|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
1-389 |
0e+00 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 612.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 1 MLKLSKNSFYTGQVCELFTASQAQQAREFHRQIEGYQPTPLVSLPHLAKQLGVKAILVKDESKRFGLNAFKVLGGSYALG 80
Cdd:PRK08206 7 KNNIADNKPYDGADLPLLSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALGGAYAVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 81 RQLAKHLGIDISEINLKTVAS----KLEKPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECI 156
Cdd:PRK08206 87 RLLAEKLGLDISELSFEELTSgevrEKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 157 VTEVNYDDTVRMANQTAQDNGWMLVQDTAWDGYEEIPTWISQGYMTMADEAIEQAQALEfGAPTHVLLQAGVGAMAGGVL 236
Cdd:PRK08206 167 ITDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEMG-VPPTHVFLQAGVGSLAGAVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 237 GYLADKLGADTFETIIAEPAAADCIFRSGEKGEMVNVTGEMNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDDNVSATGM 316
Cdd:PRK08206 246 GYFAEVYGEQRPHFVVVEPDQADCLYQSAVDGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDEVAALGM 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588536696 317 RILGNPLSGDDQVISGESGAITLGLLFTLCREGADQAVRDELGLNQDATIMLFSTEGDTNQPRYRDIVWNGLH 389
Cdd:PRK08206 326 RILANPLGGDPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEGKY 398
|
|
| 2_3_DAP_am_ly |
TIGR03528 |
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ... |
10-387 |
0e+00 |
|
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.
Pssm-ID: 274631 Cd Length: 396 Bit Score: 601.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 10 YTGQVCELFTASQAQQAREFHRQIEGYQPTPLVSLPHLAKQLGVKAILVKDESKRFGLNAFKVLGGSYALGRQLAKHLGI 89
Cdd:TIGR03528 13 TNGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSYAIGKYLAEKLGK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 90 DISEI-----NLKTVASKLeKPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDD 164
Cdd:TIGR03528 93 DISELsfeklKSNEIREKL-GDITFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGAECTITDLNYDD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 165 TVRMANQTAQDNGWMLVQDTAWDGYEEIPTWISQGYMTMADEAIEQAQALEFGAPTHVLLQAGVGAMAGGVLGYLADKLG 244
Cdd:TIGR03528 172 AVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAGAVQGYFASVYG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 245 ADTFETIIAEPAAADCIFRSGEK--GEMVNVTGEMNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDDNVSATGMRILGNP 322
Cdd:TIGR03528 252 EERPITVIVEPDKADCIYRSAIAddGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWVAAKGMRILGNP 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1588536696 323 LSGDDQVISGESGAITLGLLFTLCREGADQAVRDELGLNQDATIMLFSTEGDTNQPRYRDIVWNG 387
Cdd:TIGR03528 332 LKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
|
|
| diampropi_NH3ly |
TIGR01747 |
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ... |
17-386 |
1.93e-175 |
|
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]
Pssm-ID: 130808 Cd Length: 376 Bit Score: 493.64 E-value: 1.93e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 17 LFTASQAQQAREFHRQIEGYQPTPLVSLPHLAKQLGVKAILVKDESKRFGLNAFKVLGGSYALGRQLAKHLGIDISEIN- 95
Cdd:TIGR01747 1 LFSQSQAKLALAFHKKIPGYRPTPLCALDHLANLLGLKKILVKDESKRFGLNAFKMLGGSYAIAQYLAEKLHLDIETLSf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 96 --LKTVASKLE-KPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQT 172
Cdd:TIGR01747 81 ehLKNDAIGEKmGQATFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 173 AQDNGWMLVQDTAWDGYEEIPTWISQGYMTMADEAIEQAQALEFGAPTHVLLQAGVGAMAGGVLGYLADKLGADTFETII 252
Cdd:TIGR01747 161 AQQHGWVVVQDTAWEGYEKIPTWIMQGYATLADEAVEQLREMGSVTPTHVLLQAGVGSMAGGVLGYFVDVYSENNPHSIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 253 AEPAAADCIFRSGEK--GEMVNVTGEMNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDDNVSATGMRILGNPLSGDDQVI 330
