|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
10-320 |
4.99e-157 |
|
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: 441.74 E-value: 4.99e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 10 KTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQG---CKHFVCSSAGNAGMATAYAARRLGLPATIV 86
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 87 VPSTTPALTIERLKNEGATVEVVGEML-DEAIQLAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL--SAKPGAI 163
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLqsQEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 164 VLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFS 243
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158508517 244 EVISDQEAVTAIEKFVDDEKILVEPACGAALAAVYSGVVCRLQAEgRLQTPLASLVVIVCGGSNISLAQLQALKAQL 320
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
10-304 |
5.24e-66 |
|
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: 209.47 E-value: 5.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 10 KTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGHLCkMKAKQGCK--HFVCSSAGNAGMATAYAARRLGLPATIVV 87
Cdd:pfam00291 7 PTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLL-LRLKEGEGgkTVVEASSGNHGRALAAAAARLGLKVTIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 88 PSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 167
Cdd:pfam00291 86 PEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 168 GGGGLLCGVVQGLREvGWEDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGV-NTVGAQTLKLFYEHPIFSEVI 246
Cdd:pfam00291 166 GGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgDEPGALALDLLDEYVGEVVTV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158508517 247 SDQEAVTAIEKFVDDEKILVEPACGAALAAVysgvvcRLQAEGRLQtPLASLVVIVCG 304
Cdd:pfam00291 245 SDEEALEAMRLLARREGIVVEPSSAAALAAL------KLALAGELK-GGDRVVVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
9-318 |
2.67e-61 |
|
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: 198.34 E-value: 2.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 9 VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVV 87
Cdd:COG1171 23 RRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaYNALASLSEEERARGVVAASAGNHAQGVAYAARLLGIPATIVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 88 PSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAK-----P-- 160
Cdd:COG1171 103 PETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQLPDLdavfvPvg 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 161 -----GAIVLSvggggllcgvvqgLREVGWeDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVGAQTLKL 235
Cdd:COG1171 182 gggliAGVAAA-------------LKALSP-DIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 236 FYEHPIFSEVISDQEAVTAIEKFVDDEKILVEPACGAALAAVYSGvvcRLQAEGRlqtplaSLVVIVCGGsNISLAQLQA 315
Cdd:COG1171 248 LRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------RVVVVLSGG-NIDPDRLAE 317
|
...
gi 158508517 316 LKA 318
Cdd:COG1171 318 ILE 320
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
2-308 |
1.41e-54 |
|
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: 180.38 E-value: 1.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 2 AAQESLH---VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGckhFVCSSAGNAGMATAY 74
Cdd:cd01562 6 AAAARIKpvvRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 75 AARRLGLPATIVVPSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:cd01562 83 AAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 155 TLsAKPGAIvlsvggggllcgvvqgLREVG---------------WEDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSV 219
Cdd:cd01562 162 QV-PDLDAV----------------FVPVGgggliagiatavkalSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 220 AKALGVNTVGAQTLKLFYEHPifSEVI--SDQEAVTAIEKFVDDEKILVEPACGAALAAVYSGvvcRLQAEGRlqtplaS 297
Cdd:cd01562 225 ADGLAVKRPGELTFEIIRKLV--DDVVtvSEDEIAAAMLLLFEREKLVAEPAGALALAALLSG---KLDLKGK------K 293
|
330
....*....|.
