|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
35-345 |
1.44e-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: 444.05 E-value: 1.44e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 35 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQG---CRHFVCSSAGNAGMATAYAARRLGIPATIV 111
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 112 VPNTTPALTIERLKNEGATVEVVGEML-DEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL--SAKPGAI 188
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLqsQEKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 189 VLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFS 268
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937136 269 EVISDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgRLQTPLASLVVIVCGGSNISLAQLQALKVQL 345
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
35-329 |
8.41e-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: 459749 [Multi-domain] Cd Length: 295 Bit Score: 212.56 E-value: 8.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 35 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCkMKAKQGC--RHFVCSSAGNAGMATAYAARRLGIPATIVV 112
Cdd:pfam00291 7 PTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLL-LRLKEGEggKTVVEASSGNHGRALAAAAARLGLKVTIVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 113 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 192
Cdd:pfam00291 86 PEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 193 GGGGLLCGVVQGLREvGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGV-NTVGAQTLKLFYEHPIFSEVI 271
Cdd:pfam00291 166 GGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgDEPGALALDLLDEYVGEVVTV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568937136 272 SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEGRlqtplasLVVIVCG 329
Cdd:pfam00291 245 SDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR-------VVVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
34-342 |
1.06e-60 |
|
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: 197.57 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 34 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 112
Cdd:COG1171 23 RRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaYNALASLSEEERARGVVAASAGNHAQGVAYAARLLGIPATIVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 113 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAK-----P-- 185
Cdd:COG1171 103 PETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQLPDLdavfvPvg 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 186 -----GAIVLSvggggllcgvvqgLREVGWeDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKL 260
Cdd:COG1171 182 gggliAGVAAA-------------LKALSP-DIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 261 FYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYSrvvcrlqdeGRLQTPLASLVVIVCGGsNISLAQLQA 340
Cdd:COG1171 248 LRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLA---------GKERLKGKRVVVVLSGG-NIDPDRLAE 317
|
..
gi 568937136 341 LK 342
Cdd:COG1171 318 IL 319
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
27-333 |
2.13e-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: 183.07 E-value: 2.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 27 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGcrhFVCSSAGNAGMATAY 99
Cdd:cd01562 6 AAAARIKpvvRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 100 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 179
Cdd:cd01562 83 AAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 180 TLsAKPGAIVlsvggggllcgvvqglrevgwedVP----------------------IIAMETFGAHSFHAAIKEGKLVT 237
Cdd:cd01562 162 QV-PDLDAVF-----------------------VPvggggliagiatavkalspntkVIGVEPEGAPAMAQSLAAGKPVT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 238 LPKITSVAKALGVNTVGAQTLKLFYEHPifSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVysrvvcrlqDEGR 315
Cdd:cd01562 218 LPEVDTIADGLAVKRPGELTFEIIRKLV--DDVVtvSEDEIAAAMLLLFEREKLVAEPAGALALAAL---------LSGK 286
|
330
....*....|....*...
