|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
10-407 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 848.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 10 FKTGPDERGYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARIFFKR 89
Cdd:PRK04346 1 TYTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLGGAKIYLKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 90 EDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGATVN 169
Cdd:PRK04346 81 EDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 170 PVTAGNGTLKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGSNA 249
Cdd:PRK04346 161 PVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 250 IGLFHPFLDDRDVEIVGVEAGGHGVDIENgHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHSWL 329
Cdd:PRK04346 241 IGIFHPFIDDESVRLIGVEAAGKGLETGK-HAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYL 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516954248 330 RDTGRVQYVPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGKLLGMDI 407
Cdd:PRK04346 320 KDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLLGVIL 397
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
8-407 |
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: 847.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 8 NSFKTGPDERGYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARIFF 87
Cdd:COG0133 2 SSLYSLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLGGAKIYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 88 KREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGAT 167
Cdd:COG0133 82 KREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 168 VNPVTAGNGTLKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGS 247
Cdd:COG0133 162 VVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 248 NAIGLFHPFLDDRDVEIVGVEAGGHGVDIENgHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHS 327
Cdd:COG0133 242 NAIGIFYPFLDDESVRLIGVEAGGKGLETGE-HAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 328 WLRDTGRVQYVPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGKLLGMDI 407
Cdd:COG0133 321 YLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGLED 400
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
18-403 |
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: 686.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 18 GYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARIFFKREDLNHTGS 97
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGGAKIYLKREDLNHTGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 98 HKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGATVNPVTAGNGT 177
Cdd:TIGR00263 81 HKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 178 LKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGSNAIGLFHPFL 257
Cdd:TIGR00263 161 LKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 258 DDRDVEIVGVEAGGHGVDIENgHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHSWLRDTGRVQY 337
Cdd:TIGR00263 241 DDPSVQLIGVEAGGLGIDTHK-HAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATY 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516954248 338 VPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGKLL 403
Cdd:TIGR00263 320 EAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
38-399 |
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: 656.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 38 ELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTR 117
Cdd:cd06446 5 ELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 118 IIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGATVNPVTAGNGTLKDAMNEALRDWVSNVEDTY 197
Cdd:cd06446 85 VIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNVEDTH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 198 YLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGSNAIGLFHPFLDDRDVEIVGVEAGGHGVDIE 277
Cdd:cd06446 165 YLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGLETG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 278 nGHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHSWLRDTGRVQYVPIVDQEALDAFQVCTRVEG 357
Cdd:cd06446 245 -GHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLARTEG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 516954248 358 IIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTV 399
Cdd:cd06446 324 IIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
63-390 |
1.37e-35 |
|
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: 132.43 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 63 YAGRPSKLYFAEGLTKHLGGaRIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPC 142
Cdd:pfam00291 3 LGIGPTPLVRLPRLSKELGV-DVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 143 FVYMGATDVerqAPNVFRMKLLGATVNPVtagNGTLKDAMNEAlRDWVSNVEDTYYLigtaagpHPY-PELVRDFQSVIG 221
Cdd:pfam00291 82 TIVVPEDAP---PGKLLLMRALGAEVVLV---GGDYDEAVAAA-RELAAEGPGAYYI-------NQYdNPLNIEGYGTIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 222 TEaraqMLEQEGRLPDMIIAAVGGGSNAIGLFHPFLDDR-DVEIVGVEAggHGVDIengHAASMTGGRPGVLHGNRTYll 300
Cdd:pfam00291 148 LE----ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGpDVRVIGVEP--EGAPA---LARSLAAGRPVPVPVADTI-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 301 qdADGqileghsvsAGLDYPGVGPEHSWLRDT-GRVQYVPivDQEALDAFQVCTRVEGIIPALESAHAIAQAIKV-APTM 378
Cdd:pfam00291 217 --ADG---------LGVGDEPGALALDLLDEYvGEVVTVS--DEEALEAMRLLARREGIVVEPSSAAALAALKLAlAGEL 283
|
330
....*....|..
