKENI 373
Cdd:pfam00291 217 ----ADGLGVG-DEPGALALDLLDEYVGEV--VTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLaLAGELKGGDRV 289
|
....*.
gi 523630390 374 LICLSG 379
Cdd:pfam00291 290 VVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
4-395 |
0e+00 |
|
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: 731.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 4 ENQQGYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLN 83
Cdd:COG0133 8 PDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLGGAKIYLKREDLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 84 HTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSS 163
Cdd:COG0133 88 HTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAEVVPVTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 164 GTATLKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMF 243
Cdd:COG0133 168 GSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGSNAIGIF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 244 YGFIQDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGR 323
Cdd:COG0133 248 YPFLDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDTGR 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523630390 324 VSYVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEVSRLRKGE 395
Cdd:COG0133 328 AEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGLE 399
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
5-396 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 727.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 5 NQQGYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLNH 84
Cdd:PRK04346 6 DENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLGGAKIYLKREDLNH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 85 TGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSSG 164
Cdd:PRK04346 86 TGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVVPVTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 165 TATLKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMFY 244
Cdd:PRK04346 166 SRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNAIGIFH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 245 GFIQDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGRV 324
Cdd:PRK04346 246 PFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLKDIGRA 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523630390 325 SYVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEVSRLRKGEF 396
Cdd:PRK04346 326 EYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLLGVIL 397
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
5-396 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 639.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 5 NQQGYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLNH 84
Cdd:PRK13028 10 DADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEELGGAQIYLKREDLNH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 85 TGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSSG 164
Cdd:PRK13028 90 TGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLGAEVVPVTRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 165 TATLKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMFY 244
Cdd:PRK13028 170 GRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNAIGLFS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 245 GFIQDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGRV 324
Cdd:PRK13028 250 AFLDDESVRLVGVEPAGRGLDLGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPEHAYLKDIGRV 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523630390 325 SYVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEVSR-LRKGEF 396
Cdd:PRK13028 330 EYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAPELSKDETILVNLSGRGDKDIDYVAEmLGLGET 402
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
25-388 |
0e+00 |
|
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: 626.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 25 ALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLNHTGAHKINNTIGQVLIAKAMG 104
Cdd:cd06446 2 ALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLGGAKIYLKREDLNHTGAHKINNALGQALLAKRMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 105 KTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSSGTATLKDATSEAMRDWALNVS 184
Cdd:cd06446 82 KKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 185 NTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMFYGFIQDKKVKLFGIEAGGYSS 264
Cdd:cd06446 162 DTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 265 NPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGRVSYVSVDDEGALDAFIEVCRI 344
Cdd:cd06446 242 ETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLART 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 523630390 345 EGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEV 388
Cdd:cd06446 322 EGIIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
8-391 |
0e+00 |
|
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: 591.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 8 GYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVWGGAKIWLKREDLNHTGA 87
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGGAKIYLKREDLNHTGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 88 HKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSSGTAT 167
Cdd:TIGR00263 81 HKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 168 LKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMFYGFI 247
Cdd:TIGR00263 161 LKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 248 QDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGRVSYV 327
Cdd:TIGR00263 241 DDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATYE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523630390 328 SVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEVSRL 391
Cdd:TIGR00263 321 AITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKY 384
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
5-386 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 570.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 5 NQQGYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVwGGAKIWLKREDLNH 84
Cdd:PRK13803 219 DPAGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSDI-YGARIYLKREDLNH 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 85 TGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVSSG 164
Cdd:PRK13803 298 TGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIPVLSG 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 165 TATLKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGMFY 244
Cdd:PRK13803 378 SKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIGIFY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 245 GFIQDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSGRV 324
Cdd:PRK13803 458 HFLDDPSVKLIGVEAGGKGVNTGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANLFETGRA 537
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523630390 325 SYVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVA 386
Cdd:PRK13803 538 IYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKDIVIVNLSGRGDKDIP 599
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
8-395 |
3.73e-180 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 506.98 E-value: 3.73e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 8 GYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLTYAERLSKVW-----GGAKIWLKREDL 82
Cdd:PLN02618 17 GRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEHYkradgEGPEIYLKREDL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 83 NHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKVVGVS 162
Cdd:PLN02618 97 NHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEVRPVH 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 163 SGTATLKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKKINDKLPNAVIACVGGGSNAIGM 242
Cdd:PLN02618 177 SGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSNAMGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 243 FYGFIQDKKVKLFGIEAGGYSSNPGSHSATIQFGRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGVGPEHAYFHKSG 322
Cdd:PLN02618 257 FHEFIDDEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYPGVGPEHSFLKDTG 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523630390 323 RVSYVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKENILICLSGRGDKDVAEVSRLRKGE 395
Cdd:PLN02618 337 RAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNTAIKYLQVS 409
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
4-390 |
1.50e-149 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 439.46 E-value: 1.50e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 4 ENQQGYFGEFGGRYSPEILHDALVELETTYKKLKKNKHFKKELEYYRKNYIGRPSPLT----YAERLSKVWG-GAKIWLK 78
Cdd:PRK13802 273 EHQGPYWGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTeaprFAERVKEKTGlDARVFLK 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 79 REDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGEEDLRRQELNAIRMRMLGAKV 158
Cdd:PRK13802 353 REDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGAEV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 159 VGVSSGTATLKDATSEAMRDWALNVSNTHYIVGSSIGPHPFPTIVRDFQSVIGIESRKQFKK---INDklPNAVIACVGG 235
Cdd:PRK13802 433 VEVTLGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDwygIDH--PDAICACVGG 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 236 GSNAIGMFYGFIQDKKVKLFGIEAGGYSSNPGSHSatIQF----GRTGFLHGTKTLVIQDDFGQIVPAHSVSAGLDYPGV 311
Cdd:PRK13802 511 GSNAIGVMNAFLDDERVNLYGYEAGGNGPESGKHA--IRFapgtGELGMFQGAKSYLLENDEGQTLDTYSISAGLDYASV 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 312 GPEHAYFHKSGRVSYVSVDDEGALDAFIEVCRIEGIIPALETAH----AFRYAKDLAKSMSKKENILICLSGRGDKDVAE 387
Cdd:PRK13802 589 GPEHAWLKDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHavagAYKAAADLKAKGYEHPVMIVNISGRGDKDMNT 668
|
...
gi 523630390 388 VSR 390
Cdd:PRK13802 669 AGK 671
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
46-381 |
2.51e-60 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 201.17 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 46 LEYYRknyIGRPSPLTYAERLSKVWG-GAKIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATV 124
Cdd:PRK12391 69 REIYR---LWRPTPLIRARRLEKALGtPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 125 GAMFQMKTVVYM-----GEEDLRRqelnaIRMRMLGAKVVGVSS-----GTATLKD----------ATSEAMRDwALNVS 184
Cdd:PRK12391 146 CALFGLECTVFMvrvsyEQKPYRR-----SLMETYGAEVIPSPSdlteaGRKILAEdpdhpgslgiAISEAVED-AAKRP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 185 NTHYIVGSSIgPHpfptiVRDFQSVIGIESRKQFKKINDKlPNAVIACVGGGSNAIGMFYGFIQDK-----KVKLFGIEA 259
Cdd:PRK12391 220 DTKYALGSVL-NH-----VLLHQTVIGLEAKKQLELAGEY-PDVVIGCVGGGSNFAGLAFPFLGDKlegkkDTRFIAVEP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 260 ggySSNPgshSAT-----IQFGRT-GFLHGTKTLVIQDDFgqiVPAHSVSAGLDYPGVGPEHAYFHKSGRVSYVSVDDEG 333
Cdd:PRK12391 293 ---AACP---TLTkgeyaYDFGDTaGLTPLLKMYTLGHDF---VPPPIHAGGLRYHGMAPLVSLLVHEGLIEARAYPQTE 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 523630390 334 ALDAFIEVCRIEGIIPALETAHAFRYAKDLA---KSMSKKENILICLSGRG 381
Cdd:PRK12391 364 VFEAAVLFARTEGIVPAPESSHAIAAAIDEAlkaKEEGEEKVILFNLSGHG 414
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
58-380 |
1.92e-59 |
|
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: 193.12 E-value: 1.92e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 58 SPLTYAERLSKvWGGAKIWLKREDLNHTGAHKINNTIGQVLIAKAMG---KTRIIAETGaGQHGVATATVGAMFQMKTVV 134
Cdd:cd00640 1 TPLVRLKRLSK-LGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTG-GNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 135 YMGEEDlrrQELNAIRMRMLGAKVVGVssgTATLKDATSEAMRDWAlNVSNTHYIvgssigpHPF-PTIVRDFQSVIGIE 213
Cdd:cd00640 79 VMPEGA---SPEKVAQMRALGAEVVLV---PGDFDDAIALAKELAE-EDPGAYYV-------NQFdNPANIAGQGTIGLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 214 SRKQFKkinDKLPNAVIACVGGGSNAIGMFYGFIQDK-KVKLFGIEAGgyssnpgshsatiqfgrtgflhgtktlviqdd 292
Cdd:cd00640 145 ILEQLG---GQKPDAVVVPVGGGGNIAGIARALKELLpNVKVIGVEPE-------------------------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 293 fgqivpahsvsagldypgvgpehayfhksgrvsYVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLAKSMSKKEN 372
Cdd:cd00640 190 ---------------------------------VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKT 236
|
....*...
