|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
11-320 |
1.96e-152 |
|
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: 430.18 E-value: 1.96e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 11 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELL-DEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWE--KPGAIA 164
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 165 LSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSE 244
Cdd:cd06448 162 CSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302563349 245 VISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREgNLQAPLPSLVVIVCGGSNISLAQLRALKEQL 320
Cdd:cd06448 242 VVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
5-304 |
2.72e-55 |
|
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: 181.74 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 5 EPLHVRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRwAKQGCA--HFVCSSAGNAGMAAAYAARQLGVP 82
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEGgkTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 83 ATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGA 162
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 163 IALSVGGGGLLCGVVQGLQEvGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVK-TVGAQALKLFQEHPI 241
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302563349 242 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCG 304
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR-------VVVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
6-318 |
1.40e-50 |
|
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: 170.60 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 6 PLHVRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRW-AKQGCAHFVCSSagnagmaaayaaRQLGVPAT 84
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLsEEERARGVVAASagnhaqgvayaaRLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALwekP---- 160
Cdd:COG1171 100 IVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQL---Pdlda 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 161 -----------GAIALSvggggllcgvvqgLQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 229
Cdd:COG1171 176 vfvpvggggliAGVAAA-------------LKALSP-DIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 230 AQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHviqKLQREGNlqaplpSLVVIVCGGsNIS 309
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------RVVVVLSGG-NID 311
|
....*....
gi 302563349 310 LAQLRALKE 318
Cdd:COG1171 312 PDRLAEILE 320
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
9-319 |
1.54e-30 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 120.61 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGViAASAGNHAQGVAFSAARLGLKALIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIALSV 167
Cdd:TIGR01124 96 PETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEK-GLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFVPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 168 GGGGLLCGVVQGLQEVgWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHpIFSEVIS 247
Cdd:TIGR01124 175 GGGGLAAGVAALIKQL-MPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQY-LDDIVTV 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302563349 248 DQEAV-AAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCgGSNISLAQLRALKEQ 319
Cdd:TIGR01124 253 DTDEVcAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQT-------LVAILS-GANMNFHRLRYVSER 317
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
9-319 |
5.28e-28 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 113.74 E-value: 5.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGViTASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELkeaLWEKPGAIALSv 167
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 168 ggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQA 232
Cdd:PRK12483 191 ------------FVPVGGGgliagiaayvkyvrpEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 233 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHViqklQREGNLQAPLpslvVIVCGGSNISL 310
Cdd:PRK12483 259 FELCRHY--VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYA----EREGIEGQTL----VAIDSGANVNF 328
|
....*....
gi 302563349 311 AQLRALKEQ 319
Cdd:PRK12483 329 DRLRHVAER 337
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
11-320 |
1.96e-152 |
|
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: 430.18 E-value: 1.96e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 11 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELL-DEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWE--KPGAIA 164
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 165 LSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSE 244
Cdd:cd06448 162 CSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302563349 245 VISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREgNLQAPLPSLVVIVCGGSNISLAQLRALKEQL 320
Cdd:cd06448 242 VVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
5-304 |
2.72e-55 |
|
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: 181.74 E-value: 2.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 5 EPLHVRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRwAKQGCA--HFVCSSAGNAGMAAAYAARQLGVP 82
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEGgkTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 83 ATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGA 162
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 163 IALSVGGGGLLCGVVQGLQEvGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVK-TVGAQALKLFQEHPI 241
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302563349 242 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCG 304
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR-------VVVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
6-318 |
1.40e-50 |
|
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: 170.60 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 6 PLHVRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRW-AKQGCAHFVCSSagnagmaaayaaRQLGVPAT 84
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLsEEERARGVVAASagnhaqgvayaaRLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALwekP---- 160
Cdd:COG1171 100 IVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQL---Pdlda 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 161 -----------GAIALSvggggllcgvvqgLQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 229
Cdd:COG1171 176 vfvpvggggliAGVAAA-------------LKALSP-DIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 230 AQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHviqKLQREGNlqaplpSLVVIVCGGsNIS 309
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------RVVVVLSGG-NID 311
|
....*....
