|
Name |
Accession |
Description |
Interval |
E-value |
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
1-399 |
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: 873.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 1 MTSYRNGPDAKGLFGRFGGQYVAETLMPLILDLAREYEKAKDDPAFQEELAYFQRDYVGRPSPLYFAERLTEHCGGAKIY 80
Cdd:COG0133 1 MSSLYSLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLGGAKIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 81 LKREELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYMGTTDIDRQQANVFRMKLLGA 160
Cdd:COG0133 81 LKREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 161 EVIPVTAGTGTLKDAMNEALRDWVTNVDSTFYLIGTVAGPHPYPAMVRDFQAVIGKETREQLAEKEGRLPDSLVACIGGG 240
Cdd:COG0133 161 EVVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 241 SNAMGLFHPFLDDAGVQIVGVEAAGHGIDTGKHAASLNGGVPGVLHGNRTFLLQDADGQIIDAHSISAGLDYPGIGPEHA 320
Cdd:COG0133 241 SNAIGIFYPFLDDESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595234 321 WLHDTGRVEYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVFKRAPSLPKEHIMVVNLSGRGDKDMQTVMHHMQQE 399
Cdd:COG0133 321 YLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGLE 399
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
4-396 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 872.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 4 YRNGPDAKGLFGRFGGQYVAETLMPLILDLAREYEKAKDDPAFQEELAYFQRDYVGRPSPLYFAERLTEHCGGAKIYLKR 83
Cdd:PRK04346 1 TYTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLGGAKIYLKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 84 EELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYMGTTDIDRQQANVFRMKLLGAEVI 163
Cdd:PRK04346 81 EDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 164 PVTAGTGTLKDAMNEALRDWVTNVDSTFYLIGTVAGPHPYPAMVRDFQAVIGKETREQLAEKEGRLPDSLVACIGGGSNA 243
Cdd:PRK04346 161 PVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 244 MGLFHPFLDDAGVQIVGVEAAGHGIDTGKHAASLNGGVPGVLHGNRTFLLQDADGQIIDAHSISAGLDYPGIGPEHAWLH 323
Cdd:PRK04346 241 IGIFHPFIDDESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595234 324 DTGRVEYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVFKRAPSLPKEHIMVVNLSGRGDKDMQTVMHHM 396
Cdd:PRK04346 321 DIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLL 393
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
12-396 |
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: 702.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 12 GLFGRFGGQYVAETLMPLILDLAREYEKAKDDPAFQEELAYFQRDYVGRPSPLYFAERLTEHCGGAKIYLKREELNHTGA 91
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGGAKIYLKREDLNHTGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 92 HKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYMGTTDIDRQQANVFRMKLLGAEVIPVTAGTGT 171
Cdd:TIGR00263 81 HKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 172 LKDAMNEALRDWVTNVDSTFYLIGTVAGPHPYPAMVRDFQAVIGKETREQLAEKEGRLPDSLVACIGGGSNAMGLFHPFL 251
Cdd:TIGR00263 161 LKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 252 DDAGVQIVGVEAAGHGIDTGKHAASLNGGVPGVLHGNRTFLLQDADGQIIDAHSISAGLDYPGIGPEHAWLHDTGRVEYT 331
Cdd:TIGR00263 241 DDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATYE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595234 332 SITDDEALEAFHTCCRLEGIIPALESSHALAEVFKRAPSLPKEHIMVVNLSGRGDKDMQTVMHHM 396
Cdd:TIGR00263 321 AITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
8-396 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 697.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 8 PDAKGLFGRFGGQYVAETLMPLILDLAREYEKAKDDPAFQEELAYFQRDYVGRPSPLYFAERLTEHCGGAKIYLKREELN 87
Cdd:PRK13028 9 PDADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEELGGAQIYLKREDLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 88 HTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYMGTTDIDRQQANVFRMKLLGAEVIPVTA 167
Cdd:PRK13028 89 HTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLGAEVVPVTR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 168 GTGTLKDAMNEALRDWVTNVDSTFYLIGTVAGPHPYPAMVRDFQAVIGKETREQLAEKEGRLPDSLVACIGGGSNAMGLF 247
Cdd:PRK13028 169 GGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNAIGLF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 248 HPFLDDAGVQIVGVEAAGHGIDTGKHAASLNGGVPGVLHGNRTFLLQDADGQIIDAHSISAGLDYPGIGPEHAWLHDTGR 327
Cdd:PRK13028 249 SAFLDDESVRLVGVEPAGRGLDLGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPEHAYLKDIGR 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595234 328 VEYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVFKRAPSLPKEHIMVVNLSGRGDKDMQTVMHHM 396
Cdd:PRK13028 329 VEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAPELSKDETILVNLSGRGDKDIDYVAEML 397
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
32-392 |
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: 669.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 32 DLAREYEKAKDDPAFQEELAYFQRDYVGRPSPLYFAERLTEHCGGAKIYLKREELNHTGAHKINNCIGQILLARRMGKKR 111
Cdd:cd06446 5 ELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 112 IIAETGAGMHGVATATVAARFGLQCVIYMGTTDIDRQQANVFRMKLLGAEVIPVTAGTGTLKDAMNEALRDWVTNVDSTF 191
Cdd:cd06446 85 VIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNVEDTH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 192 YLIGTVAGPHPYPAMVRDFQAVIGKETREQLAEKEGRLPDSLVACIGGGSNAMGLFHPFLDDAGVQIVGVEAAGHGIDTG 271
