|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
1-396 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 795.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 1 MYPYPNEIGRYGDFGGKFVPETLMQPLDEIQTAFKQIKDDPAFREEYYKLLKDYSGRPTALTYADRVTEYLGGAKIYLKR 80
Cdd:PRK04346 1 TYTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLGGAKIYLKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 81 EDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVFMGEEDVARQSLNVFRMKLLGAEVV 160
Cdd:PRK04346 81 EDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 161 PVTSGNGTLKDATNEAIRYWVQHCEDHFYMIGSVVGPHPYPQVVREFQKMIGEEAKDQLKRIEGTMPDKVVACVGGGSNA 240
Cdd:PRK04346 161 PVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 241 MGMFQAFLN-EDVELIGAEAAGKGIDTPLHAATISKGTVGVIHGSLTYLIQDEFGQIIEPYSISAGLDYPGIGPEHAYLH 319
Cdd:PRK04346 241 IGIFHPFIDdESVRLIGVEAAGKGLETGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124494415 320 KSGRVTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDRGQLILVCLSGRGDKDVNTLMNVLEEEV 396
Cdd:PRK04346 321 DIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLLGVIL 397
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
1-395 |
0e+00 |
|
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439903 Cd Length: 400 Bit Score: 794.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 1 MYPYPNEIGRYGDFGGKFVPETLMQPLDEIQTAFKQIKDDPAFREEYYKLLKDYSGRPTALTYADRVTEYLGGAKIYLKR 80
Cdd:COG0133 4 LYSLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLGGAKIYLKR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 81 EDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVFMGEEDVARQSLNVFRMKLLGAEVV 160
Cdd:COG0133 84 EDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAEVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 161 PVTSGNGTLKDATNEAIRYWVQHCEDHFYMIGSVVGPHPYPQVVREFQKMIGEEAKDQLKRIEGTMPDKVVACVGGGSNA 240
Cdd:COG0133 164 PVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGSNA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 241 MGMFQAFLN-EDVELIGAEAAGKGIDTPLHAATISKGTVGVIHGSLTYLIQDEFGQIIEPYSISAGLDYPGIGPEHAYLH 319
Cdd:COG0133 244 IGIFYPFLDdESVRLIGVEAGGKGLETGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHAYLK 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124494415 320 KSGRVTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDRGQLILVCLSGRGDKDVNTLMNVLEEE 395
Cdd:COG0133 324 DTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGLE 399
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
1-393 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 656.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 1 MYPYPNEIGRYGDFGGKFVPETLMQPLDEIQTAFKQIKDDPAFREEYYKLLKDYSGRPTALTYADRVTEYLGGAKIYLKR 80
Cdd:PRK13028 5 LKSMPDADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEELGGAQIYLKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 81 EDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVFMGEEDVARQSLNVFRMKLLGAEVV 160
Cdd:PRK13028 85 EDLNHTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLGAEVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 161 PVTSGNGTLKDATNEAIRYWVQHCEDHFYMIGSVVGPHPYPQVVREFQKMIGEEAKDQLKRIEGTMPDKVVACVGGGSNA 240
Cdd:PRK13028 165 PVTRGGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 241 MGMFQAFLN-EDVELIGAEAAGKGIDTPLHAATISKGTVGVIHGSLTYLIQDEFGQIIEPYSISAGLDYPGIGPEHAYLH 319
Cdd:PRK13028 245 IGLFSAFLDdESVRLVGVEPAGRGLDLGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPEHAYLK 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124494415 320 KSGRVTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDRGQLILVCLSGRGDKDVNTLMNVLE 393
Cdd:PRK13028 325 DIGRVEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAPELSKDETILVNLSGRGDKDIDYVAEMLG 398
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
25-387 |
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: 650.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 25 QPLDEIQTAFKQIKDDPAFREEYYKLLKDYSGRPTALTYADRVTEYLGGAKIYLKREDLNHTGSHKINNALGQALLAKKM 104
Cdd:cd06446 1 PALEELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLGGAKIYLKREDLNHTGAHKINNALGQALLAKRM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 105 GKTKIIAETGAGQHGVAAATVAAKFGFSCTVFMGEEDVARQSLNVFRMKLLGAEVVPVTSGNGTLKDATNEAIRYWVQHC 184
Cdd:cd06446 81 GKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 185 EDHFYMIGSVVGPHPYPQVVREFQKMIGEEAKDQLKRIEGTMPDKVVACVGGGSNAMGMFQAFLN-EDVELIGAEAAGKG 263
Cdd:cd06446 161 EDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINdKDVKLIGVEAGGCG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 264 IDTPLHAATISKGTVGVIHGSLTYLIQDEFGQIIEPYSISAGLDYPGIGPEHAYLHKSGRVTYDSITDEEAVDALKLLSE 343
Cdd:cd06446 241 LETGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLAR 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 124494415 344 KEGILPAIESAHALAKAFKLAKGMDRGQLILVCLSGRGDKDVNT 387
Cdd:cd06446 321 TEGIIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQT 364
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
9-389 |
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: 639.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 9 GRYGDFGGKFVPETLMQPLDEIQTAFKQIKDDPAFREEYYKLLKDYSGRPTALTYADRVTEYLGGAKIYLKREDLNHTGS 88
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGGAKIYLKREDLNHTGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 89 HKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVFMGEEDVARQSLNVFRMKLLGAEVVPVTSGNGT 168
Cdd:TIGR00263 81 HKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 169 LKDATNEAIRYWVQHCEDHFYMIGSVVGPHPYPQVVREFQKMIGEEAKDQLKRIEGTMPDKVVACVGGGSNAMGMFQAFL 248