gi 516954248 379 AKDKTIIVNLSG 390
Cdd:pfam00291 284 KGGDRVVVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
10-407 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 848.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 10 FKTGPDERGYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARIFFKR 89
Cdd:PRK04346 1 TYTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHLGGAKIYLKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 90 EDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGATVN 169
Cdd:PRK04346 81 EDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMKLLGAEVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 170 PVTAGNGTLKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGSNA 249
Cdd:PRK04346 161 PVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 250 IGLFHPFLDDRDVEIVGVEAGGHGVDIENgHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHSWL 329
Cdd:PRK04346 241 IGIFHPFIDDESVRLIGVEAAGKGLETGK-HAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVGPEHAYL 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516954248 330 RDTGRVQYVPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGKLLGMDI 407
Cdd:PRK04346 320 KDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLLGVIL 397
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
8-407 |
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: 847.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 8 NSFKTGPDERGYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARIFF 87
Cdd:COG0133 2 SSLYSLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLGGAKIYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 88 KREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGAT 167
Cdd:COG0133 82 KREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFRMKLLGAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 168 VNPVTAGNGTLKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGS 247
Cdd:COG0133 162 VVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 248 NAIGLFHPFLDDRDVEIVGVEAGGHGVDIENgHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHS 327
Cdd:COG0133 242 NAIGIFYPFLDDESVRLIGVEAGGKGLETGE-HAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPGVGPEHA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 328 WLRDTGRVQYVPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGKLLGMDI 407
Cdd:COG0133 321 YLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAKYLGLED 400
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
6-404 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 696.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 6 QPNSFKTGPDERGYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARI 85
Cdd:PRK13028 1 MTSYLKSMPDADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEELGGAQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 86 FFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLG 165
Cdd:PRK13028 81 YLKREDLNHTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVFRMKLLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 166 ATVNPVTAGNGTLKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGG 245
Cdd:PRK13028 161 AEVVPVTRGGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 246 GSNAIGLFHPFLDDRDVEIVGVEAGGHGVDIENgHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPE 325
Cdd:PRK13028 241 GSNAIGLFSAFLDDESVRLVGVEPAGRGLDLGE-HAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYPGVGPE 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516954248 326 HSWLRDTGRVQYVPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGKLLG 404
Cdd:PRK13028 320 HAYLKDIGRVEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAPELSKDETILVNLSGRGDKDIDYVAEMLG 398
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
18-403 |
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: 686.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 18 GYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARIFFKREDLNHTGS 97
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEALGGAKIYLKREDLNHTGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 98 HKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGATVNPVTAGNGT 177
Cdd:TIGR00263 81 HKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIPVTSGSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 178 LKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGSNAIGLFHPFL 257
Cdd:TIGR00263 161 LKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 258 DDRDVEIVGVEAGGHGVDIENgHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHSWLRDTGRVQY 337
Cdd:TIGR00263 241 DDPSVQLIGVEAGGLGIDTHK-HAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHETGRATY 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516954248 338 VPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGKLL 403
Cdd:TIGR00263 320 EAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
38-399 |
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: 656.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 38 ELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHLGGARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTR 117