Cdd:cd06446 165 YLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGLETG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 272 KHAASLNGGVPGVLHGNRTFLLQDADGQIIDAHSISAGLDYPGIGPEHAWLHDTGRVEYTSITDDEALEAFHTCCRLEGI 351
Cdd:cd06446 245 GHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLARTEGI 324
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15595234 352 IPALESSHALAEVFKRAPSLPKEHIMVVNLSGRGDKDMQTV 392
Cdd:cd06446 325 IPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
8-400 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 638.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 8 PDAKGLFGRFGGQYVAETLMPLILDLAREYEKAKDDPAFQEELAYFQRDYVGRPSPLYFAERLTEH-----CGGAKIYLK 82
Cdd:PLN02618 13 PDSFGRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEHykradGEGPEIYLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 83 REELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYMGTTDIDRQQANVFRMKLLGAEV 162
Cdd:PLN02618 93 REDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 163 IPVTAGTGTLKDAMNEALRDWVTNVDSTFYLIGTVAGPHPYPAMVRDFQAVIGKETREQLAEKEGRLPDSLVACIGGGSN 242
Cdd:PLN02618 173 RPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 243 AMGLFHPFLDDAGVQIVGVEAAGHGIDTGKHAASLNGGVPGVLHGNRTFLLQDADGQIIDAHSISAGLDYPGIGPEHAWL 322
Cdd:PLN02618 253 AMGLFHEFIDDEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYPGVGPEHSFL 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595234 323 HDTGRVEYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVFKRAPSLPKEHIMVVNLSGRGDKDMQTVMHHMQQES 400
Cdd:PLN02618 333 KDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNTAIKYLQVSS 410
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
8-401 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 634.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 8 PDAKGLFGRFGGQYVAETLMPLILDLAREYEKAKDDPAFQEELAYFQRDYVGRPSPLYFAERLTEHcGGAKIYLKREELN 87
Cdd:PRK13803 218 SDPAGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSDI-YGARIYLKREDLN 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 88 HTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYMGTTDIDRQQANVFRMKLLGAEVIPVTA 167
Cdd:PRK13803 297 HTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIPVLS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 168 GTGTLKDAMNEALRDWVTNVDSTFYLIGTVAGPHPYPAMVRDFQAVIGKETREQLAEKEGRLPDSLVACIGGGSNAMGLF 247
Cdd:PRK13803 377 GSKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIGIF 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 248 HPFLDDAGVQIVGVEAAGHGIDTGKHAASLNGGVPGVLHGNRTFLLQDADGQIIDAHSISAGLDYPGIGPEHAWLHDTGR 327
Cdd:PRK13803 457 YHFLDDPSVKLIGVEAGGKGVNTGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANLFETGR 536
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595234 328 VEYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVFKRAPSLPKEHIMVVNLSGRGDKDMQTVMHHMQQESK 401
Cdd:PRK13803 537 AIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKDIVIVNLSGRGDKDIPTLKEYFENLPQ 610
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
14-391 |
2.91e-176 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 508.03 E-value: 2.91e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 14 FGRFGGQYVAETLMPLILDLAREYEKAKDDPAFQEELAYFQRDYVGRPSPLY----FAERLTEHCG-GAKIYLKREELNH 88
Cdd:PRK13802 279 WGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTeaprFAERVKEKTGlDARVFLKREDLNH 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 89 TGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYMGTTDIDRQQANVFRMKLLGAEVIPVTAG 168
Cdd:PRK13802 359 TGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGAEVVEVTLG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 169 TGTLKDAMNEALRDWVTNVDSTFYLIGTVAGPHPYPAMVRDFQAVIGKETREQLAEKEG-RLPDSLVACIGGGSNAMGLF 247
Cdd:PRK13802 439 DRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiDHPDAICACVGGGSNAIGVM 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 248 HPFLDDAGVQIVGVEAAGHGIDTGKHAASLNGGVP--GVLHGNRTFLLQDADGQIIDAHSISAGLDYPGIGPEHAWLHDT 325
Cdd:PRK13802 519 NAFLDDERVNLYGYEAGGNGPESGKHAIRFAPGTGelGMFQGAKSYLLENDEGQTLDTYSISAGLDYASVGPEHAWLKDI 598
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 326 GRVEYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVFKRAPSLPK---EH-IMVVNLSGRGDKDMQT 391
Cdd:PRK13802 599 GRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAAADLKAkgyEHpVMIVNISGRGDKDMNT 668
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
62-384 |
1.03e-61 |
|
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: 199.28 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 62 SPLYFAERLTEhCGGAKIYLKREELNHTGAHKINNCIGQILLARRMG---KKRIIAETGaGMHGVATATVAARFGLQCVI 138
Cdd:cd00640 1 TPLVRLKRLSK-LGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTG-GNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 139 YMGTTDidrQQANVFRMKLLGAEVIPVtagTGTLKDAMNEALRDWVTNVDSTFyligtvagPHPY-PAMVRDFQAVIGKE 217
Cdd:cd00640 79 VMPEGA---SPEKVAQMRALGAEVVLV---PGDFDDAIALAKELAEEDPGAYY--------VNQFdNPANIAGQGTIGLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 218 TREQLaekEGRLPDSLVACIGGGSNAMGLFHPFL-DDAGVQIVGVEAaghgidtgkhaaslnggvpgvlhgnrtfllqda 296
Cdd:cd00640 145 ILEQL---GGQKPDAVVVPVGGGGNIAGIARALKeLLPNVKVIGVEP--------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 297 dgqiidahsisagldypgigpehawlhdtgrvEYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVFKRAPSLPKEHI 376
Cdd:cd00640 189 --------------------------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKT 236
|
....*...