gi 568937136 316 LQTPLASLVVIVCGGsNI 333
Cdd:cd01562 287 LDLKGKKVVVVLSGG-NI 303
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
36-330 |
7.19e-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: 180.02 E-value: 7.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKM---KAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 112
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLaeeEGKLPKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 113 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL-SAKPGAIvls 191
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 192 vggggllcgvvqglrevgwedvpIIAMETFGAHS-FHAAIKEGKLvtLPKItsvakalgvntVGAQTlklfyehpiFSEV 270
Cdd:cd00640 158 -----------------------VVPVGGGGNIAgIARALKELLP--NVKV-----------IGVEP---------EVVT 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 271 ISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGrlqTPLASLVVIVCGG 330
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 ... |
36-335 |
4.76e-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: 4.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLckmKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIV 111
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 112 VPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLS--------- 182
Cdd:TIGR01127 78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEE-GRVFVHPFDDEFVMAGQGTIGLEIMEDIPdvdtvivpv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 183 AKPGAIVLSVGGGGLLCgvvqglrevgwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFY 262
Cdd:TIGR01127 157 GGGGLISGVASAAKQIN-----------PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937136 263 EHpiFSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVcrlQDEGRlqtplaSLVVIVCGGsNISL 335
Cdd:TIGR01127 226 EY--VDDVVtvDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKV---DVKGK------KIAVVLSGG-NIDL 288
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
27-332 |
1.93e-32 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 125.30 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 27 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHL-CKMKAKQGCRHFVCSSAGNAGMATAYAAR 102
Cdd:PRK08639 14 KAAKRLKdvvPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 103 RLGIPATIVVPNTTPALTIERLK---NEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 179
Cdd:PRK08639 94 HLGIPGVIFMPVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 180 TLS--AKPGAIVLSVGGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQT 257
Cdd:PRK08639 173 QLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937136 258 LKLFYEHPifSEVIS-DQEAVSA--LEKFvDDEKILVEPACGAALAAVysrvvcrlqDEGRLQTPLASLVVIVCGGSN 332
Cdd:PRK08639 252 FEILKDVV--DDVVLvPEGAVCTtiLELY-NKEGIVAEPAGALSIAAL---------ELYKDEIKGKTVVCVISGGNN 317
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
34-346 |
6.41e-32 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 125.29 E-value: 6.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 34 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 112
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAyNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 113 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELketLSAKPGAIVLS- 191
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAIf 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 192 -----VGGGGLLCGVVQGLRevgwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHpi 266
Cdd:PRK12483 192 vpvggGGLIAGIAAYVKYVR----PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHY-- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 267 FSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVySRVVCRLQDEGRlqtplaSLVVIVcGGSNISLAQLQ--ALK 342
Cdd:PRK12483 266 VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGI-KKYAEREGIEGQ------TLVAID-SGANVNFDRLRhvAER 337
|
....
gi 568937136 343 VQLG 346
Cdd:PRK12483 338 AELG 341
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
34-329 |
3.03e-30 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 120.24 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 34 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCrhfVCSSAGNAGMATAYAARRLGIPAT 109
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 110 IVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIV 189
Cdd:PRK09224 96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 190 LSvggggllcgvvqglreVG---------------WEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVG 254
Cdd:PRK09224 175 VP----------------VGgggliagvaayikqlRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568937136 255 AQTLKLFYEHpiFSEVIS-DQEAVSALEKFV-DDEKILVEPAcGA-ALAAVySRVVCRLQDEGRlqtplaSLVVIVCG 329
Cdd:PRK09224 239 EETFRLCQEY--VDDVITvDTDEICAAIKDVfEDTRSIAEPA-GAlALAGL-KKYVAQHGIEGE------TLVAILSG 306
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
26-302 |
5.02e-30 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 118.46 E-value: 5.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 26 MAAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAA 101
Cdd:PRK07334 11 RAAAARLAgqvLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGaLNKLLLLTEEERARGVIAMSAGNHAQGVAYHA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 102 RRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELketL 181
Cdd:PRK07334 91 QRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVALEM---L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 182 SAKP------------GAIvlsvgggGLLCGVVQGLRevgwEDVPIIAMETFGAHSFHAAIKEgklVTLPKITS-VAKAL 248
Cdd:PRK07334 167 EDAPdldtlvvpigggGLI-------SGMATAAKALK----PDIEIIGVQTELYPSMYAAIKG---VALPCGGStIAEGI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568937136 249 GVNTVGAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAV 302
