|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
6-300 |
5.02e-85 |
|
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: 258.38 E-value: 5.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 6 TPLILHPGLSTPT-RRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRK---VVCPSGGNAGLATAVAAANLGLKACIVV 81
Cdd:cd06448 2 TPLIESTALSKTAgCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNEcvhVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 82 PNTTPETTRARIRKTGAEVIVHGKVW-DEANQRAKELAKG-ADTEYVPAFDHPVLWEGHSTMVDEI---LEDCPQVDALV 156
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENdPGPVYVHPFDDPLIWEGHSSMVDEIaqqLQSQEKVDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 157 TSVGGGGLLAGLLTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAAQVAAWPVQHILDFPHECV 236
Cdd:cd06448 162 CSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517758762 237 VLSDDEAIMGVVRYANDLRQLVEPACGVSLAIAYldHPAI----AEAHD-----VVIVVCGGVSISAQLVAGW 300
Cdd:cd06448 242 VVSDRDAVQACLRFADDERILVEPACGAALAVVY--SGKIldlqLEVLLtpldnVVVVVCGGSNITLEQLKEY 312
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
4-289 |
1.17e-56 |
|
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: 186.01 E-value: 1.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 4 IRTPLILHPGLSTPT-RRIWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGN----------Aglatavaaa 71
Cdd:COG1171 23 RRTPLLRSPTLSERLgAEVYLKLENLQPTGSFKLRGaYNALASLSEEERARGVVAASAGNhaqgvayaarL--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 72 nLGLKACIVVPNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQ 151
Cdd:COG1171 94 -LGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQLPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 152 VDALVTSVGGGGLlAGLLTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAAQVAAWPVQHILDF 231
Cdd:COG1171 173 LDAVFVPVGGGGL-IAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEILRDL 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 517758762 232 PHECVVLSDDEAIMGVVRYANDLRQLVEPACGVSLAiAYLDHPAIAEAHDVVIVVCGG 289
Cdd:COG1171 252 VDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVVLSGG 308
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
1-288 |
1.14e-51 |
|
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: 172.11 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 1 MLHIRTPLILHPGLSTPT-RRIWLKLENLQPSGSFKLRGMGLLCSQAAE-QGKRKVVCPSGGNAGLATAVAAANLGLKAC 78
Cdd:pfam00291 3 LGIGPTPLVRLPRLSKELgVDVYLKLESLNPTGSFKDRGALNLLLRLKEgEGGKTVVEASSGNHGRALAAAAARLGLKVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 79 IVVPNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAK-GADTEYVPAFDHPVLWEGHSTMVDEILEDC-PQVDALV 156
Cdd:pfam00291 83 IVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAeGPGAYYINQYDNPLNIEGYGTIGLEILEQLgGDPDAVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 157 TSVgGGGLLAGLLTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAAQV-AAWPVQHILDFPHEC 235
Cdd:pfam00291 163 VPV-GGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVGEV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 517758762 236 VVLSDDEAIMGVVRYANDLRQLVEPACGVSLAIAYL-DHPAIAEAHDVVIVVCG 288
Cdd:pfam00291 242 VTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLaLAGELKGGDRVVVVLTG 295
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
4-289 |
5.27e-50 |
|
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: 168.05 E-value: 5.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 4 IRTPLILHPGLSTPTR-RIWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVV 81
Cdd:cd01562 16 RRTPLLTSPTLSELLGaEVYLKCENLQKTGSFKIRGaYNKLLSLSEEERAKGVVAASAGNHAQGVAYAAKLLGIPATIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 82 PNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALVTSVGG 161
Cdd:cd01562 96 PETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEILEQVPDLDAVFVPVGG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 162 GgLLAGLLTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAAQVAAWPVQHILDFPHECVVLSDD 241
Cdd:cd01562 176 G-GLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEIIRKLVDDVVTVSED 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 517758762 242 EAIMGVVRYANDLRQLVEPACGVSLAIAYLDHPAIAEAHdVVIVVCGG 289
Cdd:cd01562 255 EIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKK-VVVVLSGG 301
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
6-289 |
2.07e-44 |
|
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: 151.51 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 6 TPLILHPGLSTPT-RRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRK---VVCPSGGNAGLATAVAAANLGLKACIVV 81
