|
Name |
Accession |
Description |
Interval |
E-value |
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
9-413 |
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: 839.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 9 NSLRSQPDASGHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALRaeappg 88
Cdd:COG0133 2 SSLYSLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLG------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 89 kGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFR 168
Cdd:COG0133 76 -GAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 169 MKLLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLI 248
Cdd:COG0133 155 MKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 249 APVGGGSNAIGLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPG 327
Cdd:COG0133 235 ACVGGGSNAIGIFYPFLDDESVRLIGVEAGGKGLEtGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 328 IGPEHSWLHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVAT 407
Cdd:COG0133 315 VGPEHAYLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAK 394
|
....*.
gi 523701105 408 ALGVEI 413
Cdd:COG0133 395 YLGLED 400
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
11-413 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 837.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 11 LRSQPDASGHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALraeappgKG 90
Cdd:PRK04346 1 TYTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHL-------GG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 91 AKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFRMK 170
Cdd:PRK04346 74 AKIYLKREDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 171 LLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLIAP 250
Cdd:PRK04346 154 LLGAEVVPVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVAC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 251 VGGGSNAIGLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPGIG 329
Cdd:PRK04346 234 VGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLEtGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 330 PEHSWLHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVATAL 409
Cdd:PRK04346 314 PEHAYLKDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLL 393
|
....
gi 523701105 410 GVEI 413
Cdd:PRK04346 394 GVIL 397
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
19-409 |
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 523701105 19 GHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALraeappgKGAKIYLKRE 98
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEAL-------GGAKIYLKRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 99 ELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFRMKLLGAEVIP 178
Cdd:TIGR00263 74 DLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 179 VVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLIAPVGGGSNAI 258
Cdd:TIGR00263 154 VTSGSGTLKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 259 GLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPGIGPEHSWLHE 337
Cdd:TIGR00263 234 GIFYAFIDDPSVQLIGVEAGGLGIDtHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHE 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523701105 338 IGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVATAL 409
Cdd:TIGR00263 314 TGRATYEAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
39-405 |
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: 640.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 39 ELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALraeappgKGAKIYLKREELNHTGAHKINNCIGQALLA 118
Cdd:cd06446 5 ELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYL-------GGAKIYLKREDLNHTGAHKINNALGQALLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 119 RRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFRMKLLGAEVIPVVSGSQTLKDAMNDALRHWV 198
Cdd:cd06446 78 KRMGKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 199 SNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLIAPVGGGSNAIGLFHPFLDDAEVKMIGVEAA 278
Cdd:cd06446 158 TNVEDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 279 GEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPGIGPEHSWLHEIGRVDYMPITDDEALASFQK 357
Cdd:cd06446 238 GCGLEtGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 523701105 358 LSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTV 405
Cdd:cd06446 318 LARTEGIIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
63-396 |
3.35e-38 |
|
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: 139.37 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 63 SYVGRPNPLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATV 142
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKEL--------GVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 143 AALFGMECKIFMGAKDVERqkpNVFRMKLLGAEVIPVVSGSQTLKDAMNDALRHWvsnvHDTFYIigtaagpHPY-PELV 221
Cdd:pfam00291 74 AARLGLKVTIVVPEDAPPG---KLLLMRALGAEVVLVGGDYDEAVAAARELAAEG----PGAYYI-------NQYdNPLN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 222 RDFQSIIGREAREQIleleGRLPDMLIAPVGGGSNAIGLFHPF-LDDAEVKMIGVEAAGeglqgkhAASLAGGksgilhg 300
Cdd:pfam00291 140 IEGYGTIGLEILEQL----GGDPDAVVVPVGGGGLIAGIARGLkELGPDVRVIGVEPEG-------APALARS------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 301 nrtyLLQDEDGQITEAHSISAGLDYPGIGPEHSW-LHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEK 379
Cdd:pfam00291 202 ----LAAGRPVPVPVADTIADGLGVGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKL 277
|
330
....*....|....*...
gi 523701105 380 V-APTLDADQILIVNLSG 396
Cdd:pfam00291 278 AlAGELKGGDRVVVVLTG 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
9-413 |
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: 839.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 9 NSLRSQPDASGHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALRaeappg 88
Cdd:COG0133 2 SSLYSLPDEKGYFGEFGGRFVPETLMPALDELEEAYEKAKNDPEFQAELDYLLKDYVGRPTPLYFAERLSEKLG------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 89 kGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFR 168
Cdd:COG0133 76 -GAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVVYMGEEDIERQALNVFR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 169 MKLLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLI 248
Cdd:COG0133 155 MKLLGAEVVPVTSGSRTLKDAVNEALRDWVTNVDDTHYLIGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 249 APVGGGSNAIGLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPG 327
Cdd:COG0133 235 ACVGGGSNAIGIFYPFLDDESVRLIGVEAGGKGLEtGEHAATLTKGRPGVLHGARTYLLQDEDGQILETHSISAGLDYPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 328 IGPEHSWLHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVAT 407
Cdd:COG0133 315 VGPEHAYLKDTGRAEYVSVTDDEALEAFQLLSRTEGIIPALESAHALAYALKLAPELSKDQIIVVNLSGRGDKDVDTVAK 394
|
....*.