gi 302563349 310 LAQLRALKE 318
Cdd:COG1171 312 PDRLAEILE 320
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
9-308 |
8.47e-47 |
|
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: 159.96 E-value: 8.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVPAT 84
Cdd:cd01562 16 RRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEkPGAIa 164
Cdd:cd01562 93 IVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILEQVPD-LDAV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 165 lsvggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 229
Cdd:cd01562 170 ---------------FVPVGGGgliagiatavkalspNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 230 AQALKLFQEHPifSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQRegnlqaplpSLVVIVCGGsN 307
Cdd:cd01562 235 ELTFEIIRKLV--DDVVtvSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGK---------KVVVVLSGG-N 302
|
.
gi 302563349 308 I 308
Cdd:cd01562 303 I 303
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
11-305 |
1.65e-46 |
|
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: 157.68 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 11 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEAL-WEKPGAIals 166
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 167 vggggllcgvvqglqevgwgdvpVIAMETFGAhsfhaattagklvslpkITSVAKAL-----GVKTVGAQAlklfqehpi 241
Cdd:cd00640 158 -----------------------VVPVGGGGN-----------------IAGIARALkellpNVKVIGVEP--------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302563349 242 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYshviqKLQREGNLQAPlpsLVVIVCGG 305
Cdd:cd00640 189 EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAAL-----KLAKKLGKGKT---VVVILTGG 244
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
9-319 |
1.54e-30 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 120.61 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGViAASAGNHAQGVAFSAARLGLKALIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIALSV 167
Cdd:TIGR01124 96 PETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEK-GLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFVPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 168 GGGGLLCGVVQGLQEVgWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHpIFSEVIS 247
Cdd:TIGR01124 175 GGGGLAAGVAALIKQL-MPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQY-LDDIVTV 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302563349 248 DQEAV-AAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCgGSNISLAQLRALKEQ 319
Cdd:TIGR01124 253 DTDEVcAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQT-------LVAILS-GANMNFHRLRYVSER 317
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
9-319 |
5.28e-28 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 113.74 E-value: 5.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGViTASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELkeaLWEKPGAIALSv 167
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 168 ggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQA 232
Cdd:PRK12483 191 ------------FVPVGGGgliagiaayvkyvrpEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 233 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHViqklQREGNLQAPLpslvVIVCGGSNISL 310
Cdd:PRK12483 259 FELCRHY--VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYA----EREGIEGQTL----VAIDSGANVNF 328
|
....*....
gi 302563349 311 AQLRALKEQ 319
Cdd:PRK12483 329 DRLRHVAER 337
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
9-307 |
8.51e-25 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 103.35 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHF-CKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK08639 24 PETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACRHLGIPGVIFM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLK---NEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKP---- 160
Cdd:PRK08639 104 PVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILEQLEKEGspdy 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 161 --------GAIALSVGGggllcgvvqgLQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQA 232
Cdd:PRK08639 183 vfvpvgggGLISGVTTY----------LKERSP-KTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 233 LKLFQEHPifSEVIS-DQEAV-AAIEKFVDDEKILVEPAcGA----ALAAVYSHVIQKlqregnlqaplpSLVVIVCGGS 306
Cdd:PRK08639 252 FEILKDVV--DDVVLvPEGAVcTTILELYNKEGIVAEPA-GAlsiaALELYKDEIKGK------------TVVCVISGGN 316
|
.