Cdd:TIGR00263 161 LKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 249 -NEDVELIGAEAAGKGIDTPLHAATISKGTVGVIHGSLTYLIQDEFGQIIEPYSISAGLDYPGIGPEHAYLHKSGRVTYD 327
Cdd:TIGR00263 241 dDPSVQLIGVEAGGLGIDTHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATYE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124494415 328 SITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDRGQLILVCLSGRGDKDVNTLM 389
Cdd:TIGR00263 321 AITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIA 382
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
5-388 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 629.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 5 PNEIGRYGDFGGKFVPETLMQPLDEIQTAFKQIKDDPAFREEYYKLLKDYSGRPTALTYADRVTEYlGGAKIYLKREDLN 84
Cdd:PRK13803 218 SDPAGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSDI-YGARIYLKREDLN 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 85 HTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVFMGEEDVARQSLNVFRMKLLGAEVVPVTS 164
Cdd:PRK13803 297 HTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIPVLS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 165 GNGTLKDATNEAIRYWVQHCEDHFYMIGSVVGPHPYPQVVREFQKMIGEEAKDQLKRIEGTMPDKVVACVGGGSNAMGMF 244
Cdd:PRK13803 377 GSKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIGIF 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 245 QAFLNED-VELIGAEAAGKGIDTPLHAATISKGTVGVIHGSLTYLIQDEFGQIIEPYSISAGLDYPGIGPEHAYLHKSGR 323
Cdd:PRK13803 457 YHFLDDPsVKLIGVEAGGKGVNTGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANLFETGR 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124494415 324 VTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDRGQLILVCLSGRGDKDVNTL 388
Cdd:PRK13803 537 AIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKDIVIVNLSGRGDKDIPTL 601
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
5-395 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 565.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 5 PNEIGRYGDFGGKFVPETLMQPLDEIQTAFKQIKDDPAFREEYYKLLKDYSGRPTALTYADRVTEYL-----GGAKIYLK 79
Cdd:PLN02618 13 PDSFGRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEHYkradgEGPEIYLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 80 REDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVFMGEEDVARQSLNVFRMKLLGAEV 159
Cdd:PLN02618 93 REDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 160 VPVTSGNGTLKDATNEAIRYWVQHCEDHFYMIGSVVGPHPYPQVVREFQKMIGEEAKDQLKRIEGTMPDKVVACVGGGSN 239
Cdd:PLN02618 173 RPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 240 AMGMFQAFLN-EDVELIGAEAAGKGIDTPLHAATISKGTVGVIHGSLTYLIQDEFGQIIEPYSISAGLDYPGIGPEHAYL 318
Cdd:PLN02618 253 AMGLFHEFIDdEDVRLIGVEAAGFGLDSGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYPGVGPEHSFL 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124494415 319 HKSGRVTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDRGQLILVCLSGRGDKDVNTLMNVLEEE 395
Cdd:PLN02618 333 KDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNTAIKYLQVS 409
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
11-387 |
8.73e-161 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 468.35 E-value: 8.73e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 11 YGDFGGKFVPETLMQPLDEIQTAFKQIKDDPAFREEYYKLLKDYSGRPTALT----YADRVTEYLG-GAKIYLKREDLNH 85
Cdd:PRK13802 279 WGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTeaprFAERVKEKTGlDARVFLKREDLNH 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 86 TGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVFMGEEDVARQSLNVFRMKLLGAEVVPVTSG 165
Cdd:PRK13802 359 TGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARMRMLGAEVVEVTLG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 166 NGTLKDATNEAIRYWVQHCEDHFYMIGSVVGPHPYPQVVREFQKMIGEEAKDQLKRIEGT-MPDKVVACVGGGSNAMGMF 244
Cdd:PRK13802 439 DRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGIdHPDAICACVGGGSNAIGVM 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 245 QAFL-NEDVELIGAEAAGKGIDTPLHAATISKGT--VGVIHGSLTYLIQDEFGQIIEPYSISAGLDYPGIGPEHAYLHKS 321
Cdd:PRK13802 519 NAFLdDERVNLYGYEAGGNGPESGKHAIRFAPGTgeLGMFQGAKSYLLENDEGQTLDTYSISAGLDYASVGPEHAWLKDI 598
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124494415 322 GRVTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLA-----KGMDRGQLIlVCLSGRGDKDVNT 387
Cdd:PRK13802 599 GRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAAadlkaKGYEHPVMI-VNISGRGDKDMNT 668
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
59-380 |
8.16e-66 |
|
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: 209.68 E-value: 8.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 59 TALTYADRVTEyLGGAKIYLKREDLNHTGSHKINNALGQALLAKKMG---KTKIIAETGaGQHGVAAATVAAKFGFSCTV 135
Cdd:cd00640 1 TPLVRLKRLSK-LGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTG-GNTGIALAAAAARLGLKCTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 136 FMGEEDvarQSLNVFRMKLLGAEVVPVTsgnGTLKDATNEAIRYWVQHcEDHFYMIGSVvgpHPYpqvVREFQKMIGEEA 215
Cdd:cd00640 79 VMPEGA---SPEKVAQMRALGAEVVLVP---GDFDDAIALAKELAEED-PGAYYVNQFD---NPA---NIAGQGTIGLEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 216 KDQLkriEGTMPDKVVACVGGGSNAMGMFQAF--LNEDVELIGAEAagkgidtplhaatiskgtvgvihgsltyliqdef 293
Cdd:cd00640 146 LEQL---GGQKPDAVVVPVGGGGNIAGIARALkeLLPNVKVIGVEP---------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 294 gqiiepysisagldypgigpehaylhksgrvTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDRGQLI 373
Cdd:cd00640 189 -------------------------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTV 237
|
....*..