gi 523701105 408 ALGVEI 413
Cdd:COG0133 395 YLGLED 400
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
11-413 |
0e+00 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 837.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 11 LRSQPDASGHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALraeappgKG 90
Cdd:PRK04346 1 TYTLPDENGYFGEFGGRFVPETLMPALEELEEAYEKAKNDPEFQAELDYLLKNYVGRPTPLYFAERLSEHL-------GG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 91 AKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFRMK 170
Cdd:PRK04346 74 AKIYLKREDLNHTGAHKINNVLGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLECVIYMGAEDVERQALNVFRMK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 171 LLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLIAP 250
Cdd:PRK04346 154 LLGAEVVPVTSGSRTLKDAVNEALRDWVTNVEDTHYLIGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVAC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 251 VGGGSNAIGLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPGIG 329
Cdd:PRK04346 234 VGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLEtGKHAATLTKGRPGVLHGAKTYLLQDEDGQILETHSISAGLDYPGVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 330 PEHSWLHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVATAL 409
Cdd:PRK04346 314 PEHAYLKDIGRAEYVSITDDEALEAFQLLSRLEGIIPALESSHALAYALKLAPTLGKDQIIVVNLSGRGDKDVFTVAKLL 393
|
....
gi 523701105 410 GVEI 413
Cdd:PRK04346 394 GVIL 397
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
8-410 |
0e+00 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 688.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 8 PNSLRSQPDASGHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALraeapp 87
Cdd:PRK13028 2 TSYLKSMPDADGFFGEYGGQFVPPELKPALDELEAAYEEIKKDPDFIAELRYLLKHYVGRPTPLYHAKRLSEEL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 88 gKGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVF 167
Cdd:PRK13028 76 -GGAQIYLKREDLNHTGAHKINNCLGQALLAKRMGKKRLIAETGAGQHGVATATAAALFGLECEIYMGEVDIERQHPNVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 168 RMKLLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDML 247
Cdd:PRK13028 155 RMKLLGAEVVPVTRGGRTLKEAVDSAFEDYLKDPDNTHYAIGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 248 IAPVGGGSNAIGLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYP 326
Cdd:PRK13028 235 VACVGGGSNAIGLFSAFLDDESVRLVGVEPAGRGLDlGEHAATLTLGKPGVIHGFKSYVLQDEDGEPAPVHSIAAGLDYP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 327 GIGPEHSWLHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVA 406
Cdd:PRK13028 315 GVGPEHAYLKDIGRVEYVTATDEEALDAFFLLSRTEGIIPALESSHAVAYAIKLAPELSKDETILVNLSGRGDKDIDYVA 394
|
....
gi 523701105 407 TALG 410
Cdd:PRK13028 395 EMLG 398
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
19-409 |
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 523701105 19 GHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALraeappgKGAKIYLKRE 98
Cdd:TIGR00263 1 GYFGDFGGQYVPETLMPALEELEAAFEDAKADPAFWAELNELLRNYAGRPTPLTFAPNLTEAL-------GGAKIYLKRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 99 ELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFRMKLLGAEVIP 178
Cdd:TIGR00263 74 DLNHTGAHKINNALGQALLAKRMGKKRIIAETGAGQHGVATATAAALLGLDCEVYMGAEDVERQKPNVFRMELLGAKVIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 179 VVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLIAPVGGGSNAI 258
Cdd:TIGR00263 154 VTSGSGTLKDAVNEALRDWVTSVDDTHYVLGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 259 GLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPGIGPEHSWLHE 337
Cdd:TIGR00263 234 GIFYAFIDDPSVQLIGVEAGGLGIDtHKHAATLSKGSPGVLHGMKTYLLQDEDGQILEAHSVSAGLDYPGVGPEHAYLHE 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523701105 338 IGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVATAL 409
Cdd:TIGR00263 314 TGRATYEAITDDEALEAFKLLSRNEGIIPALESSHALAHLEKIAPTLPKDQIVVVNLSGRGDKDIFTIAKYL 385
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
39-405 |
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: 640.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 39 ELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALraeappgKGAKIYLKREELNHTGAHKINNCIGQALLA 118
Cdd:cd06446 5 ELEQEFSKERYDPDFPEELRELYKDYVGRPTPLYRAKRLSEYL-------GGAKIYLKREDLNHTGAHKINNALGQALLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 119 RRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFRMKLLGAEVIPVVSGSQTLKDAMNDALRHWV 198
Cdd:cd06446 78 KRMGKKRVIAETGAGQHGVATATACALFGLECEIYMGAVDVERQPLNVFRMELLGAEVVPVPSGSGTLKDAISEAIRDWV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 199 SNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLIAPVGGGSNAIGLFHPFLDDAEVKMIGVEAA 278
Cdd:cd06446 158 TNVEDTHYLLGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 279 GEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPGIGPEHSWLHEIGRVDYMPITDDEALASFQK 357
Cdd:cd06446 238 GCGLEtGGHAAYLFGGTAGVLHGLKMYTLQDEDGQIVPPHSISAGLDYPGVGPEHAYLKDSGRVEYVAVTDEEALEAFKL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 523701105 358 LSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTV 405
Cdd:cd06446 318 LARTEGIIPALESSHAIAYAIKLAKKLGKEKVIVVNLSGRGDKDLQTV 365
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
15-406 |