Cdd:cd06446 5 ELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYLGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 118 IIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGATVNPVTAGNGTLKDAMNEALRDWVSNVEDTY 197
Cdd:cd06446 85 VIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWVTNVEDTH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 198 YLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGSNAIGLFHPFLDDRDVEIVGVEAGGHGVDIE 277
Cdd:cd06446 165 YLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGLETG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 278 nGHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHSWLRDTGRVQYVPIVDQEALDAFQVCTRVEG 357
Cdd:cd06446 245 -GHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKLLARTEG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 516954248 358 IIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTV 399
Cdd:cd06446 324 IIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
11-401 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 615.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 11 KTGPDERGYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKhLGGARIFFKRE 90
Cdd:PRK13803 215 KYLSDPAGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSD-IYGARIYLKRE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 91 DLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGATVNP 170
Cdd:PRK13803 294 DLNHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGANVIP 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 171 VTAGNGTLKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGSNAI 250
Cdd:PRK13803 374 VLSGSKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAI 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 251 GLFHPFLDDRDVEIVGVEAGGHGVDIeNGHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHSWLR 330
Cdd:PRK13803 454 GIFYHFLDDPSVKLIGVEAGGKGVNT-GEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHANLF 532
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516954248 331 DTGRVQYVPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGK 401
Cdd:PRK13803 533 ETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKDIVIVNLSGRGDKDIPTLKE 603
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
14-403 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 589.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 14 PDERGYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLYFAEGLTKHL-----GGARIFFK 88
Cdd:PLN02618 13 PDSFGRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEHYkradgEGPEIYLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 89 REDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRMKLLGATV 168
Cdd:PLN02618 93 REDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVFRMRLLGAEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 169 NPVTAGNGTLKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEGRLPDMIIAAVGGGSN 248
Cdd:PLN02618 173 RPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 249 AIGLFHPFLDDRDVEIVGVEAGGHGVDiENGHAASMTGGRPGVLHGNRTYLLQDADGQILEGHSVSAGLDYPGVGPEHSW 328
Cdd:PLN02618 253 AMGLFHEFIDDEDVRLIGVEAAGFGLD-SGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYPGVGPEHSF 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516954248 329 LRDTGRVQYVPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTIIVNLSGRGDKDVHTVGKLL 403
Cdd:PLN02618 332 LKDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNTAIKYL 406
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
7-404 |
5.61e-166 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 481.84 E-value: 5.61e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 7 PNSFKTGPdergYFGIYGGRFVAETLMPLILELQQAYEDAKADPAFKAELQALSTHYAGRPSKLY----FAEGLTKHLG- 81
Cdd:PRK13802 270 PLSEHQGP----YWGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTeaprFAERVKEKTGl 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 82 GARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYMGATDVERQAPNVFRM 161
Cdd:PRK13802 346 DARVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQALNVARM 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 162 KLLGATVNPVTAGNGTLKDAMNEALRDWVSNVEDTYYLIGTAAGPHPYPELVRDFQSVIGTEARAQMLEQEG-RLPDMII 240
Cdd:PRK13802 426 RMLGAEVVEVTLGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiDHPDAIC 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 241 AAVGGGSNAIGLFHPFLDDRDVEIVGVEAGGHGVDiENGHAASMT--GGRPGVLHGNRTYLLQDADGQILEGHSVSAGLD 318
Cdd:PRK13802 506 ACVGGGSNAIGVMNAFLDDERVNLYGYEAGGNGPE-SGKHAIRFApgTGELGMFQGAKSYLLENDEGQTLDTYSISAGLD 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 319 YPGVGPEHSWLRDTGRVQYVPIVDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMaKDK-----TIIVNLSGRGD 393
Cdd:PRK13802 585 YASVGPEHAWLKDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAAADL-KAKgyehpVMIVNISGRGD 663
|
410
....*....|.
gi 516954248 394 KDVHTVGKLLG 404
Cdd:PRK13802 664 KDMNTAGKWFG 674