Cdd:PRK07334 233 AVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAAL 286
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
47-330 |
1.11e-29 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 115.82 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 47 LAGTSVFLKMDSSQPSGSFKIRGIGHLCkMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKN 126
Cdd:PRK08246 34 FGPAPVWLKLEHLQHTGSFKARGAFNRL-LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 127 EGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLsAKPGAIvlsvggggllcgvvqgLR 206
Cdd:PRK08246 113 LGAEVVVVGAEYADALEAAQAFAAET-GALLCHAYDQPEVLAGAGTLGLEIEEQA-PGVDTV----------------LV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 207 EVG-----------WED-VPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQ 274
Cdd:PRK08246 175 AVGgggliagiaawFEGrARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568937136 275 EAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgrlqtplaSLVVIVCGG 330
Cdd:PRK08246 255 AIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGA 302
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
36-340 |
1.17e-29 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 115.95 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGH-LCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPN 114
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNkLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 115 TTPALTIERLKNEGATVEVVG-EMLDEAIQVAKALEKNnpGWVYISPFDDPLIWEGHTSLVKELKETLsAKPGAIVLSVG 193
Cdd:PRK06815 101 QASAIKLDAIRALGAEVRLYGgDALNAELAARRAAEQQ--GKVYISPYNDPQVIAGQGTIGMELVEQQ-PDLDAVFVAVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 194 GGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAK--ALGVNTvGAQTLKLFYEHPIFSEVI 271
Cdd:PRK06815 178 GGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgtAGGVEP-GAITFPLCQQLIDQKVLV 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937136 272 SDQEAVSALEKFVDDEKILVEPACGAALAAvYSRVVCRLQdeGRlqtplaSLVVIVCgGSNISLAQLQA 340
Cdd:PRK06815 256 SEEEIKEAMRLIAETDRWLIEGAAGVALAA-ALKLAPRYQ--GK------KVAVVLC-GKNIVLEKYLE 314
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
34-181 |
1.00e-28 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 113.14 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 34 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGH-LCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 112
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNaLLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICM 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568937136 113 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETL 181
Cdd:PRK07476 98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREE-GLTMVPPFDDPRIIAGQGTIGLEILEAL 165
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
34-339 |
1.32e-28 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 116.56 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 34 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 112
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAyNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 113 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 192
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEE-GRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 193 GGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVIS 272
Cdd:PLN02550 267 GGGGLIAGIAAYVKRVRPE-VKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 273 DQEAVSALEKFVDDEKILVEPACGAALAAvySRVVCR---LQDEGrlqtplaslVVIVCGGSNISLAQLQ 339
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALAG--AEAYCKyygLKDEN---------VVAITSGANMNFDRLR 404
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
36-329 |
8.14e-27 |
|
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: 108.06 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGighlckM-----KAKQ-GCRHFVCSSAGNAGMATAYAARRLGIPA 108
Cdd:cd01563 23 TPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDRG------MtvavsKAKElGVKAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 109 TIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpgWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGA 187
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN--WIYLSNSLNPYRLEGQKTIAFEIAEQLGWEvPDY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 188 IVLSVGGGGLLCGVVQG---LREVGW-EDVP-IIAMETFGAHSFHAAIKEGKLVTLP--KITSVAKALGV-NTVGA-QTL 258
Cdd:cd01563 175 VVVPVGNGGNITAIWKGfkeLKELGLiDRLPrMVGVQAEGAAPIVRAFKEGKDDIEPveNPETIATAIRIgNPASGpKAL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568937136 259 KLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGRLQTPlASLVVIVCG 329
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLK-----KLREEGIIDKG-ERVVVVLTG 319
|
|
| PLN02970 |
PLN02970 |
serine racemase |
35-338 |
7.65e-25 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 102.83 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 35 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCrhfVCSSAGNAGMATAYAARRLGIPATI 110
Cdd:PLN02970 27 RTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 111 VVPNTTPALTIERLKNEGATVeVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLsakPG--AI 188
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGII-TWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQV---PEldVI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 189 VLSVGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVnTVGAQTLklfyehPIFS 268
Cdd:PLN02970 180 IVPISGGGLISGIALAAKAIK-PSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA-SLGDLTW------PVVR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 269 E------VISDQEAVSALEKFVDDEKILVEPACGAALAAVYSrvvcrlqdEGRLQTPLAS----LVVIVCGGsNISLAQL 338