Cdd:cd00640 1 TPLVRLKRLSKLGgANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPkgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 82 PNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGA-DTEYVPAFDHPVLWEGHSTMVDEILEDCPQ--VDALVTS 158
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILEQLGGqkPDAVVVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 159 VggggllagllTGLIRHQRMDCRIVACEtqgaasfaaaiaaghpvrlPRIDTVatslgaaqvaawpvqhildfphecvvl 238
Cdd:cd00640 161 Vggggn-iagiARALKELLPNVKVIGVE-------------------PEVVTV--------------------------- 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 517758762 239 SDDEAIMGVVRYANDLRQLVEPACGVSLAIAYLDHPAIAEAHDVVIVVCGG 289
Cdd:cd00640 194 SDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
3-289 |
7.95e-35 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 128.53 E-value: 7.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 3 HIR-TPLILHPGLSTPTRRIWLKLENLQPSGSFKLRGM--GLLCSQAAEQGkrkVVCPSGGNAGLATAVAAANLGLKACI 79
Cdd:PRK08246 20 HIRrTPVLEADGAGFGPAPVWLKLEHLQHTGSFKARGAfnRLLAAPVPAAG---VVAASGGNAGLAVAYAAAALGVPATV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 80 VVPNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALVTSV 159
Cdd:PRK08246 97 FVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 160 GGGGLLAGLLTGLIRHQrmdcRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAAQVAAWPVQHILDFPHECVVLS 239
Cdd:PRK08246 177 GGGGLIAGIAAWFEGRA----RVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVS 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 517758762 240 DDEAIMGVVRYANDLRQLVEPACGVSLAI----AYLdhPAIAEAhdVVIVVCGG 289
Cdd:PRK08246 253 DEAIIAARRALWEELRLAVEPGAATALAAllsgAYV--PAPGER--VAVVLCGA 302
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
4-269 |
1.63e-28 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 114.89 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 4 IRTPLILHPGLSTPTR-RIWLKLENLQPSGSFKLRGMGLLCSQ-AAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVV 81
Cdd:PRK12483 36 RETPLQRAPNLSARLGnQVLLKREDLQPVFSFKIRGAYNKMARlPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 82 PNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCP-QVDALVTSVg 160
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPgPLDAIFVPV- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 161 GGGLLAGLLTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAAQVAAWPVQHILDFPHECVVLSD 240
Cdd:PRK12483 195 GGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVDEVVTVST 274
|
250 260
....*....|....*....|....*....
gi 517758762 241 DEAIMGVVRYANDLRQLVEPACgvSLAIA 269
Cdd:PRK12483 275 DELCAAIKDIYDDTRSITEPAG--ALAVA 301
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
5-289 |
1.74e-26 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 106.20 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILHPGLSTPTRR-IWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVP 82
Cdd:PRK07476 19 RTPLVASASLSARAGVpVWLKLETLQPTGSFKLRGaTNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 83 NTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALVTSVgGG 162
Cdd:PRK07476 99 RLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEALPDVATVLVPL-SG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 163 GLLAGLLTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAA-----QVAAWPVQHILDfpheCVV 237
Cdd:PRK07476 178 GGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADSLGGGigldnRYTFAMCRALLD----DVV 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 517758762 238 LSDDEAIMGVVRYANDL-RQLVEPACGVSLAiAYLDHPAIAEAHDVVIVVCGG 289
Cdd:PRK07476 254 LLDEAEIAAGIRHAYREeRLVVEGAGAVGIA-ALLAGKIAARDGPIVVVVSGA 305
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
5-289 |
2.34e-26 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 107.58 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILHPGLSTPTR-RIWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVP 82
Cdd:PRK08639 25 ETPLQRNDYLSEKYGaNVYLKREDLQPVRSYKLRGaYNAISQLSDEELAAGVVCASAGNHAQGVAYACRHLGIPGVIFMP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 83 NTTPETTRARIRKTGA---EVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQ---VDALV 156
Cdd:PRK08639 105 VTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEKegsPDYVF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 157 TSVGGGGLLAGLLTGlIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATslGAA--QVAAWPVQHILDFPHE 234