gi 158508517 298 LVVIVCGGsNI 308
Cdd:cd01562 294 VVVVLSGG-NI 303
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
11-305 |
1.93e-54 |
|
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: 178.09 E-value: 1.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGHLCKM---KAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVV 87
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLaeeEGKLPKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 88 PSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL-SAKPGAIvls 166
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 167 vggggllcgvvqglrevgwedvpIIAMETFGAHS-FHAAVKEGKLvtLPKItsvakalgvntVGAQTlklfyehpiFSEV 245
Cdd:cd00640 158 -----------------------VVPVGGGGNIAgIARALKELLP--NVKV-----------IGVEP---------EVVT 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 246 ISDQEAVTAIEKFVDDEKILVEPACGAALAAVYSGVvcrlqaegRLQTPLASLVVIVCGG 305
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLA--------KKLGKGKTVVVILTGG 244
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
11-310 |
2.48e-38 |
|
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130197 [Multi-domain] Cd Length: 380 Bit Score: 139.88 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCkhfVCSSAGNAGMATAYAARRLGLPATIV 86
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANLSEDQRQRGV---VAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 87 VPSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSaKPGAIVLS 166
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEE-GRVFVHPFDDEFVMAGQGTIGLEIMEDIP-DVDTVIVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 167 VGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVI 246
Cdd:TIGR01127 156 VGGGGLISGVASAAKQIN-PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTV 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158508517 247 SDQEAVTAIEKFVDDEKILVEPACGAALAAVYSGVVcrlQAEGRlqtplaSLVVIVCGGsNISL 310
Cdd:TIGR01127 235 DEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKV---DVKGK------KIAVVLSGG-NIDL 288
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
9-321 |
1.68e-32 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 126.45 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 9 VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVV 87
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAyNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 88 PSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELketLSAKPGAIVLS- 166
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAIf 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 167 -----VGGGGLLCGVVQGLRevgwEDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHpi 241
Cdd:PRK12483 192 vpvggGGLIAGIAAYVKYVR----PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHY-- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 242 FSEVI--SDQEAVTAIEKFVDDEKILVEPACGAALAAVySGVVCRLQAEGRlqtplaSLVVIVcGGSNISLAQLQ--ALK 317
Cdd:PRK12483 266 VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGI-KKYAEREGIEGQ------TLVAID-SGANVNFDRLRhvAER 337
|
....
gi 158508517 318 AQLG 321
Cdd:PRK12483 338 AELG 341
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
2-307 |
3.06e-32 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 124.15 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 2 AAQESLH---VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGHL-CKMKAKQGCKHFVCSSAGNAGMATAYAAR 77
Cdd:PRK08639 14 KAAKRLKdvvPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 78 RLGLPATIVVPSTTPALTIERLK---NEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PRK08639 94 HLGIPGVIFMPVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 155 TLS--AKPGAIVLSVGGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVGAQT 232
Cdd:PRK08639 173 QLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158508517 233 LKLFYEHPifSEVIS-DQEAV-TAIEKFVDDEKILVEPACGAALAAVysgvvcrlqAEGRLQTPLASLVVIVCGGSN 307
Cdd:PRK08639 252 FEILKDVV--DDVVLvPEGAVcTTILELYNKEGIVAEPAGALSIAAL---------ELYKDEIKGKTVVCVISGGNN 317
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
9-304 |
9.10e-31 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 121.01 E-value: 9.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 9 VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCkhfVCSSAGNAGMATAYAARRLGLPAT 84
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 85 IVVPSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIV 164
Cdd:PRK09224 96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 165 LSvggggllcgvvqglreVG---------------WEDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVG 229
Cdd:PRK09224 175 VP----------------VGgggliagvaayikqlRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 230 AQTLKLFYEHpiFSEVI---SDqEAVTAIEKFVDDEKILVEPAcGA-ALAAV--YsgvVCRLQAEGRlqtplaSLVVIVC 303
Cdd:PRK09224 239 EETFRLCQEY--VDDVItvdTD-EICAAIKDVFEDTRSIAEPA-GAlALAGLkkY---VAQHGIEGE------TLVAILS 305
|
.
gi 158508517 304 G 304
Cdd:PRK09224 306 G 306
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
27-305 |
6.43e-29 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 113.13 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 27 VFLKMDSSQPSGSFKIRGIGHLCkMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVPSTTPALTIERLKNEGATV 106
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNRL-LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 107 EVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKP---------GAIvlsvgggGLLCGVV 177
Cdd:PRK08246 118 VVVGAEYADALEAAQAFAAET-GALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDtvlvavgggGLI-------AGIAAWF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 178 QGLREVgwedvpiIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQEAVTAIEK 257
Cdd:PRK08246 190 EGRARV-------VAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRA 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 158508517 258 FVDDEKILVEPACGAALAAVYSGVVCRLQAEgrlqtplaSLVVIVCGG 305
Cdd:PRK08246 263 LWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGA 302
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
9-275 |
9.55e-29 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 116.17 E-value: 9.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 9 VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVV 87
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAyNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 88 PSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 167
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEE-GRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 168 GGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVIS 247
Cdd:PLN02550 267 GGGGLIAGIAAYVKRVRPE-VKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
|
250 260
....*....|....*....|....*...
