|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
64-470 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 867.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 64 AAGSDPALWQRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRR 143
Cdd:PLN02618 2 PPGSDPTGFQRPDSFGRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEHYKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 144 ENGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALN 223
Cdd:PLN02618 82 ADGEGPEIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 224 VFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPD 303
Cdd:PLN02618 162 VFRMRLLGAEVRPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 304 VLVACVGGGSNAMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLD 383
Cdd:PLN02618 242 VLVACVGGGSNAMGLFHEFIDDEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 384 YPGVGPEHSFFKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQT 463
Cdd:PLN02618 322 YPGVGPEHSFLKDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNT 401
|
....*..
gi 15239755 464 VAKYLDV 470
Cdd:PLN02618 402 AIKYLQV 408
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
73-470 |
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: 828.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 73 QRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRrengeGPLIY 152
Cdd:COG0133 6 SLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLG-----GAKIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 153 LKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGA 232
Cdd:COG0133 81 LKREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 233 EVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGG 312
Cdd:COG0133 161 EVVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 313 SNAMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHS 392
Cdd:COG0133 241 SNAIGIFYPFLDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239755 393 FFKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLDV 470
Cdd:COG0133 321 YLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGL 398
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
96-464 |
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: 675.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 96 ALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRrengeGPLIYLKREDLNHTGAHKINNAVAQALL 175
Cdd:cd06446 2 ALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLG-----GAKIYLKREDLNHTGAHKINNALGQALL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 176 AKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDW 255
Cdd:cd06446 77 AKRMGKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 256 VTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSNAMGLFHEFVNDTEVRMIGVEA 335
Cdd:cd06446 157 VTNVEDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 336 AGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFFKDMGRAEYYSITDEEALEAFK 415
Cdd:cd06446 237 GGCGLETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFK 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15239755 416 RVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTV 464
Cdd:cd06446 317 LLARTEGIIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
79-468 |
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: 662.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 79 GRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYrrengEGPLIYLKREDL 158
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEAL-----GGAKIYLKREDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 159 NHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVH 238
Cdd:TIGR00263 76 NHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 239 SGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSNAMGL 318
Cdd:TIGR00263 156 SGSGTLKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 319 FHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFFKDMG 398
Cdd:TIGR00263 236 FYAFIDDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 399 RAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYL 468
Cdd:TIGR00263 316 RATYEAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
127-455 |
5.09e-44 |
|
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: 156.32 E-value: 5.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 127 RESPLYFAERLTEHYrrengeGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGL 206
Cdd:pfam00291 6 GPTPLVRLPRLSKEL------GVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 207 ECIIYMGAQDmerQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWvtnvetTHYILGSVAGpHPYPMMVrdfHAVI 286
Cdd:pfam00291 80 KVTIVVPEDA---PPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEG------PGAYYINQYD-NPLNIEG---YGTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 287 GKEtrkqALEKWGGKPDVLVACVGGGSNAMGLFHEFV-NDTEVRMIGVEAAGfgldsgkhAATLTKGdvgvlhgamsyLL 365
Cdd:pfam00291 147 GLE----ILEQLGGDPDAVVVPVGGGGLIAGIARGLKeLGPDVRVIGVEPEG--------APALARS-----------LA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 366 QDDDGQIIEPHSISAGLDYPGVGPEHSF-FKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLE-KLCPTL 443
Cdd:pfam00291 204 AGRPVPVPVADTIADGLGVGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKlALAGEL 283
|
330
....*....|..
gi 15239755 444 SDGTRVVLNFSG 455
Cdd:pfam00291 284 KGGDRVVVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
64-470 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 867.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 64 AAGSDPALWQRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRR 143
Cdd:PLN02618 2 PPGSDPTGFQRPDSFGRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEHYKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 144 ENGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALN 223
Cdd:PLN02618 82 ADGEGPEIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 224 VFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPD 303
Cdd:PLN02618 162 VFRMRLLGAEVRPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 304 VLVACVGGGSNAMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLD 383
Cdd:PLN02618 242 VLVACVGGGSNAMGLFHEFIDDEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 384 YPGVGPEHSFFKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQT 463
Cdd:PLN02618 322 YPGVGPEHSFLKDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNT 401
|
....*..