gi 124494415 374 LVCLSGR 380
Cdd:cd00640 238 VVILTGG 244
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
46-381 |
5.81e-59 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 197.71 E-value: 5.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 46 EYYKLlkdysGRPTALTYADRVTEYLG-GAKIYLKREDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAAT 124
Cdd:PRK12391 70 EIYRL-----WRPTPLIRARRLEKALGtPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 125 VAAKFGFSCTVFMgeedvARQSLNV--FR---MKLLGAEVVPVTSGN---------------GTLKDATNEAIRYWVQHc 184
Cdd:PRK12391 145 ACALFGLECTVFM-----VRVSYEQkpYRrslMETYGAEVIPSPSDLteagrkilaedpdhpGSLGIAISEAVEDAAKR- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 185 EDHFYMIGSVVgPHpypqvVREFQKMIGEEAKDQLKRIeGTMPDKVVACVGGGSNAMGMFQAFL------NEDVELIGAE 258
Cdd:PRK12391 219 PDTKYALGSVL-NH-----VLLHQTVIGLEAKKQLELA-GEYPDVVIGCVGGGSNFAGLAFPFLgdklegKKDTRFIAVE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 259 aagkgidtPLHAATISKGTVGVIHGS---LT-----YLIQDEFgqiIEPYSISAGLDYPGIGPEHAYLHKSGRVTYDSIT 330
Cdd:PRK12391 292 --------PAACPTLTKGEYAYDFGDtagLTpllkmYTLGHDF---VPPPIHAGGLRYHGMAPLVSLLVHEGLIEARAYP 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 124494415 331 DEEAVDALKLLSEKEGILPAIESAHALAKAFKLA---KGMDRGQLILVCLSGRG 381
Cdd:PRK12391 361 QTEVFEAAVLFARTEGIVPAPESSHAIAAAIDEAlkaKEEGEEKVILFNLSGHG 414
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
46-381 |
2.14e-50 |
|
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport and metabolism]; Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440961 Cd Length: 433 Bit Score: 175.32 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 46 EYYKLlkdysGRPTALTYADRVTEYLGG-AKIYLKREDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAAT 124
Cdd:COG1350 71 EIYRL-----WRPSPLYRARRLEKALGTpAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALSF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 125 VAAKFGFSCTVFMgeedVA--------RQSLnvfrMKLLGAEVVPVTS---------------GNGTLKDATNEAIRYWV 181
Cdd:COG1350 146 ACALFGLECTVYM----VKvsyeqkpyRRSM----METYGAEVIPSPSdlteagrkilaedpdTPGSLGIAISEAVEDAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 182 QHcEDHFYMIGSV---VGPHpypqvvrefQKMIGEEAKDQLKRIeGTMPDKVVACVGGGSNAMGMFQAFLNE------DV 252
Cdd:COG1350 218 TR-DDTKYALGSVlnhVLLH---------QTVIGLEAKKQLEKA-GEYPDVVIGCAGGGSNFAGLAFPFLRDklrgkkDV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 253 ELIGAEaagkgidtPLHAATISKG--------TVGvihgsLTYLIQ-----DEFgqiiEPYSISA-GLDYPGIGPEHAYL 318
Cdd:COG1350 287 RFIAVE--------PAACPTLTRGvyaydfgdTAG-----LTPLLKmytlgHDF----IPPPIHAgGLRYHGMAPLVSQL 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124494415 319 HKSGRVTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLA---KGMDRGQLILVCLSGRG 381
Cdd:COG1350 350 YHDGLIEAVAYPQLEVFEAGVLFARTEGIVPAPESAHAIKAAIDEAlkcKEEGEEKTILFNLSGHG 415
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
57-379 |
3.81e-45 |
|
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: 157.47 E-value: 3.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 57 RPTALTYADRVTEYLGGaKIYLKREDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVF 136
Cdd:pfam00291 6 GPTPLVRLPRLSKELGV-DVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 137 MGEEDVARqslNVFRMKLLGAEVVPVtsgNGTLKDATNEAIRYwVQHcEDHFYMIGSVVGPHpypqvVREFQKMIGEEAK 216
Cdd:pfam00291 85 VPEDAPPG---KLLLMRALGAEVVLV---GGDYDEAVAAAREL-AAE-GPGAYYINQYDNPL-----NIEGYGTIGLEIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 217 DQLkrieGTMPDKVVACVGGGSNAMGMFQAF--LNEDVELIGAEAAGkgidTPLHAATISKGTVGVIHGSLTyliqdefg 294
Cdd:pfam00291 152 EQL----GGDPDAVVVPVGGGGLIAGIARGLkeLGPDVRVIGVEPEG----APALARSLAAGRPVPVPVADT-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 295 qIIEpySISAGlDYPGIGPEHAYLHKSGRVTydSITDEEAVDALKLLSEKEGILPAIESAHALAKA-FKLAKGMDRGQLI 373
Cdd:pfam00291 216 -IAD--GLGVG-DEPGALALDLLDEYVGEVV--TVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRV 289
|
....*.
gi 124494415 374 LVCLSG 379
Cdd:pfam00291 290 VVVLTG 295
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
59-395 |
1.84e-25 |
|
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: 106.44 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 59 TALTYADRVTEYLGGaKIYLKREDLNHTGSHKinnALGQALL---AKKMGKTKII-AETGAGqhGVAAATVAAKFGFSCT 134
Cdd:COG0498 67 TPLVKAPRLADELGK-NLYVKEEGHNPTGSFK---DRAMQVAvslALERGAKTIVcASSGNG--SAALAAYAARAGIEVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 135 VFMGEEDVA----RQslnvfrMKLLGAEVVPVtsgNGTLKDATNEAIRYwvqhCEDH-FYMIGSVvgpHPYpqvVREFQK 209
Cdd:COG0498 141 VFVPEGKVSpgqlAQ------MLTYGAHVIAV---DGNFDDAQRLVKEL----AADEgLYAVNSI---NPA---RLEGQK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 210 MIGEEAKDQLkrieGTMPDKVVACVGGGSNAMGMFQAFLnEDVE---------LIGAEAAG---------KGID--TPLH 269
Cdd:COG0498 202 TYAFEIAEQL----GRVPDWVVVPTGNGGNILAGYKAFK-ELKElglidrlprLIAVQATGcnpiltafeTGRDeyEPER 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 270 AATISKG-TVGVihgsltyliqdefgqiiePYSISAGLDypgigpehaYLHKSGRVTYdSITDEEAVDALKLLSEKEGIL 348
Cdd:COG0498 277 PETIAPSmDIGN------------------PSNGERALF---------ALRESGGTAV-AVSDEEILEAIRLLARREGIF 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 124494415 349 PAIESAHALAKAFKLAK--GMDRGQLILVCLSGRGDKDVNTLMNVLEEE 395
Cdd:COG0498 329 VEPATAVAVAGLRKLREegEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
59-384 |
3.48e-24 |
|
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: 101.90 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 59 TALTYADRVTEYLGGAKIYLKREDLNHTGSHKinnALGQALL---AKKMGKTKIIAETgAGQHGVAAATVAAKFGFSCTV 135
Cdd:cd01563 23 TPLVRAPRLGERLGGKNLYVKDEGLNPTGSFK---DRGMTVAvskAKELGVKAVACAS-TGNTSASLAAYAARAGIKCVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 136 FMGeEDVARQSLNvfRMKLLGAEVVPVtsgNGTLKDATNEAirywVQHCEDH-FYMIGSVvgpHPYpqvvR-EFQKMIGE 213
Cdd:cd01563 99 FLP-AGKALGKLA--QALAYGATVLAV---EGNFDDALRLV----RELAEENwIYLSNSL---NPY----RlEGQKTIAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 214 EAKDQLkriEGTMPDKVVACVGGGSNAMGMFQAFL--------NEDVELIGAEAAGkgidtplhAATISKgtvGVIHGsl 285
Cdd:cd01563 162 EIAEQL---GWEVPDYVVVPVGNGGNITAIWKGFKelkelgliDRLPRMVGVQAEG--------AAPIVR---AFKEG-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 286 tyliQDEFGQIIEPYSISAGLD--YPGIGPEH-AYLHKSGRvTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKAFK 362
Cdd:cd01563 226 ----KDDIEPVENPETIATAIRigNPASGPKAlRAVRESGG-TAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKK 300
|
330 340
....*....|....*....|....