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
70-391 |
1.38e-59 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 193.89 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 70 LYFAEGLTKhLGGARIFFKREDLNHTGSHKINNCLGQILLAKRMG---KTRIIAETGaGQHGVASATVAARFGLPCFVYM 146
Cdd:cd00640 3 LVRLKRLSK-LGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTG-GNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 147 GATDverQAPNVFRMKLLGATVNPVTagnGTLKDAMNEALRDWVSNvEDTYYLigtaagpHPY-PELVRDFQSVIGTEAR 225
Cdd:cd00640 81 PEGA---SPEKVAQMRALGAEVVLVP---GDFDDAIALAKELAEED-PGAYYV-------NQFdNPANIAGQGTIGLEIL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 226 AQMleqEGRLPDMIIAAVGGGSNAIGLFHPFL-DDRDVEIVGVEAGGHGVDienghaasmtggrpgvlhgnrtyllqdad 304
Cdd:cd00640 147 EQL---GGQKPDAVVVPVGGGGNIAGIARALKeLLPNVKVIGVEPEVVTVS----------------------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 305 gqileghsvsagldypgvgpehswlrdtgrvqyvpivDQEALDAFQVCTRVEGIIPALESAHAIAQAIKVAPTMAKDKTI 384
Cdd:cd00640 195 -------------------------------------DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTV 237
|
....*..
gi 516954248 385 IVNLSGR 391
Cdd:cd00640 238 VVILTGG 244
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
65-392 |
1.03e-58 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 197.32 E-value: 1.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 65 GRPSKLYFAEGLTKHLG-GARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCF 143
Cdd:PRK12391 75 WRPTPLIRARRLEKALGtPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACALFGLECT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 144 VYMGATDVErQAPnvFR---MKLLGATVNP----VT-AG----------NGTLKDAMNEALRDWVSNvEDTYYLIGTAAg 205
Cdd:PRK12391 155 VFMVRVSYE-QKP--YRrslMETYGAEVIPspsdLTeAGrkilaedpdhPGSLGIAISEAVEDAAKR-PDTKYALGSVL- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 206 PHpypelVRDFQSVIGTEARAQMlEQEGRLPDMIIAAVGGGSNAIGLFHPFLDD-----RDVEIVGVEAgghgvdiengh 280
Cdd:PRK12391 230 NH-----VLLHQTVIGLEAKKQL-ELAGEYPDVVIGCVGGGSNFAGLAFPFLGDklegkKDTRFIAVEP----------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 281 AA--SMTGGR--------PGVLHGNRTYLLqdadgqileGHSV------SAGLDYPGVGPEHSWLRDTGRVQYVPIVDQE 344
Cdd:PRK12391 293 AAcpTLTKGEyaydfgdtAGLTPLLKMYTL---------GHDFvpppihAGGLRYHGMAPLVSLLVHEGLIEARAYPQTE 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 516954248 345 ALDAFQVCTRVEGIIPALESAHAIAQAIKVApTMAKD----KTIIVNLSGRG 392
Cdd:PRK12391 364 VFEAAVLFARTEGIVPAPESSHAIAAAIDEA-LKAKEegeeKVILFNLSGHG 414
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
65-392 |
1.17e-52 |
|
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport and metabolism]; Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440961 Cd Length: 433 Bit Score: 181.48 E-value: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 65 GRPSKLYFAEGLTKHLGG-ARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCF 143
Cdd:COG1350 76 WRPSPLYRARRLEKALGTpAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALSFACALFGLECT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 144 VYMgatdVE---RQAPnvFR---MKLLGATVNP----VT-AG----------NGTLKDAMNEALRDWVSNvEDTYYLIGT 202
Cdd:COG1350 156 VYM----VKvsyEQKP--YRrsmMETYGAEVIPspsdLTeAGrkilaedpdtPGSLGIAISEAVEDAATR-DDTKYALGS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 203 AAGpHpypelVRDFQSVIGTEARAQMlEQEGRLPDMIIAAVGGGSNAIGLFHPFLDD-----RDVEIVGVEAgghgvdie 277
Cdd:COG1350 229 VLN-H-----VLLHQTVIGLEAKKQL-EKAGEYPDVVIGCAGGGSNFAGLAFPFLRDklrgkKDVRFIAVEP-------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 278 nghAA--SMTGGRPGVLHGN--------RTYLLqdadgqileGH-----SVSA-GLDYPGVGPEHSWLRDTGRVQYVPIV 341
Cdd:COG1350 294 ---AAcpTLTRGVYAYDFGDtagltpllKMYTL---------GHdfippPIHAgGLRYHGMAPLVSQLYHDGLIEAVAYP 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 516954248 342 DQEALDAFQVCTRVEGIIPALESAHAIAQAIKVA---PTMAKDKTIIVNLSGRG 392
Cdd:COG1350 362 QLEVFEAGVLFARTEGIVPAPESAHAIKAAIDEAlkcKEEGEEKTILFNLSGHG 415
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
63-390 |
1.37e-35 |
|
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: 132.43 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 63 YAGRPSKLYFAEGLTKHLGGaRIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPC 142
Cdd:pfam00291 3 LGIGPTPLVRLPRLSKELGV-DVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 143 FVYMGATDVerqAPNVFRMKLLGATVNPVtagNGTLKDAMNEAlRDWVSNVEDTYYLigtaagpHPY-PELVRDFQSVIG 221
Cdd:pfam00291 82 TIVVPEDAP---PGKLLLMRALGAEVVLV---GGDYDEAVAAA-RELAAEGPGAYYI-------NQYdNPLNIEGYGTIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 222 TEaraqMLEQEGRLPDMIIAAVGGGSNAIGLFHPFLDDR-DVEIVGVEAggHGVDIengHAASMTGGRPGVLHGNRTYll 300
Cdd:pfam00291 148 LE----ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGpDVRVIGVEP--EGAPA---LARSLAAGRPVPVPVADTI-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 301 qdADGqileghsvsAGLDYPGVGPEHSWLRDT-GRVQYVPivDQEALDAFQVCTRVEGIIPALESAHAIAQAIKV-APTM 378
Cdd:pfam00291 217 --ADG---------LGVGDEPGALALDLLDEYvGEVVTVS--DEEALEAMRLLARREGIVVEPSSAAALAALKLAlAGEL 283
|
330
....*....|..