gi 15239755 464 VAKYLDV 470
Cdd:PLN02618 402 AIKYLQV 408
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
73-470 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 833.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 73 QRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRrengeGPLIY 152
Cdd:PRK04346 3 TLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLG-----GAKIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 153 LKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGA 232
Cdd:PRK04346 78 LKREDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 233 EVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGG 312
Cdd:PRK04346 158 EVVPVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 313 SNAMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHS 392
Cdd:PRK04346 238 SNAIGIFHPFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHA 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239755 393 FFKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLDV 470
Cdd:PRK04346 318 YLKDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLLGV 395
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
73-470 |
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: 828.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 73 QRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRrengeGPLIY 152
Cdd:COG0133 6 SLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLG-----GAKIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 153 LKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGA 232
Cdd:COG0133 81 LKREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 233 EVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGG 312
Cdd:COG0133 161 EVVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 313 SNAMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHS 392
Cdd:COG0133 241 SNAIGIFYPFLDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239755 393 FFKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLDV 470
Cdd:COG0133 321 YLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGL 398
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
75-469 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 678.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 75 PDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYrrengEGPLIYLK 154
Cdd:PRK13028 9 PDADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEEL-----GGAQIYLK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 155 REDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEV 234
Cdd:PRK13028 84 REDLNHTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLGAEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 235 RGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSN 314
Cdd:PRK13028 164 VPVTRGGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 315 AMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFF 394
Cdd:PRK13028 244 AIGLFSAFLDDESVRLVGVEPAGRGLDLGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPEHAYL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239755 395 KDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLD 469
Cdd:PRK13028 324 KDIGRVEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAPELSKDETILVNLSGRGDKDIDYVAEMLG 398
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
96-464 |
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: 675.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 96 ALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRrengeGPLIYLKREDLNHTGAHKINNAVAQALL 175
Cdd:cd06446 2 ALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLG-----GAKIYLKREDLNHTGAHKINNALGQALL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 176 AKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDW 255
Cdd:cd06446 77 AKRMGKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 256 VTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSNAMGLFHEFVNDTEVRMIGVEA 335
Cdd:cd06446 157 VTNVEDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 336 AGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFFKDMGRAEYYSITDEEALEAFK 415
Cdd:cd06446 237 GGCGLETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFK 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15239755 416 RVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTV 464
Cdd:cd06446 317 LLARTEGIIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
79-468 |
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: 662.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 79 GRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYrrengEGPLIYLKREDL 158
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEAL-----GGAKIYLKREDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 159 NHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVH 238
Cdd:TIGR00263 76 NHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 239 SGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSNAMGL 318
Cdd:TIGR00263 156 SGSGTLKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 319 FHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFFKDMG 398
Cdd:TIGR00263 236 FYAFIDDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 399 RAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYL 468
Cdd:TIGR00263 316 RATYEAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
75-469 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 631.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 75 PDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYrrengeGPLIYLK 154
Cdd:PRK13803 218 SDPAGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSDIY------GARIYLK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 155 REDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEV 234
Cdd:PRK13803 292 REDLNHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 235 RGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSN 314
Cdd:PRK13803 372 IPVLSGSKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSN 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 315 AMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFF 394
Cdd:PRK13803 452 AIGIFYHFLDDPSVKLIGVEAGGKGVNTGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANL 531
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239755 395 KDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLD 469
Cdd:PRK13803 532 FETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKDIVIVNLSGRGDKDIPTLKEYFE 606
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
81-468 |
1.19e-167 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 488.77 E-value: 1.19e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 81 FGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRRENGEGPLIYLKREDLNH 160
Cdd:PRK13802 279 WGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTEAPRFAERVKEKTGLDARVFLKREDLNH 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 161 TGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVHSG 240
Cdd:PRK13802 359 TGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGAEVVEVTLG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 241 TATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETrKQALEKWGG--KPDVLVACVGGGSNAMGL 318
Cdd:PRK13802 439 DRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEA-KQQLQDWYGidHPDAICACVGGGSNAIGV 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 319 FHEFVNDTEVRMIGVEAAGFGLDSGKHAATLT--KGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFFKD 396
Cdd:PRK13802 518 MNAFLDDERVNLYGYEAGGNGPESGKHAIRFApgTGELGMFQGAKSYLLENDEGQTLDTYSISAGLDYASVGPEHAWLKD 597
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239755 397 MGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLS----DGTRVVLNFSGRGDKDVQTVAKYL 468
Cdd:PRK13802 598 IGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAAADLKakgyEHPVMIVNISGRGDKDMNTAGKWF 673
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
129-456 |
8.38e-63 |
|
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: 203.90 E-value: 8.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 129 SPLYFAERLTEHYRREngegplIYLKREDLNHTGAHKINNAVAQALLAKRLG---KKRIIAETGaGQHGVATATVCARFG 205
Cdd:cd00640 1 TPLVRLKRLSKLGGAN------IYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTG-GNTGIALAAAAARLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 206 LECIIYMGAQDmerQALNVFRMRLLGAEVRGVHSGtatLKDATSEAIRDWVTNvETTHYILGSVagpHPYpmmVRDFHAV 285
Cdd:cd00640 74 LKCTIVMPEGA---SPEKVAQMRALGAEVVLVPGD---FDDAIALAKELAEED-PGAYYVNQFD---NPA---NIAGQGT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 286 IGKETRKQALEKwggKPDVLVACVGGGSNAMGLFHEFVNDT-EVRMIGVEaagfgldsgkhaatltkgdvgvlhgamsyl 364
Cdd:cd00640 141 IGLEILEQLGGQ---KPDAVVVPVGGGGNIAGIARALKELLpNVKVIGVE------------------------------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 365 lqdddgqiiephsisagldypgvgpehsffkdmgrAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLS 444
Cdd:cd00640 188 -----------------------------------PEVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG 232
|
330
....*....|..