gi 15595234 377 MVVNLSGR 384
Cdd:cd00640 237 VVVILTGG 244
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
58-390 |
5.37e-54 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 184.61 E-value: 5.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 58 VGRPSPLYFAERLTEHCG-GAKIYLKREELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQC 136
Cdd:PRK12391 74 LWRPTPLIRARRLEKALGtPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACALFGLEC 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 137 VIYMGTTDIDRQQANVFRMKLLGAEVIP----VT-AG----------TGTLKDAMNEALRDWVTNvDSTFYLIGTVAgPH 201
Cdd:PRK12391 154 TVFMVRVSYEQKPYRRSLMETYGAEVIPspsdLTeAGrkilaedpdhPGSLGIAISEAVEDAAKR-PDTKYALGSVL-NH 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 202 pypamVRDFQAVIGKETREQLaEKEGRLPDSLVACIGGGSNAMGLFHPFLDD-----AGVQIVGVEAAG----------- 265
Cdd:PRK12391 232 -----VLLHQTVIGLEAKKQL-ELAGEYPDVVIGCVGGGSNFAGLAFPFLGDklegkKDTRFIAVEPAAcptltkgeyay 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 266 -HGiDTGKHAASL------NGGVPGVLHgnrtfllqdadgqiidahsiSAGLDYPGIGPEHAWLHDTGRVEYTSITDDEA 338
Cdd:PRK12391 306 dFG-DTAGLTPLLkmytlgHDFVPPPIH--------------------AGGLRYHGMAPLVSLLVHEGLIEARAYPQTEV 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15595234 339 LEAFHTCCRLEGIIPALESSHALAEVF---KRAPSLPKEHIMVVNLSGRGDKDMQ 390
Cdd:PRK12391 365 FEAAVLFARTEGIVPAPESSHAIAAAIdeaLKAKEEGEEKVILFNLSGHGLLDLA 419
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
59-390 |
6.83e-45 |
|
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: 160.68 E-value: 6.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 59 GRPSPLYFAERLTEHCGG-AKIYLKREELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCV 137
Cdd:COG1350 76 WRPSPLYRARRLEKALGTpAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALSFACALFGLECT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 138 IYMgttdidrqqanV--------FR---MKLLGAEVIP----VT-AG----------TGTLKDAMNEALRDWVTNvDSTF 191
Cdd:COG1350 156 VYM-----------VkvsyeqkpYRrsmMETYGAEVIPspsdLTeAGrkilaedpdtPGSLGIAISEAVEDAATR-DDTK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 192 YLIGTVAGpHpypamVRDFQAVIGKETREQLaEKEGRLPDSLVACIGGGSNAMGLFHPFLDD-----AGVQIVGVEAAG- 265
Cdd:COG1350 224 YALGSVLN-H-----VLLHQTVIGLEAKKQL-EKAGEYPDVVIGCAGGGSNFAGLAFPFLRDklrgkKDVRFIAVEPAAc 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 266 -----------HGiDTGKHAASL------NGGVPGVLHgnrtfllqdadgqiidahsiSAGLDYPGIGPEHAWLHDTGRV 328
Cdd:COG1350 297 ptltrgvyaydFG-DTAGLTPLLkmytlgHDFIPPPIH--------------------AGGLRYHGMAPLVSQLYHDGLI 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595234 329 EYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVF---KRAPSLPKEHIMVVNLSGRGDKDMQ 390
Cdd:COG1350 356 EAVAYPQLEVFEAGVLFARTEGIVPAPESAHAIKAAIdeaLKCKEEGEEKTILFNLSGHGHFDLA 420
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
60-383 |
1.56e-41 |
|
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: 148.23 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 60 RPSPLYFAERLTEHCGGaKIYLKREELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIY 139
Cdd:pfam00291 6 GPTPLVRLPRLSKELGV-DVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 140 MGTTDIdrqQANVFRMKLLGAEVIPVTAGTGTLKDAMNEALRDWvtnvdSTFYLIGTVAGPHpypamVRDFQAVIGKETR 219
Cdd:pfam00291 85 VPEDAP---PGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEG-----PGAYYINQYDNPL-----NIEGYGTIGLEIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 220 EQLaekeGRLPDSLVACIGGGSNAMGLFHPFLDDAG-VQIVGVEAAGhgidtgkhAASLNGGvpgvLHGNRTFLLQDADg 298
Cdd:pfam00291 152 EQL----GGDPDAVVVPVGGGGLIAGIARGLKELGPdVRVIGVEPEG--------APALARS----LAAGRPVPVPVAD- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 299 qiidahSISAGLDYPGIGPEHAW-LHDTGRVEYTSITDDEALEAFHTCCRLEGIIPALESSHALAEV-FKRAPSLPKEHI 376
Cdd:pfam00291 215 ------TIADGLGVGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDR 288
|
....*..