Cdd:TIGR01747 241 VEPDKADCLYQSAVKkdGDIVNVGGDMATIMAGLACGEPNPISWEILRNCTSQFISAQDSVAAKGMRVLGAPYGGDPRII 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1588536696 331 SGESGAITLGLLFTLCREGADQAVRDELGLNQDATIMLFSTEGDTNQPRYRDIVWN 386
Cdd:TIGR01747 321 SGESGAVGLGLLAAVMYHPQYQSLMEKLQLDKDAVVLVISTEGDTDPDHYREIVWE 376
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
16-391 |
3.72e-89 |
|
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: 272.30 E-value: 3.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 16 ELFTASQAQQAREFHRQIegYQPTPLVSLPHLAKQLGVKaILVKDESKRFgLNAFKVLGGSYALGRqlakhlgidisein 95
Cdd:COG1171 4 LMPTLADIEAAAARIAGV--VRRTPLLRSPTLSERLGAE-VYLKLENLQP-TGSFKLRGAYNALAS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 96 lktvASKLEKPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQD 175
Cdd:COG1171 66 ----LSEEERARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 176 NGWMLVQDTAwdgyeeiPTWISQGYMTMADEAIEQAQALefgapTHVLLQAGVGAMAGGVLGYLADkLGADTfETIIAEP 255
Cdd:COG1171 142 EGATFVHPFD-------DPDVIAGQGTIALEILEQLPDL-----DAVFVPVGGGGLIAGVAAALKA-LSPDI-RVIGVEP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 256 AAADCIFRSGEKGEMVNVTGeMNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDDNVSATGMRILGNPLsgddQVISGESG 335
Cdd:COG1171 208 EGAAAMYRSLAAGEPVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERT----KIVVEPAG 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1588536696 336 AITLGLLftlcREGADQAvrdelglnQDATIMLFSTEGDTNQPRYRDIVWNGLHHS 391
Cdd:COG1171 283 AAALAAL----LAGKERL--------KGKRVVVVLSGGNIDPDRLAEILERGLVGE 326
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
35-348 |
7.84e-46 |
|
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: 159.40 E-value: 7.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 35 GYQPTPLVSLPHLAKQLGVKaILVKDESKRFGLnAFKVLGGSYALGRqLAKHLGIDiseinlktvasklekplVFTTATA 114
Cdd:pfam00291 4 GIGPTPLVRLPRLSKELGVD-VYLKLESLNPTG-SFKDRGALNLLLR-LKEGEGGK-----------------TVVEASS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 115 GNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQ-TAQDNGWMLVqdtawDGYEEip 193
Cdd:pfam00291 64 GNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARElAAEGPGAYYI-----NQYDN-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 194 TWISQGYMTMADEAIEQAQalefGAPTHVLLQAGVGAMAGGVLGYLadKLGADTFETIIAEPAAADCIFRSGEKGEMVNV 273
Cdd:pfam00291 137 PLNIEGYGTIGLEILEQLG----GDPDAVVVPVGGGGLIAGIARGL--KELGPDVRVIGVEPEGAPALARSLAAGRPVPV 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1588536696 274 TgEMNSIMAGLACG-EPNPVTWPVLRDCSNHFVSVDDNVSATGMRILGNplsgDDQVISGESGAITL-GLLFTLCRE 348
Cdd:pfam00291 211 P-VADTIADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLAR----REGIVVEPSSAAALaALKLALAGE 282
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
30-319 |
5.45e-31 |
|
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: 119.90 E-value: 5.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 30 HRQIEGY-QPTPLVSLPHLAKQLGVKaILVKDES-KRFGlnAFKVLGGSYALgRQLAKHlgidiseinlktvasKLEKPL 107
Cdd:cd01562 8 AARIKPVvRRTPLLTSPTLSELLGAE-VYLKCENlQKTG--SFKIRGAYNKL-LSLSEE---------------ERAKGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 108 VftTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVQdtAWD 187
Cdd:cd01562 69 V--AASAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIH--PFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 188 GYEEIPtwiSQGymTMADEAIEQAQALEFgapthVLLQAGVGAMAGGVlgYLADKLGADTFETIIAEPAAADCIFRSGEK 267
Cdd:cd01562 145 DPDVIA---GQG--TIGLEILEQVPDLDA-----VFVPVGGGGLIAGI--ATAVKALSPNTKVIGVEPEGAPAMAQSLAA 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1588536696 268 GEMVNVtGEMNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDDNVSATGMRIL 319
Cdd:cd01562 213 GKPVTL-PEVDTIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLL 263
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
39-260 |
6.47e-31 |
|
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: 118.00 E-value: 6.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 39 TPLVSLPHLAKQLGVKaILVKDESKRFGLnAFKVLGGSYALgrQLAKHLGidiseinlktvaskLEKPLVFTTATAGNHG 118