0e+00 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 620.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 15 PDASGHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALraeappgkGAKIY 94
Cdd:PRK13803 218 SDPAGRYGTFGGAYVPETLMANLQELQESYTKIIKSNEFQKTFKRLLQNYAGRPTPLTEAKRLSDIY--------GARIY 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 95 LKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVFRMKLLGA 174
Cdd:PRK13803 290 LKREDLNHTGSHKINNALGQALLAKRMGKTRIIAETGAGQHGVATATACALFGLKCTIFMGEEDIKRQALNVERMKLLGA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 175 EVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDMLIAPVGGG 254
Cdd:PRK13803 370 NVIPVLSGSKTLKDAVNEAIRDWVASVPDTHYLIGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGG 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 255 SNAIGLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYPGIGPEHS 333
Cdd:PRK13803 450 SNAIGIFYHFLDDPSVKLIGVEAGGKGVNtGEHAATIKKGRKGVLHGSMTYLMQDENGQILEPHSISAGLDYPGIGPMHA 529
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523701105 334 WLHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVA 406
Cdd:PRK13803 530 NLFETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSHALAYLKEGRKKFKKKDIVIVNLSGRGDKDIPTLK 602
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
8-412 |
0e+00 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 600.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 8 PNSLRSQPDASGHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALRAEApp 87
Cdd:PLN02618 6 DPTGFQRPDSFGRFGKFGGKYVPETLMTALSELEAAFNALATDPEFQEELAGILKDYVGRETPLYFAERLTEHYKRAD-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 88 GKGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQKPNVF 167
Cdd:PLN02618 84 GEGPEIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIVYMGAQDMERQALNVF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 168 RMKLLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEGRLPDML 247
Cdd:PLN02618 164 RMRLLGAEVRPVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 248 IAPVGGGSNAIGLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLAGGKSGILHGNRTYLLQDEDGQITEAHSISAGLDYP 326
Cdd:PLN02618 244 VACVGGGSNAMGLFHEFIDDEDVRLIGVEAAGFGLDsGKHAATLTKGEVGVLHGAMSYLLQDEDGQIIEPHSISAGLDYP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 327 GIGPEHSWLHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDADQILIVNLSGRGDKDIFTVA 406
Cdd:PLN02618 324 GVGPEHSFLKDTGRAEYYSVTDEEALEAFQRLSRLEGIIPALETSHALAYLEKLCPTLPDGTKVVVNCSGRGDKDVNTAI 403
|
....*.
gi 523701105 407 TALGVE 412
Cdd:PLN02618 404 KYLQVS 409
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
4-410 |
5.72e-167 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 484.53 E-value: 5.72e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 4 SMTLPNSLRSQPdasgHFGAFGGRYVAETLMPLILELEKVYKEAKQDPAFDAEFTELLRSYVGRPNPLYHAARLTEALRA 83
Cdd:PRK13802 266 SETTPLSEHQGP----YWGQFGGRYVPEALITALDELERVYTQAKADPEFHKELATLNQRYVGRPSPLTEAPRFAERVKE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 84 EAppGKGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAKDVERQK 163
Cdd:PRK13802 342 KT--GLDARVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQIDARRQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 164 PNVFRMKLLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHPYPELVRDFQSIIGREAREQILELEG-R 242
Cdd:PRK13802 420 LNVARMRMLGAEVVEVTLGDRILKDAINEALRDWVTNVKDTHYLLGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiD 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 243 LPDMLIAPVGGGSNAIGLFHPFLDDAEVKMIGVEAAGEGLQ-GKHAASLA--GGKSGILHGNRTYLLQDEDGQITEAHSI 319
Cdd:PRK13802 500 HPDAICACVGGGSNAIGVMNAFLDDERVNLYGYEAGGNGPEsGKHAIRFApgTGELGMFQGAKSYLLENDEGQTLDTYSI 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 320 SAGLDYPGIGPEHSWLHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLDAD----QILIVNLS 395
Cdd:PRK13802 580 SAGLDYASVGPEHAWLKDIGRVNYSWATDEEAMNAFKDLCETEGIIPAIESSHAVAGAYKAAADLKAKgyehPVMIVNIS 659
|
410
....*....|....*
gi 523701105 396 GRGDKDIFTVATALG 410
Cdd:PRK13802 660 GRGDKDMNTAGKWFG 674
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
70-397 |
3.41e-57 |
|
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: 187.72 E-value: 3.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 70 PLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKINNCIGQALLARRMGK--KKVIAETGAGQHGVATATVAALFG 147
Cdd:cd00640 2 PLVRLKRLSKLG--------GANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKlpKGVIIESTGGNTGIALAAAAARLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 148 MECKIFMGAKDverQKPNVFRMKLLGAEVIPVVSGsqtLKDAMNDALRHWVSNvHDTFYIigtaagpHPY-PELVRDFQS 226
Cdd:cd00640 74 LKCTIVMPEGA---SPEKVAQMRALGAEVVLVPGD---FDDAIALAKELAEED-PGAYYV-------NQFdNPANIAGQG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 227 IIGREAREQileLEGRLPDMLIAPVGGGSNAIGLFHPFL-DDAEVKMIGVEAageglqgkhaaslaggksgilhgnrtyl 305
Cdd:cd00640 140 TIGLEILEQ---LGGQKPDAVVVPVGGGGNIAGIARALKeLLPNVKVIGVEP---------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 306 lqdedgqiteahsisagldypgigpehswlheigrvDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEKVAPTLD 385
Cdd:cd00640 189 ------------------------------------EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLG 232
|
330
....*....|..