gi 158508517 248 DQEAVTAIEKFVDDEKILVEPACGAALA 275
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALA 373
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
1-277 |
1.19e-28 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 113.83 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 1 MAAQESLH---VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCKHFVCSSAGNAGMATAYAA 76
Cdd:PRK07334 11 RAAAARLAgqvLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGaLNKLLLLTEEERARGVIAMSAGNHAQGVAYHA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 77 RRLGLPATIVVPSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELketL 156
Cdd:PRK07334 91 QRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVALEM---L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 157 SAKP------------GAIvlsvgggGLLCGVVQGLRevgwEDVPIIAMETFGAHSFHAAVKEgklVTLPKITS-VAKAL 223
Cdd:PRK07334 167 EDAPdldtlvvpigggGLI-------SGMATAAKALK----PDIEIIGVQTELYPSMYAAIKG---VALPCGGStIAEGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 158508517 224 GVNTVGAQTLKLFYEHPIFSEVISDQEAVTAIEKFVDDEKILVEPACGAALAAV 277
Cdd:PRK07334 233 AVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAAL 286
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
11-315 |
6.47e-28 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 110.55 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGH-LCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVPS 89
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNkLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 90 TTPALTIERLKNEGATVEVVG-EMLDEAIQLAKALEKNnpGWVYISPFDDPLIWEGHTSLVKELKETLsAKPGAIVLSVG 168
Cdd:PRK06815 101 QASAIKLDAIRALGAEVRLYGgDALNAELAARRAAEQQ--GKVYISPYNDPQVIAGQGTIGMELVEQQ-PDLDAVFVAVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 169 GGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAK--ALGVNTvGAQTLKLFYEHPIFSEVI 246
Cdd:PRK06815 178 GGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgtAGGVEP-GAITFPLCQQLIDQKVLV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158508517 247 SDQEAVTAIEKFVDDEKILVEPACGAALAAVYsgvvcRLQAEGRLQTplasLVVIVCgGSNISLAQLQA 315
Cdd:PRK06815 256 SEEEIKEAMRLIAETDRWLIEGAAGVALAAAL-----KLAPRYQGKK----VAVVLC-GKNIVLEKYLE 314
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
9-156 |
2.74e-27 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 108.90 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 9 VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGH-LCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVV 87
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNaLLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICM 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158508517 88 PSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETL 156
Cdd:PRK07476 98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREE-GLTMVPPFDDPRIIAGQGTIGLEILEAL 165
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
11-304 |
6.64e-26 |
|
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: 104.98 E-value: 6.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVAGT-SVFLKMDSSQPSGSFKIRGighlckM-----KAKQ-GCKHFVCSSAGNAGMATAYAARRLGLPA 83
Cdd:cd01563 23 TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRG------MtvavsKAKElGVKAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 84 TIVVPSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpgWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGA 162
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN--WIYLSNSLNPYRLEGQKTIAFEIAEQLGWEvPDY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 163 IVLSVGGGGLLCGVVQG---LREVGW-EDVP-IIAMETFGAHSFHAAVKEGKLVTLP--KITSVAKALGV-NTVGA-QTL 233
Cdd:cd01563 175 VVVPVGNGGNITAIWKGfkeLKELGLiDRLPrMVGVQAEGAAPIVRAFKEGKDDIEPveNPETIATAIRIgNPASGpKAL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158508517 234 KLFYEHPIFSEVISDQEAVTAIEKFVDDEKILVEPACGAALAAVYsgvvcRLQAEGRLQTPlASLVVIVCG 304
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLK-----KLREEGIIDKG-ERVVVVLTG 319
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
10-316 |
1.44e-23 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 99.07 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 10 KTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGC-KHFVCSSAGNAGMATAYAARRLGLPATIVV 87
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVlNHLLELKEQGKLpDKIVAYSTGNHGQAVAYASKLFGIKTRIYL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 88 PSTTPALTIERLKNEGATVEVVgEMLDEAIQlaKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 167
Cdd:PRK06608 103 PLNTSKVKQQAALYYGGEVILT-NTRQEAEE--KAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFASC 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 168 GGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAVKEGKLVTLPKI-TSVAKALGVNTVGAQTLKLFYEHPIFSEVi 246
Cdd:PRK06608 180 GGGGLISGTYLAKELIS-PTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKKLDDFYLV- 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 247 SDQEAVTAIEKFVDDEKILVEPACGAALAAVYSGVvcrlqaegRLQTPLASLVVIVCGGsNISLAQLQAL 316