gi 523630390 373 ILICLSGR 380
Cdd:cd00640 237 VVVILTGG 244
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
46-386 |
6.61e-50 |
|
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: 173.78 E-value: 6.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 46 LEYYRknyIGRPSPLTYAERLSKVWGG-AKIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATV 124
Cdd:COG1350 70 REIYR---LWRPSPLYRARRLEKALGTpAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALSFA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 125 GAMFQMKTVVYM-----GEEDLRRqelnaIRMRMLGAKVVGVSS-----GTATLKD----------ATSEAMRDwALNVS 184
Cdd:COG1350 147 CALFGLECTVYMvkvsyEQKPYRR-----SMMETYGAEVIPSPSdlteaGRKILAEdpdtpgslgiAISEAVED-AATRD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 185 NTHYIVGSSIGpHpfptiVRDFQSVIGIESRKQFKKINDKlPNAVIACVGGGSNAIGMFYGFIQDK-----KVKLFGIE- 258
Cdd:COG1350 221 DTKYALGSVLN-H-----VLLHQTVIGLEAKKQLEKAGEY-PDVVIGCAGGGSNFAGLAFPFLRDKlrgkkDVRFIAVEp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 259 -------AGGYssnpgshsaTIQFGRT-GF--LHGTKTLviQDDFgqiVPAHSVSAGLDYPGVGPEHAYFHKSGRVSYVS 328
Cdd:COG1350 294 aacptltRGVY---------AYDFGDTaGLtpLLKMYTL--GHDF---IPPPIHAGGLRYHGMAPLVSQLYHDGLIEAVA 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523630390 329 VDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLA---KSMSKKENILICLSGRGDKDVA 386
Cdd:COG1350 360 YPQLEVFEAGVLFARTEGIVPAPESAHAIKAAIDEAlkcKEEGEEKTILFNLSGHGHFDLA 420
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
56-379 |
1.11e-34 |
|
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: 129.74 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 56 RPSPLTYAERLSKVWGGaKIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVY 135
Cdd:pfam00291 6 GPTPLVRLPRLSKELGV-DVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 136 MGEEDLRRqelNAIRMRMLGAKVVGVSSGTATLKDATSEAMRDWalnvSNTHYIVGSSigpHPFptiVRDFQSVIGIESR 215
Cdd:pfam00291 85 VPEDAPPG---KLLLMRALGAEVVLVGGDYDEAVAAARELAAEG----PGAYYINQYD---NPL---NIEGYGTIGLEIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 216 KQFkkinDKLPNAVIACVGGGSNAIGMFYGFIQDK-KVKLFGIEAGGYSSNPGSHSAtiqfGRTGFLHGTKTLviqddfg 294
Cdd:pfam00291 152 EQL----GGDPDAVVVPVGGGGLIAGIARGLKELGpDVRVIGVEPEGAPALARSLAA----GRPVPVPVADTI------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 295 qivpAHSVSAGlDYPGVGPEHAYFHKSGRVsyVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKD-LAKSMSKKENI 373
Cdd:pfam00291 217 ----ADGLGVG-DEPGALALDLLDEYVGEV--VTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLaLAGELKGGDRV 289
|
....*.