gi 516954248 379 AKDKTIIVNLSG 390
Cdd:pfam00291 284 KGGDRVVVVLTG 295
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
66-289 |
3.48e-16 |
|
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: 78.68 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 66 RPSKLYFAEGLTKHLGgARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTR-IIAETgAGQHGVASATVAARFGLPCFV 144
Cdd:cd01562 16 RRTPLLTSPTLSELLG-AEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKgVVAAS-AGNHAQGVAYAAKLLGIPATI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 145 YMGATdverqAPN--VFRMKLLGATVnpVTAGNgTLKDAMNEALRDwvsnVEDT-YYLIgtaagpHPY--PELVRDfQSV 219
Cdd:cd01562 94 VMPET-----APAakVDATRAYGAEV--VLYGE-DFDEAEAKAREL----AEEEgLTFI------HPFddPDVIAG-QGT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516954248 220 IGTEaraqMLEQEGRLpDMIIAAVGGG------SNAIGLFHPflddrDVEIVGVEAGGhgvdiENGHAASMTGGRP 289
Cdd:cd01562 155 IGLE----ILEQVPDL-DAVFVPVGGGgliagiATAVKALSP-----NTKVIGVEPEG-----APAMAQSLAAGKP 215
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
70-406 |
7.59e-14 |
|
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: 72.54 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 70 LYFAEGLTKHLGGaRIFFKREDLNHTGSHK-------INnclgqilLAKRMGKTRIIAETgAGQHGVASATVAARFGLPC 142
Cdd:COG0498 69 LVKAPRLADELGK-NLYVKEEGHNPTGSFKdramqvaVS-------LALERGAKTIVCAS-SGNGSAALAAYAARAGIEV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 143 FVYMGATDVerqaPNVFR--MKLLGATVNPVtagNGTLKDAMNEALRdwVSNVEDTYyligtAAGP-HPYpelVRDFQSV 219
Cdd:COG0498 140 FVFVPEGKV----SPGQLaqMLTYGAHVIAV---DGNFDDAQRLVKE--LAADEGLY-----AVNSiNPA---RLEGQKT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 220 IGTEAraqmLEQEGRLPDMIIAAVGGGSNAIGLFHPFLDDRDV-------EIVGVEAGGHGvDIenghAASMTGGRPGVl 292
Cdd:COG0498 203 YAFEI----AEQLGRVPDWVVVPTGNGGNILAGYKAFKELKELglidrlpRLIAVQATGCN-PI----LTAFETGRDEY- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 293 hgnrtyllqdadgQILEGHSVSAGLDYPG-VGPEHSW--LRDTGRVqYVPIVDQEALDAFQVCTRVEGIIPALESAHAIA 369
Cdd:COG0498 273 -------------EPERPETIAPSMDIGNpSNGERALfaLRESGGT-AVAVSDEEILEAIRLLARREGIFVEPATAVAVA 338
|
330 340 350
....*....|....*....|....*....|....*....
gi 516954248 370 QAIKVA--PTMAKDKTIIVNLSGRGDKDVHTVGKLLGMD 406
Cdd:COG0498 339 GLRKLReeGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
70-395 |
2.34e-13 |
|
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: 70.31 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 70 LYFAEGLTKHLGGARIFFKREDLNHTGSHKInncLGQILL---AKRMGKTRIIAETgAGQHGVASATVAARFGLPCFVYM 146
Cdd:cd01563 25 LVRAPRLGERLGGKNLYVKDEGLNPTGSFKD---RGMTVAvskAKELGVKAVACAS-TGNTSASLAAYAARAGIKCVVFL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 147 GAtDVERQapNVFRMKLLGATVNPVtagNGTLKDAMNEAL----RDW--VSNVEDTYYLIGtaagphpypelvrdfQSVI 220
Cdd:cd01563 101 PA-GKALG--KLAQALAYGATVLAV---EGNFDDALRLVRelaeENWiyLSNSLNPYRLEG---------------QKTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 221 GTEaraqMLEQEG-RLPDMIIAAVGGGSNAIGLFHPFLD-------DRDVEIVGVEAggHGVDienghaasmtggrPGVL 292
Cdd:cd01563 160 AFE----IAEQLGwEVPDYVVVPVGNGGNITAIWKGFKElkelgliDRLPRMVGVQA--EGAA-------------PIVR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 293 HGNRTyllQDADGQILEGHSVSAGLDypgVGPEHSW------LRDTGRvQYVPIVDQEALDAFQVCTRVEGIIPALESAH 366
Cdd:cd01563 221 AFKEG---KDDIEPVENPETIATAIR---IGNPASGpkalraVRESGG-TAVAVSDEEILEAQKLLARTEGIFVEPASAA 293
|
330 340 350
....*....|....*....|....*....|.