Cdd:PRK06608 258 EEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWL--------KTQSKPQKLLVILSGG-NIDPILYNEL 318
|
|
| PLN02970 |
PLN02970 |
serine racemase |
10-313 |
5.98e-22 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 94.36 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 10 KTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCkhfVCSSAGNAGMATAYAARRLGLPATI 85
Cdd:PLN02970 27 RTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 86 VVPSTTPALTIERLKNEGATVeVVGEMLDEAIQLAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLsakPG--AI 163
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGII-TWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQV---PEldVI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 164 VLSVGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVnTVGAQTLklfyehPIFS 243
Cdd:PLN02970 180 IVPISGGGLISGIALAAKAIK-PSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA-SLGDLTW------PVVR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 244 E------VISDQEAVTAIEKFVDDEKILVEPACGAALAAVYSgvvcrlqaEGRLQTPLAS----LVVIVCGGsNISLAQL 313
Cdd:PLN02970 252 DlvddviTVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALS--------DSFRSNPAWKgcknVGIVLSGG-NVDLGVL 322
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
2-156 |
1.10e-19 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 87.87 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 2 AAQESLH---VKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGckhFVCSSAGNAGMATAY 74
Cdd:PRK08638 16 EAKQRLAgriRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 75 AARRLGLPATIVVPSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILE 171
|
..
gi 158508517 155 TL 156
Cdd:PRK08638 172 DL 173
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
10-311 |
5.15e-19 |
|
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: 86.06 E-value: 5.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 10 KTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVP 88
Cdd:TIGR02991 19 ETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGaTNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 89 STTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE------TLSAKPGA 162
Cdd:TIGR02991 99 ELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADR-GLTMLPPFDHPDIVAGQGTLGLEVVEqmpdlaTVLVPLSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 163 IVLSVGGGGLLCGVVQGLREVGwedvpiIAMETFGAhsFHAAVKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIF 242
Cdd:TIGR02991 178 GGLASGVAMAVKAARPDTRVIG------VSMERGAA--MKASLQAGRPVLVAELPTLADSLGGGIGLDNRVTFAMCKALL 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158508517 243 SEVI--SDQEAVTAIEKFVDDEKILVEPACGAALAAVYSGvvcRLQAEGRlqtplaslVVIVCGGSNISLA 311
Cdd:TIGR02991 250 DEIVlvSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAG---KIKNPGP--------CAVIVSGRNIDMD 309
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
11-304 |
7.57e-19 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 86.21 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVAG-TSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCKHFVCSSAGNAGMA-TAYAArRLGLPATIVVP 88
Cdd:PRK08197 80 TPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAwAAYAA-RAGIRATIFMP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 89 STTPALTIERLKNEGATVEVVGEMLDEAIQL-AKALEKNnpGWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGAIVLS 166
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIvAEAVAEY--GWFDVSTLKEPYRIEGKKTMGLELAEQLGWRlPDVILYP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 167 VGGGGLLCGVVQGLRE---VGW--EDVP-IIAMETFG----AHSFHAAVKEGKL----VTLPKITSVAKALGVNTVgaqt 232
Cdd:PRK08197 237 TGGGVGLIGIWKAFDEleaLGWigGKRPrLVAVQAEGcapiVKAWEEGKEESEFwedaHTVAFGIRVPKALGDFLV---- 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158508517 233 LKLFYEHPIFSEVISDQEAVTAIEKFVDDEKILVEPACGAALAAVYsgvvcRLQAEGRLQtPLASLVVIVCG 304
Cdd:PRK08197 313 LDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAAR-----QLRESGWLK-GDERVVLFNTG 378
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
27-276 |
1.70e-18 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 84.68 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 27 VFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVPSTTPALTIERLKNEGAT 105
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGaLNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 106 VEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKetlSAKPGAIVLSVGGGGLLCGVVQGLREVGw 185
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIELA---AHAPDVVIVPIGGGGLASGVALALKSQG- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 186 edVPIIAMETFGAHSFHAAVKeGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQEAVTAIEKFVDDEKIL 265
Cdd:PRK08813 205 --VRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVI 281
|
250
....*....|.