Cdd:cd00640 1 TPLVRLKRLSKLGGAN-IYLKLEFLNPTG-SFKDRGALNLI--LLAEEEG--------------KLPKGVIIESTGGNTG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 119 TGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDN-GWMLVQDtawdgyeEIPTWIS 197
Cdd:cd00640 63 IALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQ-------FDNPANI 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1588536696 198 QGYMTMADEAIEQaqaLEFGAPTHVLLQAGVGAMAGGVLGYLadKLGADTFETIIAEPAAADC 260
Cdd:cd00640 136 AGQGTIGLEILEQ---LGGQKPDAVVVPVGGGGNIAGIARAL--KELLPNVKVIGVEPEVVTV 193
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
24-342 |
2.90e-19 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 87.44 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 24 QQAREFHRQIEGY-QPTPLVSLPHLAKQLGVKAILVKDESKRFGlnAFKVLGGSYALgRQLAKHlgidiseinlktvask 102
Cdd:PRK06815 5 DAILEAHQRLRPQvRVTPLEHSPLLSQHTGCEVYLKCEHLQHTG--SFKFRGASNKL-RLLNEA---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 103 lEKPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVQ 182
Cdd:PRK06815 66 -QRQQGVITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYIS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 183 DtawdgYEEIPTWISQGymTMADEAIEQAQALEfgaptHVLLQAGVGAMAGGVLGYLaDKLGADTfETIIAEPAAADCIF 262
Cdd:PRK06815 145 P-----YNDPQVIAGQG--TIGMELVEQQPDLD-----AVFVAVGGGGLISGIATYL-KTLSPKT-EIIGCWPANSPSLY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 263 RSGEKGEMVNVTgEMNSIMAGLACG-EPNPVTWPVLRDCSNHFVSVDDNVSATGMRILgnpLSGDDQVISGESGAITLGL 341
Cdd:PRK06815 211 TSLEAGEIVEVA-EQPTLSDGTAGGvEPGAITFPLCQQLIDQKVLVSEEEIKEAMRLI---AETDRWLIEGAAGVALAAA 286
|
.
gi 1588536696 342 L 342
Cdd:PRK06815 287 L 287
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
19-310 |
8.15e-19 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 87.55 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 19 TASQAQQAREFHRQIEG-YQPTPLVSLPHLAKQLGVKAILvkdesKRFGLNA---FKvLGGSYALGRQLakhlgidisei 94
Cdd:PRK08639 5 MTVSAKDIDKAAKRLKDvVPETPLQRNDYLSEKYGANVYL-----KREDLQPvrsYK-LRGAYNAISQL----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 95 nlktvaSKLEKPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGA---ECIVTEVNYDDTVRMANQ 171
Cdd:PRK08639 68 ------SDEELAAGVVCASAGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 172 TAQDNGWMLVqdtawDGYEEIPTWISQGymTMADEAIEQAQALefGAPTHVLLQAGVGAMAGGVLGYLADkLGADTfETI 251
Cdd:PRK08639 142 YAEETGATFI-----PPFDDPDVIAGQG--TVAVEILEQLEKE--GSPDYVFVPVGGGGLISGVTTYLKE-RSPKT-KII 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1588536696 252 IAEPAAADCIFRSGEKGEMVNVTgEMNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDDN 310
Cdd:PRK08639 211 GVEPAGAASMKAALEAGKPVTLE-KIDKFVDGAAVARVGDLTFEILKDVVDDVVLVPEG 268
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
39-349 |
8.66e-18 |
|
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: 83.41 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 39 TPLVSLPHLAKQLGVKAILVKDEskrfGLN---AFKVLGGSYALGRqlAKHLGIDiseinlkTVAsklekplvftTATAG 115
Cdd:cd01563 23 TPLVRAPRLGERLGGKNLYVKDE----GLNptgSFKDRGMTVAVSK--AKELGVK-------AVA----------CASTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 116 NHGTGVA-WAAREmGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVQdtawdgyeEIPT 194
Cdd:cd01563 80 NTSASLAaYAARA-GIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSN--------SLNP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 195 WISQGYMTMADEAIEQaqaLEFGAPTHVLLQAGVGamaGGVLGY-----------LADKLGAdtfeTIIAEPAAADCIFR 263
Cdd:cd01563 151 YRLEGQKTIAFEIAEQ---LGWEVPDYVVVPVGNG---GNITAIwkgfkelkelgLIDRLPR----MVGVQAEGAAPIVR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 264 SGEKG-EMVNVTGEMNSIMAGLACGepNPVTWP----VLRDCSNHFVSVDDNVSATGMRILGNplsgDDQVISGESGAIT 338
Cdd:cd01563 221 AFKEGkDDIEPVENPETIATAIRIG--NPASGPkalrAVRESGGTAVAVSDEEILEAQKLLAR----TEGIFVEPASAAS 294
|
330
....*....|.