gi 124494415 363 LA-KGM-DRGQLILVCLSGRGDKD 384
Cdd:cd01563 301 LReEGIiDKGERVVVVLTGHGLKD 324
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
73-383 |
1.01e-20 |
|
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: 91.42 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 73 GAKIYLKREDLNHTGSHKINNALGQALLAKKMGKTK---IIAETGAGQHGVAAATVAAKFGFSCTVFMGEE-DVARQSLn 148
Cdd:cd01561 16 GAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKpgtTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETmSEEKRKL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 149 vfrMKLLGAEVVPVTsgnGTLKDATNEAIRYWVQHCEDH--FYMigsvvgPHPY-----PQVvreFQKMIGEEAKDQLKR 221
Cdd:cd01561 95 ---LRALGAEVILTP---EAEADGMKGAIAKARELAAETpnAFW------LNQFenpanPEA---HYETTAPEIWEQLDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 222 iegtMPDKVVACVGGGSNAMGMFQAF--LNEDVELIGAEAAGkgidtplhAATISKGTVGvihgsltyliqdefgqiieP 299
Cdd:cd01561 160 ----KVDAFVAGVGTGGTITGVARYLkeKNPNVRIVGVDPVG--------SVLFSGGPPG-------------------P 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 300 YSIsagldyPGIGpehaylhkSGRVT-------YD---SITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDR 369
Cdd:cd01561 209 HKI------EGIG--------AGFIPenldrslIDevvRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGP 274
|
330
....*....|....
gi 124494415 370 GQLILVCLSGRGDK 383
Cdd:cd01561 275 GKTIVTILPDSGER 288
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
57-379 |
2.88e-19 |
|
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: 87.54 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 57 RPTALTYADRVTEYLGgAKIYLKREDLNHTGSHKINNALGQALLAKKMGKTK-IIAETgAGQHGVAAATVAAKFGFSCTV 135
Cdd:cd01562 16 RRTPLLTSPTLSELLG-AEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAAS-AGNHAQGVAYAAKLLGIPATI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 136 FMgEEDVARQSLNvfRMKLLGAEVVPVtsgNGTLKDATNEAIRYwvqhCEDH-FYMIgsvvgpHPY--PQVVrEFQKMIG 212
Cdd:cd01562 94 VM-PETAPAAKVD--ATRAYGAEVVLY---GEDFDEAEAKAREL----AEEEgLTFI------HPFddPDVI-AGQGTIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 213 EEAKDQLKriegtMPDKVVACVGGGSNAMGMFQAF--LNEDVELIGAE-----------AAGKGIDTPlHAATISKGTVG 279
Cdd:cd01562 157 LEILEQVP-----DLDAVFVPVGGGGLIAGIATAVkaLSPNTKVIGVEpegapamaqslAAGKPVTLP-EVDTIADGLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 280 VIHGSLTY-LIQDEFGQIIepysisagldypgigpehaylhksgrvtydSITDEEAVDALKLLSEKEGILpaIESAHALA 358
Cdd:cd01562 231 KRPGELTFeIIRKLVDDVV------------------------------TVSEDEIAAAMLLLFEREKLV--AEPAGALA 278
|
330 340
....*....|....*....|..
gi 124494415 359 KAFKLAKGMD-RGQLILVCLSG 379
Cdd:cd01562 279 LAALLSGKLDlKGKKVVVVLSG 300
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
57-394 |
3.04e-18 |
|
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: 84.70 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 57 RPTALTYADRVTEYLGgAKIYLKREDLNHTGSHKIN---NALGQalLAKKMGKTKIIAETgAGQHGVAAATVAAKFGFSC 133
Cdd:COG1171 23 RRTPLLRSPTLSERLG-AEVYLKLENLQPTGSFKLRgayNALAS--LSEEERARGVVAAS-AGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 134 TVFMGeEDVARQSLNvfRMKLLGAEVVPVtsgNGTLKDATNEAIRYwvqhCEDH-FYMIgsvvgpHPY--PQVVrEFQKM 210
Cdd:COG1171 99 TIVMP-ETAPAVKVA--ATRAYGAEVVLH---GDTYDDAEAAAAEL----AEEEgATFV------HPFddPDVI-AGQGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 211 IGEEAKDQLKRIegtmpDKVVACVGGGSNAMGMFQAF--LNEDVELIGAE-----------AAGKGIDTPlHAATISKGT 277
Cdd:COG1171 162 IALEILEQLPDL-----DAVFVPVGGGGLIAGVAAALkaLSPDIRVIGVEpegaaamyrslAAGEPVTLP-GVDTIADGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 278 -VGVIhGSLTY-LIQDEFGQIIepysisagldypgigpehaylhksgrvtydSITDEEAVDALKLLSEKEGIL--PAieS 353
Cdd:COG1171 236 aVGRP-GELTFeILRDLVDDIV------------------------------TVSEDEIAAAMRLLLERTKIVvePA--G 282
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 124494415 354 AHALAkAFKLAKGMDRGQLILVCLSGrGDKDVNTLMNVLEE 394
Cdd:COG1171 283 AAALA-ALLAGKERLKGKRVVVVLSG-GNIDPDRLAEILER 321
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
57-380 |
9.61e-18 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 83.20 E-value: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 57 RPTALTYADRVTEyLGGAKIYLKREDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFSCTVF 136
Cdd:PRK06815 19 RVTPLEHSPLLSQ-HTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 137 MgEEDVARQSLNvfRMKLLGAEVVPVtsGNGTLKdATNEAIRYWVQHcedhfymiGSV-VGPHPYPQVVREfQKMIGEEA 215
Cdd:PRK06815 98 A-PEQASAIKLD--AIRALGAEVRLY--GGDALN-AELAARRAAEQQ--------GKVyISPYNDPQVIAG-QGTIGMEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 216 KDQLKRIegtmpDKVVACVGGGSNAMGMFQAF--LNEDVELIGAEaagkgidtPLHAATiskgtvgvIHGSLtyliqdEF 293
Cdd:PRK06815 163 VEQQPDL-----DAVFVAVGGGGLISGIATYLktLSPKTEIIGCW--------PANSPS--------LYTSL------EA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 294 GQIIEPYSI------SAGldypGIGPEHAYLHKSGRVTYDSI--TDEEAVDALKLLSEKEGILpaIESAH--ALAKAFKL 363
Cdd:PRK06815 216 GEIVEVAEQptlsdgTAG----GVEPGAITFPLCQQLIDQKVlvSEEEIKEAMRLIAETDRWL--IEGAAgvALAAALKL 289
|
330
....*....|....*..
