|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
10-320 |
4.15e-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: 442.12 E-value: 4.15e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQG---CRHFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 87 VPNTTPALTIERLKNEGATVEVVGEML-DEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL--SAKPGAI 163
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLqsQEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 164 VLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFS 243
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52783414 244 EVISDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgRLQTPLASLVVIVCGGSNISLAQLQALKVQL 320
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
10-304 |
8.93e-67 |
|
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: 425586 [Multi-domain] Cd Length: 295 Bit Score: 211.40 E-value: 8.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCkMKAKQGC--RHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:pfam00291 7 PTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLL-LRLKEGEggKTVVEASSGNHGRALAAAAARLGLKVTIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 167
Cdd:pfam00291 86 PEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 168 GGGGLLCGVVQGLREvGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGV-NTVGAQTLKLFYEHPIFSEVI 246
Cdd:pfam00291 166 GGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgFEPGALALDLLDEYVGEVVTV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414 247 SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEGRlqtplasLVVIVCG 304
Cdd:pfam00291 245 SDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR-------VVVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine dehydratase [Amino acid transport and metabolism]; |
2-316 |
1.20e-58 |
|
Threonine dehydratase [Amino acid transport and metabolism];
Pssm-ID: 224092 [Multi-domain] Cd Length: 347 Bit Score: 192.05 E-value: 1.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQgcRHFVCSSAGNAGMATAY 74
Cdd:COG1171 14 AAAARLKgvvNPTPLQRSPSLSERLGAEIYLKRENLQPVGSFKIRGaynkLSSLSEEEERA--AGVIAASAGNHAQGVAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 75 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:COG1171 92 AAKRLGIKATIVMPETTPKIKVDATRGYGAEVILHGDNFDDAYAAAEELAEEE-GLTFVPPFDDPDVIAGQGTIALEILE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 155 TLSAKPGAIVLSVGGGGLLCGVVQGLREVGWeDVPIIAMETFGAHSFHAAIKEGKL-VTLPKITSVAKALGVNTVGAQTL 233
Cdd:COG1171 171 QLPDLPDAVFVPVGGGGLISGIATALKALSP-EIKVIGVEPEGAPSMYASLKAGKIvVVLPDVGTIADGLAVKRPGDLTF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 234 KLFYEHPifSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgrlqtplaSLVVIVCGGsNISLA 311
Cdd:COG1171 250 EILRELV--DDIVlvDEDEICAAMRDLFERTKIIAEPAGALALAALLAGKIEPLQGK--------TVVVILSGG-NIDFE 318
|
....*
gi 52783414 312 QLQAL 316
Cdd:COG1171 319 RLAEV 323
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
2-308 |
3.89e-55 |
|
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: 181.53 E-value: 3.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGcrhFVCSSAGNAGMATAY 74
Cdd:cd01562 6 AAAARIKpvvRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 75 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:cd01562 83 AAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 155 TLsAKPGAIvlsvggggllcgvvqgLREVG---------------WEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSV 219
Cdd:cd01562 162 QV-PDLDAV----------------FVPVGgggliagiatavkalSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 220 AKALGVNTVGAQTLKLFYEHPifSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVysrvvcrlqDEGRLQTPLAS 297
Cdd:cd01562 225 ADGLAVKRPGELTFEIIRKLV--DDVVtvSEDEIAAAMLLLFEREKLVAEPAGALALAAL---------LSGKLDLKGKK 293
|
330
....*....|.