Cdd:PRK08639 185 VPVGGGGLISGVTTY-LKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVD--GAAvaRVGDLTFEILKDVVDD 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517758762 235 CVVLSDD---EAIM------GVVryandlrqlVEPAcGvSLAIAYLDHPAIA-EAHDVVIVVCGG 289
Cdd:PRK08639 262 VVLVPEGavcTTILelynkeGIV---------AEPA-G-ALSIAALELYKDEiKGKTVVCVISGG 315
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
4-267 |
3.31e-25 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 105.22 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 4 IRTPLILHPGLSTPTR-RIWLKLENLQPSGSFKLRG----MGLLcsqAAEQGKRKVVCPSGGNAGLATAVAAANLGLKAC 78
Cdd:PRK09224 19 QETPLEKAPKLSARLGnQVLLKREDLQPVFSFKLRGaynkMAQL---TEEQLARGVITASAGNHAQGVALSAARLGIKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 79 IVVPNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQ-VDA--- 154
Cdd:PRK09224 96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAvfv 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 155 ------LVTSVggggllagllTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRI----DTVATslgaAQVAAWP 224
Cdd:PRK09224 176 pvggggLIAGV----------AAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVglfaDGVAV----KRIGEET 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 517758762 225 ---VQHILDfphECVVLSDDE---AIMGVVryaNDLRQLVEPACGVSLA 267
Cdd:PRK09224 242 frlCQEYVD---DVITVDTDEicaAIKDVF---EDTRSIAEPAGALALA 284
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
4-289 |
1.16e-24 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 102.66 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 4 IRTPLILHPGLSTPT-RRIWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVV 81
Cdd:PRK07334 22 LRTPCVHSRTLSQITgAEVWLKFENLQFTASFKERGaLNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIVM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 82 PNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALVTSVGG 161
Cdd:PRK07334 102 PRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLEDAPDLDTLVVPIGG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 162 GGLLAGLLTGLiRHQRMDCRIVACETQG-AASFAAAIAAGHPVrlpRIDTVATSLGAAQVAAWPVQHILDFPHECVVLSD 240
Cdd:PRK07334 182 GGLISGMATAA-KALKPDIEIIGVQTELyPSMYAAIKGVALPC---GGSTIAEGIAVKQPGQLTLEIVRRLVDDILLVSE 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 517758762 241 DEAIMGVVRYANDLRQLVEPACGVSLAiAYLDHPAIAEAHDVVIVVCGG 289
Cdd:PRK07334 258 ADIEQAVSLLLEIEKTVVEGAGAAGLA-ALLAYPERFRGRKVGLVLSGG 305
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
3-298 |
2.10e-24 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 100.54 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 3 HIR-TPLILHPGLSTPTR-RIWLKLENLQPSGSFKLRG----MGLLcsqAAEQGKRKVVCPSGGNAGLATAVAAANLGLK 76
Cdd:PRK06815 17 QVRvTPLEHSPLLSQHTGcEVYLKCEHLQHTGSFKFRGasnkLRLL---NEAQRQQGVITASSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 77 ACIVVPNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALV 156
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQPDLDAVF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 157 TSVGGGGlLAGLLTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVA--TSLGAAQVA-AWPV-QHILDfp 232
Cdd:PRK06815 174 VAVGGGG-LISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSdgTAGGVEPGAiTFPLcQQLID-- 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517758762 233 hECVVLSDDEaIMGVVR-YANDLRQLVEPACGVSLAiAYLDHPAIAEAHDVVIVVCGG-VSISAQLVA 298
Cdd:PRK06815 251 -QKVLVSEEE-IKEAMRlIAETDRWLIEGAAGVALA-AALKLAPRYQGKKVAVVLCGKnIVLEKYLEA 315
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
4-146 |
6.92e-23 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 98.84 E-value: 6.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 4 IRTPLILHPGLSTPTR-RIWLKLENLQPSGSFKLRGM-GLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVV 81
Cdd:PLN02550 108 IESPLQLAKKLSERLGvKVLLKREDLQPVFSFKLRGAyNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517758762 82 PNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEIL 146
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIV 252
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
5-163 |
2.17e-22 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 95.19 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILHPGLSTPTR-RIWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVP 82
Cdd:PRK08638 27 KTPLPRSNYLSERCKgEIFLKLENMQRTGSFKIRGaFNKLSSLTDAEKRKGVVACSAGNHAQGVALSCALLGIDGKVVMP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 83 NTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALVTSVGGG 162
Cdd:PRK08638 107 KGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTVIVPIGGG 186
|
.