gi 1588536696 339 LGLLFTLCREG 349
Cdd:cd01563 295 LAGLKKLREEG 305
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
17-319 |
9.52e-18 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 83.12 E-value: 9.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 17 LFTASQAQQAREFHRQieGYQPTPLVSLPHLAKQLGVkAILVKDESKRfGLNAFKVLGGSYALGRQLAKHlgidiseinl 96
Cdd:PRK06110 2 MFTLAELEAAAAVVYA--AMPPTPQYRWPLLAERLGC-EVWVKHENHT-PTGAFKVRGGLVYFDRLARRG---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 97 ktvasklEKPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDN 176
Cdd:PRK06110 68 -------PRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 177 GWMLVqdtawdgyeeiPT---WISQGYMTMADEAIEQAQALEFgapthVLLQAGVGAmagGVLGYLA--DKLGADTfETI 251
Cdd:PRK06110 141 GLHMV-----------PSfhpDLVRGVATYALELFRAVPDLDV-----VYVPIGMGS---GICGAIAarDALGLKT-RIV 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1588536696 252 IAEPAAADCIFRSGEKGEMvnVTGEMNSIMA-GLACGEPNPVTWPVLRDCSNHFVSVDDNVSATGMRIL 319
Cdd:PRK06110 201 GVVSAHAPAYALSFEAGRV--VTTPVATTLAdGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAY 267
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
110-282 |
7.98e-17 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 80.38 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 110 TTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVQdtawdGY 189
Cdd:PRK08246 72 VAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCH-----AY 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 190 EEIPTWISQGymTMADEAIEQAqalefGAPTHVLLQAGVGAMAGGVLGYLADKLgadtfETIIAEPAAADCIFRSGEKGE 269
Cdd:PRK08246 147 DQPEVLAGAG--TLGLEIEEQA-----PGVDTVLVAVGGGGLIAGIAAWFEGRA-----RVVAVEPEGAPTLHAALAAGE 214
|
170
....*....|...
gi 1588536696 270 MVNVtgEMNSIMA 282
Cdd:PRK08246 215 PVDV--PVSGIAA 225
|
|
| PLN02970 |
PLN02970 |
serine racemase |
111-339 |
9.48e-16 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 77.41 E-value: 9.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 111 TATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVQDtawdgYE 190
Cdd:PLN02970 80 THSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHP-----YN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 191 EIPTWISQGymTMADEAIEQAQALEFgapthVLLQAGVGAMAGGVLgyLADKLGADTFETIIAEPAAADCIFRSGEKGEM 270
Cdd:PLN02970 155 DGRVISGQG--TIALEFLEQVPELDV-----IIVPISGGGLISGIA--LAAKAIKPSIKIIAAEPKGADDAAQSKAAGEI 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1588536696 271 VNVTgEMNSIMAGLAcGEPNPVTWPVLRDCSNHFVSVDDNVSATGMRILGNPLsgddQVISGESGAITL 339
Cdd:PLN02970 226 ITLP-VTNTIADGLR-ASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERL----KVVVEPSGAIGL 288
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
30-309 |
1.74e-13 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 70.96 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 30 HRQIEGY-QPTPLVSLPHLAKQLGVKaILVKDES-KRFGlnAFKVLGGsyalgrqlakhlgidiseinLKTVASKLEK-- 105
Cdd:PRK06608 14 HNRIKQYlHLTPIVHSESLNEMLGHE-IFFKVESlQKTG--AFKVRGV--------------------LNHLLELKEQgk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 106 -PLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTevnydDTVRMANQTA-QDNGwmlvQD 183
Cdd:PRK06608 71 lPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILT-----NTRQEAEEKAkEDEE----QG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 184 TAWdgyeeIPTWISQ----GYMTMADEAIEQaqaLEFgAPTHVLLQAGVGAMAGGVlgYLADKLGADTFETIIAEPAAAD 259