gi 52783414 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 |
8.44e-55 |
|
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: 178.86 E-value: 8.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKM---KAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLaeeEGKLPKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL-SAKPGAIvls 166
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 167 vggggllcgvvqglrevgwedvpIIAMETFGAHS-FHAAIKEGKLvtLPKItsvakalgvntVGAQTlklfyehpiFSEV 245
Cdd:cd00640 158 -----------------------VVPVGGGGNIAgIARALKELLP--NVKV-----------IGVEP---------EVVT 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 246 ISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGrlqTPLASLVVIVCGG 305
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAAL-----KLAKKL---GKGKTVVVILTGG 244
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
11-310 |
7.94e-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: 138.34 E-value: 7.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLckmKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 87 VPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSaKPGAIVLS 166
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEE-GRVFVHPFDDEFVMAGQGTIGLEIMEDIP-DVDTVIVP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 167 VGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVI 246
Cdd:TIGR01127 156 VGGGGLISGVASAAKQIN-PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTV 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52783414 247 SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVcrlQDEGRlqtplaSLVVIVCGGsNISL 310
Cdd:TIGR01127 235 DEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKV---DVKGK------KIAVVLSGG-NIDL 288
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
2-307 |
1.84e-32 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 124.53 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHL-CKMKAKQGCRHFVCSSAGNAGMATAYAAR 77
Cdd:PRK08639 14 KAAKRLKdvvPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 78 RLGIPATIVVPNTTPALTIERLK---NEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PRK08639 94 HLGIPGVIFMPVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 155 TLS--AKPGAIVLSVGGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQT 232
Cdd:PRK08639 173 QLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414 233 LKLFYEHPifSEVIS-DQEAVSA--LEKFvDDEKILVEPACGAALAAVysrvvcrlqDEGRLQTPLASLVVIVCGGSN 307
Cdd:PRK08639 252 FEILKDVV--DDVVLvPEGAVCTtiLELY-NKEGIVAEPAGALSIAAL---------ELYKDEIKGKTVVCVISGGNN 317
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
9-321 |
2.51e-32 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 125.68 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 9 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAyNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELketLSAKPGAIVLS- 166
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAIf 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 167 -----VGGGGLLCGVVQGLRevgwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHpi 241
Cdd:PRK12483 192 vpvggGGLIAGIAAYVKYVR----PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHY-- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 242 FSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVySRVVCRLQDEGRlqtplaSLVVIVcGGSNISLAQLQ--ALK 317
Cdd:PRK12483 266 VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGI-KKYAEREGIEGQ------TLVAID-SGANVNFDRLRhvAER 337
|
....
gi 52783414 318 VQLG 321
Cdd:PRK12483 338 AELG 341
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
9-304 |
1.76e-30 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 120.24 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 9 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCrhfVCSSAGNAGMATAYAARRLGIPAT 84
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 85 IVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIV 164
Cdd:PRK09224 96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 165 LSvggggllcgvvqglreVG---------------WEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVG 229
Cdd:PRK09224 175 VP----------------VGgggliagvaayikqlRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414 230 AQTLKLFYEHpiFSEVIS-DQEAVSALEKFV-DDEKILVEPAcGA-ALAAVySRVVCRLQDEGRlqtplaSLVVIVCG 304
Cdd:PRK09224 239 EETFRLCQEY--VDDVITvDTDEICAAIKDVfEDTRSIAEPA-GAlALAGL-KKYVAQHGIEGE------TLVAILSG 306
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
1-277 |
2.45e-30 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 118.46 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 1 MAAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAA 76
Cdd:PRK07334 11 RAAAARLAgqvLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGaLNKLLLLTEEERARGVIAMSAGNHAQGVAYHA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 77 RRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELketL 156
Cdd:PRK07334 91 QRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVALEM---L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 157 SAKP------------GAIvlsvgggGLLCGVVQGLRevgwEDVPIIAMETFGAHSFHAAIKEgklVTLPKITS-VAKAL 223
Cdd:PRK07334 167 EDAPdldtlvvpigggGLI-------SGMATAAKALK----PDIEIIGVQTELYPSMYAAIKG---VALPCGGStIAEGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 52783414 224 GVNTVGAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAV 277