gi 517758762 163 G 163
Cdd:PRK08638 187 G 187
|
|
| PLN02970 |
PLN02970 |
serine racemase |
5-289 |
3.77e-22 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 94.75 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILHPGL-STPTRRIWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVP 82
Cdd:PLN02970 27 RTPVLTSSSLdALAGRSLFFKCECFQKGGAFKFRGaCNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYIVVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 83 NTTPETTRARIRKTGAEVIvhgkvWDEANQRAKE-----LAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALVT 157
Cdd:PLN02970 107 KNAPACKVDAVIRYGGIIT-----WCEPTVESREavaarVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 158 SVGGGGLLAGLLTGLiRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVA----TSLGAaqvAAWPVqhILDFPH 233
Cdd:PLN02970 182 PISGGGLISGIALAA-KAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIAdglrASLGD---LTWPV--VRDLVD 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 234 ECVVLSDDEAIMGVVRYANDLRQLVEPACGVSLAIA----YLDHPAIAEAHDVVIVVCGG 289
Cdd:PLN02970 256 DVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAAlsdsFRSNPAWKGCKNVGIVLSGG 315
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
5-289 |
2.34e-21 |
|
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.
Pssm-ID: 132036 [Multi-domain] Cd Length: 317 Bit Score: 92.22 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILHPGLSTPT-RRIWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVP 82
Cdd:TIGR02991 19 ETPLVESPSLSELCgVPVHLKLEHRQTTGSFKLRGaTNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 83 NTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVdALVTSVGGG 162
Cdd:TIGR02991 99 ELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVVEQMPDL-ATVLVPLSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 163 GLLAGLLTGLIRHQRMDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAAQVAAWPVQHIL--DFPHECVVLSD 240
Cdd:TIGR02991 178 GGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLGGGIGLDNRVTFAMckALLDEIVLVSE 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 517758762 241 DEAIMGVVRYANDLRQLVEPACGVslAIAYLDHPAIAEAHDVVIVVCGG 289
Cdd:TIGR02991 258 AEIAAGIRHAYAEEREIVEGAGAV--GIAALLAGKIKNPGPCAVIVSGR 304
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
6-288 |
6.76e-21 |
|
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: 91.12 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 6 TPLILHPGLST--PTRRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVPN 83
Cdd:cd01563 23 TPLVRAPRLGErlGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTGNTSASLAAYAARAGIKCVVFLPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 84 TTPETTRARIRKTGAEVI-VHGKVwDEANQRAKELAKGaDTEYVPAFDHPVLWEGHSTMVDEILE----DCPqvDALV-- 156
Cdd:cd01563 103 GKALGKLAQALAYGATVLaVEGNF-DDALRLVRELAEE-NWIYLSNSLNPYRLEGQKTIAFEIAEqlgwEVP--DYVVvp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 157 -------TSVGGGGLLAGLLTGLIRHQRMdcriVACETQGAASFAAAIAAG--HPVRLPRIDTVATSLGAAQVAAWPvqH 227
Cdd:cd01563 179 vgnggniTAIWKGFKELKELGLIDRLPRM----VGVQAEGAAPIVRAFKEGkdDIEPVENPETIATAIRIGNPASGP--K 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517758762 228 ILDFPHE----CVVLSDDEAIMGVVRYANDLRQLVEPACGVSLA--IAYLDHPAIAEAHDVVIVVCG 288
Cdd:cd01563 253 ALRAVREsggtAVAVSDEEILEAQKLLARTEGIFVEPASAASLAglKKLREEGIIDKGERVVVVLTG 319
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
21-152 |
3.21e-19 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 86.60 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 21 IWLKLENLQPSGSFKLRGMGLLCSQAAEQG-KRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETTRARIRKTGAE 99
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGdERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 517758762 100 VIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQV 152
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAHAPDV 182
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
5-159 |
1.92e-17 |
|
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: 80.64 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILHPGLSTPTR-RIWLKLENLQPSGSFKLRgMGL-LCSQAAEQGKRK----VVCPSGGNAGLATAVAAANLGLKAC 78
Cdd:cd01561 2 NTPLVRLNRLSPGTGaEIYAKLEFFNPGGSVKDR-IALyMIEDAEKRGLLKpgttIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 79 IVVPNTTPETTRARIRKTGAEVIV---HGKVW-DEANQRAKELAKGADTEYVP-AFDHPVLWEGH--STMvDEILEDCP- 150
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILtpeAEADGmKGAIAKARELAAETPNAFWLnQFENPANPEAHyeTTA-PEIWEQLDg 159
|
....*....