gi 15595234 377 MVVNLSG 383
Cdd:pfam00291 289 VVVVLTG 295
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
63-395 |
5.28e-19 |
|
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: 87.95 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 63 PLYFAERLTEHCGGaKIYLKREELNHTGAHK-------INncigqilLARRMGKKRII-AETGAGmhGVATATVAARFGL 134
Cdd:COG0498 68 PLVKAPRLADELGK-NLYVKEEGHNPTGSFKdramqvaVS-------LALERGAKTIVcASSGNG--SAALAAYAARAGI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 135 QCVIYM---GTTDIDRQQANVFrmkllGAEVIPVtagTGTLKDAMNEALRdwVTNvDSTFYLIGTVagpHPYpamVRDFQ 211
Cdd:COG0498 138 EVFVFVpegKVSPGQLAQMLTY-----GAHVIAV---DGNFDDAQRLVKE--LAA-DEGLYAVNSI---NPA---RLEGQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 212 AVIGKETREQLaekeGRLPDSLVACIGGGSNAMGLFHPF--LDDAGV-----QIVGVEAAGHG-IdtgkhAASLNGGVPG 283
Cdd:COG0498 201 KTYAFEIAEQL----GRVPDWVVVPTGNGGNILAGYKAFkeLKELGLidrlpRLIAVQATGCNpI-----LTAFETGRDE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 284 VlhgnrtfllqdadgQIIDAHSISAGLDypgIG-P---EHAW--LHDTGRVeYTSITDDEALEAFHTCCRLEGIIPALES 357
Cdd:COG0498 272 Y--------------EPERPETIAPSMD---IGnPsngERALfaLRESGGT-AVAVSDEEILEAIRLLARREGIFVEPAT 333
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15595234 358 SHALA--EVFKRAPSLPKEHIMVVNLSGRGDKDMQTVMHH 395
Cdd:COG0498 334 AVAVAglRKLREEGEIDPDEPVVVLSTGHGLKFPDAVREA 373
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
63-389 |
6.43e-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: 77.55 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 63 PLYFAERLTEHCGgAKIYLKREELNHTGAHKINNCIGQILLARRMGKKR---IIAETGAGMHGVATATVAARFGLQCVIY 139
Cdd:cd01561 4 PLVRLNRLSPGTG-AEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKpgtTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 140 M-GTTDIDRQQAnvfrMKLLGAEVIPVT-AGTGTLKDAMNEAlRDWVTNVDSTFYligtvagPHPY--PAMVRDFQAVIG 215
Cdd:cd01561 83 MpETMSEEKRKL----LRALGAEVILTPeAEADGMKGAIAKA-RELAAETPNAFW-------LNQFenPANPEAHYETTA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 216 KETREQLAEKegrlPDSLVACIGGGSNAMGL------FHPflddaGVQIVGVEAAGHGIdtgkhaasLNGGVPGvlhgnr 289
Cdd:cd01561 151 PEIWEQLDGK----VDAFVAGVGTGGTITGVarylkeKNP-----NVRIVGVDPVGSVL--------FSGGPPG------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 290 tfllqdadgqiidAHSIsagldyPGIGpehawlhdTGRV----------EYTSITDDEALEAFHTCCRLEGIIPALESSH 359
Cdd:cd01561 208 -------------PHKI------EGIG--------AGFIpenldrslidEVVRVSDEEAFAMARRLAREEGLLVGGSSGA 260
|
330 340 350
....*....|....*....|....*....|
gi 15595234 360 ALAEVFKRAPSLPKEHIMVVNLSGRGDKDM 389
Cdd:cd01561 261 AVAAALKLAKRLGPGKTIVTILPDSGERYL 290
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
48-298 |
1.90e-15 |
|
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: 76.61 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 48 EELAYFQRDYVgRPSPLYFAERLTEHCGgAKIYLKREELNHTGAHKIN---NCIGQilLARRMGKKRIIAETgAGMHGVA 124
Cdd:COG1171 12 EAAAARIAGVV-RRTPLLRSPTLSERLG-AEVYLKLENLQPTGSFKLRgayNALAS--LSEEERARGVVAAS-AGNHAQG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 125 TATVAARFGLQCVIYM-GTTDIDRQQAnvfrMKLLGAEVipVTAGtGTLKDAMNEALR-----DWVtnvdstfyLIgtva 198
Cdd:COG1171 87 VAYAARLLGIPATIVMpETAPAVKVAA----TRAYGAEV--VLHG-DTYDDAEAAAAElaeeeGAT--------FV---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 199 gpHPY-PAMVRDFQAVIGKETREQLAEkegrlPDSLVACIGGGS------NAMGLFHPflddaGVQIVGVEAAGHgiDTg 271
Cdd:COG1171 148 --HPFdDPDVIAGQGTIALEILEQLPD-----LDAVFVPVGGGGliagvaAALKALSP-----DIRVIGVEPEGA--AA- 212
|
250 260
....*....|....*....|....*..