Cdd:PRK06608 142 FYY-----IHPSDSDstiaGAGTLCYEALQQ---LGF-SPDAIFASCGGGGLISGT--YLAKELISPTSLLIGSEPLNAN 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1588536696 260 CIFRSGEKGEMVNVTGEMNSIMAGLACGEPNPVTWPVLRDCsNHFVSVDD 309
Cdd:PRK06608 211 DAYLSLKNNKIYRLNYSPNTIADGLKTLSVSARTFEYLKKL-DDFYLVEE 259
|
|
| THD1 |
TIGR02079 |
threonine dehydratase; This model represents threonine dehydratase, the first step in the ... |
38-390 |
3.77e-13 |
|
threonine dehydratase; This model represents threonine dehydratase, the first step in the pathway converting threonine into isoleucine. At least two other clades of biosynthetic threonine dehydratases have been characterized by models (TIGR01124 and TIGR01127). Those sequences described by this model are exclusively found in species containg the rest of the isoleucine pathway and which are generally lacking in members of the those other two clades of threonine dehydratases. Members of this clade are also often gene clustered with other elements of the isoleucine pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 273957 [Multi-domain] Cd Length: 409 Bit Score: 70.16 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 38 PTPLVSLPHLAKQLGVKAILVKDESKRfgLNAFKVLGGSYALGRqlakhlgidiseinlktvASKLEKPLVFTTATAGNH 117
Cdd:TIGR02079 16 HTPLQLNERLSEKYGANIYLKREDLQP--VRSYKIRGAYNFLKQ------------------LSDAQLAKGVVCASAGNH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 118 GTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAE---CIVTEVNYDDTVRMANQTAQDNGWMLvqdtawdgyeeIPT 194
Cdd:TIGR02079 76 AQGFAYACRHLGVHGTVFMPATTPKQKIDRVKIFGGEfieIILVGDTFDQCAAAAREHVEDHGGTF-----------IPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 195 W----ISQGYMTMADEAIEQAQAlefgAPTHVLLQAGVGAMAGGVLGYLADKlgaDTFETIIA-EPAAADCIFRSGEKGE 269
Cdd:TIGR02079 145 FddprIIEGQGTVAAEILDQLPE----KPDYVVVPVGGGGLISGLTTYLAGT---SPKTKIIGvEPEGAPSMKASLEAGE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 270 MVNVTgEMNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDDNVSATGMRILGNplsgDDQVISGESGAITLGLLFTLCREG 349
Cdd:TIGR02079 218 VVTLD-KIDNFVDGAAVKRVGDLNFKALKDVPDEVTLVPEGAVCTTILDLYN----LEGIVAEPAGALSIAALERLGEEI 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1588536696 350 ADQAVRDEL-GLNQDATimlfstegDTNQPRYRDIVWNGLHH 390
Cdd:TIGR02079 293 KGKTVVCVVsGGNNDIE--------RTEEIRERSLLYEGLKH 326
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
39-371 |
1.27e-12 |
|
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: 68.69 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 39 TPLVSLPHLAKQLGVKaILVKDEskrfGLN---AFKVLGgSYALGRqLAKHLGIdiseinlKTVAsklekplvftTATAG 115
Cdd:COG0498 67 TPLVKAPRLADELGKN-LYVKEE----GHNptgSFKDRA-MQVAVS-LALERGA-------KTIV----------CASSG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 116 NhgTGVAWAA--REMGQKAVVYMPKGSSqASVNRIQ--GLGAECIVTEVNYDDTVRMANQTAQDNGWMLVQDTAWDGYEe 191
Cdd:COG0498 123 N--GSAALAAyaARAGIEVFVFVPEGKV-SPGQLAQmlTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINPARLE- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 192 iptwisqGYMTMADEAIEQAQAlefgAPTHVLLqaGVGAmAGGVLG-YLA----DKLGADT----FETIIAEPAAAdcIF 262
Cdd:COG0498 199 -------GQKTYAFEIAEQLGR----VPDWVVV--PTGN-GGNILAgYKAfkelKELGLIDrlprLIAVQATGCNP--IL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 263 RSGEKGEMVNVTGEMNSIMAGLACGepNPVTWP----VLRDCSNHFVSVDDNVSATGMRILGNpLSGddqvISGE-SGAI 337
Cdd:COG0498 263 TAFETGRDEYEPERPETIAPSMDIG--NPSNGEralfALRESGGTAVAVSDEEILEAIRLLAR-REG----IFVEpATAV 335
|
330 340 350
....*....|....*....|....*....|....