Cdd:PLN02970 252 DlvddviTVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALS--------DSFRSNPAWKgcknVGIVLSGG-NVDLGVL 322
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
35-341 |
3.09e-24 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 101.39 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 35 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKaKQGCR--HFVCSSAGNAGMATAYAARRLGIPATIV 111
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVlNHLLELK-EQGKLpdKIVAYSTGNHGQAVAYASKLFGIKTRIY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 112 VPNTTPALTIERLKNEGATVEVVgEMLDEAIQvaKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLS 191
Cdd:PRK06608 102 LPLNTSKVKQQAALYYGGEVILT-NTRQEAEE--KAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFAS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 192 VGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKI-TSVAKALGVNTVGAQTLKL------FYEH 264
Cdd:PRK06608 179 CGGGGLISGTYLAKELIS-PTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYlkklddFYLV 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937136 265 PIFSEVISDQEAVSALekfvddeKILVEPACGAALAAVYSRVvcrlqdegRLQTPLASLVVIVCGGsNISLAQLQAL 341
Cdd:PRK06608 258 EEYEIYYWTAWLTHLL-------KVICEPSSAINMVAVVNWL--------KTQSKPQKLLVILSGG-NIDPILYNEL 318
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
27-181 |
9.67e-21 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 91.34 E-value: 9.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 27 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGcrhFVCSSAGNAGMATAY 99
Cdd:PRK08638 16 EAKQRLAgriRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 100 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 179
Cdd:PRK08638 93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILE 171
|
..
gi 568937136 180 TL 181
Cdd:PRK08638 172 DL 173
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
52-301 |
6.81e-20 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 89.30 E-value: 6.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 52 VFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNEGAT 130
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGaLNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 131 VEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKetlSAKPGAIVLSVGGGGLLCGVVQGLREVGw 210
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIELA---AHAPDVVIVPIGGGGLASGVALALKSQG- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 211 edVPIIAMETFGAHSFHAAIKeGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKIL 290
Cdd:PRK08813 205 --VRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVI 281
|
250
....*....|.
gi 568937136 291 VEPACGAALAA 301
Cdd:PRK08813 282 AEGAGALALAA 292
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
35-179 |
1.32e-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: 87.99 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 35 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVP 113
Cdd:TIGR02991 19 ETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGaTNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMS 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937136 114 NTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 179
Cdd:TIGR02991 99 ELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADR-GLTMLPPFDHPDIVAGQGTLGLEVVE 163
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
36-329 |
1.20e-18 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 86.21 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMA-TAYAArRLGIPATIVVP 113
Cdd:PRK08197 80 TPLLPLPRLGKaLGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAwAAYAA-RAGIRATIFMP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 114 NTTPALTIERLKNEGATVEVV-GEMLDEAIQVAKALEKNnpGWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGAIVLS 191
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVdGLISDAGKIVAEAVAEY--GWFDVSTLKEPYRIEGKKTMGLELAEQLGWRlPDVILYP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 192 VGGGGLLCGVVQGLRE---VGW--EDVP-IIAMETFG----AHSFHAAIKEGKL----VTLPKITSVAKALGVNTVgaqt 257
Cdd:PRK08197 237 TGGGVGLIGIWKAFDEleaLGWigGKRPrLVAVQAEGcapiVKAWEEGKEESEFwedaHTVAFGIRVPKALGDFLV---- 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568937136 258 LKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGRLQtPLASLVVIVCG 329
Cdd:PRK08197 313 LDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAAR-----QLRESGWLK-GDERVVLFNTG 378
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
27-341 |
8.61e-18 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 82.76 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 27 AAQESL----HvKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAA 101
Cdd:PRK07048 13 AAAARLagvaH-RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaYNALSQFSPEQRRAGVVTFSSGNHAQAIALSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 102 RRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE-- 179
Cdd:PRK07048 92 RLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER-GLTLIPPYDHPHVIAGQGTAAKELFEev 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 180 ----TLSAKPGAIVLSVGGGGLLCGVVQGLREVGWEdvPIIAMEtfGAHSFHAaikeGKLVTLPKITSVAKalgvntvGA 255
Cdd:PRK07048 171 gpldALFVCLGGGGLLSGCALAARALSPGCKVYGVE--PEAGND--GQQSFRS----GEIVHIDTPRTIAD-------GA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 256 QTLKL-FYEHPIFSE------VISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcrlqdEGRLQTPLASLVVIVC 328
Cdd:PRK07048 236 QTQHLgNYTFPIIRRlvddivTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAAL---------RGKVPLKGKRVGVIIS 306
|
330
....*....|...