gi 124494415 364 AKGMdRGQLILVCLSGR 380
Cdd:PRK06815 290 APRY-QGKKVAVVLCGK 305
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
73-383 |
3.60e-16 |
|
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: 78.55 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 73 GAKIYLKREDLNHTGSHK-------INNALGQALLAKkmGKTkiIAETGAGQHGVAAATVAAKFGFSCTVFMGEE-DVAR 144
Cdd:COG0031 27 GAEIYAKLESFNPGGSVKdrialsmIEDAEKRGLLKP--GGT--IVEATSGNTGIGLAMVAAAKGYRLILVMPETmSKER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 145 QSLnvfrMKLLGAEVVpVTSGNGTLKDATNEAIR-------YWV--QH-----CEDHFymigsvvgphpypqvvrefqKM 210
Cdd:COG0031 103 RAL----LRAYGAEVV-LTPGAEGMKGAIDKAEElaaetpgAFWpnQFenpanPEAHY--------------------ET 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 211 IGEEAKDQLkriEGTmPDKVVACVG-GGSnAMGMFQAF--LNEDVELIGAEAAGkgidtplhAATISKGTVGvihgslTY 287
Cdd:COG0031 158 TGPEIWEQT---DGK-VDAFVAGVGtGGT-ITGVGRYLkeRNPDIKIVAVEPEG--------SPLLSGGEPG------PH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 288 LIQdefgqiiepysisagldypGIGPEH--AYLHKSgrvTYD---SITDEEAVDALKLLSEKEGILPAIESAHALAKAFK 362
Cdd:COG0031 219 KIE-------------------GIGAGFvpKILDPS---LIDeviTVSDEEAFAMARRLAREEGILVGISSGAAVAAALR 276
|
330 340
....*....|....*....|.
gi 124494415 363 LAKGMDRGQLILVCLSGRGDK 383
Cdd:COG0031 277 LAKRLGPGKTIVTILPDSGER 297
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
23-395 |
9.03e-13 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 68.64 E-value: 9.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 23 LMQPLDEIQTAFKQIKddpafreEYYKLlkdysgrpTALTYADRVTEYLGgAKIYLKREDLNHTGSHKINNALGQALLAK 102
Cdd:PRK06608 3 LLQNPQNIAAAHNRIK-------QYLHL--------TPIVHSESLNEMLG-HEIFFKVESLQKTGAFKVRGVLNHLLELK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 103 KMGK--TKIIAETgAGQHGVAAATVAAKFGFSCTVFMgeedvarqSLNVFRMKL-----LGAEVVpvtsgngtLKDATNE 175
Cdd:PRK06608 67 EQGKlpDKIVAYS-TGNHGQAVAYASKLFGIKTRIYL--------PLNTSKVKQqaalyYGGEVI--------LTNTRQE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 176 AIRYWVQHCEDHFYMIgsvvgpHPY--PQVVREfQKMIGEEAKDQLkrieGTMPDKVVACVGGGSNAMGMFQA--FLNED 251
Cdd:PRK06608 130 AEEKAKEDEEQGFYYI------HPSdsDSTIAG-AGTLCYEALQQL----GFSPDAIFASCGGGGLISGTYLAkeLISPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 252 VELIGAEaagkgidtPLHA--ATISkgtvgVIHGSLTYLIQdefgqiiEPYSISAGLDYPGIgpehaylhksGRVTYDSI 329
Cdd:PRK06608 199 SLLIGSE--------PLNAndAYLS-----LKNNKIYRLNY-------SPNTIADGLKTLSV----------SARTFEYL 248
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124494415 330 tdeEAVDALKLLSEKE---------GILPAI---ESAHALAKAFKLAKGMDRGQLILVCLSGrGDKDVNTLMNVLEEE 395
Cdd:PRK06608 249 ---KKLDDFYLVEEYEiyywtawltHLLKVIcepSSAINMVAVVNWLKTQSKPQKLLVILSG-GNIDPILYNELWKED 322
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
59-348 |
2.16e-11 |
|
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: 64.36 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 59 TALTYADRVTEYLGG-AKIYLKREDLN---HTGSHKINNALGQALLAKKMGKTKIIAeTGAGQ--HGVAAATVAAKFGFS 132
Cdd:cd06449 1 TPIQYLPRLSEHLGGkVEIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKGADTLVT-VGGIQsnHTRQVAAVAAKLGLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 133 CTVFM-----GEEDVARQSLNVFRMKLLGAEVVPVTSGNGTlkdatnEAIRYWvqhcEDHFYMIgSVVGPHPYPQVVREF 207
Cdd:cd06449 80 CVLVQenwvpYSDAVYDRVGNILLSRIMGADVRLVSAGFDI------GIRKSF----EEAAEEV-EAKGGKPYVIPAGGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 208 QKMIG--------EEAKDQLKrIEGTMPDKVVACVGGGSNAMGMFQ--AFLNEDVELIGAEAAGKGIDTPLHAATISKGT 277
Cdd:cd06449 149 EHPLGglgyvgfvLEIAQQEE-ELGFKFDSIVVCSVTGSTHAGLSVglAALGRQRRVIGIDASAKPEKTKAQVLRIAQAK 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124494415 278 V---GVIHGSLTYLIQDEFGqiiepysisagldYPGIGpehaylhksgrvtydsITDEEAVDALKLLSEKEGIL 348
Cdd:cd06449 228 LaeeGLEVKEEDVVLDDDYA-------------APEYG----------------IPNDETIEAIKLCARLEGII 272
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
73-376 |
1.56e-10 |
|
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: 61.93 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 73 GAKIYLKREDLNHTGSHK---INNALGQALLAKKMGKTKIIAETGaGQHGVAAATVAAKFGFSCTVFMGEEDVARQslnV 149
Cdd:cd06448 15 GCNVFLKLENLQPSGSFKirgIGHLCQKSAKQGLNECVHVVCSSG-GNAGLAAAYAARKLGVPCTIVVPESTKPRV---V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 150 FRMKLLGAEVVpvtSGNGTLKDATNEAIRywvqhcedhfYMIGSVVGP---HPY--PQVVREFQKMIgEEAKDQLKriEG 224
Cdd:cd06448 91 EKLRDEGATVV---VHGKVWWEADNYLRE----------ELAENDPGPvyvHPFddPLIWEGHSSMV-DEIAQQLQ--SQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 225 TMPDKVVACVGGGSNAMGMFQAFLN---EDVELIGAEAagKGIDTpLHAAtISKGTvgvihgsltyLIQDEfgqiiEPYS 301
Cdd:cd06448 155 EKVDAIVCSVGGGGLLNGIVQGLERngwGDIPVVAVET--EGAHS-LNAS-LKAGK----------LVTLP-----KITS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 302 ISAGLDYPGIGPEHAYLHKSGRVTYDSITDEEAVDALKLLSEKEGIL--PA-------IESAHALAKAFKLAKGMDRGQL 372
Cdd:cd06448 216 VATSLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILvePAcgaalavVYSGKILDLQLEVLLTPLDNVV 295
|
....