gi 158508517 266 VEPACGAALAA 276
Cdd:PRK08813 282 AEGAGALALAA 292
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
11-276 |
1.38e-17 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 82.94 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVaGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVPST 90
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 91 TPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSakPGAIVLSVGGG 170
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN-GLYNVTPEYNIIGLEGQKTIAFELWEEIN--PTHVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 171 GLLCGVVQGLREV----GWEDVP-IIAMETFGAHSFHAAVkegklVTLPKITSVAKALGvntvgaqtlkLFYEHPIFSE- 244
Cdd:PRK05638 223 SYLYSIYKGFKELleigVIEEIPkLIAVQTERCNPIASEI-----LGNKTKCNETKALG----------LYVKNPVMKEy 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 158508517 245 ------------VISDQEAVTAIEKFVDDEKILVEPACGAALAA 276
Cdd:PRK05638 288 vseaikesggtaVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPA 331
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
10-277 |
1.56e-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: 81.41 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 10 KTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGC----KHFVCSSAGNAGMATAYAARRLGLPATI 85
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 86 VVPSTTPALTIERLKNEGATVEVVGEMLDE----AIQLAKALEKNNPGWVYISPFDDPLIWEGH-TSLVKELKETLSAKP 160
Cdd:cd01561 82 VMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLNQFENPANPEAHyETTAPEIWEQLDGKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 161 GAIVLSVGGGGLLCGVVQGLREVgWEDVPIIAMETFGAHSFHAAVKEGKLVTlpkitsvakALGVNTVGAqtlklFYEHP 240
Cdd:cd01561 162 DAFVAGVGTGGTITGVARYLKEK-NPNVRIVGVDPVGSVLFSGGPPGPHKIE---------GIGAGFIPE-----NLDRS 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 158508517 241 IFSEV--ISDQEAVTAIEKFVDDEKILVEPACGAALAAV 277
Cdd:cd01561 227 LIDEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVAAA 265
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
11-277 |
2.42e-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: 81.78 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVPST 90
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPEG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 91 -TPALTIERLKNEGATVEVVGEMLDEAIQLAKALeKNNPGWVYISPFDdpliW---EGHTSLVKELKETLSAKPGAIVLS 166
Cdd:COG0498 147 kVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKEL-AADEGLYAVNSIN----ParlEGQKTYAFEIAEQLGRVPDWVVVP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 167 VggggllcgvvqG--------------LREVGW-EDVP-IIAMETFGAHSFHAAVKEGKLVTLPK-ITSVAKALGV-NTV 228
Cdd:COG0498 222 T-----------GnggnilagykafkeLKELGLiDRLPrLIAVQATGCNPILTAFETGRDEYEPErPETIAPSMDIgNPS 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 158508517 229 -GAQTLKLFYEHPIFSEVISDQEAVTAIEKFVDDEKILVEPACGAALAAV 277
Cdd:COG0498 291 nGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGL 340
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
2-316 |
2.49e-17 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 81.22 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 2 AAQESL----HvKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCKHFvcsSAGNAGMATA 73
Cdd:PRK07048 13 AAAARLagvaH-RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAGVVTF---SSGNHAQAIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 74 YAARRLGLPATIVVPSTTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELK 153
Cdd:PRK07048 89 LSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER-GLTLIPPYDHPHVIAGQGTAAKELF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 154 E------TLSAKPGAIVLSVGGGGLLCGVVQGLREVGWEdvPIIAMEtfGAHSFHAavkeGKLVTLPKITSVAKalgvnt 227
Cdd:PRK07048 168 EevgpldALFVCLGGGGLLSGCALAARALSPGCKVYGVE--PEAGND--GQQSFRS----GEIVHIDTPRTIAD------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 228 vGAQTLKL-FYEHPIFSE------VISDQEAVTAIEKFVDDEKILVEPACGAALAAVYSGVVcrlQAEGRlqtplaSLVV 300
Cdd:PRK07048 234 -GAQTQHLgNYTFPIIRRlvddivTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKV---PLKGK------RVGV 303
|
330
....*....|....*.