gi 523630390 374 LICLSG 379
Cdd:pfam00291 290 VVVLTG 295
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
59-390 |
4.24e-16 |
|
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: 79.09 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 59 PLTYAERLSKVWGGaKIWLKREDLNHTGAHKinnTIG-QVLI--AKAMGKTRII-AETGAGqhGVATATVGAMFQMKTVV 134
Cdd:COG0498 68 PLVKAPRLADELGK-NLYVKEEGHNPTGSFK---DRAmQVAVslALERGAKTIVcASSGNG--SAALAAYAARAGIEVFV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 135 YMGEEDL----RRQelnairMRMLGAKVVGVSSGTATLKDATSEAMRDWALnvsnthYIVGSsIgpHPFptiVRDFQSVI 210
Cdd:COG0498 142 FVPEGKVspgqLAQ------MLTYGAHVIAVDGNFDDAQRLVKELAADEGL------YAVNS-I--NPA---RLEGQKTY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 211 GIESRKQFkkinDKLPNAVIACVGGGSNAIGMFYGF-------IQDKKVKLFGIEAGGysSNPgshsatiqfgrtgFLHG 283
Cdd:COG0498 204 AFEIAEQL----GRVPDWVVVPTGNGGNILAGYKAFkelkelgLIDRLPRLIAVQATG--CNP-------------ILTA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 284 TKTlviQDDFGQIVPAHSVSAGLDYPG-VGPEHAYFH--KSGRVSyVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYA 360
Cdd:COG0498 265 FET---GRDEYEPERPETIAPSMDIGNpSNGERALFAlrESGGTA-VAVSDEEILEAIRLLARREGIFVEPATAVAVAGL 340
|
330 340 350
....*....|....*....|....*....|..
gi 523630390 361 KDLAKS--MSKKENILICLSGRGDKDVAEVSR 390
Cdd:COG0498 341 RKLREEgeIDPDEPVVVLSTGHGLKFPDAVRE 372
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
59-384 |
3.86e-14 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 72.63 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 59 PLTYAERLSKVWGGAKIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETgAGQHGVATATVGAMFQMKTVVYMGe 138
Cdd:cd01563 24 PLVRAPRLGERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACAS-TGNTSASLAAYAARAGIKCVVFLP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 139 EDLRRQELnaIRMRMLGAKVVGVSSGTATLKDATSEAMRD---WALNVSNTHYIVGssigphpfptivrdfQSVIGIESR 215
Cdd:cd01563 102 AGKALGKL--AQALAYGATVLAVEGNFDDALRLVRELAEEnwiYLSNSLNPYRLEG---------------QKTIAFEIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 216 KQfkkINDKLPNAVIACVGGGSNAIGMFYGF-------IQDKKVKLFGIEAGGYSSnpgshsatiqfgrtgFLHGTKtlV 288
Cdd:cd01563 165 EQ---LGWEVPDYVVVPVGNGGNITAIWKGFkelkelgLIDRLPRMVGVQAEGAAP---------------IVRAFK--E 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 289 IQDDFGQIVPAHSVSAGLD--YPGVGPE--HAYFHKSGRVsyVSVDDEGALDAFIEVCRIEGIIPALETAHAFRYAKDLA 364
Cdd:cd01563 225 GKDDIEPVENPETIATAIRigNPASGPKalRAVRESGGTA--VAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLR 302
|
330 340
....*....|....*....|..