gi 124494415 373 ILVC 376
Cdd:cd06448 296 VVVC 299
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
58-261 |
3.03e-10 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 61.36 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 58 PTALTYADRVTE-YlgGAKIYLKREDLNHTGSHKIN---NALGQalLAKKmGKTKIIAETGAGQH--GVAAAtvAAKFGF 131
Cdd:PRK08639 25 ETPLQRNDYLSEkY--GANVYLKREDLQPVRSYKLRgayNAISQ--LSDE-ELAAGVVCASAGNHaqGVAYA--CRHLGI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 132 SCTVFMgeeDVA--RQSLNvfRMKLLGAEVVPVTSGNGTLKDATNEAIRYwvqhCEDH-FYMIgsvvgpHPY--PQVVrE 206
Cdd:PRK08639 98 PGVIFM---PVTtpQQKID--QVRFFGGEFVEIVLVGDTFDDSAAAAQEY----AEETgATFI------PPFddPDVI-A 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124494415 207 FQKMIGEEAKDQLKriEGTMPDKVVACVGGGSNAMGMfQAFLNE---DVELIGAEAAG 261
Cdd:PRK08639 162 GQGTVAVEILEQLE--KEGSPDYVFVPVGGGGLISGV-TTYLKErspKTKIIGVEPAG 216
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
53-348 |
6.58e-10 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 59.85 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 53 DYSGRPTALTYADRVTEYLgGAKIYLKREDLnhTGS-------HKINNALGQALLAkkmGKTKIIAeTGAGQ--HGVAAA 123
Cdd:PRK03910 10 ELAGLPTPLEPLPRLSAAL-GPDIYIKRDDL--TGLalggnktRKLEFLLADALAQ---GADTLIT-AGAIQsnHARQTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 124 TVAAKFGFSCTVFMGE-----EDVARQSLNVFRMKLLGAEVVPVTSGNgtlkDAtNEAIRYWVQHCED---HFYMI---G 192
Cdd:PRK03910 83 AAAAKLGLKCVLLLENpvpteAENYLANGNVLLDDLFGAEIHVVPAGT----DM-DAQLEELAEELRAqgrRPYVIpvgG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 193 S-VVGPHPYPQVVREFQKMIGEEAKDqlkriegtmPDKVVACVG-GGSNA---MGMfqAFLNEDVELIGAeaagkGIDTP 267
Cdd:PRK03910 158 SnALGALGYVACALEIAQQLAEGGVD---------FDAVVVASGsGGTHAglaAGL--AALGPDIPVIGV-----TVSRS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 268 lhAATISKGTVGVIHGSLTYLiqdEFGQIIEPYSISAGLDYpgIGPehAYlhksgrvtydSITDEEAVDALKLLSEKEGI 347
Cdd:PRK03910 222 --AAEQEPKVAKLAQATAELL---GLPTEIPRADIRLWDDY--VGP--GY----------GVPTDEMLEAVKLLARTEGI 282
|
.
gi 124494415 348 L 348
Cdd:PRK03910 283 L 283
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
57-271 |
1.12e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 59.20 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 57 RPTALTYADRVTeyLGGAKIYLKREDLNHTGSHKINNALgQALLAKKMGKTKIIAETGaGQHGVAAATVAAKFGFSCTVF 136
Cdd:PRK08246 22 RRTPVLEADGAG--FGPAPVWLKLEHLQHTGSFKARGAF-NRLLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVPATVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 137 MGEedVARQSlNVFRMKLLGAEVVPVtsgngtlKDATNEAIRYWVQHCEDHfymiGSVVgPHPYPQV-VREFQKMIGEEA 215
Cdd:PRK08246 98 VPE--TAPPA-KVARLRALGAEVVVV-------GAEYADALEAAQAFAAET----GALL-CHAYDQPeVLAGAGTLGLEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 124494415 216 KDQlkrieGTMPDKVVACVGGGSNAMGMFQAFLNEdVELIGAEAAGkgidTP-LHAA 271
Cdd:PRK08246 163 EEQ-----APGVDTVLVAVGGGGLIAGIAAWFEGR-ARVVAVEPEG----APtLHAA 209
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
59-380 |
3.30e-09 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 57.79 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 59 TALTYADRVTEYLGGAKIYLKREDLNHTGSHKINNALGQALLAKKMGKTKIIAETgAGQHGVAAATVAAKFGFSCTVFMG 138
Cdd:PRK06381 16 TPLLRARKLEEELGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGT-CGNYGASIAYFARLYGLKAVIFIP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 139 EedvARQSLNVFRMKLLGAEVVPVtsgNGTLKDATNEAIRYwvqhCEDHFYMIGSVVGPHPYPQVvrEFQKMIGEEAKDQ 218
Cdd:PRK06381 95 R---SYSNSRVKEMEKYGAEIIYV---DGKYEEAVERSRKF----AKENGIYDANPGSVNSVVDI--EAYSAIAYEIYEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 219 LkrieGTMPDKVVACVGGGSNAMGMFQAFlnedVELIGAEAAGKgidTP-LHAATISKGTVGV---IHGS--LTYLIQDE 292
Cdd:PRK06381 163 L----GDVPDAVAVPVGNGTTLAGIYHGF----RRLYDRGKTSR---MPrMIGVSTSGGNQIVesfKRGSseVVDLEVDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 293 FGQ--IIEPYSISAGLDypgigpehayLHKSGRVTYDS------ITDEEAVDALKLLSEKEGI--LPAieSAHALAKAFK 362
Cdd:PRK06381 232 IREtaVNEPLVSYRSFD----------GDNALEAIYDShgyafgFSDDEMVKYAELLRRMEGLnaLPA--SASALAALVK 299
|
330
....*....|....*...