gi 1588536696 338 TLGllftlcreGADQAvRDELGLNQDATIMLFST 371
Cdd:COG0498 336 AVA--------GLRKL-REEGEIDPDEPVVVLST 360
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
39-178 |
1.06e-11 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 65.79 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 39 TPLVSLPHLAKQLGVKAILVKDEskrfGLN---AFKVLGGSYALGRqlAKHLGIdiseinlktvaSKLEKPlvfttaTAG 115
Cdd:PRK08197 80 TPLLPLPRLGKALGIGRLWVKDE----GLNptgSFKARGLAVGVSR--AKELGV-----------KHLAMP------TNG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1588536696 116 NhgTGVAWA--AREMGQKAVVYMPKGSSQASVNRIQGLGAEciVTEVN--YDDTVRMANQTAQDNGW 178
Cdd:PRK08197 137 N--AGAAWAayAARAGIRATIFMPADAPEITRLECALAGAE--LYLVDglISDAGKIVAEAVAEYGW 199
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
97-309 |
4.79e-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: 63.09 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 97 KTVASKLEKPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVT-EVNYDDTVRMANQ-TAQ 174
Cdd:cd06448 42 KSAKQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHgKVWWEADNYLREElAEN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 175 DNGWMLVQ----DTAWDGYEeiptwisqgymTMADEAIEQAQalEFGAPTHVLLQAGVGAMAGGVLGYLaDKLGADTFET 250
Cdd:cd06448 122 DPGPVYVHpfddPLIWEGHS-----------SMVDEIAQQLQ--SQEKVDAIVCSVGGGGLLNGIVQGL-ERNGWGDIPV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1588536696 251 IIAEPAAADCIFRSGEKGEMVNVTgEMNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDD 309
Cdd:cd06448 188 VAVETEGAHSLNASLKAGKLVTLP-KITSVATSLGAKTVSSQALEYAQEHNIKSEVVSD 245
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
39-268 |
6.19e-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: 62.76 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 39 TPLVSLPHLAKQLGVKaILVKDESkrfgLNafkvLGGSyalgrqlAKH---LGIdiseInLKTVASKLEKPLvfTT---A 112
Cdd:COG0031 14 TPLVRLNRLSPGPGAE-IYAKLES----FN----PGGS-------VKDriaLSM----I-EDAEKRGLLKPG--GTiveA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 113 TAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVT--EVNYDDTVRMANQTAQ--DNGWMLVQDT---A 185
Cdd:COG0031 71 TSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTpgAEGMKGAIDKAEELAAetPGAFWPNQFEnpaN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 186 WDGYEEiptwisqgymTMADEAIEQAQalefGAPTHVLLQAGVGAMAGGVLGYLADKlGADTfETIIAEPaaADCIFRSG 265
Cdd:COG0031 151 PEAHYE----------TTGPEIWEQTD----GKVDAFVAGVGTGGTITGVGRYLKER-NPDI-KIVAVEP--EGSPLLSG 212
|
...
gi 1588536696 266 EKG 268
Cdd:COG0031 213 GEP 215
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
39-308 |
1.40e-10 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 62.89 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 39 TPLVSLPHLAKQLGvKAILVKDESKRfGLNAFKVLGGSYALGRqlakhlgidiseinlkTVASKLEKPLVftTATAGNHG 118
Cdd:PRK12483 38 TPLQRAPNLSARLG-NQVLLKREDLQ-PVFSFKIRGAYNKMAR----------------LPAEQLARGVI--TASAGNHA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 119 TGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVQDtawdgYEEIPTWISQ 198
Cdd:PRK12483 98 QGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPP-----FDDPDVIAGQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 199 GymTMADEAIEQAQalefGAPTHVLLQAGVGAMAGGVLGYLadKLGADTFETIIAEPAAADCIFRSGEKGEMVnVTGEMN 278
Cdd:PRK12483 173 G--TVAMEILRQHP----GPLDAIFVPVGGGGLIAGIAAYV--KYVRPEIKVIGVEPDDSNCLQAALAAGERV-VLGQVG 243
|
250 260 270
....*....|....*....|....*....|
gi 1588536696 279 SIMAGLACGEPNPVTWPVLRDCSNHFVSVD 308
Cdd:PRK12483 244 LFADGVAVAQIGEHTFELCRHYVDEVVTVS 273
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
37-271 |
1.55e-10 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 62.46 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 37 QPTPLVSLPHLAKQLGVKaILVKDESkRFGLNAFKvLGGSYALGRQLAkhlgidiseinlktvASKLEKPLVftTATAGN 116
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQ-VLLKRED-LQPVFSFK-LRGAYNKMAQLT---------------EEQLARGVI--TASAGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 117 HGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVQ---DtawdgyeeiP 193
Cdd:PRK09224 79 HAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHpfdD---------P 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 194 TWIS-QGymTMADEAIEQAQalefGAPTHVLLQAGVGAMAGGVLGYLAdKLGADTfeTIIA-EPAAADCIFRSGEKGEMV 271