gi 15239755 445 DGTRVVLNFSGR 456
Cdd:cd00640 233 KGKTVVVILTGG 244
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
125-469 |
1.05e-59 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 201.56 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 125 VGRESPLYFAERLTEHYrrenGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARF 204
Cdd:PRK12391 74 LWRPTPLIRARRLEKAL----GTPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACALF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 205 GLECIIYMGAQDME----RQALnvfrMRLLGAEV-----RGVHSGTATLKD----------ATSEAIRDWVTNvETTHYI 265
Cdd:PRK12391 150 GLECTVFMVRVSYEqkpyRRSL----METYGAEVipspsDLTEAGRKILAEdpdhpgslgiAISEAVEDAAKR-PDTKYA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 266 LGSVAgphPYPMMvrdFHAVIGKETRKQaLEKWGGKPDVLVACVGGGSNAMGLFHEFVND-----TEVRMIGVEAAGfgl 340
Cdd:PRK12391 225 LGSVL---NHVLL---HQTVIGLEAKKQ-LELAGEYPDVVIGCVGGGSNFAGLAFPFLGDklegkKDTRFIAVEPAA--- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 341 dsgkhAATLTKG-------DV-GVLHGAMSYLLQDDdgqIIEPHSISAGLDYPGVGPEHSFFKDMGRAEYYSITDEEALE 412
Cdd:PRK12391 295 -----CPTLTKGeyaydfgDTaGLTPLLKMYTLGHD---FVPPPIHAGGLRYHGMAPLVSLLVHEGLIEARAYPQTEVFE 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 413 AFKRVSRLEGIIPALETSHALAY---LEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLD 469
Cdd:PRK12391 367 AAVLFARTEGIVPAPESSHAIAAaidEALKAKEEGEEKVILFNLSGHGLLDLAAYDAYLA 426
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
126-469 |
5.87e-52 |
|
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: 181.10 E-value: 5.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 126 GRESPLYFAERLtehyrrengEGPL-----IYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATV 200
Cdd:COG1350 76 WRPSPLYRARRL---------EKALgtpakIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALSFA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 201 CARFGLECIIYMGAQDME----RQALnvfrMRLLGAEV-----------RGV------HSGtaTLKDATSEAIRDWVTNv 259
Cdd:COG1350 147 CALFGLECTVYMVKVSYEqkpyRRSM----METYGAEVipspsdlteagRKIlaedpdTPG--SLGIAISEAVEDAATR- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 260 ETTHYILGSVAGpHpypmmVRDFHAVIGKETRKQaLEKWGGKPDVLVACVGGGSNAMGLFHEFVND-----TEVRMIGVE 334
Cdd:COG1350 220 DDTKYALGSVLN-H-----VLLHQTVIGLEAKKQ-LEKAGEYPDVVIGCAGGGSNFAGLAFPFLRDklrgkKDVRFIAVE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 335 AAGfgldsgkhAATLTKG----DVGVLHG----AMSYLLqdddGQIIEPHSISA-GLDYPGVGPEHSFFKDMGRAEYYSI 405
Cdd:COG1350 293 PAA--------CPTLTRGvyayDFGDTAGltplLKMYTL----GHDFIPPPIHAgGLRYHGMAPLVSQLYHDGLIEAVAY 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239755 406 TDEEALEAFKRVSRLEGIIPALETSHAL--AYLEKL-CPTlsDGT-RVVL-NFSGRGDKDVQTVAKYLD 469
Cdd:COG1350 361 PQLEVFEAGVLFARTEGIVPAPESAHAIkaAIDEALkCKE--EGEeKTILfNLSGHGHFDLAAYDAYLA 427
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
127-455 |
5.09e-44 |
|
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: 156.32 E-value: 5.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 127 RESPLYFAERLTEHYrrengeGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGL 206
Cdd:pfam00291 6 GPTPLVRLPRLSKEL------GVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 207 ECIIYMGAQDmerQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWvtnvetTHYILGSVAGpHPYPMMVrdfHAVI 286