gi 124494415 363 LAKGMDRGQLILVCLSGR 380
Cdd:PRK06381 300 YLKKNGVNDNVVAVITGR 317
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
58-261 |
5.40e-08 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 54.25 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 58 PTALTYADRVteylggaKIYLKREDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAATVAAKFGFsctvfm 137
Cdd:PRK08813 39 PTPLHYAERF-------GVWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGV------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 138 geedvarQSLNVFRMKLLGAEVVPVTSGNGTLKDATN---EAIRYWVQHCEDHFYMIGSVVGPhpyPQVVREfQKMIGEE 214
Cdd:PRK08813 106 -------QAITVMPHGAPQTKIAGVAHWGATVRQHGNsydEAYAFARELADQNGYRFLSAFDD---PDVIAG-QGTVGIE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 124494415 215 akdqlkrIEGTMPDKVVACVGGGSNAMGMFQAFLNEDVELIGAEAAG 261
Cdd:PRK08813 175 -------LAAHAPDVVIVPIGGGGLASGVALALKSQGVRVVGAQVEG 214
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
45-292 |
4.71e-07 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 51.27 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 45 EEYYKLLKDYsGRPTALTYADRVTEYLGGaKIYLKREDLNHTGSHKINNALGQALLAKKMGKTKIIAETGAGQHGVAAAT 124
Cdd:PRK08638 15 IEAKQRLAGR-IRKTPLPRSNYLSERCKG-EIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 125 VAAKFGFSCTVFMGEEdvARQSlNVFRMKLLGAEVVpvtsgngtLKDAT-NEAIRYwvqhCEDHFYMIGSVVgPHPY--P 201
Cdd:PRK08638 93 SCALLGIDGKVVMPKG--APKS-KVAATCGYGAEVV--------LHGDNfNDTIAK----VEEIVEEEGRTF-IPPYddP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 202 QVVREfQKMIGEEAKDQLKRIegtmpDKVVACVGGGSNAMGMFQAF--LNEDVELIGAEA-----------AGKgIDTPL 268
Cdd:PRK08638 157 KVIAG-QGTIGLEILEDLWDV-----DTVIVPIGGGGLIAGIAVALksINPTIHIIGVQSenvhgmaasfyAGE-ITTHR 229
|
250 260
....*....|....*....|....
gi 124494415 269 HAATISKGTVGVIHGSLTYLIQDE 292
Cdd:PRK08638 230 TTGTLADGCDVSRPGNLTYEIVRE 253
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
228-387 |
2.22e-06 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 49.23 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 228 DKVVACVGGGSNAMGM--FQAFLNEDVELIGAEaagkgidtPLHAATISKGTVGvihgslTYLIQdefgqiiepySISAG 305
Cdd:PLN00011 176 DILVAGVGTGGTATGVgkFLKEKNKDIKVCVVE--------PVESAVLSGGQPG------PHLIQ----------GIGSG 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 306 LDypgigPEHAYLHKSGRVTydSITDEEAVDALKLLSEKEGILPAIESAHALAKAFKLAKGMDR-GQLILVCLSGRGDKD 384
Cdd:PLN00011 232 II-----PFNLDLTIVDEII--QVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERY 304
|
...
gi 124494415 385 VNT 387
Cdd:PLN00011 305 LST 307
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
73-390 |
1.80e-05 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 46.39 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 73 GAKIYLKREDLNHTGSHKINNALGQALLAKKMGKTK---IIAETGAGQHGVAAATVAAKFGFSCTVFMGEEdvarQSLNV 149
Cdd:PRK10717 27 GCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKpggTIVEGTAGNTGIGLALVAAARGYKTVIVMPET----QSQEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 150 FRM-KLLGAEVVPVtsgngtlkdatnEAIRYwvqHCEDHFYMIGSVVGphpypqvvREFQKMIGEEA--KDQLK------ 220
Cdd:PRK10717 103 KDLlRALGAELVLV------------PAAPY---ANPNNYVKGAGRLA--------EELVASEPNGAiwANQFDnpanre 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 221 -RIEGTMP----------DKVVACVG-GGSNA-MGMFQAFLNEDVELIGAEaagkgidtPLHAATISKGTVGVIHGslty 287
Cdd:PRK10717 160 aHYETTGPeiweqtdgkvDGFVCAVGtGGTLAgVSRYLKETNPKVKIVLAD--------PTGSALYSYYKTGELKA---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 288 liqdEFGQIIEpysisagldypGIGpehaylhkSGRVTYD----------SITDEEAVDALKLLSEKEGILPAIESAHAL 357
Cdd:PRK10717 228 ----EGSSITE-----------GIG--------QGRITANlegapiddaiRIPDEEALSTAYRLLEEEGLCLGGSSGINV 284
|
330 340 350
....*....|....*....|....*....|...