gi 15595234 272 kHAASLNGGVPGVLHGNRTFllqdADG 298
Cdd:COG1171 213 -MYRSLAAGEPVTLPGVDTI----ADG 234
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
55-265 |
5.52e-15 |
|
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: 74.83 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 55 RDYVgRPSPLYFAERLTEHCGgAKIYLKREELNHTGAHKINNCIGQILLARRMGKKR-IIAETgAGMHGVATATVAARFG 133
Cdd:cd01562 12 KPVV-RRTPLLTSPTLSELLG-AEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAAS-AGNHAQGVAYAAKLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 134 LQCVIYMGTTDIdrqQANVFRMKLLGAEVIPVTAgtgTLKDAMNEALRDwvtnVDST-FYLIgtvagpHPY--PAMVRDf 210
Cdd:cd01562 89 IPATIVMPETAP---AAKVDATRAYGAEVVLYGE---DFDEAEAKAREL----AEEEgLTFI------HPFddPDVIAG- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595234 211 QAVIGKETREQLAEkegrlPDSLVACIGGG------SNAMGLFHPflddaGVQIVGVEAAG 265
Cdd:cd01562 152 QGTIGLEILEQVPD-----LDAVFVPVGGGgliagiATAVKALSP-----NTKVIGVEPEG 202
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
63-388 |
3.67e-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: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 63 PLYFAERLTEHCGGAKIYLKREELNHTGAHKINnciGQILL---ARRMGKKRIIAETgAGMHGVATATVAARFGLQCVIY 139
Cdd:cd01563 24 PLVRAPRLGERLGGKNLYVKDEGLNPTGSFKDR---GMTVAvskAKELGVKAVACAS-TGNTSASLAAYAARAGIKCVVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 140 MGTtdiDRQQANVFRMKLLGAEVIPVtagTGTLKDAMNEAL----RDW--VTNVDSTFYLIGtvagphpypamvrdfQAV 213
Cdd:cd01563 100 LPA---GKALGKLAQALAYGATVLAV---EGNFDDALRLVRelaeENWiyLSNSLNPYRLEG---------------QKT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 214 IGKETREQLaekEGRLPDSLVACIGGGSNAMGLFHPF--LDDAGV-----QIVGVEAAGhgidtgkhAASLnggVPGVLH 286
Cdd:cd01563 159 IAFEIAEQL---GWEVPDYVVVPVGNGGNITAIWKGFkeLKELGLidrlpRMVGVQAEG--------AAPI---VRAFKE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 287 GNRTFLLQDADGQIidAHSISAGldYPGIGPE--HAwLHDT-GRVEytSITDDEALEAFHTCCRLEGIIPALESSHALAE 363
Cdd:cd01563 225 GKDDIEPVENPETI--ATAIRIG--NPASGPKalRA-VRESgGTAV--AVSDEEILEAQKLLARTEGIFVEPASAASLAG 297
|
330 340
....*....|....*....|....*..
gi 15595234 364 VFKRAPS--LPKEHIMVVNLSGRGDKD 388
Cdd:cd01563 298 LKKLREEgiIDKGERVVVVLTGHGLKD 324
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
61-277 |
1.64e-11 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 65.21 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 61 PSPLYFAERLTEHCGgAKIYLKREELNHTGAHKIN---NCIGQILLARRmgkKRIIAETGAGMH--GVATAtvAARFGLQ 135
Cdd:PRK08639 25 ETPLQRNDYLSEKYG-ANVYLKREDLQPVRSYKLRgayNAISQLSDEEL---AAGVVCASAGNHaqGVAYA--CRHLGIP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 136 CVIYM-GTTdiDRQQanVFRMKLLGAEVIPVTAGTGTLKDAMNEAlRDWVTNVDSTFylI------GTVAGphpypamvr 208
Cdd:PRK08639 99 GVIFMpVTT--PQQK--IDQVRFFGGEFVEIVLVGDTFDDSAAAA-QEYAEETGATF--IppfddpDVIAG--------- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 209 dfQAVIGKETREQLaeKEGRLPDSLVACIGGGSNAMGLFHPFLDDA-GVQIVGVEAAGhgidtgkhAASL 277
Cdd:PRK08639 163 --QGTVAVEILEQL--EKEGSPDYVFVPVGGGGLISGVTTYLKERSpKTKIIGVEPAG--------AASM 220
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
69-391 |
2.46e-11 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 63.91 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 69 RLTEHCGgAKIYLKREELNHTGAHKINNCIGQILLARRMGK----KRIIaETGAGMHGVATATVAARFGLQCVIYM-GTT 143
Cdd:COG0031 21 RLSPGPG-AEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLlkpgGTIV-EATSGNTGIGLAMVAAAKGYRLILVMpETM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 144 DIDRQQAnvfrMKLLGAEVIPVTAGTGTlKDAMNEALRdwvtnvdstfyligtVAGPHP---------YPAMVRDFQAVI 214
Cdd:COG0031 99 SKERRAL----LRAYGAEVVLTPGAEGM-KGAIDKAEE---------------LAAETPgafwpnqfeNPANPEAHYETT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 215 GKETREQLAEKegrlPDSLVACIG-GGSnAMGL------FHPflddaGVQIVGVEAAGhgidtgkhAASLNGGVPGvlhg 287
Cdd:COG0031 159 GPEIWEQTDGK----VDAFVAGVGtGGT-ITGVgrylkeRNP-----DIKIVAVEPEG--------SPLLSGGEPG---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 288 nrtfllqdadgqiidAHSIsagldyPGIGPEH-AWLHDTGRV-EYTSITDDEALEAFHTCCRLEGIIPALESSHALAEVF 365
Cdd:COG0031 217 ---------------PHKI------EGIGAGFvPKILDPSLIdEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAAL 275
|
330 340
....*....|....*....|....*.