gi 568937136 329 GGsNISLAQLQAL 341
Cdd:PRK07048 307 GG-NVDLARFAAL 318
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
36-301 |
2.41e-17 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 82.55 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSKLaGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNT 115
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 116 TPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSakPGAIVLSVGGG 195
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN-GLYNVTPEYNIIGLEGQKTIAFELWEEIN--PTHVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 196 GLLCGVVQGLREV----GWEDVP-IIAMETFGAHSFHAAIkegklVTLPKITSVAKALGvntvgaqtlkLFYEHPIFSE- 269
Cdd:PRK05638 223 SYLYSIYKGFKELleigVIEEIPkLIAVQTERCNPIASEI-----LGNKTKCNETKALG----------LYVKNPVMKEy 287
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 568937136 270 ------------VISDQEAVSALEKFVDDEKILVEPACGAALAA 301
Cdd:PRK05638 288 vseaikesggtaVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPA 331
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
35-315 |
4.72e-17 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 80.25 E-value: 4.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 35 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGC----RHFVCSSAGNAGMATAYAARRLGIPATI 110
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 111 VVPNTTPALTIERLKNEGATVEVVGEMLDE----AIQVAKALEKNNPGWVYISPFDDPLIWEGH-TSLVKELKETLSAKP 185
Cdd:cd01561 82 VMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLNQFENPANPEAHyETTAPEIWEQLDGKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 186 GAIVLSVGGGGLLCGVVQGLREVgWEDVPIIAMETFGAHSF-----HAAIKEGklvtlpkitsvakaLGVNTVGAqtlkl 260
Cdd:cd01561 162 DAFVAGVGTGGTITGVARYLKEK-NPNVRIVGVDPVGSVLFsggppGPHKIEG--------------IGAGFIPE----- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937136 261 FYEHPIFSEV--ISDQEAVSALEKFVDDEKILVEPACGAALAAVY---------SRVVCRLQDEGR 315
Cdd:cd01561 222 NLDRSLIDEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALklakrlgpgKTIVTILPDSGE 287
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
36-329 |
4.77e-16 |
|
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: 78.32 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVP-N 114
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPeG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 115 TTPALTIERLKNEGATVEVVGEMLDEAIQVAKALeKNNPGWVYISPFDdpliW---EGHTSLVKELKETLSAKPGAIVLS 191
Cdd:COG0498 147 KVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKEL-AADEGLYAVNSIN----ParlEGQKTYAFEIAEQLGRVPDWVVVP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 192 VggggllcgvvqG--------------LREVGW-EDVP-IIAMETFGAHSFHAAIKEGKLVTLPK-ITSVAKALGV-NTV 253
Cdd:COG0498 222 T-----------GnggnilagykafkeLKELGLiDRLPrLIAVQATGCNPILTAFETGRDEYEPErPETIAPSMDIgNPS 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568937136 254 -GAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAvysrvVCRLQDEGRLQtPLASLVVIVCG 329
Cdd:COG0498 291 nGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAG-----LRKLREEGEID-PDEPVVVLSTG 361
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
36-328 |
1.69e-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: 73.16 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLrdsMALSKLA---GTSVFLKMDSSQPSGSFKIRgIGH------LCKMKAKQGcRHFVCSSAGNAGMATAYAARRLGI 106
Cdd:COG0031 14 TPL---VRLNRLSpgpGAEIYAKLESFNPGGSVKDR-IALsmiedaEKRGLLKPG-GTIVEATSGNTGIGLAMVAAAKGY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 107 PATIVVPNTTPALTIERLKNEGATVEVVGEM--LDEAIQVAKALEKNNPGWVYISPFDDPLIWEGH-TSLVKELKETLSA 183
Cdd:COG0031 89 RLILVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAAETPGAFWPNQFENPANPEAHyETTGPEIWEQTDG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 184 KPGAIVLsvggggllcgvvqG-------------LREVgWEDVPIIAMETFGAHSFhaaikEGKLVTLPKItsvaKALGV 250