gi 523630390 365 KS--MSKKENILICLSGRGDKD 384
Cdd:cd01563 303 EEgiIDKGERVVVVLTGHGLKD 324
|
|
| Acd |
COG2515 |
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ... |
50-257 |
1.93e-11 |
|
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];
Pssm-ID: 442005 [Multi-domain] Cd Length: 317 Bit Score: 64.43 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 50 RKNYIGRPSPLTYAERLSKvWGGAKIWLKREDLNHTG-----AHKINNTIGQvliAKAMGKTRIIAeTGAGQ--HGVATA 122
Cdd:COG2515 4 RLPLAFLPTPLQPLPRLSA-ALGVELWIKRDDLTGPAiggnkTRKLEYLLAD---ALAQGADTLVT-FGGAQsnHARATA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 123 TVGAMFQMKTVVYM-GEEDLRRQElNAIRMRMLGAKVVGVSSGTATLKDatsEAMRDWALNVSN---THYIV---GSSig 195
Cdd:COG2515 79 AAAAKLGLKCVLVLrGEEPTPLNG-NLLLDRLLGAELHFVSRGEYRDRD---EAMEAVAAELRArggKPYVIpegGSN-- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523630390 196 phpfPTIVRDFQSvIGIESRKQFKKINDKlPNAVIACVGGGSNAIGMFYGF-IQDKKVKLFGI 257
Cdd:COG2515 153 ----PLGALGYVE-AAAELAAQLAELGVD-FDYIVVASGSGGTLAGLVAGLaLLGSDTRVIGI 209
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
56-245 |
4.96e-10 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 60.09 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 56 RPSPLTYAERLSKVwGGAKIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVY 135
Cdd:PRK06815 19 RVTPLEHSPLLSQH-TGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 136 MgEEDLRRQELNAIrmRMLGAKVVGVssGTATLKdaTSEAMRDWALNVSNTHyivgssIGPHPFPTIVRDfQSVIGIESR 215
Cdd:PRK06815 98 A-PEQASAIKLDAI--RALGAEVRLY--GGDALN--AELAARRAAEQQGKVY------ISPYNDPQVIAG-QGTIGMELV 163
|
170 180 190
....*....|....*....|....*....|
gi 523630390 216 KQFKKIndklpNAVIACVGGGsnaiGMFYG 245
Cdd:PRK06815 164 EQQPDL-----DAVFVAVGGG----GLISG 184
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
51-236 |
4.86e-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: 57.11 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 51 KNYIgRPSPLTYAERLSKVWGgAKIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTR-IIAETgAGQHGVATATVGAMFQ 129
Cdd:cd01562 12 KPVV-RRTPLLTSPTLSELLG-AEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAAS-AGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 130 MKTVVYMgEEDLRRQELNAirMRMLGAKVVgvssgtatLKDATSEAMRDWALNVSNTH---YIvgssigpHPF--PTIVR 204
Cdd:cd01562 89 IPATIVM-PETAPAAKVDA--TRAYGAEVV--------LYGEDFDEAEAKARELAEEEgltFI-------HPFddPDVIA 150
|
170 180 190
....*....|....*....|....*....|....
gi 523630390 205 DfQSVIGIEsrkqfkkINDKLPN--AVIACVGGG 236
Cdd:cd01562 151 G-QGTIGLE-------ILEQVPDldAVFVPVGGG 176
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
51-236 |
9.74e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 56.32 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 51 KNYIgRPSPLTYAERLSKvWGGAKIWLKREDLNHTGAHKINNTIGQVLIAKAMGK--TRIIAETgAGQHGVATATVGAMF 128
Cdd:PRK06608 18 KQYL-HLTPIVHSESLNE-MLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TGNHGQAVAYASKLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 129 QMKTVVYMgEEDLRRQELNAIrmRMLGAKVVgvssGTATLKDATSEAMRDwalNVSNTHYIvgssigpHPFptivrDFQS 208
Cdd:PRK06608 95 GIKTRIYL-PLNTSKVKQQAA--LYYGGEVI----LTNTRQEAEEKAKED---EEQGFYYI-------HPS-----DSDS 152
|
170 180 190
....*....|....*....|....*....|....
gi 523630390 209 VIG------IESRKQFkkinDKLPNAVIACVGGG 236
Cdd:PRK06608 153 TIAgagtlcYEALQQL----GFSPDAIFASCGGG 182
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
56-237 |
3.10e-08 |
|
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: 54.66 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 56 RPSPLTYAERLSKVWGgAKIWLKREDLNHTGAHKIN---NTIGQvlIAKAMGKTRIIAETgAGQHGVATATVGAMFQMKT 132
Cdd:COG1171 23 RRTPLLRSPTLSERLG-AEVYLKLENLQPTGSFKLRgayNALAS--LSEEERARGVVAAS-AGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 133 VVYMGEE--DLRRQelnaiRMRMLGAKVVgvssgtatLKDATSEAMRDWALNVSNTH---YIvgssigpHPF--PTIVRD 205
Cdd:COG1171 99 TIVMPETapAVKVA-----ATRAYGAEVV--------LHGDTYDDAEAAAAELAEEEgatFV-------HPFddPDVIAG 158
|
170 180 190
....*....|....*....|....*....|....