gi 302563349 307 N 307
Cdd:PRK08639 317 N 317
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
9-314 |
3.01e-24 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 102.52 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCahfVCSSAGNAGMAAAYAARQLGVPAT 84
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIA 164
Cdd:PRK09224 96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 165 LSvggggllcgvvqglqeVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 229
Cdd:PRK09224 175 VP----------------VGGGgliagvaayikqlrpEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 230 AQALKLFQEHpiFSEVI---SDqEAVAAIEKFVDDEKILVEPAcGA-ALAAVYSHVIQ-KLQREgnlqaplpSLVVIVCg 304
Cdd:PRK09224 239 EETFRLCQEY--VDDVItvdTD-EICAAIKDVFEDTRSIAEPA-GAlALAGLKKYVAQhGIEGE--------TLVAILS- 305
|
330
....*....|
gi 302563349 305 GSNISLAQLR 314
Cdd:PRK09224 306 GANMNFDRLR 315
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
8-305 |
7.58e-24 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 99.26 E-value: 7.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 8 HVR-TPI--RDSMALSKVAgtsVYLKMDSAQPSGSFKIRGIGHFCkRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPAT 84
Cdd:PRK08246 20 HIRrTPVleADGAGFGPAP---VWLKLEHLQHTGSFKARGAFNRL-LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKP---- 160
Cdd:PRK08246 96 VFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAET-GALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDtvlv 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 161 -----GAIAlsvggggllcgvvqGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKL 235
Cdd:PRK08246 175 avgggGLIA--------------GIAAWFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFAL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 236 FQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKlqregnlqAPLPSLVVIVCGG 305
Cdd:PRK08246 241 ARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVP--------APGERVAVVLCGA 302
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
9-318 |
7.92e-23 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 98.84 E-value: 7.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGViCSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIALSV 167
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEE-GRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 168 GGGGLLCGVVQGLQEVGwGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVIS 247
Cdd:PLN02550 267 GGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302563349 248 DQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpslVVIVCGGSNISLAQLRALKE 318
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDEN--------VVAITSGANMNFDRLRIVTE 408
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
9-156 |
9.00e-23 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 96.57 E-value: 9.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH-FVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARgVVTASTGNHGRALAYAARALGIRATICM 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302563349 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEAL 156
Cdd:PRK07476 98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREE-GLTMVPPFDDPRIIAGQGTIGLEILEAL 165
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
8-315 |
3.21e-20 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 89.37 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 8 HVR-TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVP 82
Cdd:PRK06815 17 QVRvTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 83 ATIVVPSTTPALTIERLKNEGATVKVVGELLDEAfELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALwEKPGA 162
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVRLYGGDALNA-ELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ-PDLDA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 163 IALSVGGGGLLCGVVQGLQEVGwGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAK--ALGVKTvGAQALKLFQEHP 240
Cdd:PRK06815 172 VFVAVGGGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgtAGGVEP-GAITFPLCQQLI 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302563349 241 IFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAvyshvIQKLQREGNLQaplpSLVVIVCgGSNISLAQLRA 315
Cdd:PRK06815 250 DQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAA-----ALKLAPRYQGK----KVAVVLC-GKNIVLEKYLE 314
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
9-280 |
7.15e-20 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 89.18 E-value: 7.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 9 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIghfCKRWAK-------------------QGCAHfvcssagnag 69
Cdd:PRK07334 22 LRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGA---LNKLLLlteeerargviamsagnhaQGVAY---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 70 maaayAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIV 149
Cdd:PRK07334 89 -----HAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 150 KELKEALwekP------------GAIAlsvggggllcgvvqGLQEVGWG---DVPVIAMETfgaHSFHAATTAGKLVSLP 214
Cdd:PRK07334 163 LEMLEDA---PdldtlvvpigggGLIS--------------GMATAAKAlkpDIEIIGVQT---ELYPSMYAAIKGVALP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302563349 215 KITS-VAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSH 280
Cdd:PRK07334 223 CGGStIAEGIAVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAY 289
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
10-320 |
9.20e-19 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 85.56 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 10 RTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVPATI 85
Cdd:PRK08638 27 KTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGIDGKV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 86 VVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIAl 165
Cdd:PRK08638 104 VMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTVIV- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 166 svggggllcgvvqglqEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGA 230
Cdd:PRK08638 182 ----------------PIGGGgliagiavalksinpTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 231 QALKLFQEhpIFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCGGsNI 308
Cdd:PRK08638 246 LTYEIVRE--LVDDIVlvSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKK-------VVAIISGG-NV 315
|
330
....*....|..