Cdd:COG0031 169 KVDAFVA-------------GvgtggtitgvgryLKER-NPDIKIVAVEPEGSPLL-----SGGEPGPHKI----EGIGA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 251 NTVGAqtlklFYEHPIFSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVySRVVCRLQDEGRlqtplasLVVIVC 328
Cdd:COG0031 226 GFVPK-----ILDPSLIDEVItvSDEEAFAMARRLAREEGILVGISSGAAVAAA-LRLAKRLGPGKT-------IVTILP 292
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
19-319 |
4.42e-13 |
|
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: 68.95 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 19 REPLFTAMAAQESLHVK-TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMA 96
Cdd:TIGR00260 5 REFLPVTEKDLVDLGEGvTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 97 TAYAARRLGIPATIVVPNTtpalTIERLK-----NEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHT 171
Cdd:TIGR00260 85 AAAYAGKAGLKVVVLYPAG----KISLGKlaqalGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLEGQK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 172 SLVKELKETLSAK-PGAIVLSVGGGGLLCGVVQG---LREVGWEDVPI-IAMETFGAHSF-HAAIKEGKLVTLPKITSVA 245
Cdd:TIGR00260 161 TYAFEAVEQLGWEaPDKVVVPVPNSGNFGAIWKGfkeKKMLGLDSLPVkRGIQAEGAADIvRAFLEGGQWEPIETPETLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 246 KALGV-NTV-GAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVY-----------SRVVCRLQD 312
Cdd:TIGR00260 241 TAMDIgNPAnWPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLklvekgtadpaERVVCALTG 320
|
....*..
gi 568937136 313 EGrLQTP 319
Cdd:TIGR00260 321 NG-LKDP 326
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
49-301 |
3.43e-10 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 60.52 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 49 GTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNEG 128
Cdd:PRK06450 64 KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 129 ATVEVVGEMLDEaiqVAKALEknNPGWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGAIVLSVGGGGLLCGVVQGLR- 206
Cdd:PRK06450 144 AEVVRVRGSRED---VAKAAE--NSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKiPNYVFIPVSAGTLLLGVYSGFKh 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 207 --EVG-WEDVP-IIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALgvntVGAQTLKLFYEHPIFSE-----VISDQEAV 277
Cdd:PRK06450 219 llDSGvISEMPkIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADAL----VSTRPFLLDYMVKALSEygeciVVSDNEIV 294
|
250 260
....*....|....*....|....
gi 568937136 278 SAlEKFVDDEKILVEPACGAALAA 301
Cdd:PRK06450 295 EA-WKELAKKGLLVEYSSATVYAA 317
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
44-338 |
3.96e-10 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 60.39 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 44 LSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQ-GCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTpalTI 121
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGgLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGN---SV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 122 ErlKNE-----GATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFddpliwegHTSLVKELK----ETLSAKP------- 185
Cdd:PRK06110 107 E--KNAamralGAELIEHGEDFQAAREEAARLAAER-GLHMVPSF--------HPDLVRGVAtyalELFRAVPdldvvyv 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 186 ---------GAIVLSvggggllcgvvqglREVGWeDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQ 256
Cdd:PRK06110 176 pigmgsgicGAIAAR--------------DALGL-KTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 257 TLKLFYEHpiFSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVysrvvcrLQDEGRLQtplASLVVIVCGGSNIS 334
Cdd:PRK06110 241 ALEVIRAG--ADRIVrvTDDEVAAAMRAYFTDTHNVAEGAGAAALAAA-------LQERERLA---GKRVGLVLSGGNID 308
|
....