Cdd:pfam00291 80 KVTIVVPEDA---PPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEG------PGAYYINQYD-NPLNIEG---YGTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 287 GKEtrkqALEKWGGKPDVLVACVGGGSNAMGLFHEFV-NDTEVRMIGVEAAGfgldsgkhAATLTKGdvgvlhgamsyLL 365
Cdd:pfam00291 147 GLE----ILEQLGGDPDAVVVPVGGGGLIAGIARGLKeLGPDVRVIGVEPEG--------APALARS-----------LA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 366 QDDDGQIIEPHSISAGLDYPGVGPEHSF-FKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLE-KLCPTL 443
Cdd:pfam00291 204 AGRPVPVPVADTIADGLGVGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKlALAGEL 283
|
330
....*....|..
gi 15239755 444 SDGTRVVLNFSG 455
Cdd:pfam00291 284 KGGDRVVVVLTG 295
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
130-469 |
1.36e-18 |
|
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: 87.18 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 130 PLYFAERLTEHYRREngegplIYLKREDLNHTGAHKinnAVAQALL---AKRLGKKRIIAETgAGQHGVATATVCARFGL 206
Cdd:COG0498 68 PLVKAPRLADELGKN------LYVKEEGHNPTGSFK---DRAMQVAvslALERGAKTIVCAS-SGNGSAALAAYAARAGI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 207 ECIIYMGAQDM----ERQalnvfrMRLLGAEVRGVHsGT-----ATLKDATSEaiRDWvtnvetthYILGSVagpHPYpm 277
Cdd:COG0498 138 EVFVFVPEGKVspgqLAQ------MLTYGAHVIAVD-GNfddaqRLVKELAAD--EGL--------YAVNSI---NPA-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 278 mVRDFHAVIGKEtrkqALEKWGGKPDVLVACVGGGSNAMGL---FHEFVNDTEV----RMIGVEAAGFgldsGKHAATLT 350
Cdd:COG0498 196 -RLEGQKTYAFE----IAEQLGRVPDWVVVPTGNGGNILAGykaFKELKELGLIdrlpRLIAVQATGC----NPILTAFE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 351 KGdvgvlhgamsyllqDDDGQIIEPHSISAGLDYPG-VGPEHSFF--KDMGrAEYYSITDEEALEAFKRVSRLEGIIPAL 427
Cdd:COG0498 267 TG--------------RDEYEPERPETIAPSMDIGNpSNGERALFalRESG-GTAVAVSDEEILEAIRLLARREGIFVEP 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15239755 428 ETSHALAYLEKLC--PTLSDGTRVVLNFSGRGDKDVQTVAKYLD 469
Cdd:COG0498 332 ATAVAVAGLRKLReeGEIDPDEPVVVLSTGHGLKFPDAVREALG 375
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
142-469 |
5.11e-16 |
|
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: 78.32 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 142 RRENGEGPLIYLKREDLNHTGAHKINNAVA---QALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYM-GAQDM 217
Cdd:cd01561 10 RLSPGTGAEIYAKLEFFNPGGSVKDRIALYmieDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIVMpETMSE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 218 ERQALnvfrMRLLGAEVRGVhsgTATLKDATSEAIRdwvtnvetthyILGSVAGPHPYPMMVRDF--------HAvigKE 289
Cdd:cd01561 90 EKRKL----LRALGAEVILT---PEAEADGMKGAIA-----------KARELAAETPNAFWLNQFenpanpeaHY---ET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 290 TRKQALEKWGGKPDVLVACVGGGSNAMGL---FHEfvNDTEVRMIGVEAAGFGLDSGKHAAtltkgdvgvlhgamsyllq 366
Cdd:cd01561 149 TAPEIWEQLDGKVDAFVAGVGTGGTITGVaryLKE--KNPNVRIVGVDPVGSVLFSGGPPG------------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 367 dddgqiiePHSIsagldyPGVGpeHSFFKDMGRAEYY----SITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPT 442
Cdd:cd01561 208 --------PHKI------EGIG--AGFIPENLDRSLIdevvRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKR 271
|
330 340
....*....|....*....|....*..