gi 523701105 386 ADQILIVNLSGR 397
Cdd:cd00640 233 KGKTVVVILTGG 244
|
|
| PRK12391 |
PRK12391 |
TrpB-like pyridoxal phosphate-dependent enzyme; |
65-398 |
5.42e-53 |
|
TrpB-like pyridoxal phosphate-dependent enzyme;
Pssm-ID: 237087 Cd Length: 427 Bit Score: 182.30 E-value: 5.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 65 VGRPNPLYHAARLTEALraeappGKGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATVAA 144
Cdd:PRK12391 74 LWRPTPLIRARRLEKAL------GTPAKIYYKYEGVSPTGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSALALACA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 145 LFGMECKIFMgAKDVERQKPnvFR---MKLLGAEVIPVVS-----GSQTLK--------------DAMNDALRHwvsnvH 202
Cdd:PRK12391 148 LFGLECTVFM-VRVSYEQKP--YRrslMETYGAEVIPSPSdlteaGRKILAedpdhpgslgiaisEAVEDAAKR-----P 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 203 DTFYIIGTAAgPHpypelVRDFQSIIGREAREQiLELEGRLPDMLIAPVGGGSNAIGLFHPFLDD-----AEVKMIGVEA 277
Cdd:PRK12391 220 DTKYALGSVL-NH-----VLLHQTVIGLEAKKQ-LELAGEYPDVVIGCVGGGSNFAGLAFPFLGDklegkKDTRFIAVEP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 278 AGeglqgkhAASLAGGKSgilhgnrTYLLQDEDG--QITEAHSI----------SAGLDYPGIGPEHSWLHEIGRVDYMP 345
Cdd:PRK12391 293 AA-------CPTLTKGEY-------AYDFGDTAGltPLLKMYTLghdfvpppihAGGLRYHGMAPLVSLLVHEGLIEARA 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 523701105 346 ITDDEALASFQKLSALEGIIPALESAHAIASAEKVA---PTLDADQILIVNLSGRG 398
Cdd:PRK12391 359 YPQTEVFEAAVLFARTEGIVPAPESSHAIAAAIDEAlkaKEEGEEKVILFNLSGHG 414
|
|
| COG1350 |
COG1350 |
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport ... |
59-398 |
2.92e-45 |
|
Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) [Amino acid transport and metabolism]; Predicted alternative tryptophan synthase beta-subunit (paralog of TrpB) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440961 Cd Length: 433 Bit Score: 161.84 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 59 ELLRSYvgRPNPLYHAARLTEALraeappGKGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVA 138
Cdd:COG1350 71 EIYRLW--RPSPLYRARRLEKAL------GTPAKIYYKYEGVSPAGSHKPNTAVAQAYYNKKEGIKRLTTETGAGQWGSA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 139 TATVAALFGMECKIFMgAKDVERQKPnvFR---MKLLGAEVIPVVS-----GSQTLKD--------------AMNDALRH 196
Cdd:COG1350 143 LSFACALFGLECTVYM-VKVSYEQKP--YRrsmMETYGAEVIPSPSdlteaGRKILAEdpdtpgslgiaiseAVEDAATR 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 197 wvsnvHDTFYIIGTAAGpHpypelVRDFQSIIGREAREQiLELEGRLPDMLIAPVGGGSNAIGLFHPFLDD-----AEVK 271
Cdd:COG1350 220 -----DDTKYALGSVLN-H-----VLLHQTVIGLEAKKQ-LEKAGEYPDVVIGCAGGGSNFAGLAFPFLRDklrgkKDVR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 272 MIGVEAAGeglqgkhAASLAGGKSGILHGN---RTYLLQdedgQITEAH-----SISA-GLDYPGIGPEHSWLHEIGRVD 342
Cdd:COG1350 288 FIAVEPAA-------CPTLTRGVYAYDFGDtagLTPLLK----MYTLGHdfippPIHAgGLRYHGMAPLVSQLYHDGLIE 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523701105 343 YMPITDDEALASFQKLSALEGIIPALESAHAIASA------------EKVaptldadqILIvNLSGRG 398
Cdd:COG1350 357 AVAYPQLEVFEAGVLFARTEGIVPAPESAHAIKAAidealkckeegeEKT--------ILF-NLSGHG 415
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
63-396 |
3.35e-38 |
|
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: 139.37 E-value: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 63 SYVGRPNPLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATATV 142
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKEL--------GVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 143 AALFGMECKIFMGAKDVERqkpNVFRMKLLGAEVIPVVSGSQTLKDAMNDALRHWvsnvHDTFYIigtaagpHPY-PELV 221
Cdd:pfam00291 74 AARLGLKVTIVVPEDAPPG---KLLLMRALGAEVVLVGGDYDEAVAAARELAAEG----PGAYYI-------NQYdNPLN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 222 RDFQSIIGREAREQIleleGRLPDMLIAPVGGGSNAIGLFHPF-LDDAEVKMIGVEAAGeglqgkhAASLAGGksgilhg 300
Cdd:pfam00291 140 IEGYGTIGLEILEQL----GGDPDAVVVPVGGGGLIAGIARGLkELGPDVRVIGVEPEG-------APALARS------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 301 nrtyLLQDEDGQITEAHSISAGLDYPGIGPEHSW-LHEIGRVDYMPITDDEALASFQKLSALEGIIPALESAHAIASAEK 379
Cdd:pfam00291 202 ----LAAGRPVPVPVADTIADGLGVGDEPGALALdLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKL 277
|
330
....*....|....*...