gi 523630390 206 fQSVIGIEsrkqfkkINDKLPN--AVIACVGGGS 237
Cdd:COG1171 159 -QGTIALE-------ILEQLPDldAVFVPVGGGG 184
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
57-264 |
2.94e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 51.94 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 57 PSPLTYAERLSkvwggakIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQH--GVATATVGAMFQMKTVV 134
Cdd:PRK08813 39 PTPLHYAERFG-------VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHaqGVAWSAYRLGVQAITVM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 135 YMGEEDlrrqelnairmrmlgAKVVGVSSGTATLK---DATSEAMRdWALNVSNTH-YIVGSSIGPhpfPTIVRDfQSVI 210
Cdd:PRK08813 112 PHGAPQ---------------TKIAGVAHWGATVRqhgNSYDEAYA-FARELADQNgYRFLSAFDD---PDVIAG-QGTV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 523630390 211 GIEsrkqfkkINDKLPNAVIACVGGGSNAIGMFYGfIQDKKVKLFGIEAGGYSS 264
Cdd:PRK08813 172 GIE-------LAAHAPDVVIVPIGGGGLASGVALA-LKSQGVRVVGAQVEGVDS 217
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
50-180 |
2.30e-06 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 49.06 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 50 RKNYIGRPSPLTYAERLSKVWgGAKIWLKREDLnhTG-------AHKINNTIGQvliAKAMGKTRIIAeTGAGQ--HGVA 120
Cdd:PRK03910 8 RLELAGLPTPLEPLPRLSAAL-GPDIYIKRDDL--TGlalggnkTRKLEFLLAD---ALAQGADTLIT-AGAIQsnHARQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523630390 121 TATVGAMFQMKTVVYMGEEDLRRQEL-----NAIRMRMLGAKVVGVSSGTatlkDATsEAMRDWA 180
Cdd:PRK03910 81 TAAAAAKLGLKCVLLLENPVPTEAENylangNVLLDDLFGAEIHVVPAGT----DMD-AQLEELA 140
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
58-374 |
5.30e-06 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 47.80 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 58 SPLTYAERLSKVWGG-AKIWLKREDLN---HTGAHKINNTIGQVLIAKAMGKTRIIAeTGAGQ--HGVATATVGAMFQMK 131
Cdd:cd06449 1 TPIQYLPRLSEHLGGkVEIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKGADTLVT-VGGIQsnHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 132 TVVYM-----GEEDLRRQELNAIRMRMLGAKVVGVSSGTAT-LKDATSEAMRDWALNVSNTHYI-VGSSigPHPFPTI-- 202
Cdd:cd06449 80 CVLVQenwvpYSDAVYDRVGNILLSRIMGADVRLVSAGFDIgIRKSFEEAAEEVEAKGGKPYVIpAGGS--EHPLGGLgy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 203 VRdfqsvIGIESRKQFKKINDKLPNAVIACVGGGSNAiGMFYGFIQD-KKVKLFGIEAGGYSSNPGSHSATIQFGRT--- 278
Cdd:cd06449 158 VG-----FVLEIAQQEEELGFKFDSIVVCSVTGSTHA-GLSVGLAALgRQRRVIGIDASAKPEKTKAQVLRIAQAKLaee 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 279 GFLHGTKTLVIQDDFGqivpahsvsagldYPGVGpehayfhksgrvsyvsVDDEGALDAFIEVCRIEGII--PALEtAHA 356
Cdd:cd06449 232 GLEVKEEDVVLDDDYA-------------APEYG----------------IPNDETIEAIKLCARLEGIItdPVYE-GKS 281
|
330 340
....*....|....*....|
gi 523630390 357 FRYAKDLAKSMSKKE--NIL 374
Cdd:cd06449 282 MQGMIDLVRNGEFKEgsKVL 301
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
57-264 |