Cdd:PRK07334 233 AVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAAL 286
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
22-305 |
7.17e-30 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 115.44 E-value: 7.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 22 LAGTSVFLKMDSSQPSGSFKIRGIGHLCkMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKN 101
Cdd:PRK08246 34 FGPAPVWLKLEHLQHTGSFKARGAFNRL-LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 102 EGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLsAKPGAIvlsvggggllcgvvqgLR 181
Cdd:PRK08246 113 LGAEVVVVGAEYADALEAAQAFAAET-GALLCHAYDQPEVLAGAGTLGLEIEEQA-PGVDTV----------------LV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 182 EVG-----------WED-VPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQ 249
Cdd:PRK08246 175 AVGgggliagiaawFEGrARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414 250 EAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgrlqtplaSLVVIVCGG 305
Cdd:PRK08246 255 AIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGA 302
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
11-315 |
1.35e-29 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 114.79 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGH-LCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPN 89
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNkLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 90 TTPALTIERLKNEGATVEVVG-EMLDEAIQVAKALEKNnpGWVYISPFDDPLIWEGHTSLVKELKETLsAKPGAIVLSVG 168
Cdd:PRK06815 101 QASAIKLDAIRALGAEVRLYGgDALNAELAARRAAEQQ--GKVYISPYNDPQVIAGQGTIGMELVEQQ-PDLDAVFVAVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 169 GGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAK--ALGVNTvGAQTLKLFYEHPIFSEVI 246
Cdd:PRK06815 178 GGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgtAGGVEP-GAITFPLCQQLIDQKVLV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52783414 247 SDQEAVSALEKFVDDEKILVEPACGAALAAvYSRVVCRLQdeGRlqtplaSLVVIVCgGSNISLAQLQA 315
Cdd:PRK06815 256 SEEEIKEAMRLIAETDRWLIEGAAGVALAA-ALKLAPRYQ--GK------KVAVVLC-GKNIVLEKYLE 314
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
9-156 |
6.75e-29 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 113.14 E-value: 6.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 9 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGH-LCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNaLLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICM 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52783414 88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETL 156
Cdd:PRK07476 98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREE-GLTMVPPFDDPRIIAGQGTIGLEILEAL 165
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
9-314 |
1.07e-28 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 116.17 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 9 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAyNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 167
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEE-GRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 168 GGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVIS 247
Cdd:PLN02550 267 GGGGLIAGIAAYVKRVRPE-VKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 248 DQEAVSALEKFVDDEKILVEPACGAALAAvySRVVCR---LQDEGrlqtplaslVVIVCGGSNISLAQLQ 314
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALAG--AEAYCKyygLKDEN---------VVAITSGANMNFDRLR 404
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
11-304 |
1.07e-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: 107.29 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGighlckM-----KAKQ-GCRHFVCSSAGNAGMATAYAARRLGIPA 83
Cdd:cd01563 23 TPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDRG------MtvavsKAKElGVKAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 84 TIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpgWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGA 162
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN--WIYLSNSLNPYRLEGQKTIAFEIAEQLGWEvPDY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 163 IVLSVGGGGLLCGVVQG---LREVGW-EDVP-IIAMETFGAHSFHAAIKEGKLVTLP--KITSVAKALGV-NTVGA-QTL 233
Cdd:cd01563 175 VVVPVGNGGNITAIWKGfkeLKELGLiDRLPrMVGVQAEGAAPIVRAFKEGKDDIEPveNPETIATAIRIgNPASGpKAL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52783414 234 KLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGRLQTPlASLVVIVCG 304
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLK-----KLREEGIIDKG-ERVVVVLTG 319
|
|
| PLN02970 |
PLN02970 |
serine racemase |
10-313 |
1.13e-24 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 101.68 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCrhfVCSSAGNAGMATAYAARRLGIPATI 85
Cdd:PLN02970 27 RTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 86 VVPNTTPALTIERLKNEGATVeVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLsakPG--AI 163
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGII-TWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQV---PEldVI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 164 VLSVGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVnTVGAQTLklfyehPIFS 243
Cdd:PLN02970 180 IVPISGGGLISGIALAAKAIK-PSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA-SLGDLTW------PVVR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 244 E------VISDQEAVSALEKFVDDEKILVEPACGAALAAVYSrvvcrlqdEGRLQTPLAS----LVVIVCGGsNISLAQL 313