gi 302563349 309 SLAQLRALKEQL 320
Cdd:PRK08638 316 DLSRVSQITGHV 327
|
|
| PLN02970 |
PLN02970 |
serine racemase |
10-313 |
1.24e-18 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 85.12 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 10 RTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCahfVCSSAGNAGMAAAYAARQLGVPATI 85
Cdd:PLN02970 27 RTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 86 VVPSTTPALTIERLKNEGATVkVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEAL--------- 156
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGII-TWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVpeldviivp 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 157 WEKPGAIAlsvggggLLCGVVQGLQEvgwgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKtVGAQALKLF 236
Cdd:PLN02970 183 ISGGGLIS-------GIALAAKAIKP----SIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS-LGDLTWPVV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 237 QEhpIFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKlqregNLQAPLPSLV-VIVCGGsNISLAQL 313
Cdd:PLN02970 251 RD--LVDDVItvDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRS-----NPAWKGCKNVgIVLSGG-NVDLGVL 322
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
11-304 |
6.81e-18 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 82.64 E-value: 6.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 11 TPIRDSMALSKVAGT-SVYLKMDSAQPSGSFKIRG----IGHfckrwAKQ-GCAHFVCSSAGNAGMAAAYAARQLGVPAT 84
Cdd:cd01563 23 TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGmtvaVSK-----AKElGVKAVACASTGNTSASLAAYAARAGIKCV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpgWVYIPPFDDPLIWEGHASIVKELKEAL-WEKPGAI 163
Cdd:cd01563 98 VFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN--WIYLSNSLNPYRLEGQKTIAFEIAEQLgWEVPDYV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 164 ALSVGGGGLLCGVVQG---LQEVGWGD-VP-VIAMETFGAHSFHAATTAGK--LVSLPKITSVAKAL--GVKTVGAQALK 234
Cdd:cd01563 176 VVPVGNGGNITAIWKGfkeLKELGLIDrLPrMVGVQAEGAAPIVRAFKEGKddIEPVENPETIATAIriGNPASGPKALR 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 235 LFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviQKLQREGNLqAPLPSLVVIVCG 304
Cdd:cd01563 256 AVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGL-----KKLREEGII-DKGERVVVVLTG 319
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
11-319 |
6.21e-14 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 71.34 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 11 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGC--AHFVCSSAGNAGMAAAYAARQLGVPATIVVP 88
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYSTGNHGQAVAYASKLFGIKTRIYLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 89 STTPALTIERLKNEGATVKVVgELLDEAFElaKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIALS-- 166
Cdd:PRK06608 104 LNTSKVKQQAALYYGGEVILT-NTRQEAEE--KAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFAScg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 167 -VGGGGLLCGVVQGLQEvgwgDVPVIAMETFGAHSFHAATTAGKLVSLPKI-TSVAKALGVKTVGAQALKLFQEHPIFSE 244
Cdd:PRK06608 181 gGGLISGTYLAKELISP----TSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKKLDDFYL 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302563349 245 ViSDQEAVAAIEKFVDDEKILVEPACGAALAAvyshVIQKLQRegnlQAPLPSLVVIVCGGsNISLAQLRALKEQ 319
Cdd:PRK06608 257 V-EEYEIYYWTAWLTHLLKVICEPSSAINMVA----VVNWLKT----QSKPQKLLVILSGG-NIDPILYNELWKE 321
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
10-316 |
7.44e-13 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 68.12 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 10 RTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCAHFvcsSAGNAGMAAAYAARQLGVPATI 85
Cdd:PRK07048 24 RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAGVVTF---SSGNHAQAIALSARLLGIPATI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 86 VVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELkealwekpgaial 165
Cdd:PRK07048 101 VMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER-GLTLIPPYDHPHVIAGQGTAAKEL------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 166 svggggllcgvvqgLQEVGWGDV-------------------------PVIAMETF----GAHSFHaattAGKLVSLPKI 216
Cdd:PRK07048 167 --------------FEEVGPLDAlfvclggggllsgcalaaralspgcKVYGVEPEagndGQQSFR----SGEIVHIDTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 217 TSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviqklqREGNLQAPLP 296
Cdd:PRK07048 229 RTIADGAQTQHLGNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAA---------LRGKVPLKGK 299
|
330 340
....*....|....*....|
gi 302563349 297 SLVVIVCGGsNISLAQLRAL 316
Cdd:PRK07048 300 RVGVIISGG-NVDLARFAAL 318
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
27-276 |
3.45e-12 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 66.57 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 27 VYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH-FVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGAT 105
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERpVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 106 VKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEalwEKPGAIALSVGGGGLLCGVVQGLQEVGw 185
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIELAA---HAPDVVIVPIGGGGLASGVALALKSQG- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 186 gdVPVIAMETFGAHSFhAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKIL 265
Cdd:PRK08813 205 --VRVVGAQVEGVDSM-ARAIRGDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVI 281
|
250
....*....|.