6.78e-06 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 47.88 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 57 PSPLTYAERLSKVWGgAKIWLKREDLNHTGAHKIN---NTIGQvLIAKAMGKTRIIAEtgAGQH--GVATATvgAMFQMK 131
Cdd:PRK08639 25 ETPLQRNDYLSEKYG-ANVYLKREDLQPVRSYKLRgayNAISQ-LSDEELAAGVVCAS--AGNHaqGVAYAC--RHLGIP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 132 TVVYMgEEDLRRQELNAIrmRMLGAKVVGVSSGTATLKDATSEAMRDWALNvsNTHYIvgssigpHPF--PTIVRDfQSV 209
Cdd:PRK08639 99 GVIFM-PVTTPQQKIDQV--RFFGGEFVEIVLVGDTFDDSAAAAQEYAEET--GATFI-------PPFddPDVIAG-QGT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 523630390 210 IGIESRKQFKKINDklPNAVIACVGGGSNAIGMfYGFIQD--KKVKLFGIEAGGYSS 264
Cdd:PRK08639 166 VAVEILEQLEKEGS--PDYVFVPVGGGGLISGV-TTYLKErsPKTKIIGVEPAGAAS 219
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
57-348 |
9.31e-05 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 44.25 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 57 PSPLTYAERLSKVWGG-AKIWLKREDLNHTGAHKINNTIG-QVLIAKAMGKTriiAET----GAGQ--HGVATATVGAMF 128
Cdd:PRK12390 15 PTPIHPLKRLSAHLGGkVELYAKREDCNSGLAFGGNKTRKlEYLVPDALAQG---ADTlvsiGGVQsnHTRQVAAVAAHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 129 QMKTVV----YMGEEDLRRQELNAIRM-RMLGAKVVGVSSG-TATLKDATSEAMRDwALNVSNTHYIVGSSIGPHPFPTI 202
Cdd:PRK12390 92 GMKCVLvqenWVNYEDAVYDRVGNILLsRIMGADVRLVPDGfDIGIRKSWEDALED-VRAAGGKPYAIPAGASDHPLGGL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 203 vrdfqSVIGI--ESRKQFKKINDKLPNAVIACVGGGSNAiGMFYGFI-QDKKVKLFGIEAggySSNPGSHSATIqfgrTG 279
Cdd:PRK12390 171 -----GFVGFaeEVRAQEAELGFKFDYIVVCSVTGSTQA-GMVVGFAaDGRARRVIGIDA---SAKPEQTRAQV----LR 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 280 FLHGTKTLViqdDFGQIVPAHSVSAGLDYpgVGPEHAyfhksgrvsyvsVDDEGALDAfIEVC-RIEGII 348
Cdd:PRK12390 238 IARNTAELV---ELGRDITEDDVVLDERY--AGPEYG------------LPNEGTLEA-IRLCaRLEGML 289
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
56-180 |
6.86e-04 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 41.09 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 56 RPSPLTYAErlSKVWGGAKIWLKREDLNHTGAHK----INNtigqvLIAKAMGKTRIIAETGaGQHGVATATVGAMFQMK 131
Cdd:PRK08246 22 RRTPVLEAD--GAGFGPAPVWLKLEHLQHTGSFKargaFNR-----LLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVP 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 523630390 132 TVVYMGEEdlrRQELNAIRMRMLGAKVVGVSSGTAtlkDATsEAMRDWA 180
Cdd:PRK08246 94 ATVFVPET---APPAKVARLRALGAEVVVVGAEYA---DAL-EAAQAFA 135
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
59-177 |
3.32e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 39.18 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523630390 59 PLTYAERLSKVWGgAKIWLKREDLNHTGAHKINNTIGQVLIAKAMGKTRIIAETGAGQHGVATATVGAMFQMKTVVYMGE 138
Cdd:PRK07476 21 PLVASASLSARAG-VPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICMSR 99
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 523630390 139 edLRRQ-ELNAIrmRMLGAKVVGVSSGTatlKDATSEAMR 177
Cdd:PRK07476 100 --LVPAnKVDAI--RALGAEVRIVGRSQ---DDAQAEVER 132
|
|
| |