Cdd:PLN02970 252 DlvddviTVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALS--------DSFRSNPAWKgcknVGIVLSGG-NVDLGVL 322
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
10-316 |
1.76e-24 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 101.39 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKaKQGCR--HFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVlNHLLELK-EQGKLpdKIVAYSTGNHGQAVAYASKLFGIKTRIY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 87 VPNTTPALTIERLKNEGATVEVVgEMLDEAIQvaKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLS 166
Cdd:PRK06608 102 LPLNTSKVKQQAALYYGGEVILT-NTRQEAEE--KAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFAS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 167 VGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKI-TSVAKALGVNTVGAQTLKL------FYEH 239
Cdd:PRK06608 179 CGGGGLISGTYLAKELIS-PTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYlkklddFYLV 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52783414 240 PIFSEVISDQEAVSALekfvddeKILVEPACGAALAAVYSRVvcrlqdegRLQTPLASLVVIVCGGsNISLAQLQAL 316
Cdd:PRK06608 258 EEYEIYYWTAWLTHLL-------KVICEPSSAINMVAVVNWL--------KTQSKPQKLLVILSGG-NIDPILYNEL 318
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
2-156 |
9.31e-21 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 90.95 E-value: 9.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGcrhFVCSSAGNAGMATAY 74
Cdd:PRK08638 16 EAKQRLAgriRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 75 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILE 171
|
..
gi 52783414 155 TL 156
Cdd:PRK08638 172 DL 173
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
27-276 |
4.99e-20 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 89.30 E-value: 4.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 27 VFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNEGAT 105
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGaLNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 106 VEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKetlSAKPGAIVLSVGGGGLLCGVVQGLREVGw 185
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIELA---AHAPDVVIVPIGGGGLASGVALALKSQG- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 186 edVPIIAMETFGAHSFHAAIKeGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKIL 265
Cdd:PRK08813 205 --VRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVI 281
|
250
....*....|.
gi 52783414 266 VEPACGAALAA 276
Cdd:PRK08813 282 AEGAGALALAA 292
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
10-154 |
1.30e-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: 87.60 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVP 88
Cdd:TIGR02991 19 ETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGaTNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMS 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414 89 NTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:TIGR02991 99 ELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADR-GLTMLPPFDHPDIVAGQGTLGLEVVE 163
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
11-304 |
9.31e-19 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 85.82 E-value: 9.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMA-TAYAArRLGIPATIVVP 88
Cdd:PRK08197 80 TPLLPLPRLGKaLGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAwAAYAA-RAGIRATIFMP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 89 NTTPALTIERLKNEGATVEVV-GEMLDEAIQVAKALEKNnpGWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGAIVLS 166
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVdGLISDAGKIVAEAVAEY--GWFDVSTLKEPYRIEGKKTMGLELAEQLGWRlPDVILYP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 167 VGGGGLLCGVVQGLRE---VGW--EDVP-IIAMETFG----AHSFHAAIKEGKL----VTLPKITSVAKALGVNTVgaqt 232
Cdd:PRK08197 237 TGGGVGLIGIWKAFDEleaLGWigGKRPrLVAVQAEGcapiVKAWEEGKEESEFwedaHTVAFGIRVPKALGDFLV---- 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52783414 233 LKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGRLQtPLASLVVIVCG 304
Cdd:PRK08197 313 LDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAAR-----QLRESGWLK-GDERVVLFNTG 378
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
2-316 |
5.74e-18 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 82.76 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 2 AAQESL----HvKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAA 76
Cdd:PRK07048 13 AAAARLagvaH-RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaYNALSQFSPEQRRAGVVTFSSGNHAQAIALSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 77 RRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE-- 154
Cdd:PRK07048 92 RLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER-GLTLIPPYDHPHVIAGQGTAAKELFEev 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 155 ----TLSAKPGAIVLSVGGGGLLCGVVQGLREVGWEdvPIIAMEtfGAHSFHAaikeGKLVTLPKITSVAKalgvntvGA 230
Cdd:PRK07048 171 gpldALFVCLGGGGLLSGCALAARALSPGCKVYGVE--PEAGND--GQQSFRS----GEIVHIDTPRTIAD-------GA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 231 QTLKL-FYEHPIFSE------VISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcrlqdEGRLQTPLASLVVIVC 303
Cdd:PRK07048 236 QTQHLgNYTFPIIRRlvddivTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAAL---------RGKVPLKGKRVGVIIS 306
|
330
....*....|...