gi 523701105 380 V-APTLDADQILIVNLSG 396
Cdd:pfam00291 278 AlAGELKGGDRVVVVLTG 295
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
70-412 |
5.21e-17 |
|
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: 82.17 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 70 PLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKInncIGQALL---ARRMGKKKVIAETgAGQHGVATATVAALF 146
Cdd:COG0498 68 PLVKAPRLADEL--------GKNLYVKEEGHNPTGSFKD---RAMQVAvslALERGAKTIVCAS-SGNGSAALAAYAARA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 147 GMECKIFMGAKDVERQKpnVFRMKLLGAEVIpVVSGsqTLKDAMNDALRhwVSNVHDtfyiIGTAAGPHPYpelVRDFQS 226
Cdd:COG0498 136 GIEVFVFVPEGKVSPGQ--LAQMLTYGAHVI-AVDG--NFDDAQRLVKE--LAADEG----LYAVNSINPA---RLEGQK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 227 IIGREAREQIleleGRLPDMLIAPVGGGSNAIGLFHPFLDDAEV-------KMIGVEAAGEglqgkhaaslaggkSGILH 299
Cdd:COG0498 202 TYAFEIAEQL----GRVPDWVVVPTGNGGNILAGYKAFKELKELglidrlpRLIAVQATGC--------------NPILT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 300 GNRTyllQDEDGQITEAHSISAGLDypgIG-PEhSW---LHEI----GRVDYmpITDDEALASFQKLSALEGIIPALESA 371
Cdd:COG0498 264 AFET---GRDEYEPERPETIAPSMD---IGnPS-NGeraLFALresgGTAVA--VSDEEILEAIRLLARREGIFVEPATA 334
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 523701105 372 HAIASAEKVA--PTLDADQILIVNLSGRGDKDIFTVATALGVE 412
Cdd:COG0498 335 VAVAGLRKLReeGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
70-401 |
1.82e-16 |
|
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: 79.56 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 70 PLYHAARLTEALraeappgKGAKIYLKREELNHTGAHKINnciGQALL---ARRMGKKKVIAETgAGQHGVATATVAALF 146
Cdd:cd01563 24 PLVRAPRLGERL-------GGKNLYVKDEGLNPTGSFKDR---GMTVAvskAKELGVKAVACAS-TGNTSASLAAYAARA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 147 GMECKIFMGAkDVERQKpnVFRMKLLGAEVIPVVSG-SQTLKDAMNDALRHW--VSNVHDTFYIIGtaagphpypelvrd 223
Cdd:cd01563 93 GIKCVVFLPA-GKALGK--LAQALAYGATVLAVEGNfDDALRLVRELAEENWiyLSNSLNPYRLEG-------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 224 fQSIIGREAREQileLEGRLPDMLIAPVGGGSNAIGLFHPFLD-------DAEVKMIGVEAAGeglqgkhAASLA-GGKS 295
Cdd:cd01563 156 -QKTIAFEIAEQ---LGWEVPDYVVVPVGNGGNITAIWKGFKElkelgliDRLPRMVGVQAEG-------AAPIVrAFKE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 296 GilhgnrtyllQDEDGQITEAHSISAGLDypgIGPEHSW---LHEI----GRVDymPITDDEALASFQKLSALEGIIPAL 368
Cdd:cd01563 225 G----------KDDIEPVENPETIATAIR---IGNPASGpkaLRAVresgGTAV--AVSDEEILEAQKLLARTEGIFVEP 289
|
330 340 350
....*....|....*....|....*....|....*
gi 523701105 369 ESAHAIASAEKVAP--TLDADQILIVNLSGRGDKD 401
Cdd:cd01563 290 ASAASLAGLKKLREegIIDKGERVVVVLTGHGLKD 324
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
59-294 |
9.66e-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: 77.14 E-value: 9.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 59 ELLRSYVgRPNPLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKI----NNcigQALLARRMGKKKVIAETgAGQ 134
Cdd:cd01562 9 ARIKPVV-RRTPLLTSPTLSELL--------GAEVYLKCENLQKTGSFKIrgayNK---LLSLSEEERAKGVVAAS-AGN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 135 HGVATATVAALFGMECKIFMgAKDVERQKpnVFRMKLLGAEVIPVVSGSQtlkDAMNDALRhwVSNVHDTFYIigtaagp 214
Cdd:cd01562 76 HAQGVAYAAKLLGIPATIVM-PETAPAAK--VDATRAYGAEVVLYGEDFD---EAEAKARE--LAEEEGLTFI------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 215 HPY--PELVRDfQSIIGREAREQILELegrlpDMLIAPVGGG------SNAIGLFHPflddaEVKMIGVEAAGeglQGKH 286
Cdd:cd01562 141 HPFddPDVIAG-QGTIGLEILEQVPDL-----DAVFVPVGGGgliagiATAVKALSP-----NTKVIGVEPEG---APAM 206
|
....*...