gi 517758762 151 QVDALVTSV 159
Cdd:cd01561 160 KVDAFVAGV 168
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
20-299 |
8.37e-17 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 79.29 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 20 RIWLKLENLQPSGSFKLRG-MGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETTRARIRKTGA 98
Cdd:PRK07048 40 QVFFKCENFQRMGAFKFRGaYNALSQFSPEQRRAGVVTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 99 EVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALVTSVGGGGLLAGLLTGLiRHQRM 178
Cdd:PRK07048 120 EVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELFEEVGPLDALFVCLGGGGLLSGCALAA-RALSP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 179 DCRIVACETQGAASFAAAIAAGHPVRLPRIDTVA-----TSLGAAQVAAwpVQHILDfphECVVLSDDEAIMGVVRYAND 253
Cdd:PRK07048 199 GCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIAdgaqtQHLGNYTFPI--IRRLVD---DIVTVSDAELVDAMRFFAER 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 517758762 254 LRQLVEPACGVSLAiAYLDHPAIAEAHDVVIVVCGG-VSIS--AQLVAG 299
Cdd:PRK07048 274 MKIVVEPTGCLGAA-AALRGKVPLKGKRVGVIISGGnVDLArfAALLSG 321
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
20-158 |
1.16e-16 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 79.04 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 20 RIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKR--KVVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETTRARIRKTG 97
Cdd:PRK06608 39 EIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLpdKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYG 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517758762 98 AEVIVHgKVWDEANQRAKElAKGADTEYVPAFDHPVLWEGHSTMVDEILEDC-PQVDALVTS 158
Cdd:PRK06608 119 GEVILT-NTRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLgFSPDAIFAS 178
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
21-300 |
2.03e-14 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 72.72 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 21 IWLKLENLQPSGSFKLRGmGLLCSQA---AEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETTRARIRKTG 97
Cdd:PRK06110 38 VWVKHENHTPTGAFKVRG-GLVYFDRlarRGPRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 98 AEVIVHGKVWDEANQRAKELAKGADTEYVPAFdHPVLWEGHSTMVDEILEDCPQVDALVTSVGGGGLLAGLLTGLiRHQR 177
Cdd:PRK06110 117 AELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRAVPDLDVVYVPIGMGSGICGAIAAR-DALG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 178 MDCRIVACETQGAASFAAAIAAGHPVRLPRIDTVATSLGAAQVAAWPVQHILDFPHECVVLSDDEAIMGVVRYANDLRQL 257
Cdd:PRK06110 195 LKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNV 274
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 517758762 258 VEPACGVSLAIAYLDHPAIAeAHDVVIVVCGGvSISAQLVAGW 300
Cdd:PRK06110 275 AEGAGAAALAAALQERERLA-GKRVGLVLSGG-NIDRAVFARV 315
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
6-147 |
4.18e-14 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 71.96 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 6 TPLILHPGLSTPT--RRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVPN 83
Cdd:PRK08197 80 TPLLPLPRLGKALgiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPA 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 84 TTPETTRARIRKTGAEVI-VHGKVWDEANQRAKELAKgadteyVPAFD-----HPVLWEGHSTMVDEILE 147
Cdd:PRK08197 160 DAPEITRLECALAGAELYlVDGLISDAGKIVAEAVAE------YGWFDvstlkEPYRIEGKKTMGLELAE 223
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
6-119 |
5.95e-14 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 71.77 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 6 TPLILHPGLS-TPTRRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVP-N 83
Cdd:COG0498 67 TPLVKAPRLAdELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPeG 146
|
90 100 110
....*....|....*....|....*....|....*..