gi 15595234 366 KRAPSLPKEHIMVVNLSGRGDKDMQT 391
Cdd:COG0031 276 RLAKRLGPGKTIVTILPDSGERYLST 301
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
62-383 |
2.03e-09 |
|
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: 58.20 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 62 SPLYFAERLTEH-CGGAKIYLKREELNHTGA------HKINNCIGQILlarRMGKKRIIAETGA-GMHGVATATVAARFG 133
Cdd:cd06449 1 TPIQYLPRLSEHlGGKVEIYAKRDDCNSGLAfggnkiRKLEYLLPDAL---AKGADTLVTVGGIqSNHTRQVAAVAAKLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 134 LQCVIYM-----GTTDIDRQQANVFRMKLLGAEVIPVTAGTGT-LKDAMNEALRDwVTNVDSTFYLIGTVAGPHPYPAMV 207
Cdd:cd06449 78 LKCVLVQenwvpYSDAVYDRVGNILLSRIMGADVRLVSAGFDIgIRKSFEEAAEE-VEAKGGKPYVIPAGGSEHPLGGLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 208 RdFQAVIgkETREQLAEkEGRLPDSLVACIGGGSNAMGLFHPF-LDDAGVQIVGVEAAGHGIDTgkhaaslnggVPGVLH 286
Cdd:cd06449 157 Y-VGFVL--EIAQQEEE-LGFKFDSIVVCSVTGSTHAGLSVGLaALGRQRRVIGIDASAKPEKT----------KAQVLR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 287 GNRTFLLqdADGQIIDAHSISagLDYPGIGPEHAwlhdtgrveytsITDDEALEAFHTCCRLEGII--PALE--SSHALA 362
Cdd:cd06449 223 IAQAKLA--EEGLEVKEEDVV--LDDDYAAPEYG------------IPNDETIEAIKLCARLEGIItdPVYEgkSMQGMI 286
|
330 340
....*....|....*....|.
gi 15595234 363 EVFKRAPSLPKEHIMVVNLSG 383
Cdd:cd06449 287 DLVRNGEFKEGSKVLFIHLGG 307
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
50-352 |
2.22e-09 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 58.30 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 50 LAYFQR-DYVGRPSPLYFAERLTEHCGgAKIYLKREELnhTG-------AHKINNCIGQillARRMGKKRIIAeTGA--G 119
Cdd:PRK03910 3 LARFPRlELAGLPTPLEPLPRLSAALG-PDIYIKRDDL--TGlalggnkTRKLEFLLAD---ALAQGADTLIT-AGAiqS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 120 MHGVATATVAARFGLQCVIY----MGTTDIDRQQ-ANVFRMKLLGAEVIPVTAGTGtlkdaMNEALRDWVTNVDStfyli 194
Cdd:PRK03910 76 NHARQTAAAAAKLGLKCVLLlenpVPTEAENYLAnGNVLLDDLFGAEIHVVPAGTD-----MDAQLEELAEELRA----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 195 gtvAGPHPYpamvrdfqaVI----------------GKETREQLAEkEGRLPDSLV-ACIGGGSNAmGLFhpflddAGVQ 257
Cdd:PRK03910 146 ---QGRRPY---------VIpvggsnalgalgyvacALEIAQQLAE-GGVDFDAVVvASGSGGTHA-GLA------AGLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 258 IVGVEAAGHGIDTGKHAASLNGGVPGVLHGNRTFLlqdADGQIIDAHSISAGLDYpgIGPEHAwlhdtgrveytsITDDE 337
Cdd:PRK03910 206 ALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL---GLPTEIPRADIRLWDDY--VGPGYG------------VPTDE 268
|
330
....*....|....*
gi 15595234 338 ALEAFHTCCRLEGII 352
Cdd:PRK03910 269 MLEAVKLLARTEGIL 283
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
55-240 |
2.68e-09 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 58.17 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 55 RDYVgRPSPLYFAERLTEHcGGAKIYLKREELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGL 134
Cdd:PRK06815 15 RPQV-RVTPLEHSPLLSQH-TGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 135 QCVIYMGTtdiDRQQANVFRMKLLGAEVipVTAGTGTLK---DAMNEALRDWVTNVdSTFYLIGTVAGphpypamvrdfQ 211
Cdd:PRK06815 93 PVTVYAPE---QASAIKLDAIRALGAEV--RLYGGDALNaelAARRAAEQQGKVYI-SPYNDPQVIAG-----------Q 155
|
170 180
....*....|....*....|....*....