gi 15239755 443 LSDGTRVVLNFSGRGDkdvqtvaKYLD 469
Cdd:cd01561 272 LGPGKTIVTILPDSGE-------RYLS 291
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
130-460 |
2.17e-15 |
|
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: 76.86 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 130 PLYFAERLTEHYRRENgegplIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETgAGQHGVATATVCARFGLECI 209
Cdd:cd01563 24 PLVRAPRLGERLGGKN-----LYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACAS-TGNTSASLAAYAARAGIKCV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 210 IYMGAqDMERQALNvfRMRLLGAEVRGVHSGTATLKDATSEAIRD---WVTNVETTHYILGSvagphpypmmvrdfhAVI 286
Cdd:cd01563 98 VFLPA-GKALGKLA--QALAYGATVLAVEGNFDDALRLVRELAEEnwiYLSNSLNPYRLEGQ---------------KTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 287 GKETrkqaLEKWGGK-PDVLVACVGGGSNAMGL---FHEFVN----DTEVRMIGVEAAGfgldsgkhAATLTKGdvgvlh 358
Cdd:cd01563 160 AFEI----AEQLGWEvPDYVVVPVGNGGNITAIwkgFKELKElgliDRLPRMVGVQAEG--------AAPIVRA------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 359 gamsYLLQDDDGQIIE-PHSISAGLDypgVGPEHSFFKDM-------GRAEyySITDEEALEAFKRVSRLEGIIPALETS 430
Cdd:cd01563 222 ----FKEGKDDIEPVEnPETIATAIR---IGNPASGPKALravresgGTAV--AVSDEEILEAQKLLARTEGIFVEPASA 292
|
330 340 350
....*....|....*....|....*....|..
gi 15239755 431 HALAYLEKLCP--TLSDGTRVVLNFSGRGDKD 460
Cdd:cd01563 293 ASLAGLKKLREegIIDKGERVVVVLTGHGLKD 324
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
115-338 |
1.67e-14 |
|
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: 74.06 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 115 RELAGILKDYVgRESPLYFAERLTEHYRREngegplIYLKREDLNHTGAHKINNAVAQALLAKRLGKKR-IIAETgAGQH 193
Cdd:cd01562 5 LAAAARIKPVV-RRTPLLTSPTLSELLGAE------VYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAAS-AGNH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 194 GVATATVCARFGLECIIYM--GAQDMERQAlnvfrMRLLGAEVrgVHSGtATLKDATSEAIRDwvtnVETTHYILgsVag 271
Cdd:cd01562 77 AQGVAYAAKLLGIPATIVMpeTAPAAKVDA-----TRAYGAEV--VLYG-EDFDEAEAKAREL----AEEEGLTF--I-- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239755 272 pHPY--PMMVRDfHAVIGKETRKQAlekwgGKPDVLVACVGGGSNAMGL---FHEFVNDTEVrmIGVEAAGF 338
Cdd:cd01562 141 -HPFddPDVIAG-QGTIGLEILEQV-----PDLDAVFVPVGGGGLIAGIataVKALSPNTKV--IGVEPEGA 203
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
115-338 |
2.78e-12 |
|
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: 67.37 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 115 RELAGILKDYVgRESPLYFAERLTEHYRREngegplIYLKREDLNHTGAHKIN---NAVAQalLAKRLGKKRIIAETgAG 191
Cdd:COG1171 12 EAAAARIAGVV-RRTPLLRSPTLSERLGAE------VYLKLENLQPTGSFKLRgayNALAS--LSEEERARGVVAAS-AG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 192 QHGVATATVCARFGLECIIYM--GAQDMERQAlnvfrMRLLGAEVRgVHSGtaTLKDATSEAIRDwvtnVETTHYILgsV 269
Cdd:COG1171 82 NHAQGVAYAARLLGIPATIVMpeTAPAVKVAA-----TRAYGAEVV-LHGD--TYDDAEAAAAEL----AEEEGATF--V 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239755 270 agpHPY-PMMVRDFHAVIGKEtrkqALEKWgGKPDVLVACVGGG---SNAMGLFHEFVNDTEVrmIGVEAAGF 338
Cdd:COG1171 148 ---HPFdDPDVIAGQGTIALE----ILEQL-PDLDAVFVPVGGGgliAGVAAALKALSPDIRV--IGVEPEGA 210
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
129-424 |
1.13e-10 |
|