gi 52783414 304 GGsNISLAQLQAL 316
Cdd:PRK07048 307 GG-NVDLARFAAL 318
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
11-276 |
2.73e-17 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 82.17 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSKLaGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNT 90
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 91 TPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSakPGAIVLSVGGG 170
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN-GLYNVTPEYNIIGLEGQKTIAFELWEEIN--PTHVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 171 GLLCGVVQGLREV----GWEDVP-IIAMETFGAHSFHAAIkegklVTLPKITSVAKALGvntvgaqtlkLFYEHPIFSE- 244
Cdd:PRK05638 223 SYLYSIYKGFKELleigVIEEIPkLIAVQTERCNPIASEI-----LGNKTKCNETKALG----------LYVKNPVMKEy 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 52783414 245 ------------VISDQEAVSALEKFVDDEKILVEPACGAALAA 276
Cdd:PRK05638 288 vseaikesggtaVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPA 331
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
10-290 |
4.10e-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: 79.87 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGC----RHFVCSSAGNAGMATAYAARRLGIPATI 85
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 86 VVPNTTPALTIERLKNEGATVEVVGEMLDE----AIQVAKALEKNNPGWVYISPFDDPLIWEGH-TSLVKELKETLSAKP 160
Cdd:cd01561 82 VMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLNQFENPANPEAHyETTAPEIWEQLDGKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 161 GAIVLSVGGGGLLCGVVQGLREVgWEDVPIIAMETFGAHSF-----HAAIKEGklvtlpkitsvakaLGVNTVGAqtlkl 235
Cdd:cd01561 162 DAFVAGVGTGGTITGVARYLKEK-NPNVRIVGVDPVGSVLFsggppGPHKIEG--------------IGAGFIPE----- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414 236 FYEHPIFSEV--ISDQEAVSALEKFVDDEKILVEPACGAALAAVY---------SRVVCRLQDEGR 290
Cdd:cd01561 222 NLDRSLIDEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALklakrlgpgKTIVTILPDSGE 287
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; |
11-303 |
3.89e-15 |
|
Cysteine synthase [Amino acid transport and metabolism];
Pssm-ID: 223110 [Multi-domain] Cd Length: 300 Bit Score: 74.49 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRgIGH------LCKMKAKQGcRHFVCSSAGNAGMATAYAARRLGIPAT 84
Cdd:COG0031 12 TPLVRLNRLSPGTGVEIYAKLESFNPGGSVKDR-IALymiedaEKRGLLKPG-GTIVEATSGNTGIALAMVAAAKGYRLI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 85 IVVPNTTPALTIERLKNEGATVEVV---GEMLDEAIQVAKALEKNNPGWVYISP-FDDPLIWEGH-TSLVKELKETLSAK 159
Cdd:COG0031 90 IVMPETMSQERRKLLRALGAEVILTpgaPGNMKGAIERAKELAAEIPGYAVWLNqFENPANPEAHyETTGPEIWQQTDGK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 160 PGAIVLSVGGGGLLCGVVQGLREVgWEDVPIIAMETFGAHSFHAAIKEGKLvtlpkitsvaKALGVNTVgaqTLKLFYEH 239
Cdd:COG0031 170 VDAFVAGVGTGGTITGVARYLKER-NPNVRIVAVDPEGSVLLSGGEGPHKI----------EGIGAGFV---PENLDLDL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52783414 240 PIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVysRVVCRLQDEGrlqtplASLVVIVC 303
Cdd:COG0031 236 IDEVIRVSDEEAIATARRLAREEGLLVGISSGAALAAA--LKLAKELPAG------KTIVTILP 291
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; |
11-276 |
6.34e-14 |
|
Threonine synthase [Amino acid transport and metabolism];
Pssm-ID: 223572 [Multi-domain] Cd Length: 411 Bit Score: 71.97 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALS---KLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:COG0498 77 TPLYKAPALAaplGVLNDNLYVKELGHNPTGSFKDRGMTVLVSLAKELGAKTILCASSGNTGASAAAYAARAGLKVFVLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 88 PNT-TPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAK------- 159