gi 15595234 212 AVIGKEtreqLAEKEGRLPDSLVACIGGG 240
Cdd:PRK06815 156 GTIGME----LVEQQPDLDAVFVAVGGGG 180
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
75-271 |
8.48e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 56.50 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 75 GGAKIYLKREELNHTGAHK----INNcigqiLLARRMGKKRIIAETGaGMHGVATATVAARFGLQCVIYMGTTdidRQQA 150
Cdd:PRK08246 35 GPAPVWLKLEHLQHTGSFKargaFNR-----LLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVPATVFVPET---APPA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 151 NVFRMKLLGAEVipVTAGTgTLKDAMnEALRDWVTNVDSTFYligtvagpHPY--PAMVRDfQAVIGKETREQlaekeGR 228
Cdd:PRK08246 106 KVARLRALGAEV--VVVGA-EYADAL-EAAQAFAAETGALLC--------HAYdqPEVLAG-AGTLGLEIEEQ-----AP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595234 229 LPDSLVACIGGGsnamGLFhpflddAGV--------QIVGVE-----------AAGHGIDTG 271
Cdd:PRK08246 168 GVDTVLVAVGGG----GLI------AGIaawfegraRVVAVEpegaptlhaalAAGEPVDVP 219
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
44-240 |
8.64e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 56.70 E-value: 8.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 44 PAFQEELAYFQR--DYVgRPSPLYFAERLTeHCGGAKIYLKREELNHTGAHKINNCIGQILLARRMGK--KRIIAETgAG 119
Cdd:PRK06608 5 QNPQNIAAAHNRikQYL-HLTPIVHSESLN-EMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 120 MHGVATATVAARFGLQCVIYM--GTTDIDRQQANVFrmkllGAEVIPvtagTGTLKDAMNEALRDwvtNVDSTFYLigtv 197
Cdd:PRK06608 82 NHGQAVAYASKLFGIKTRIYLplNTSKVKQQAALYY-----GGEVIL----TNTRQEAEEKAKED---EEQGFYYI---- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15595234 198 agpHPYpamvrDFQAVI---GKETREQLAEKeGRLPDSLVACIGGG 240
Cdd:PRK06608 146 ---HPS-----DSDSTIagaGTLCYEALQQL-GFSPDAIFASCGGG 182
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
61-265 |
6.09e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 50.78 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 61 PSPLYFAERLtehcggaKIYLKREELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYM 140
Cdd:PRK08813 39 PTPLHYAERF-------GVWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 141 GTtdidrqqanvfrmkllGAeviPVTAGTGTLKdaMNEALRDWVTNVDSTFYLIGTVAGPHPYP--AMVRDFQAVIGKET 218
Cdd:PRK08813 112 PH----------------GA---PQTKIAGVAH--WGATVRQHGNSYDEAYAFARELADQNGYRflSAFDDPDVIAGQGT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15595234 219 REqlAEKEGRLPDSLVACIGGGSNAMGLFHPfLDDAGVQIVGVEAAG 265
Cdd:PRK08813 171 VG--IELAAHAPDVVIVPIGGGGLASGVALA-LKSQGVRVVGAQVEG 214
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
62-384 |
1.18e-06 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 50.09 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 62 SPLYFAERLTEHCGGAKIYLKREELNHTGAHKINNCIGQILLARRMGKKRIIAETgAGMHGVATATVAARFGLQCVIYmg 141
Cdd:PRK06381 16 TPLLRARKLEEELGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGT-CGNYGASIAYFARLYGLKAVIF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 142 ttdIDRQQAN--VFRMKLLGAEVIPVtagTGTLKDAMnEALRDWVTnvDSTFYligtVAGP---HPYPAMvrDFQAVIGK 216
Cdd:PRK06381 93 ---IPRSYSNsrVKEMEKYGAEIIYV---DGKYEEAV-ERSRKFAK--ENGIY----DANPgsvNSVVDI--EAYSAIAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 217 ETREQLaekeGRLPDSLVACIGGGSNAMGLFHPF--LDDAGV-----QIVGVEAAGHG--IDTGKHAAS--LNGGVPGV- 284
Cdd:PRK06381 158 EIYEAL----GDVPDAVAVPVGNGTTLAGIYHGFrrLYDRGKtsrmpRMIGVSTSGGNqiVESFKRGSSevVDLEVDEIr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 285 -------LHGNRTFLLQDADGQIIDAHsisagldypgigpehawlhdtGRVEYtsITDDEALEAFHTCCRLEGI--IPAL 355
Cdd:PRK06381 234 etavnepLVSYRSFDGDNALEAIYDSH---------------------GYAFG--FSDDEMVKYAELLRRMEGLnaLPAS 290
|
330 340
....*....|....*....|....*....
gi 15595234 356 ESSHALAEVFKRAPSLPKEHIMVvnLSGR 384
Cdd:PRK06381 291 ASALAALVKYLKKNGVNDNVVAV--ITGR 317
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
63-362 |
1.42e-06 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 50.00 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 63 PLYFAERLTEHCGGAKIYLKREELNHTGAHKINNCIGQILLARRMGKKRIIAETgAGMHGVATATVAARFGLQCVIYMgt 142
Cdd:PRK08197 81 PLLPLPRLGKALGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPT-NGNAGAAWAAYAARAGIRATIFM-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 143 tDIDRQQANVFRMKLLGAEVIPVtagTGTLKDA---MNEALRDWvtnvdsTFYLIGTVAGPHpypamvrdfqAVIGKETR 219
Cdd:PRK08197 158 -PADAPEITRLECALAGAELYLV---DGLISDAgkiVAEAVAEY------GWFDVSTLKEPY----------RIEGKKTM 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 220 E-QLAEKEG-RLPDSLVACIGGGSNAMGLFHPFLddagvqivgvEAAGHGIDTGKH----AASLNGGVPGVlhgnRTFLL 293