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: 62.44 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 129 SPLYFAERLTEHYrrenGEGPLIYLKREDLNHTGA------HKINNAVAQALlakRLGKKRIIAeTGAGQ--HGVATATV 200
Cdd:cd06449 1 TPIQYLPRLSEHL----GGKVEIYAKRDDCNSGLAfggnkiRKLEYLLPDAL---AKGADTLVT-VGGIQsnHTRQVAAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 201 CARFGLECIIYM-----GAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPY 275
Cdd:cd06449 73 AAKLGLKCVLVQenwvpYSDAVYDRVGNILLSRIMGADVRLVSAGFDIGIRKSFEEAAEEVEAKGGKPYVIPAGGSEHPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 276 PMMVRdFHAVIgkETRKQaLEKWGGKPDVLVACVGGGSNAMGLFHEFVNDT-EVRMIGVEAagfgldSGKHAATLTKGDV 354
Cdd:cd06449 153 GGLGY-VGFVL--EIAQQ-EEELGFKFDSIVVCSVTGSTHAGLSVGLAALGrQRRVIGIDA------SAKPEKTKAQVLR 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 355 GVLHGAMSYLLQDDDGQIIephsisagLDYPGVGPEhsffkdmgraeyYSITDEEALEAFKRVSRLEGII 424
Cdd:cd06449 223 IAQAKLAEEGLEVKEEDVV--------LDDDYAAPE------------YGIPNDETIEAIKLCARLEGII 272
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
130-424 |
2.74e-09 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 58.30 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 130 PLYFAERLTEHYrrengeGPLIYLKREDLnhTG-------AHKINNAVAQALlakRLGKKRIIAeTGAGQ--HGVATATV 200
Cdd:PRK03910 17 PLEPLPRLSAAL------GPDIYIKRDDL--TGlalggnkTRKLEFLLADAL---AQGADTLIT-AGAIQsnHARQTAAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 201 CARFGLECIIYMGAQDMERQAL-----NVFRMRLLGAEVRGVHSGTatlkDATsEAIRDWVTNVETthyilgsvAGPHPY 275
Cdd:PRK03910 85 AAKLGLKCVLLLENPVPTEAENylangNVLLDDLFGAEIHVVPAGT----DMD-AQLEELAEELRA--------QGRRPY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 276 pmmvrdfhaVI----------------GKETRKQALEKwGGKPDVLVACVGGGSNAMGL---FHEFVNDTEVRMIGVEAA 336
Cdd:PRK03910 152 ---------VIpvggsnalgalgyvacALEIAQQLAEG-GVDFDAVVVASGSGGTHAGLaagLAALGPDIPVIGVTVSRS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 337 gfgldsgkhAATLTKGDVGVLHGAMSYLlqdDDGQIIEPHSISAGLDYpgVGPehsffkdmGraeyYSITDEEALEAFKR 416
Cdd:PRK03910 222 ---------AAEQEPKVAKLAQATAELL---GLPTEIPRADIRLWDDY--VGP--------G----YGVPTDEMLEAVKL 275
|
....*...
gi 15239755 417 VSRLEGII 424
Cdd:PRK03910 276 LARTEGIL 283
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
121-337 |
3.81e-09 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 58.28 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 121 LKDYVgRESPLYFAERLTEHYRREngegplIYLKREDLNHTGAHKIN---NAVAQalLAKRLGKKRIIAETgAGQH--GV 195
Cdd:PRK08639 19 LKDVV-PETPLQRNDYLSEKYGAN------VYLKREDLQPVRSYKLRgayNAISQ--LSDEELAAGVVCAS-AGNHaqGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 196 ATAtvCARFGLECIIYMGAQdMERQALNvfRMRLLGAEVRGVHSGTATLKDATSEAIRDwvtnVETT--HYIlgsvagpH 273
Cdd:PRK08639 89 AYA--CRHLGIPGVIFMPVT-TPQQKID--QVRFFGGEFVEIVLVGDTFDDSAAAAQEY----AEETgaTFI-------P 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 274 PYpmmvRDFHAVIGKET-RKQALEKWG--GKPDVLVACVGGGSNAMGL---FHEFVNDTEVrmIGVEAAG 337
Cdd:PRK08639 153 PF----DDPDVIAGQGTvAVEILEQLEkeGSPDYVFVPVGGGGLISGVttyLKERSPKTKI--IGVEPAG 216
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
121-334 |
2.55e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 55.55 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 121 LKDYVgRESPLYFAERLTEHYRREngegplIYLKREDLNHTGAHKINNAVAQALLAKRLGK--KRIIAETgAGQHGVATA 198