gi 517758762 84 TTPETTRARIRKTGAEVI-VHGkVWDEANQRAKELAK 119
Cdd:COG0498 147 KVSPGQLAQMLTYGAHVIaVDG-NFDDAQRLVKELAA 182
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
10-159 |
2.25e-12 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 66.77 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 10 LHPGLsTPTRRI----WLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTT 85
Cdd:PRK08329 60 LTPPI-TPTVKRsikvYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNA 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517758762 86 PETTRARIRKTGAEV-IVHGKVWdEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILEDCPQVDALVTSV 159
Cdd:PRK08329 139 SKEKISLLSRLGAELhFVEGDRM-EVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPV 212
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
5-159 |
3.81e-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: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILHPGLSTPTR-RIWLKLENLQPSGSFKLR-GMGLLcSQAAEQGKRK----VVCPSGGN----------Aglatav 68
Cdd:COG0031 13 NTPLVRLNRLSPGPGaEIYAKLESFNPGGSVKDRiALSMI-EDAEKRGLLKpggtIVEATSGNtgiglamvaaA------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 69 aaanLGLKACIVVPNTTPETTRARIRKTGAEVIV--HGKVWDEANQRAKELAK---GAdteYVPA-FDHPVLWEGH-STM 141
Cdd:COG0031 86 ----KGYRLILVMPETMSKERRALLRAYGAEVVLtpGAEGMKGAIDKAEELAAetpGA---FWPNqFENPANPEAHyETT 158
|
170
....*....|....*....
gi 517758762 142 VDEILEDCP-QVDALVTSV 159
Cdd:COG0031 159 GPEIWEQTDgKVDAFVAGV 177
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
6-148 |
6.70e-10 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 59.44 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 6 TPLILHPGLSTPTRRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTT 85
Cdd:PRK05638 67 TPLIRARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRKV 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517758762 86 PETTRARIRKTGAEVIVHGKVWDEANQRAKELAKGADTEYVPAFDHPVLWEGHSTMVDEILED 148
Cdd:PRK05638 147 DKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEE 209
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
16-148 |
3.91e-09 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 57.05 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 16 TPTRR---IWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETTRAR 92
Cdd:PRK06450 59 TPLIKkgnIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQ 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 93 IRKTGAEVI-VHGkvwdeanqRAKELAKGADTE---YVPAFDHPVLWEGHSTMVDEILED 148
Cdd:PRK06450 139 IESYGAEVVrVRG--------SREDVAKAAENSgyyYASHVLQPQFRDGIRTLAYEIAKD 190
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
5-119 |
5.77e-08 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 53.15 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILHPGLSTP--TRRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVP 82
Cdd:TIGR00260 22 VTPLFRAPALAANvgIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYP 101
|
90 100 110
....*....|....*....|....*....|....*....
gi 517758762 83 N-TTPETTRARIRKTGAEVI-VHGKvWDEANQRAKELAK 119
Cdd:TIGR00260 102 AgKISLGKLAQALGYNAEVVaIDGN-FDDAQRLVKQLFE 139
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
6-159 |
1.52e-07 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 52.17 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 6 TPLILHPGLSTPT-RRIWLKLENLQPSGSFKLRGmGLLCSQAAE-QGKRK----VVCPSGGNAGLATAVAAANLGLKACI 79
Cdd:PRK10717 14 TPLIRLNRASEATgCEILGKAEFLNPGGSVKDRA-ALNIIWDAEkRGLLKpggtIVEGTAGNTGIGLALVAAARGYKTVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 80 VVPNTTPETTRARIRKTGAEVI-------------VHGkvwdeANQRAKELAKGADTEYVPA--FDHPVLWEGH-STMVD 143
Cdd:PRK10717 93 VMPETQSQEKKDLLRALGAELVlvpaapyanpnnyVKG-----AGRLAEELVASEPNGAIWAnqFDNPANREAHyETTGP 167
|
170
....*....|....*..