gi 516954248 367 AIAQAIKVAP--TMAKDKTIIVNLSGRGDKD 395
Cdd:cd01563 294 SLAGLKKLREegIIDKGERVVVVLTGHGLKD 324
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
66-297 |
4.14e-12 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 66.60 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 66 RPSKLYFAEGLTKHLGgARIFFKREDLNHTGSHKIN---NCLGQilLAKRMGKTRIIAETgAGQHGVASATVAARFGLPC 142
Cdd:COG1171 23 RRTPLLRSPTLSERLG-AEVYLKLENLQPTGSFKLRgayNALAS--LSEEERARGVVAAS-AGNHAQGVAYAARLLGIPA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 143 FVYM--GATDVERQApnvfrMKLLGATVnpVTAGnGTLKDAMNEALRDwvsnVEDT-YYLIgtaagpHPY-PELVRDFQS 218
Cdd:COG1171 99 TIVMpeTAPAVKVAA-----TRAYGAEV--VLHG-DTYDDAEAAAAEL----AEEEgATFV------HPFdDPDVIAGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 219 VIGTEaraqMLEQEGRLpDMIIAAVGGGS------NAIGLFHPflddrDVEIVGVEAGGHgvdieNGHAASMTGGRPGVL 292
Cdd:COG1171 161 TIALE----ILEQLPDL-DAVFVPVGGGGliagvaAALKALSP-----DIRVIGVEPEGA-----AAMYRSLAAGEPVTL 225
|
....*
gi 516954248 293 HGNRT 297
Cdd:COG1171 226 PGVDT 230
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
82-394 |
1.39e-11 |
|
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: 64.84 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 82 GARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTR---IIAETGAGQHGVASATVAARFGLPCFVYMGAT-DVERQApn 157
Cdd:cd01561 16 GAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKpgtTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETmSEEKRK-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 158 vfRMKLLGATVNPVT-AGNGTLKDAMNEALR------DWV--------SNVEDTYYliGTAagphpyPELVRDFqsvigt 222
Cdd:cd01561 94 --LLRALGAEVILTPeAEADGMKGAIAKARElaaetpNAFwlnqfenpANPEAHYE--TTA------PEIWEQL------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 223 earaqmleqEGRLpDMIIAAVG-GGSNA-IGLF----HPflddrDVEIVGVEAGGHGVDIENGHAASMTGG-----RPGV 291
Cdd:cd01561 158 ---------DGKV-DAFVAGVGtGGTITgVARYlkekNP-----NVRIVGVDPVGSVLFSGGPPGPHKIEGigagfIPEN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 292 LHGNRtyllqdadgqILEGHSVSagldypgvgpehswlrdtgrvqyvpivDQEALDAFQVCTRVEGIIPALESAHAIAQA 371
Cdd:cd01561 223 LDRSL----------IDEVVRVS---------------------------DEEAFAMARRLAREEGLLVGGSSGAAVAAA 265
|
330 340
....*....|....*....|...
gi 516954248 372 IKVAPTMAKDKTIIVNLSGRGDK 394
Cdd:cd01561 266 LKLAKRLGPGKTIVTILPDSGER 288
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
76-246 |
4.71e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 63.64 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 76 LTKHLGGARIFFKREDLNHTGSHKINNCLGQILLAKRMGK--TRIIAETgAGQHGVASATVAARFGLPCFVYM--GATDV 151
Cdd:PRK06608 31 SLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TGNHGQAVAYASKLFGIKTRIYLplNTSKV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 152 ERQAPNVFrmkllGATVNpVTAgngTLKDAMNEALRDwvsNVEDTYYLigtaagpHPYpelvrDFQSVI---GTeARAQM 228
Cdd:PRK06608 110 KQQAALYY-----GGEVI-LTN---TRQEAEEKAKED---EEQGFYYI-------HPS-----DSDSTIagaGT-LCYEA 164
|
170
....*....|....*...
gi 516954248 229 LEQEGRLPDMIIAAVGGG 246
Cdd:PRK06608 165 LQQLGFSPDAIFASCGGG 182
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
80-288 |
7.01e-11 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 62.66 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 80 LGGARIFFKREDLNHTGSHKINNCLGQiLLAKRMGKTRIIAETGaGQHGVASATVAARFGLPCFVYMGATdverqAP--N 157
Cdd:PRK08246 34 FGPAPVWLKLEHLQHTGSFKARGAFNR-LLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVPATVFVPET-----APpaK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 158 VFRMKLLGATVnpVTAGnGTLKDAMnEALRDWvsnVEDTyyligTAAGPHPY--PELVRDfQSVIGTEaraqmLEQEGRL 235