Cdd:PRK09224 150 DVIAgQG--TIAMEILQQHP----HPLDAVFVPVGGGGLIAGVAAYIK-QLRPEI--KVIGvEPEDSACLKAALEAGERV 220
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
39-271 |
1.77e-10 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 62.63 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 39 TPLVSLPHLAKQLGVKAILvkdesKRFGLN---AFKvLGGSYALGRQLAKhlgidiseinlktvaSKLEKPLVftTATAG 115
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLL-----KREDLQpvfSFK-LRGAYNMMAKLPK---------------EQLDKGVI--CSSAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 116 NHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVqdTAWDGYEEIptw 195
Cdd:PLN02550 167 NHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFI--PPFDHPDVI--- 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1588536696 196 ISQGYMTMadEAIEQAQalefgAPTH-VLLQAGVGAMAGGVLGYLadKLGADTFETIIAEPAAADCIFRSGEKGEMV 271
Cdd:PLN02550 242 AGQGTVGM--EIVRQHQ-----GPLHaIFVPVGGGGLIAGIAAYV--KRVRPEVKIIGVEPSDANAMALSLHHGERV 309
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
110-178 |
2.66e-10 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 60.88 E-value: 2.66e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1588536696 110 TTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGW 178
Cdd:PRK06381 67 TVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGI 135
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
38-235 |
2.66e-10 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 61.18 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 38 PTPLvslpHLAKQLGVkaILVKDESKRFGlnAFKVLGgsyALGRQLAkhlGIDISEinlktvasklEKPLVftTATAGNH 117
Cdd:PRK08813 39 PTPL----HYAERFGV--WLKLENLQRTG--SYKVRG---ALNALLA---GLERGD----------ERPVI--CASAGNH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 118 GTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLVqdTAWDGYEEIPtwiS 197
Cdd:PRK08813 93 AQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFL--SAFDDPDVIA---G 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1588536696 198 QGYMtmadeAIEQAQAlefgAPTHVLLQAGVGAMAGGV 235
Cdd:PRK08813 168 QGTV-----GIELAAH----APDVVIVPIGGGGLASGV 196
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
39-268 |
4.37e-10 |
|
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: 60.22 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 39 TPLVSLPHLAKQLGVKaILVKDESkrfgLNAfkvlGGS-----------YALGRQLAKHLGIdISEinlktvasklekpl 107
Cdd:cd01561 3 TPLVRLNRLSPGTGAE-IYAKLEF----FNP----GGSvkdrialymieDAEKRGLLKPGTT-IIE-------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 108 vfttATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECI-VTEVNYDDT---VRMANQTAQ--DNGWMLV 181
Cdd:cd01561 59 ----PTSGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVIlTPEAEADGMkgaIAKARELAAetPNAFWLN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 182 Q--DTA-WDGYEEiptwisqgymTMADEAIEQAQalefGAPTHVLLQAGVGAMAGGVLGYLADKLGAdtFETIIAEPAAA 258
Cdd:cd01561 135 QfeNPAnPEAHYE----------TTAPEIWEQLD----GKVDAFVAGVGTGGTITGVARYLKEKNPN--VRIVGVDPVGS 198
|
250
....*....|
gi 1588536696 259 DcIFRSGEKG 268
Cdd:cd01561 199 V-LFSGGPPG 207
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
111-181 |
1.18e-07 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 53.20 E-value: 1.18e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1588536696 111 TATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLV 181
Cdd:PRK08638 80 ACSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFI 150
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
25-235 |
1.87e-07 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 52.28 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 25 QARefhRQIEGYQP-TPLVSLPHLAKQLGVKAILVKDESKRFGlnAFKVLGGSYALgrqlakhlgidiseinLKTVASKL 103
Cdd:PRK07476 8 RAR---RRIAGRVRrTPLVASASLSARAGVPVWLKLETLQPTG--SFKLRGATNAL----------------LSLSAQER 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 104 EKPLVftTATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDtvrmanqtAQDNGWMLVQD 183
Cdd:PRK07476 67 ARGVV--TASTGNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDD--------AQAEVERLVRE 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1588536696 184 TawdGYEEIPTW----ISQGYMTMADEAIEQAQALEfgaptHVLLQAGVGAMAGGV 235
Cdd:PRK07476 137 E---GLTMVPPFddprIIAGQGTIGLEILEALPDVA-----TVLVPLSGGGLASGV 184
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