gi 158508517 301 IVCGGsNISLAQLQAL 316
Cdd:PRK07048 304 IISGG-NVDLARFAAL 318
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
11-303 |
2.15e-14 |
|
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: 72.39 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLrdsMALSKVA---GTSVFLKMDSSQPSGSFKIRgIGH------LCKMKAKQGcKHFVCSSAGNAGMATAYAARRLGL 81
Cdd:COG0031 14 TPL---VRLNRLSpgpGAEIYAKLESFNPGGSVKDR-IALsmiedaEKRGLLKPG-GTIVEATSGNTGIGLAMVAAAKGY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 82 PATIVVPSTTPALTIERLKNEGATVEVVGEM--LDEAIQLAKALEKNNPGWVYISPFDDPLIWEGH-TSLVKELKETLSA 158
Cdd:COG0031 89 RLILVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAAETPGAFWPNQFENPANPEAHyETTGPEIWEQTDG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 159 KPGAIVLsvggggllcgvvqG-------------LREVgWEDVPIIAMETFGAHSFhaavkEGKLVTLPKItsvaKALGV 225
Cdd:COG0031 169 KVDAFVA-------------GvgtggtitgvgryLKER-NPDIKIVAVEPEGSPLL-----SGGEPGPHKI----EGIGA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 226 NTVGAqtlklFYEHPIFSEVI--SDQEAVTAIEKFVDDEKILVEPACGAALAAvysgvVCRLQAEgrlQTPLASLVVIVC 303
Cdd:COG0031 226 GFVPK-----ILDPSLIDEVItvSDEEAFAMARRLAREEGILVGISSGAAVAA-----ALRLAKR---LGPGKTIVTILP 292
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
4-277 |
8.68e-14 |
|
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: 70.87 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 4 QESLHVK-TPLRDSMALSK-VAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGL 81
Cdd:TIGR00260 15 LVDLGEGvTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 82 PATIVVPSTtpalTIERLK-----NEGATVEVVGEMLDEAIQLAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL 156
Cdd:TIGR00260 95 KVVVLYPAG----KISLGKlaqalGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLEGQKTYAFEAVEQL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 157 SAK-PGAIVLSVGGGGLLCGVVQG---LREVGWEDVPI-IAMETFGAHSFHAAVKE-GKLVTLPKITSVAKALGV-NTV- 228
Cdd:TIGR00260 171 GWEaPDKVVVPVPNSGNFGAIWKGfkeKKMLGLDSLPVkRGIQAEGAADIVRAFLEgGQWEPIETPETLSTAMDIgNPAn 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 158508517 229 GAQTLKLFYEHPIFSEVISDQEAVTAIEKFVDDEKILVEPACGAALAAV 277
Cdd:TIGR00260 251 WPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAAL 299
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
19-313 |
6.46e-10 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 59.24 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 19 LSKVAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQ-GCKHFVCSSAGNAGMATAYAARRLGLPATIVVPSTTpalTI 96
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGgLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGN---SV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 97 ErlKNE-----GATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFddpliwegHTSLVKELK----ETLSAKP------- 160
Cdd:PRK06110 107 E--KNAamralGAELIEHGEDFQAAREEAARLAAER-GLHMVPSF--------HPDLVRGVAtyalELFRAVPdldvvyv 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 161 ---------GAIVLSVGGggllcgvvqGLRevgwedVPIIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALGVNTVGAQ 231
Cdd:PRK06110 176 pigmgsgicGAIAARDAL---------GLK------TRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 232 TLKLFYEHpiFSEVI--SDQEAVTAIEKFVDDEKILVEPACGAALAAVysgvvcrLQAEGRLQtplASLVVIVCGGSNIS 309
Cdd:PRK06110 241 ALEVIRAG--ADRIVrvTDDEVAAAMRAYFTDTHNVAEGAGAAALAAA-------LQERERLA---GKRVGLVLSGGNID 308
|
....