Cdd:PRK08246 107 VARLRALGAEV--VVVG-AEYADAL-EAAQAF---AAET-----GALLCHAYdqPEVLAG-AGTLGLE-----IEEQAPG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516954248 236 PDMIIAAVGGGSNAIGLFHPFLDDRDVeiVGVE-----------AGGHGVDIE-NGHAASMTGGR 288
Cdd:PRK08246 169 VDTVLVAVGGGGLIAGIAAWFEGRARV--VAVEpegaptlhaalAAGEPVDVPvSGIAADSLGAR 231
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
82-289 |
8.87e-11 |
|
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: 62.70 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 82 GARIFFKREDLNHTGSHK---INNCLGQILLAKRMGKTRIIAETGaGQHGVASATVAARFGLPCFVYMGATDVERQapnV 158
Cdd:cd06448 15 GCNVFLKLENLQPSGSFKirgIGHLCQKSAKQGLNECVHVVCSSG-GNAGLAAAYAARKLGVPCTIVVPESTKPRV---V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 159 FRMKLLGATVnpVTAGNgTLKDAMNEALRDWVSNVEDTYYLigtaagpHPYP-ELVRDFQSVIGTEARAQMLEQEgrLPD 237
Cdd:cd06448 91 EKLRDEGATV--VVHGK-VWWEADNYLREELAENDPGPVYV-------HPFDdPLIWEGHSSMVDEIAQQLQSQE--KVD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516954248 238 MIIAAVGGGSNAIGLFHPfLDDR---DVEIVGVEAggHGVDIENghaASMTGGRP 289
Cdd:cd06448 159 AIVCSVGGGGLLNGIVQG-LERNgwgDIPVVAVET--EGAHSLN---ASLKAGKL 207
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
66-267 |
7.09e-10 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 59.71 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 66 RPSKLYFAEGLTKHlGGARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVY 145
Cdd:PRK06815 19 RVTPLEHSPLLSQH-TGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 146 M--GATDVERQApnvfrMKLLGATVnpVTAGNGTLKDAMneALRDWVSNVEDTYYligtaagpHPYPEL-VRDFQSVIGT 222
Cdd:PRK06815 98 ApeQASAIKLDA-----IRALGAEV--RLYGGDALNAEL--AARRAAEQQGKVYI--------SPYNDPqVIAGQGTIGM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516954248 223 EaraqMLEQEGRLpDMIIAAVGGGS--NAIGLFHPFLDDrDVEIVGV 267
Cdd:PRK06815 161 E----LVEQQPDL-DAVFVAVGGGGliSGIATYLKTLSP-KTEIIGC 201
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
76-256 |
1.34e-07 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 53.08 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 76 LTKHLGGARIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETgAGQHGVASATVAARFGLPCFVYMGATDVErqa 155
Cdd:PRK08197 88 LGKALGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPT-NGNAGAAWAAYAARAGIRATIFMPADAPE--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 156 PNVFRMKLLGATVNPVtagNGTLKDA---MNEALRDW----VSNVEDTYYLIGtaagphpypelvrdfQSVIGTEaraqM 228
Cdd:PRK08197 164 ITRLECALAGAELYLV---DGLISDAgkiVAEAVAEYgwfdVSTLKEPYRIEG---------------KKTMGLE----L 221
|
170 180
....*....|....*....|....*....
gi 516954248 229 LEQEG-RLPDMIIAAVGGGSNAIGLFHPF 256
Cdd:PRK08197 222 AEQLGwRLPDVILYPTGGGVGLIGIWKAF 250
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
76-359 |
1.19e-06 |
|
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.
Pssm-ID: 107210 Cd Length: 307 Bit Score: 49.73 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 76 LTKHLGGAR-IFFKREDLN---HTGSHKINNCLGQILLAKRMGKTRIIAeTGAGQ--HGVASATVAARFGLPC------F 143
Cdd:cd06449 9 LSEHLGGKVeIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKGADTLVT-VGGIQsnHTRQVAAVAAKLGLKCvlvqenW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 144 VYMGATDVERQApNVFRMKLLGATVNPVTAGNGTlkdAMNEALRDWVSNVEDT---YYLIGTAAGPHPYPEL--VRDFQS 218
Cdd:cd06449 88 VPYSDAVYDRVG-NILLSRIMGADVRLVSAGFDI---GIRKSFEEAAEEVEAKggkPYVIPAGGSEHPLGGLgyVGFVLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 219 VigtearAQMLEQEGRLPDMIIAAVGGGSNAIGLFHPF-LDDRDVEIVGVEAGGHGVDIenghaasmtggRPGVLHgnrt 297
Cdd:cd06449 164 I------AQQEEELGFKFDSIVVCSVTGSTHAGLSVGLaALGRQRRVIGIDASAKPEKT-----------KAQVLR---- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516954248 298 yLLQDADGQILEGHSVS-AGLDYPGVGPEHSwlrdtgrvqyvpIVDQEALDAFQVCTRVEGII 359
Cdd:cd06449 223 -IAQAKLAEEGLEVKEEdVVLDDDYAAPEYG------------IPNDETIEAIKLCARLEGII 272