111-319 |
4.62e-07 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 51.17 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 111 TATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLvqdtawdgye 190
Cdd:PRK07048 77 TFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTL---------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 191 eIPTW----ISQGYMTMADEAIEQAQALEFgapthVLLQAGVGAMAGGVLgyLADKLGADTFETIIAEPAAADCIFRSGE 266
Cdd:PRK07048 147 -IPPYdhphVIAGQGTAAKELFEEVGPLDA-----LFVCLGGGGLLSGCA--LAARALSPGCKVYGVEPEAGNDGQQSFR 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1588536696 267 KGEMVNVTGEmNSIMAGLACGEPNPVTWPVLRDCSNHFVSVDDNVSATGMRIL 319
Cdd:PRK07048 219 SGEIVHIDTP-RTIADGAQTQHLGNYTFPIIRRLVDDIVTVSDAELVDAMRFF 270
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
111-181 |
4.33e-06 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 48.35 E-value: 4.33e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1588536696 111 TATAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTEVNYDDTVRMANQTAQDNGWMLV 181
Cdd:PRK07334 76 AMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFV 146
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
21-241 |
2.40e-05 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 46.56 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 21 SQAQQAREFHRQIEGYQ------PTPLVSLPHLAKQLGVKAIL-VKDESKRFGLN---AFKVlggSYALGRQLakhlgid 90
Cdd:PRK13802 303 TQAKADPEFHKELATLNqryvgrPSPLTEAPRFAERVKEKTGLdARVFLKREDLNhtgAHKI---NNALGQAL------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 91 iseinlktVASKLEKPLVFTTATAGNHGTGVAWAAREMGQKAVVYMPK--GSSQA-SVNRIQGLGAEciVTEVNYDDTV- 166
Cdd:PRK13802 373 --------LVKRMGKTRVIAETGAGQHGVATATVCAMLGLKCRIYMGQidARRQAlNVARMRMLGAE--VVEVTLGDRIl 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 167 -RMANQTAQDngWML-VQDTAW-----DGYEEIPTWISQGYMTMADEAIEQAQALeFGA--PTHVLLQAGVGAMAGGVLG 237
Cdd:PRK13802 443 kDAINEALRD--WVTnVKDTHYllgtvAGPHPFPAMVRDFQKIIGEEAKQQLQDW-YGIdhPDAICACVGGGSNAIGVMN 519
|
....
gi 1588536696 238 YLAD 241
Cdd:PRK13802 520 AFLD 523
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
28-156 |
2.44e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 43.26 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 28 EFHRQIEGY--QPTPLVSLPHLAKQLGVKAILvkdesKRFGLNAfkvlGGSYALGRQLAKHLgidiseinlktVASKLEK 105
Cdd:PRK13803 259 TFKRLLQNYagRPTPLTEAKRLSDIYGARIYL-----KREDLNH----TGSHKINNALGQAL-----------LAKRMGK 318
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1588536696 106 PLVFTTATAGNHGTGVAWAAREMGQKAVVYMPKGS--SQA-SVNRIQGLGAECI 156
Cdd:PRK13803 319 TRIIAETGAGQHGVATATACALFGLKCTIFMGEEDikRQAlNVERMKLLGANVI 372
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
21-156 |
1.05e-03 |
|
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: 40.98 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 21 SQAQQAREFHRQIEGY------QPTPLVSLPHLAKQLGVKAILVKDEskrfGLNAfkvlGGSY----ALGrQ--LAKHLG 88
Cdd:cd06446 11 SKERYDPDFPEELRELykdyvgRPTPLYRAKRLSEYLGGAKIYLKRE----DLNH----TGAHkinnALG-QalLAKRMG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1588536696 89 IdiseinlKTVasklekplvfTTAT-AGNHGTGVAWAAREMGQKAVVYMPKGS--SQAS-VNRIQGLGAECI 156
Cdd:cd06446 82 K-------KRV----------IAETgAGQHGVATATACALFGLECEIYMGAVDveRQPLnVFRMELLGAEVV 136
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
113-182 |
2.13e-03 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 39.84 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 113 TAGNHGTGVAWAAREMGQKAVVYMPKGSSQASVNRIQGLGAECIVTE-VNYDD-------TVRMANQTAQ---DNGWMLV 181
Cdd:PRK10717 71 TAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPaAPYANpnnyvkgAGRLAEELVAsepNGAIWAN 150
|
.
gi 1588536696 182 Q 182
Cdd:PRK10717 151 Q 151
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
27-154 |
7.38e-03 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 38.31 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1588536696 27 REFHRQIEGYQ--PTPLVSLPHLAKQLGVKAILVKDESkrfgLN---AFK---VLGgsYALgrqLAKHLGidiseinlkt 98
Cdd:PRK13028 49 AELRYLLKHYVgrPTPLYHAKRLSEELGGAQIYLKRED----LNhtgAHKinnCLG--QAL---LAKRMG---------- 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1588536696 99 vasklEKPLVFTTAtAGNHGTGVAWAAREMGQKAVVYMpkGS----SQA-SVNRIQGLGAE 154
Cdd:PRK13028 110 -----KKRLIAETG-AGQHGVATATAAALFGLECEIYM--GEvdieRQHpNVFRMKLLGAE 162
|
|
| |