gi 158508517 310 LAQL 313
Cdd:PRK06110 309 RAVF 312
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
9-276 |
9.53e-10 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 58.98 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 9 VKTPLrdsmalskVAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVP 88
Cdd:PRK06450 57 GRTPL--------IKKGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 89 STTPALTIERLKNEGATVEVVGEMLDEaiqLAKALEknNPGWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGAIVLSV 167
Cdd:PRK06450 129 ETASGGKLKQIESYGAEVVRVRGSRED---VAKAAE--NSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKiPNYVFIPV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 168 GGGGLLCGVVQGLR---EVG-WEDVP-IIAMETFGAHSFHAAVKEGKLVTLPKITSVAKALgvntVGAQTLKLFYEHPIF 242
Cdd:PRK06450 204 SAGTLLLGVYSGFKhllDSGvISEMPkIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADAL----VSTRPFLLDYMVKAL 279
|
250 260 270
....*....|....*....|....*....|....*....
gi 158508517 243 SE-----VISDQEAVTAiEKFVDDEKILVEPACGAALAA 276
Cdd:PRK06450 280 SEygeciVVSDNEIVEA-WKELAKKGLLVEYSSATVYAA 317
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
8-134 |
8.80e-09 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 56.04 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 8 HVKTPLRDSMALSKVAGT-SVFLKmDSSQPSG--SFKIRG-----IGHLCKM------------------KAKQGCKHFV 61
Cdd:PRK08206 42 YAPTPLVALPDLAAELGVgSILVK-DESYRFGlnAFKALGgayavARLLAEKlgldiselsfeeltsgevREKLGDITFA 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158508517 62 CSSAGNAGMATAYAARRLGLPATIVVPSTTpalTIERLKN---EGATVEVVGEMLDEAIQLAKALEKNNpGWVYIS 134
Cdd:PRK08206 121 TATDGNHGRGVAWAAQQLGQKAVIYMPKGS---SEERVDAiraLGAECIITDGNYDDSVRLAAQEAQEN-GWVVVQ 192
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
24-154 |
1.01e-08 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 55.99 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 24 GTSVFLKMDSSQPSGSFKIRGIG-HLCKMKaKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVPSTTPALTIERLKNE 102
Cdd:PRK08329 71 SIKVYFKLDYLQPTGSFKDRGTYvTVAKLK-EEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRL 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 158508517 103 GATVEVVG----EMLDEAIQLAKaleknNPGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PRK08329 150 GAELHFVEgdrmEVHEEAVKFSK-----RNNIPYVSHWLNPYFLEGTKTIAYEIYE 200
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
11-163 |
2.01e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 51.63 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVAGTS-VFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVPS 89
Cdd:PRK06381 16 TPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158508517 90 TTPALTIERLKNEGATVEVVGEMLDEAIQLAKALEKNNpGWVYISPFD--DPLIWEGHTSLVKELKETLSAKPGAI 163
Cdd:PRK06381 96 SYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKEN-GIYDANPGSvnSVVDIEAYSAIAYEIYEALGDVPDAV 170
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
11-120 |
4.98e-04 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 41.72 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 11 TPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCKHFVCSS-AGNAGMATAYAARRLGLPATIVVPS 89
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTRIIAETgAGQHGVATATACALFGLKCTIFMGE 351
|
90 100 110
....*....|....*....|....*....|....*..
gi 158508517 90 TT---PALTIERLKNEGATVEVV---GEMLDEAIQLA 120
Cdd:PRK13803 352 EDikrQALNVERMKLLGANVIPVlsgSKTLKDAVNEA 388
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
36-154 |
4.91e-03 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 38.64 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508517 36 PSGSFKIRGIGHLCKM-----KAKQGCKHFVCSSAGNAGMA-TAYAArRLGLPATIVVPSTTPALT--IERLKNeGATVE 107
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQvnrlrKMAKPVVGVGCASTGDTSAAlSAYCA-AAGIPSIVFLPADKISIAqlVQPIAN-GALVL 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 158508517 108 VVGEMLDEAIQLAKALEKNNPgwVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PLN02569 239 SIDTDFDGCMRLIREVTAELP--IYLANSLNSLRLEGQKTAAIEILQ 283
|
|
| |