Cdd:COG0498 157 PKGkVSPGKLAQMLTLGAHVIAVDGNFDDAQELVKEAANRE-GLLSAVNSINPYRLEGQKTYAFEIAEQLGWKapdhvvv 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 160 P----GAIVLSVGGGGLlcgvvqgLREVGW-EDVP-IIAMETFGAHSFHAAIKEGKLVtlPKITSVAKALGVNTVGAQTL 233
Cdd:COG0498 236 PvgngGNLLAIYKGFKE-------GLPIGKiDKAPnMNGVQAEGFSPGVYAWKEGRET--PETIAPAMDIGNPSNWERAL 306
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 52783414 234 KLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAA 276
Cdd:COG0498 307 FALRESGGLAVAVSDEEILEAIKLLAEREGILIEPHSAVAVAA 349
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
4-294 |
1.01e-12 |
|
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: 67.79 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 4 QESLHVK-TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGI 81
Cdd:TIGR00260 15 LVDLGEGvTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 82 PATIVVPNTtpalTIERLK-----NEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL 156
Cdd:TIGR00260 95 KVVVLYPAG----KISLGKlaqalGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLEGQKTYAFEAVEQL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 157 SAK-PGAIVLSVGGGGLLCGVVQG---LREVGWEDVPI-IAMETFGAHSF-HAAIKEGKLVTLPKITSVAKALGV-NTV- 228
Cdd:TIGR00260 171 GWEaPDKVVVPVPNSGNFGAIWKGfkeKKMLGLDSLPVkRGIQAEGAADIvRAFLEGGQWEPIETPETLSTAMDIgNPAn 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52783414 229 GAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVY-----------SRVVCRLQDEGrLQTP 294
Cdd:TIGR00260 251 WPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLklvekgtadpaERVVCALTGNG-LKDP 326
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
19-313 |
1.87e-10 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 60.78 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 19 LSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQ-GCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTpalTI 96
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGgLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGN---SV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 97 ErlKNE-----GATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFddpliwegHTSLVKELK----ETLSAKP------- 160
Cdd:PRK06110 107 E--KNAamralGAELIEHGEDFQAAREEAARLAAER-GLHMVPSF--------HPDLVRGVAtyalELFRAVPdldvvyv 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 161 ---------GAIVLSvggggllcgvvqglREVGWeDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQ 231
Cdd:PRK06110 176 pigmgsgicGAIAAR--------------DALGL-KTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 232 TLKLFYEHpiFSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVysrvvcrLQDEGRLQtplASLVVIVCGGSNIS 309
Cdd:PRK06110 241 ALEVIRAG--ADRIVrvTDDEVAAAMRAYFTDTHNVAEGAGAAALAAA-------LQERERLA---GKRVGLVLSGGNID 308
|
....
gi 52783414 310 LAQL 313
Cdd:PRK06110 309 RAVF 312
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
24-276 |
2.88e-10 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 60.52 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 24 GTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNEG 103
Cdd:PRK06450 64 KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 104 ATVEVVGEMLDEaiqVAKALEknNPGWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGAIVLSVGGGGLLCGVVQGLR- 181
Cdd:PRK06450 144 AEVVRVRGSRED---VAKAAE--NSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKiPNYVFIPVSAGTLLLGVYSGFKh 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 182 --EVG-WEDVP-IIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALgvntVGAQTLKLFYEHPIFSE-----VISDQEAV 252
Cdd:PRK06450 219 llDSGvISEMPkIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADAL----VSTRPFLLDYMVKALSEygeciVVSDNEIV 294
|
250 260
....*....|....*....|....