gi 517758762 144 EILEDCP-QVDALVTSV 159
Cdd:PRK10717 168 EIWEQTDgKVDGFVCAV 184
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
21-147 |
8.33e-05 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 44.03 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 21 IWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRK-----VVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETtrARIRK 95
Cdd:PLN02569 152 LWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAkpvvgVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISI--AQLVQ 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 517758762 96 ---TGAEVIVHGKVWDEANQRAKELakgadTEYVPAFD----HPVLWEGHSTMVDEILE 147
Cdd:PLN02569 230 piaNGALVLSIDTDFDGCMRLIREV-----TAELPIYLanslNSLRLEGQKTAAIEILQ 283
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
73-159 |
3.43e-04 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 41.79 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 73 LGLKACIVVPNTTPETTRARIRKTGAEVIVHGKVWDE----ANQRAKElaKG----ADTEYvPAFDHPVLW--EGHSTMV 142
Cdd:PRK08206 138 LGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDsvrlAAQEAQE--NGwvvvQDTAW-EGYEEIPTWimQGYGTMA 214
|
90
....*....|....*..
gi 517758762 143 DEILEDCPQVDALVTSV 159
Cdd:PRK08206 215 DEAVEQLKEMGVPPTHV 231
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
21-159 |
3.65e-03 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 38.60 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 21 IWLKLENLQPSGSFKLRgMGLLCSQAAEQ------GKRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETTRARIR 94
Cdd:PLN03013 140 IAAKLEIMEPCCSVKDR-IGYSMVTDAEQkgfispGKSVLVEPTSGNTGIGLAFIAASRGYRLILTMPASMSMERRVLLK 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 95 KTGAEVIVH--GKVWDEANQRAKELAKGADTEY-VPAFDHPVLWEGH-STMVDEILEDCP-QVDALVTSV 159
Cdd:PLN03013 219 AFGAELVLTdpAKGMTGAVQKAEEILKNTPDAYmLQQFDNPANPKIHyETTGPEIWDDTKgKVDIFVAGI 288
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
20-159 |
3.72e-03 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 38.45 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 20 RIWLKLENLQPSGSFKLRGMGLLCSQAAEQG-----KRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETTRARIR 94
Cdd:PLN00011 33 RIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGlitpgKSTLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIILR 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517758762 95 KTGAEVI-------VHGKVwdeanQRAKELAKGADTEYVP-AFDHPVLWEGH-STMVDEILEDCP-QVDALVTSV 159
Cdd:PLN00011 113 ALGAEVHltdqsigLKGML-----EKAEEILSKTPGGYIPqQFENPANPEIHyRTTGPEIWRDSAgKVDILVAGV 182
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
19-156 |
5.32e-03 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 38.15 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 19 RRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGGNAGLATAVAAANLGLKACIVVPNTTPETTRARIRKTGA 98
Cdd:PRK06381 31 RKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGA 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517758762 99 EVI-VHGKvWDEANQRAKELAKGADT-EYVPAFDHPVL-WEGHSTMVDEILEDCPQVDALV 156
Cdd:PRK06381 111 EIIyVDGK-YEEAVERSRKFAKENGIyDANPGSVNSVVdIEAYSAIAYEIYEALGDVPDAV 170
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
5-159 |
6.96e-03 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 37.63 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 5 RTPLILhpgLSTPTR----RIWLKLENLQPSGSFKLRGMGLLCSQAAEQ-----GKRKVVCPSGGNAGLATAVAAANLGL 75
Cdd:PLN02556 59 KTPLVY---LNKVTEgcgaYIAAKQEMFQPTSSIKDRPALAMIEDAEKKnlitpGKTTLIEPTSGNMGISLAFMAAMKGY 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517758762 76 KACIVVPNTTPETTRARIRKTGAEVIV--HGKVWDEANQRAKELAKGADTEYV-PAFDHPVLWEGH-STMVDEILEDC-P 150
Cdd:PLN02556 136 KMILTMPSYTSLERRVTMRAFGAELVLtdPTKGMGGTVKKAYELLESTPDAFMlQQFSNPANTQVHfETTGPEIWEDTlG 215
|
....*....
gi 517758762 151 QVDALVTSV 159
Cdd:PLN02556 216 QVDIFVMGI 224
|
|
| |