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
82-285 |
4.52e-06 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 48.65 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 82 GARIFFKREDLNHTGSHKIN---NCLGQilLAKRmGKTRIIAETGAGQH--GVASAtvAARFGLPCFVYMGATdVERQap 156
Cdd:PRK08639 39 GANVYLKREDLQPVRSYKLRgayNAISQ--LSDE-ELAAGVVCASAGNHaqGVAYA--CRHLGIPGVIFMPVT-TPQQ-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 157 NVFRMKLLGATVNPVTAGNGTLKDAMNEALRDwvsnVEDT-YYLIgtaagpHPYpelvrDFQSVI---GTEArAQMLEQE 232
Cdd:PRK08639 111 KIDQVRFFGGEFVEIVLVGDTFDDSAAAAQEY----AEETgATFI------PPF-----DDPDVIagqGTVA-VEILEQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 516954248 233 GRL--PDMIIAAVGGGSNAIGLFHpFLDDR--DVEIVGVEAGGhgvdienghAASMT 285
Cdd:PRK08639 175 EKEgsPDYVFVPVGGGGLISGVTT-YLKERspKTKIIGVEPAG---------AASMK 221
|
|
| PRK12390 |
PRK12390 |
1-aminocyclopropane-1-carboxylate deaminase; Provisional |
67-359 |
2.82e-05 |
|
1-aminocyclopropane-1-carboxylate deaminase; Provisional
Pssm-ID: 183494 Cd Length: 337 Bit Score: 45.79 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 67 PSKLYFAEGLTKHLGG-ARIFFKREDLNhTGshkinnclgqilLAKRMGKTR----IIAETGAGQH-------GVAS--- 131
Cdd:PRK12390 15 PTPIHPLKRLSAHLGGkVELYAKREDCN-SG------------LAFGGNKTRkleyLVPDALAQGAdtlvsigGVQSnht 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 132 ---ATVAARFGLPCFV----YMGATD-VERQAPNVFRMKLLGATVNPVTAGNGT-LKDAMNEALRDwVSNVEDTYYLIGT 202
Cdd:PRK12390 82 rqvAAVAAHLGMKCVLvqenWVNYEDaVYDRVGNILLSRIMGADVRLVPDGFDIgIRKSWEDALED-VRAAGGKPYAIPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 203 AAGPHPYPELvrdfqSVIG--TEARAQmlEQE-GRLPDMIIAAVGGGSNAIGLFHPF-LDDRDVEIVGVEAGG------- 271
Cdd:PRK12390 161 GASDHPLGGL-----GFVGfaEEVRAQ--EAElGFKFDYIVVCSVTGSTQAGMVVGFaADGRARRVIGIDASAkpeqtra 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 272 HGVDIENGHAASMTGGRPgvlhgnrtylLQDADGQILEGHSvsagldypgvGPEHSwlrdtgrvqyVPivDQEALDAFQV 351
Cdd:PRK12390 234 QVLRIARNTAELVELGRD----------ITEDDVVLDERYA----------GPEYG----------LP--NEGTLEAIRL 281
|
....*...
gi 516954248 352 CTRVEGII 359
Cdd:PRK12390 282 CARLEGML 289
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
67-275 |
1.33e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 43.85 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 67 PSKLYFAEGLTkhlggarIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVYM 146
Cdd:PRK08813 39 PTPLHYAERFG-------VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 147 --GATdverqAPNVFRMKLLGATVNpvTAGNgtlkdAMNEALRDWVSNVEDTYYLIGTAAGPhpyPELVRDfQSVIGTEA 224
Cdd:PRK08813 112 phGAP-----QTKIAGVAHWGATVR--QHGN-----SYDEAYAFARELADQNGYRFLSAFDD---PDVIAG-QGTVGIEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 516954248 225 RAQMleqegrlPDMIIAAVGGGSNAIGLFHPfLDDRDVEIVGVEAggHGVD 275
Cdd:PRK08813 176 AAHA-------PDVVIVPIGGGGLASGVALA-LKSQGVRVVGAQV--EGVD 216
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
66-292 |
1.66e-03 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 40.55 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 66 RPSKLYFAEGLTKHLGGaRIFFKREDLNHTGSHKINNCLGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCFVY 145
Cdd:PRK12483 36 RETPLQRAPNLSARLGN-QVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516954248 146 MGATDVERQAPNVfrmKLLGATVnpVTAGNgTLKDAMNEALRdwVSNVEDTYYLigtaagpHPYpelvrDFQSVI---GT 222
Cdd:PRK12483 115 MPRTTPQLKVDGV---RAHGGEV--VLHGE-SFPDALAHALK--LAEEEGLTFV-------PPF-----DDPDVIagqGT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516954248 223 EARAQMLEQEGRLpDMIIAAVGGGSNAIGLFHPFLDDR-DVEIVGVEAgghgvDIENGHAASMTGGRPGVL 292
Cdd:PRK12483 175 VAMEILRQHPGPL-DAIFVPVGGGGLIAGIAAYVKYVRpEIKVIGVEP-----DDSNCLQAALAAGERVVL 239
|
|
| |