gi 523701105 287 AASLAGGK 294
Cdd:cd01562 207 AQSLAAGK 214
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
86-392 |
3.08e-13 |
|
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: 69.85 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 86 PPGKGAKIYLKREELNHTGAHKI---NNCIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAK-DVER 161
Cdd:cd01561 12 SPGTGAEIYAKLEFFNPGGSVKDriaLYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETmSEEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 162 QKpnvfRMKLLGAEVIPVV-SGSQTLKDAMNDALRHwvSNVHDTFYII--------------GTAagphpyPELVRDFqs 226
Cdd:cd01561 92 RK----LLRALGAEVILTPeAEADGMKGAIAKAREL--AAETPNAFWLnqfenpanpeahyeTTA------PEIWEQL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 227 iigreareqilelEGRLpDMLIAPVG-GGSNA-IGLF----HPflddaEVKMIGVEAAGEGLqgkhaasLAGGKSGilhg 300
Cdd:cd01561 158 -------------DGKV-DAFVAGVGtGGTITgVARYlkekNP-----NVRIVGVDPVGSVL-------FSGGPPG---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 301 nrtyllqdedgqiteAHSIsagldyPGIGP-------EHSWLHEIGRVDympitDDEALASFQKLSALEGIIPALESAHA 373
Cdd:cd01561 208 ---------------PHKI------EGIGAgfipenlDRSLIDEVVRVS-----DEEAFAMARRLAREEGLLVGGSSGAA 261
|
330
....*....|....*....
gi 523701105 374 IASAEKVAPTLDADQiLIV 392
Cdd:cd01561 262 VAAALKLAKRLGPGK-TIV 279
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
59-279 |
3.65e-13 |
|
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: 70.07 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 59 ELLRSYVgRPNPLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKIN---NCIGQalLARRMGKKKVIAETgAGQH 135
Cdd:COG1171 16 ARIAGVV-RRTPLLRSPTLSERL--------GAEVYLKLENLQPTGSFKLRgayNALAS--LSEEERARGVVAAS-AGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 136 GVATATVAALFGMECKIFMgAKDVERQKpnVFRMKLLGAEVipVVSGSqTLKDAMNDALRH-----WVSnVHDT--FYII 208
Cdd:COG1171 84 AQGVAYAARLLGIPATIVM-PETAPAVK--VAATRAYGAEV--VLHGD-TYDDAEAAAAELaeeegATF-VHPFddPDVI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523701105 209 gtaAGphpypelvrdfQSIIGREAREQILELegrlpDMLIAPVGGGS------NAIGLFHPflddaEVKMIGVEAAG 279
Cdd:COG1171 157 ---AG-----------QGTIALEILEQLPDL-----DAVFVPVGGGGliagvaAALKALSP-----DIRVIGVEPEG 209
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
86-387 |
3.23e-11 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 63.91 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 86 PPGKGAKIYLKREELNHTGAHK------InncIGQALLARRMGKKKVIAETGAGQHGVATATVAALFGMECKIFMGAK-D 158
Cdd:COG0031 23 SPGPGAEIYAKLESFNPGGSVKdrialsM---IEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAKGYRLILVMPETmS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 159 VERQKpnvfRMKLLGAEVIpVVSGSQTLKDAMNDALR--------HWV------SNVhdTFYIIGTAagphpyPELVRDf 224
Cdd:COG0031 100 KERRA----LLRAYGAEVV-LTPGAEGMKGAIDKAEElaaetpgaFWPnqfenpANP--EAHYETTG------PEIWEQ- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 225 qsiigreareqileLEGRlPDMLIAPVG-GGSNA-IGLF----HPflddaEVKMIGVEAAGeglqgkhAASLAGGKSGil 298
Cdd:COG0031 166 --------------TDGK-VDAFVAGVGtGGTITgVGRYlkerNP-----DIKIVAVEPEG-------SPLLSGGEPG-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 299 hgnrtyllqdedgqiteAHSIsagldyPGIGPEH-SWLHEIGRVD-YMPITDDEALASFQKLSALEGIIPALESAHAIAS 376
Cdd:COG0031 217 -----------------PHKI------EGIGAGFvPKILDPSLIDeVITVSDEEAFAMARRLAREEGILVGISSGAAVAA 273
|
330
....*....|.