Cdd:PRK08197 218 GlELAEQLGwRLPDVILYPTGGGVGLIGIWKAFD----------ELEALGWIGGKRprlvAVQAEGCAPIV----KAWEE 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595234 294 QDADGQI-IDAHSISAGLDYP-GIGPE---HAwLHDTGRVEYTsITDDEALEAFHTCCRLEGIIPALESSHALA 362
Cdd:PRK08197 284 GKEESEFwEDAHTVAFGIRVPkALGDFlvlDA-VRETGGCAIA-VSDDAILAAQRELAREEGLFACPEGAATFA 355
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
25-283 |
1.18e-04 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 43.80 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 25 TLMPLILDLAREYEKAKDDPAFQEELAYFQRDY------------VGRpSPLYFAERLTEHCgGAKIYLKREELNHTGAH 92
Cdd:PLN02556 12 SSIPPSSHTLRKLFSTVGSPSFAQRLRDLPKDLpgtkiktdasqlIGK-TPLVYLNKVTEGC-GAYIAAKQEMFQPTSSI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 93 KINNCIGQILLARRM-----GKKRIIAETGAGMhGVATATVAARFGLQCVIYMGT-TDIDRQqanvFRMKLLGAEVI--- 163
Cdd:PLN02556 90 KDRPALAMIEDAEKKnlitpGKTTLIEPTSGNM-GISLAFMAAMKGYKMILTMPSyTSLERR----VTMRAFGAELVltd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 164 PVTAGTGTLKDAMnealrDWVTNVDSTFYLigtvaGPHPYPAMVRDFQAVIGKETREqlaEKEGRLpDSLVACIGGGSNA 243
Cdd:PLN02556 165 PTKGMGGTVKKAY-----ELLESTPDAFML-----QQFSNPANTQVHFETTGPEIWE---DTLGQV-DIFVMGIGSGGTV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15595234 244 MGLFHpFL--DDAGVQIVGVEAAGHGIdtgkhaasLNGGVPG 283
Cdd:PLN02556 231 SGVGK-YLksKNPNVKIYGVEPAESNV--------LNGGKPG 263
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
58-246 |
1.52e-04 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 43.63 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 58 VGRPSPLYFAERLTEHCGGAkIYLKREELNHTGAHKINNCIGQI--LLARRMGKKRIIAETGAGMHGVATAtvAARFGLQ 135
Cdd:PRK12483 34 VARETPLQRAPNLSARLGNQ-VLLKREDLQPVFSFKIRGAYNKMarLPAEQLARGVITASAGNHAQGVALA--AARLGVK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 136 CVIYMGTTdidRQQANVFRMKLLGAEVipVTAGtgtlkDAMNEALRDWVTNVDS---TFYligtvagpHPYPamvrDFQA 212
Cdd:PRK12483 111 AVIVMPRT---TPQLKVDGVRAHGGEV--VLHG-----ESFPDALAHALKLAEEeglTFV--------PPFD----DPDV 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 15595234 213 VIGKET--REQLAEKEGRLpDSLVACIGGGSNAMGL 246
Cdd:PRK12483 169 IAGQGTvaMEILRQHPGPL-DAIFVPVGGGGLIAGI 203
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
62-298 |
1.85e-04 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 43.76 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 62 SPLYFAERLTEHCGgAKIYLKREELNHTGAHKINNCIGQIL-LARRMGKKRIIAETgAGMHGVATATVAARFGLQCVIYM 140
Cdd:PLN02550 110 SPLQLAKKLSERLG-VKVLLKREDLQPVFSFKLRGAYNMMAkLPKEQLDKGVICSS-AGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 141 GTTDIDRQQANVFRmklLGAEVIPVtagtGTLKDAMNEALRDWVTNVDSTFyligtvAGPHPYPAMVRDfQAVIGKETRE 220
Cdd:PLN02550 188 PVTTPEIKWQSVER---LGATVVLV----GDSYDEAQAYAKQRALEEGRTF------IPPFDHPDVIAG-QGTVGMEIVR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 221 QLaekEGRLPDSLVACIGGGSNAMGLFHPFLDDAGVQIVGVEAAghgiDTGKHAASLNggvpgvlHGNRTFLLQD---AD 297
Cdd:PLN02550 254 QH---QGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPS----DANAMALSLH-------HGERVMLDQVggfAD 319
|
.
gi 15595234 298 G 298
Cdd:PLN02550 320 G 320
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
63-181 |
2.33e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 39.56 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 63 PLYFAERLTEHCGgAKIYLKREELNHTGAHKINNCIGQILLARRMGKKRIIAETGAGMHGVATATVAARFGLQCVIYMGT 142
Cdd:PRK07476 21 PLVASASLSARAG-VPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICMSR 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 15595234 143 TDIDRQQANVFRmklLGAEVIPVTAGTgtlKDAMNEALR 181
Cdd:PRK07476 100 LVPANKVDAIRA---LGAEVRIVGRSQ---DDAQAEVER 132
|
|
| Bac_GDH |
pfam05088 |
Bacterial NAD-glutamate dehydrogenase; This family consists of several bacterial proteins ... |
42-134 |
8.58e-03 |
|
Bacterial NAD-glutamate dehydrogenase; This family consists of several bacterial proteins which are closely related to NAD-glutamate dehydrogenase found in Streptomyces clavuligerus. Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyze the reversible oxidative deamination of glutamate to ketoglutarate and ammonia.
Pssm-ID: 428297 [Multi-domain] Cd Length: 1530 Bit Score: 38.63 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595234 42 DDPAFQEEL-AYFqrdyvgrPSPLY--FAERLTEHcggakiYLKREELnhtgAHKINNcigqiLLARRMGK---KRIIAE 115
Cdd:pfam05088 1222 DDPYLARELvRYF-------PTPLRerFAEAIARH------PLRREII----ATQLAN-----DMVNRMGItfvFRLQEE 1279
|
90 100
....*....|....*....|.
gi 15595234 116 TGAGMHGVATATVAAR--FGL 134
Cdd:pfam05088 1280 TGASVADVARAYVIARevFGL 1300
|
|
| |