gi 52783414 253 SAlEKFVDDEKILVEPACGAALAA 276
Cdd:PRK06450 295 EA-WKELAKKGLLVEYSSATVYAA 317
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
24-310 |
6.53e-09 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 56.37 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 24 GTSVFLKMDSSQPSGSFKIRGIG-HLCKMKaKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNE 102
Cdd:PRK08329 71 SIKVYFKLDYLQPTGSFKDRGTYvTVAKLK-EEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 103 GATVEVVG----EMLDEAIQVAKaleknNPGWVYISPFDDPLIWEGHTSLVKELKETLSAkPGAIVLSVGGGGLLCGVVQ 178
Cdd:PRK08329 150 GAELHFVEgdrmEVHEEAVKFSK-----RNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGV-PDYAFVPVGSGTLFLGIWK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 179 G---LREVG-WEDVP-IIAMETFGAHSF-HAAIKEGKLVTLPKITSVAKAlgvntvgAQTLKLFYEHPIFSEVISDQEAV 252
Cdd:PRK08329 224 GfkeLHEMGeISKMPkLVAVQAEGYESLcKRSKSENKLADGIAIPEPPRK-------EEMLRALEESNGFCISVGEEETR 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414 253 SALEKFVdDEKILVEPACGAALAAVYSrvvcrLQDEGRLQTplASLVVIVCGGSNISL 310
Cdd:PRK08329 297 AALHWLR-RMGFLVEPTSAVALAAYWK-----LLEEGLIEG--GSKVLLPLSGSGLKN 346
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
8-134 |
1.62e-07 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 52.19 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 8 HVKTPLRDSMALSKLAGT-SVFLKmDSSQPSG--SFKIRG-----IGHLCKM------------------KAKQGCRHFV 61
Cdd:PRK08206 42 YAPTPLVALPDLAAELGVgSILVK-DESYRFGlnAFKALGgayavARLLAEKlgldiselsfeeltsgevREKLGDITFA 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414 62 CSSAGNAGMATAYAARRLGIPATIVVPNTTpalTIERLKN---EGATVEVVGEMLDEAIQVAKALEKNNpGWVYIS 134
Cdd:PRK08206 121 TATDGNHGRGVAWAAQQLGQKAVIYMPKGS---SEERVDAiraLGAECIITDGNYDDSVRLAAQEAQEN-GWVVVQ 192
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
11-163 |
6.49e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 50.09 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSKLAGTS-VFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPN 89
Cdd:PRK06381 16 TPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414 90 TTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFD--DPLIWEGHTSLVKELKETLSAKPGAI 163
Cdd:PRK06381 96 SYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKEN-GIYDANPGSvnSVVDIEAYSAIAYEIYEALGDVPDAV 170
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
36-106 |
2.61e-03 |
|
threonine synthase
Pssm-ID: 178182 [Multi-domain] Cd Length: 484 Bit Score: 39.41 E-value: 2.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52783414 36 PSGSFKIRGIGHLCKM-----KAKQGCRHFVCSSAGNAGMA-TAYAARrLGIPATIVVPNTTPALT--IERLKNeGATV 106
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQvnrlrKMAKPVVGVGCASTGDTSAAlSAYCAA-AGIPSIVFLPADKISIAqlVQPIAN-GALV 237
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
11-120 |
2.77e-03 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 39.41 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIR---GIGHLCKMKAKQgcRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINnalGQALLAKRMGKT--RIIAETGAGQHGVATATACALFGLKCTIFM 349
|
90 100 110
....*....|....*....|....*....|....*....
gi 52783414 88 PNTT---PALTIERLKNEGATVEVV---GEMLDEAIQVA 120
Cdd:PRK13803 350 GEEDikrQALNVERMKLLGANVIPVlsgSKTLKDAVNEA 388
|
|
|