gi 523701105 377 AEKVAPTLDAD 387
Cdd:COG0031 274 ALRLAKRLGPG 284
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
68-291 |
9.67e-11 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 62.90 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 68 PNPLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKIN---NCIGQalLARRMGKKKVIAETgAGQH--GVATAtv 142
Cdd:PRK08639 25 ETPLQRNDYLSEKY--------GANVYLKREDLQPVRSYKLRgayNAISQ--LSDEELAAGVVCAS-AGNHaqGVAYA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 143 AALFGMECKIFMGAKdVERQKpnVFRMKLLGAEVIPVVSGSQTLKDAMNDALRHWVSN----VH--DTFYIIgtaAGphp 216
Cdd:PRK08639 92 CRHLGIPGVIFMPVT-TPQQK--IDQVRFFGGEFVEIVLVGDTFDDSAAAAQEYAEETgatfIPpfDDPDVI---AG--- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523701105 217 ypelvrdfQSIIGREAREQILELegRLPDMLIAPVGGGSNAIGLFHPFLDDA-EVKMIGVEAAGeglqgkhAASLA 291
Cdd:PRK08639 163 --------QGTVAVEILEQLEKE--GSPDYVFVPVGGGGLISGVTTYLKERSpKTKIIGVEPAG-------AASMK 221
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
70-276 |
4.94e-10 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 60.55 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 70 PLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKINNCIGQALLARRMGK--KKVIAETgAGQHGVATATVAALFG 147
Cdd:PRK06608 25 PIVHSESLNEML--------GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYS-TGNHGQAVAYASKLFG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 148 MECKIFMGAkdverqkpNVFRMKL-----LGAEVIPvvsgSQTLKDAMNDALRhwvSNVHDTFYIigtaagpHPYpelvr 222
Cdd:PRK06608 96 IKTRIYLPL--------NTSKVKQqaalyYGGEVIL----TNTRQEAEEKAKE---DEEQGFYYI-------HPS----- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 523701105 223 DFQSII---GREAREQILELeGRLPDMLIAPVGGGSNAIG-LFHPFLDDAEVKMIGVE 276
Cdd:PRK06608 149 DSDSTIagaGTLCYEALQQL-GFSPDAIFASCGGGGLISGtYLAKELISPTSLLIGSE 205
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
75-293 |
3.28e-09 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 57.66 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 75 ARLTEALRAEAPPGKGAKIYLKREELNHTGAHK----INNcigqaLLARRMGKKKVIAETGaGQHGVATATVAALFGMEC 150
Cdd:PRK08246 21 IRRTPVLEADGAGFGPAPVWLKLEHLQHTGSFKargaFNR-----LLAAPVPAAGVVAASG-GNAGLAVAYAAAALGVPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 151 KIFM--GAKDVERQkpnvfRMKLLGAEVipVVSGSqTLKDAMNDALRHwvsnvhdtfyIIGTAAGP-HPY--PELVRDfQ 225
Cdd:PRK08246 95 TVFVpeTAPPAKVA-----RLRALGAEV--VVVGA-EYADALEAAQAF----------AAETGALLcHAYdqPEVLAG-A 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523701105 226 SIIGREAREQileleGRLPDMLIAPVGGGSNAIGLFHPFldDAEVKMIGVEAagEGLQGKHAASLAGG 293
Cdd:PRK08246 156 GTLGLEIEEQ-----APGVDTVLVAVGGGGLIAGIAAWF--EGRARVVAVEP--EGAPTLHAALAAGE 214
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
61-254 |
4.40e-08 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 54.31 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 61 LRSYVgRPNPLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETGAGQHGVATA 140
Cdd:PRK06815 14 LRPQV-RVTPLEHSPLLSQHT--------GCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 141 TVAALFGMECKIFMgAKDVERQKPNvfRMKLLGAEVipVVSGSQTLK---DAMNDALRH---WVSNVHDTFYIIGtaagp 214
Cdd:PRK06815 85 LAAKLAGIPVTVYA-PEQASAIKLD--AIRALGAEV--RLYGGDALNaelAARRAAEQQgkvYISPYNDPQVIAG----- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 523701105 215 hpypelvrdfQSIIGREAREQILELegrlpDMLIAPVGGG 254
Cdd:PRK06815 155 ----------QGTIGMELVEQQPDL-----DAVFVAVGGG 179
|
|
| PRK03910 |
PRK03910 |
D-cysteine desulfhydrase; Validated |
62-259 |
5.63e-07 |
|
D-cysteine desulfhydrase; Validated
Pssm-ID: 179673 Cd Length: 331 Bit Score: 50.99 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 62 RSYVGRPNPLYHAARLTEALraeappgkGAKIYLKREELnhTG-------AHKINNCIGQALlarRMGKKKVIAeTGAGQ 134
Cdd:PRK03910 9 LELAGLPTPLEPLPRLSAAL--------GPDIYIKRDDL--TGlalggnkTRKLEFLLADAL---AQGADTLIT-AGAIQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 135 --HGVATATVAALFGMECKIFMGAKDVERQKP-----NVFRMKLLGAEVIPVVSGSQtlkdaMNDALRHWVSNVHdtfyi 207
Cdd:PRK03910 75 snHARQTAAAAAKLGLKCVLLLENPVPTEAENylangNVLLDDLFGAEIHVVPAGTD-----MDAQLEELAEELR----- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 523701105 208 igtAAGPHPYpelvrdfqsiigreareqilelegrlpdmlIAPVgGGSNAIG 259
Cdd:PRK03910 145 ---AQGRRPY------------------------------VIPV-GGSNALG 162
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
59-279 |
1.27e-06 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 49.70 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 59 ELLRSYVGRP--NPLYHAARLTEALRAEappgkgaKIYLKREELNHTGAHKINNCIGQALLARRMGKKKVIAETgAGQHG 136