gi 124494415 358 AKAFKLAKGMDRGQLILVCLSGRGDKDVNTLMN 390
Cdd:PRK10717 285 AAALRLARELGPGHTIVTILCDSGERYQSKLFN 317
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
59-397 |
1.34e-04 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 43.37 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 59 TALTYADRVTEylgG--AKIYLKREDLNHTGSHK-------INNALGQALLakKMGKTKIIAETgAGQHGVAAATVAAKF 129
Cdd:PLN02565 16 TPLVYLNNVVD---GcvARIAAKLEMMEPCSSVKdrigysmITDAEEKGLI--KPGESVLIEPT-SGNTGIGLAFMAAAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 130 GFSCTVFMGeedvARQSLNVfRMKLL--GAEVVPVTSGNGtLKDAtneairywVQHCEDhfymigsVVGPHPYPQVVREF 207
Cdd:PLN02565 90 GYKLIITMP----ASMSLER-RIILLafGAELVLTDPAKG-MKGA--------VQKAEE-------ILAKTPNSYILQQF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 208 Q-----KMIGEEAKDQLKRIEGTMPDKVVACVGGGSN--AMGMFQAFLNEDVELIGAEaagkgidtPLHAATISKGTVGv 280
Cdd:PLN02565 149 EnpanpKIHYETTGPEIWKGTGGKVDAFVSGIGTGGTitGAGKYLKEQNPDIKLYGVE--------PVESAVLSGGKPG- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 281 ihgslTYLIQdefgqiiepySISAGLdYPGIgpehayLHKSGRVTYDSITDEEAVDALKLLSEKEGILPAIESAHALAKA 360
Cdd:PLN02565 220 -----PHKIQ----------GIGAGF-IPGV------LDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAA 277
|
330 340 350
....*....|....*....|....*....|....*...
gi 124494415 361 FKLAK-GMDRGQLILVCLSGRGDKdvnTLMNVLEEEVK 397
Cdd:PLN02565 278 IKIAKrPENAGKLIVVIFPSFGER---YLSSVLFESVK 312
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
61-260 |
1.47e-04 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 43.76 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 61 LTYADRVTEYLGgAKIYLKREDLNHTGSHKINNALG-QALLAKKMGKTKIIAETgAGQHGVAAATVAAKFGFSCTVFMge 139
Cdd:PLN02550 112 LQLAKKLSERLG-VKVLLKREDLQPVFSFKLRGAYNmMAKLPKEQLDKGVICSS-AGNHAQGVALSAQRLGCDAVIAM-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 140 eDVARQSLNVFRMKLLGAEVVPVtsgngtlKDATNEAIRYWVQHCEDHFYMIgsvVGPHPYPQVVREfQKMIGEEAKDQL 219
Cdd:PLN02550 188 -PVTTPEIKWQSVERLGATVVLV-------GDSYDEAQAYAKQRALEEGRTF---IPPFDHPDVIAG-QGTVGMEIVRQH 255
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 124494415 220 KrieGTMPDKVVACVGGGSNA-MGMFQAFLNEDVELIGAEAA 260
Cdd:PLN02550 256 Q---GPLHAIFVPVGGGGLIAgIAAYVKRVRPEVKIIGVEPS 294
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
105-397 |
1.58e-04 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 43.61 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 105 GKTkIIAETGAGQHGVAAATVAAKFGFSCTVFM-GEEDVARQSLnvfrMKLLGAEVV---PVTSGNGTLKDAtnEAIryw 180
Cdd:PLN03013 174 GKS-VLVEPTSGNTGIGLAFIAASRGYRLILTMpASMSMERRVL----LKAFGAELVltdPAKGMTGAVQKA--EEI--- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 181 VQHCEDHfYMIGSVVGPhPYPQVVREfqkMIGEEAKDQLKrieGTMpDKVVACVGGGSN--AMGMFQAFLNEDVELIGAE 258
Cdd:PLN03013 244 LKNTPDA-YMLQQFDNP-ANPKIHYE---TTGPEIWDDTK---GKV-DIFVAGIGTGGTitGVGRFIKEKNPKTQVIGVE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 259 aagkgidtPLHAATISKGTVGvihgsltyliqdefgqiiePYSISagldypGIGPEHAYLHKSGRVTYD--SITDEEAVD 336
Cdd:PLN03013 315 --------PTESDILSGGKPG-------------------PHKIQ------GIGAGFIPKNLDQKIMDEviAISSEEAIE 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124494415 337 ALKLLSEKEGILPAIESAHALAKAFKLAKGMDR-GQLILVCLSGRGDKDVNTLMNVLEEEVK 397
Cdd:PLN03013 362 TAKQLALKEGLMVGISSGAAAAAAIKVAKRPENaGKLIAVSLFASGRDIYTPRCSSLSGKRW 423
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
57-258 |
1.18e-03 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 40.94 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 57 RPTALTYADRVTEYLGGAkIYLKREDLNHTGSHKINNALGQA--LLAKKMGKTKIIAETGAGQHGVAAAtvAAKFGFSCT 134
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQ-VLLKREDLQPVFSFKIRGAYNKMarLPAEQLARGVITASAGNHAQGVALA--AARLGVKAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 135 VFMgeeDVARQSLNVFRMKLLGAEVVpvtsgngTLKDATNEAIRYWVQHCEDHfymigSVVGPHPY--PQVVREfQKMIG 212
Cdd:PRK12483 113 IVM---PRTTPQLKVDGVRAHGGEVV-------LHGESFPDALAHALKLAEEE-----GLTFVPPFddPDVIAG-QGTVA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 124494415 213 EEAkdqLKRIEGTMpDKVVACVGGGSNAMGM--FQAFLNEDVELIGAE 258
Cdd:PRK12483 177 MEI---LRQHPGPL-DAIFVPVGGGGLIAGIaaYVKYVRPEIKVIGVE 220
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
73-257 |
4.83e-03 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 38.79 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 73 GAKIYLKREDLNHTGSHKI---NNALGQaLLAKKMGKTKIIAETGagQHGVAAATVAAKFGFSCTVFMGEEdVARQSLNV 149
Cdd:PRK07476 33 GVPVWLKLETLQPTGSFKLrgaTNALLS-LSAQERARGVVTASTG--NHGRALAYAARALGIRATICMSRL-VPANKVDA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494415 150 FRMklLGAEVVPVtsGNGTlKDATNEAIRywvqHCEDHFYmigSVVGPHPYPQVVREfQKMIGEEAKDQlkriegtMPD- 228
Cdd:PRK07476 109 IRA--LGAEVRIV--GRSQ-DDAQAEVER----LVREEGL---TMVPPFDDPRIIAG-QGTIGLEILEA-------LPDv 168
|
170 180 190
....*....|....*....|....*....|..
gi 124494415 229 -KVVACVGGGSNAMGMFQAF--LNEDVELIGA 257
Cdd:PRK07476 169 aTVLVPLSGGGLASGVAAAVkaIRPAIRVIGV 200
|
|
| |