Cdd:PRK06608 17 IKQYL-HLTPIVHSESLNEMLGHE------IFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TGNHGQAVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 199 TVCARFGLECIIYMgaqdmerqALNVFRMRL-----LGAEVRgvhsGTATLKDATSEAIRDwvtNVETTHYIlgsvagpH 273
Cdd:PRK06608 89 YASKLFGIKTRIYL--------PLNTSKVKQqaalyYGGEVI----LTNTRQEAEEKAKED---EEQGFYYI-------H 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15239755 274 PYpmmvrDFHAVI-GKETRKQ-ALEKWGGKPDVLVACVGGGSNAMG-LFHEFVNDTEVRMIGVE 334
Cdd:PRK06608 147 PS-----DSDSTIaGAGTLCYeALQQLGFSPDAIFASCGGGGLISGtYLAKELISPTSLLIGSE 205
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
121-235 |
8.12e-07 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 50.85 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 121 LKDYVgRESPLYFAERLTEHyrrENGEgplIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATV 200
Cdd:PRK06815 14 LRPQV-RVTPLEHSPLLSQH---TGCE---VYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALA 86
|
90 100 110
....*....|....*....|....*....|....*
gi 15239755 201 CARFGLECIIYMGAQdmeRQALNVFRMRLLGAEVR 235
Cdd:PRK06815 87 AKLAGIPVTVYAPEQ---ASAIKLDAIRALGAEVR 118
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
148-337 |
9.14e-07 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 50.76 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 148 GPLIYLKREDLNHTGAHK---INNAVAQALLAKRLGKKRIIAETGaGQHGVATATVCARFGLECIIYM---GAQDMerqa 221
Cdd:cd06448 15 GCNVFLKLENLQPSGSFKirgIGHLCQKSAKQGLNECVHVVCSSG-GNAGLAAAYAARKLGVPCTIVVpesTKPRV---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 222 lnVFRMRLLGAEVrgVHSGTATLKDATSEAIrdwvtnvetthyilgSVAGPHPYPMMVRDF--------HAVIGKETRKQ 293
Cdd:cd06448 90 --VEKLRDEGATV--VVHGKVWWEADNYLRE---------------ELAENDPGPVYVHPFddpliwegHSSMVDEIAQQ 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15239755 294 ALEKwgGKPDVLVACVGGGSNAMGLFH--EFVNDTEVRMIGVEAAG 337
Cdd:cd06448 151 LQSQ--EKVDAIVCSVGGGGLLNGIVQglERNGWGDIPVVAVETEG 194
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
151-470 |
2.65e-06 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 49.61 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 151 IYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETgAGQHGVATATVCARFGLECIIYMGAqdmERQALNVFRMRLL 230
Cdd:PRK08197 97 LWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPT-NGNAGAAWAAYAARAGIRATIFMPA---DAPEITRLECALA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 231 GAEVRGV-----HSGTATLKDATSEAIRDWVTNVEtthyilgsvagphPYpmmvrdfhAVIGKETRKQAL-EKWGGK-PD 303
Cdd:PRK08197 173 GAELYLVdglisDAGKIVAEAVAEYGWFDVSTLKE-------------PY--------RIEGKKTMGLELaEQLGWRlPD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 304 VLVACVGGGSNAMGL---FHE-----FVNDTEVRMIGVEAAGF-----GLDSGKHAATLTKGdvgvlhgamsyllqdddg 370
Cdd:PRK08197 232 VILYPTGGGVGLIGIwkaFDElealgWIGGKRPRLVAVQAEGCapivkAWEEGKEESEFWED------------------ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 371 qiiePHSISAGLDYPgvgpehsffKDMG-----RAEYYS------ITDEEALEAFKRVSRLEGIIPALETSHALAYLEKL 439
Cdd:PRK08197 294 ----AHTVAFGIRVP---------KALGdflvlDAVRETggcaiaVSDDAILAAQRELAREEGLFACPEGAATFAAARQL 360
|
330 340 350
....*....|....*....|....*....|...