Cdd:PRK06381 4 ELSSSEEKPPggTPLLRARKLEEELGLR-------KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGT-CGNYG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 137 VATATVAALFGMECKIFmgakdVERQKPN--VFRMKLLGAEVIpVVSGSqtlkdaMNDALRHWVSNVHDTFYIIGTAAGP 214
Cdd:PRK06381 76 ASIAYFARLYGLKAVIF-----IPRSYSNsrVKEMEKYGAEII-YVDGK------YEEAVERSRKFAKENGIYDANPGSV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523701105 215 HPYPELvrDFQSIIGREAREQIleleGRLPDMLIAPVGGGSNAIGLFHPF--LDDAEV-----KMIGVEAAG 279
Cdd:PRK06381 144 NSVVDI--EAYSAIAYEIYEAL----GDVPDAVAVPVGNGTTLAGIYHGFrrLYDRGKtsrmpRMIGVSTSG 209
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
70-261 |
1.10e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 43.80 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 70 PLYHAARLTEALraeappgkGAKIYLKREELNHTGAHKI---NNCIGQaLLARRMGKKKVIAETGagQHGVATATVAALF 146
Cdd:PRK07476 21 PLVASASLSARA--------GVPVWLKLETLQPTGSFKLrgaTNALLS-LSAQERARGVVTASTG--NHGRALAYAARAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 147 GMECKIFMGAKdVERQKPNVFRMklLGAEVIpVVSGSQtlKDAMNDALRHwvsnVHDTFYiigTAAGPHPYPELVRDfQS 226
Cdd:PRK07476 90 GIRATICMSRL-VPANKVDAIRA--LGAEVR-IVGRSQ--DDAQAEVERL----VREEGL---TMVPPFDDPRIIAG-QG 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 523701105 227 IIGreareqiLELEGRLPD--MLIAPVGGGsnaiGLF 261
Cdd:PRK07476 156 TIG-------LEILEALPDvaTVLVPLSGG----GLA 181
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
84-400 |
1.23e-03 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 40.49 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 84 EAPPGKGAKIYLKREELNHTGAHKINnciGQALLARRMGKKKV--IAETGAGQHGVATATVAALFGMECKIFMgAKDVER 161
Cdd:PRK06450 58 RTPLIKKGNIWFKLDFLNPTGSYKDR---GSVTLISYLAEKGIkqISEDSSGNAGASIAAYGAAAGIEVKIFV-PETASG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 162 QKpnVFRMKLLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHdtfyiigtaagpHPypelvrDFQSIIGREAREQILELEG 241
Cdd:PRK06450 134 GK--LKQIESYGAEVVRVRGSREDVAKAAENSGYYYASHVL------------QP------QFRDGIRTLAYEIAKDLDW 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 242 RLPDMLIAPVGGGSNAIGLFHPF---LDDAEVKMIGVEAAgegLQGKHAASLAGGKSGIlhgnrTYllqDEDGQITeahS 318
Cdd:PRK06450 194 KIPNYVFIPVSAGTLLLGVYSGFkhlLDSGVISEMPKIVA---VQTEQVSPLCAKFKGI-----SY---TPPDKVT---S 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 319 ISAGLdypgIGPEHSWLHEIGRV-----DYMPITDDEALASFQKLsALEGIIPALESAHAIASAEKVAPtldADQILIvn 393
Cdd:PRK06450 260 IADAL----VSTRPFLLDYMVKAlseygECIVVSDNEIVEAWKEL-AKKGLLVEYSSATVYAAYKKYSV---NDSVLV-- 329
|
....*..
gi 523701105 394 LSGRGDK 400
Cdd:PRK06450 330 LTGSGLK 336
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
60-298 |
2.32e-03 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 40.17 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 60 LLRSYVGR--PNPLYHAARLTEALRAEAPPGK-GAKIYLKREELNHTGAHKINNCIGQ-ALLARRMGKKKVIAETgAGQH 135
Cdd:PRK12483 18 LLADYLRKilAARVYDVARETPLQRAPNLSARlGNQVLLKREDLQPVFSFKIRGAYNKmARLPAEQLARGVITAS-AGNH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 136 GVATATVAALFGMECKIFMgakdvERQKPN--VFRMKLLGAEVipVVSGsqtlkDAMNDALRHWVSNVHD---TFYiigt 210
Cdd:PRK12483 97 AQGVALAAARLGVKAVIVM-----PRTTPQlkVDGVRAHGGEV--VLHG-----ESFPDALAHALKLAEEeglTFV---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 211 aagpHPYpelvrDFQSII---GREAREQILELEGRLpDMLIAPVGGGSNAIGL------FHPflddaEVKMIGVEAAGEG 281
Cdd:PRK12483 161 ----PPF-----DDPDVIagqGTVAMEILRQHPGPL-DAIFVPVGGGGLIAGIaayvkyVRP-----EIKVIGVEPDDSN 225
|
250
....*....|....*..
gi 523701105 282 LQgkhAASLAGGKSGIL 298
Cdd:PRK12483 226 CL---QAALAAGERVVL 239
|
|
| ACCD |
cd06449 |
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ... |
70-281 |
3.17e-03 |
|
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: 39.33 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 70 PLYHAARLTEALraeappGKGAKIYLKREELNHTGA------HKINNCIGQALlarRMGKKKVIAeTGAGQ--HGVATAT 141
Cdd:cd06449 2 PIQYLPRLSEHL------GGKVEIYAKRDDCNSGLAfggnkiRKLEYLLPDAL---AKGADTLVT-VGGIQsnHTRQVAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523701105 142 VAALFGMECKIFMGAK-----DVERQKPNVFRMKLLGAEVIPVVSGSQTLKDAMNDALRHWVSNVHDTFYIIGTAAGPHP 216
Cdd:cd06449 72 VAAKLGLKCVLVQENWvpysdAVYDRVGNILLSRIMGADVRLVSAGFDIGIRKSFEEAAEEVEAKGGKPYVIPAGGSEHP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523701105 217 YPELvrDFQSIIGrEAREQILELEGRLPDMLIAPVGGGSNA---IGLFHpflDDAEVKMIGVEAAGEG 281
Cdd:cd06449 152 LGGL--GYVGFVL-EIAQQEEELGFKFDSIVVCSVTGSTHAglsVGLAA---LGRQRRVIGIDASAKP 213
|
|
| |