gi 568937136 335 LAQL 338
Cdd:PRK06110 309 RAVF 312
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
49-335 |
7.18e-09 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 56.37 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 49 GTSVFLKMDSSQPSGSFKIRGIG-HLCKMKaKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNE 127
Cdd:PRK08329 71 SIKVYFKLDYLQPTGSFKDRGTYvTVAKLK-EEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 128 GATVEVVG----EMLDEAIQVAKaleknNPGWVYISPFDDPLIWEGHTSLVKELKETLSAkPGAIVLSVGGGGLLCGVVQ 203
Cdd:PRK08329 150 GAELHFVEgdrmEVHEEAVKFSK-----RNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGV-PDYAFVPVGSGTLFLGIWK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 204 G---LREVG-WEDVP-IIAMETFGAHSF-HAAIKEGKLVTLPKITSVAKAlgvntvgAQTLKLFYEHPIFSEVISDQEAV 277
Cdd:PRK08329 224 GfkeLHEMGeISKMPkLVAVQAEGYESLcKRSKSENKLADGIAIPEPPRK-------EEMLRALEESNGFCISVGEEETR 296
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568937136 278 SALEKFVdDEKILVEPACGAALAAVYSrvvcrLQDEGRLQTplASLVVIVCGGSNISL 335
Cdd:PRK08329 297 AALHWLR-RMGFLVEPTSAVALAAYWK-----LLEEGLIEG--GSKVLLPLSGSGLKN 346
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
19-159 |
6.45e-08 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 53.73 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 19 REPLFTAMAAQESL--------HVKTPLRDSMALSKLAGT-SVFLKmDSSQPSG--SFKIRG-----IGHLCKM------ 76
Cdd:PRK08206 20 DLPLLSQEEAKKARafhqsfpgYAPTPLVALPDLAAELGVgSILVK-DESYRFGlnAFKALGgayavARLLAEKlgldis 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 77 ------------KAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTpalTIERLKN---EGATVEVVGEMLDEA 141
Cdd:PRK08206 99 elsfeeltsgevREKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGS---SEERVDAiraLGAECIITDGNYDDS 175
|
170
....*....|....*...
gi 568937136 142 IQVAKALEKNNpGWVYIS 159
Cdd:PRK08206 176 VRLAAQEAQEN-GWVVVQ 192
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
36-188 |
7.83e-07 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 50.09 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSKLAGTS-VFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPN 114
Cdd:PRK06381 16 TPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568937136 115 TTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFD--DPLIWEGHTSLVKELKETLSAKPGAI 188
Cdd:PRK06381 96 SYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKEN-GIYDANPGSvnSVVDIEAYSAIAYEIYEALGDVPDAV 170
|
|
| PLN02569 |
PLN02569 |
threonine synthase |
61-131 |
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 568937136 61 PSGSFKIRGIGHLCKM-----KAKQGCRHFVCSSAGNAGMA-TAYAARrLGIPATIVVPNTTPALT--IERLKNeGATV 131
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQvnrlrKMAKPVVGVGCASTGDTSAAlSAYCAA-AGIPSIVFLPADKISIAqlVQPIAN-GALV 237
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
36-145 |
3.16e-03 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 39.41 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937136 36 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIR---GIGHLCKMKAKQgcRHFVCSSAGNAGMATAYAARRLGIPATIVV 112
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINnalGQALLAKRMGKT--RIIAETGAGQHGVATATACALFGLKCTIFM 349
|
90 100 110
....*....|....*....|....*....|....*....
gi 568937136 113 PNTT---PALTIERLKNEGATVEVV---GEMLDEAIQVA 145
Cdd:PRK13803 350 GEEDikrQALNVERMKLLGANVIPVlsgSKTLKDAVNEA 388
|
|
| |