gi 15239755 440 CPT--LSDGTRVVLNFSGRGDKDVQTVAKYLDV 470
Cdd:PRK08197 361 RESgwLKGDERVVLFNTGSGLKYPDTVPVVVPV 393
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
133-312 |
3.28e-06 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 48.80 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 133 FAERLTEHYRR-------ENGEGPL-IYLKREDLNHTGAHKINNAVAqALLAKRLGKKRIIAETGaGQHGVATATVCARF 204
Cdd:PRK08246 13 AAQRIAPHIRRtpvleadGAGFGPApVWLKLEHLQHTGSFKARGAFN-RLLAAPVPAAGVVAASG-GNAGLAVAYAAAAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 205 GLECIIYMGAQdmeRQALNVFRMRLLGAEVRGVHSGTAtlkdatsEAIRDWVTNVETThyilGSVAgPHPYpmmvrDFHA 284
Cdd:PRK08246 91 GVPATVFVPET---APPAKVARLRALGAEVVVVGAEYA-------DALEAAQAFAAET----GALL-CHAY-----DQPE 150
|
170 180 190
....*....|....*....|....*....|
gi 15239755 285 VI-GKETRKQALEKWGGKPD-VLVACVGGG 312
Cdd:PRK08246 151 VLaGAGTLGLEIEEQAPGVDtVLVAVGGGG 180
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
110-357 |
5.27e-04 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 42.48 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 110 DDDFQRELAGILKDyVGRESPLYFAERLTEHYrrengeGPLIYLKREDLNHTGAHKINNA---VAQaLLAKRLGKKRIIA 186
Cdd:PRK12483 20 ADYLRKILAARVYD-VARETPLQRAPNLSARL------GNQVLLKREDLQPVFSFKIRGAynkMAR-LPAEQLARGVITA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 187 ETGAGQHGVATATvcARFGLECIIYMGAQDMErqaLNVFRMRLLGAEVrgVHSGtATLKDATSEAIRdwVTNVETTHYIl 266
Cdd:PRK12483 92 SAGNHAQGVALAA--ARLGVKAVIVMPRTTPQ---LKVDGVRAHGGEV--VLHG-ESFPDALAHALK--LAEEEGLTFV- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 267 gsvagpHPYPmmvrDFHAVIGKET-RKQALEKWGGKPDVLVACVGGGSNAMGL--FHEFVNdTEVRMIGVEAAgfglDSG 343
Cdd:PRK12483 161 ------PPFD----DPDVIAGQGTvAMEILRQHPGPLDAIFVPVGGGGLIAGIaaYVKYVR-PEIKVIGVEPD----DSN 225
|
250
....*....|....
gi 15239755 344 KHAATLTKGDVGVL 357
Cdd:PRK12483 226 CLQAALAAGERVVL 239
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
129-212 |
6.47e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 41.92 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 129 SPLYFAERLTehyrrengegplIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLEC 208
Cdd:PRK08813 40 TPLHYAERFG------------VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQA 107
|
....
gi 15239755 209 IIYM 212
Cdd:PRK08813 108 ITVM 111
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
151-337 |
2.93e-03 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 39.69 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 151 IYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETgAGQHGVATATVCARFGLECIIYMGAQDMERQalnVFRMRLL 230
Cdd:PRK06381 33 IYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGT-CGNYGASIAYFARLYGLKAVIFIPRSYSNSR---VKEMEKY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 231 GAEVRGVHSgtatlkdATSEAIRDWVTNVETTHYILGSVAGPHPYPMMvrDFHAVIGKETRKQAlekwGGKPDVLVACVG 310
Cdd:PRK06381 109 GAEIIYVDG-------KYEEAVERSRKFAKENGIYDANPGSVNSVVDI--EAYSAIAYEIYEAL----GDVPDAVAVPVG 175
|
170 180 190
....*....|....*....|....*....|....
gi 15239755 311 GGSNAMGLFHEF-------VNDTEVRMIGVEAAG 337
Cdd:PRK06381 176 NGTTLAGIYHGFrrlydrgKTSRMPRMIGVSTSG 209
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
125-234 |
8.96e-03 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 38.36 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239755 125 VGRESPLYFAERLTEHYrrengeGPLIYLKREDLNHTGAHKINNAV-AQALLAKRLGKKRIIAETgAGQHGVATATVCAR 203
Cdd:PLN02550 106 VAIESPLQLAKKLSERL------GVKVLLKREDLQPVFSFKLRGAYnMMAKLPKEQLDKGVICSS-AGNHAQGVALSAQR 178
|
90 100 110
....*....|....*....|....*....|.
gi 15239755 204 FGLECIIYMGAQDMERQALNVFRmrlLGAEV 234
Cdd:PLN02550 179 LGCDAVIAMPVTTPEIKWQSVER---LGATV 206
|
|
| |