gi 302563349 266 VEPACGAALAA 276
Cdd:PRK08813 282 AEGAGALALAA 292
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
11-292 |
6.49e-09 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 56.55 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 11 TPIRDSMALSKVAG-TSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPS 89
Cdd:PRK08197 80 TPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 90 TTPALTIERLKNEGATVKVVGELLDEAFELAKAlAKNNPGWVYIPPFDDPLIWEGHASIVKELKEAL-WEKPGAI---AL 165
Cdd:PRK08197 160 DAPEITRLECALAGAELYLVDGLISDAGKIVAE-AVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLgWRLPDVIlypTG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 166 SVGGGGLLCGVVQGLQEVGW--GDVP-VIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGV---KTVGAQ-ALKLFQE 238
Cdd:PRK08197 239 GGVGLIGIWKAFDELEALGWigGKRPrLVAVQAEGCAPIVKAWEEGKEESEFWEDAHTVAFGIrvpKALGDFlVLDAVRE 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 302563349 239 HPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviQKLQREGNLQ 292
Cdd:PRK08197 319 TGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAA-----RQLRESGWLK 367
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
10-277 |
7.87e-09 |
|
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: 56.24 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 10 RTPIRDSMALSK-VAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVP 88
Cdd:TIGR00260 22 VTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 89 STtpalTIERLK-----NEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEAL-WEKPGA 162
Cdd:TIGR00260 102 AG----KISLGKlaqalGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLEGQKTYAFEAVEQLgWEAPDK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 163 IALSVGGGGLLCGVVQGLQE---VGWGDVPV-IAMETFGAHSFHAATTAGKLV---SLPKITSVAKALGVKTVGAQALKL 235
Cdd:TIGR00260 178 VVVPVPNSGNFGAIWKGFKEkkmLGLDSLPVkRGIQAEGAADIVRAFLEGGQWepiETPETLSTAMDIGNPANWPRALEA 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 302563349 236 FQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAV 277
Cdd:TIGR00260 258 FRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAAL 299
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
11-276 |
1.18e-08 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 55.97 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 11 TPIRDSMALSKVaGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPST 90
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 91 TPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALweKPGAIALSVGGG 170
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN-GLYNVTPEYNIIGLEGQKTIAFELWEEI--NPTHVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 171 GLLCGVVQG---LQEVGWGD-VP-VIAMETfgahsFHAATTAGKLVSLPKITSVAKALGV----KTVGAQALKLFQEHPI 241
Cdd:PRK05638 223 SYLYSIYKGfkeLLEIGVIEeIPkLIAVQT-----ERCNPIASEILGNKTKCNETKALGLyvknPVMKEYVSEAIKESGG 297
|
250 260 270
....*....|....*....|....*....|....*
gi 302563349 242 FSEVISDQEAVAAiEKFVDDEKILVEPACGAALAA 276
Cdd:PRK05638 298 TAVVVNEEEIMAG-EKLLAKEGIFAELSSAVVMPA 331
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
11-306 |
1.62e-08 |
|
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: 55.21 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 11 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPST 90
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPEG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 91 -TPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPG-------WVYIppfddpliwEGHASIVKELKEALWEKP-- 160
Cdd:COG0498 147 kVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLyavnsinPARL---------EGQKTYAFEIAEQLGRVPdw 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 161 -------------GAIALSVggggllcgvvqgLQEVGWGD-VP-VIAMETFGAHSFHAATTAGKLVSLPK-ITSVAKALG 224
Cdd:COG0498 218 vvvptgnggnilaGYKAFKE------------LKELGLIDrLPrLIAVQATGCNPILTAFETGRDEYEPErPETIAPSMD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 225 V-KTV-GAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviQKLQREGNLQAPLPslVVIV 302
Cdd:COG0498 286 IgNPSnGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGL-----RKLREEGEIDPDEP--VVVL 358
|
....
gi 302563349 303 CGGS 306
Cdd:COG0498 359 STGH 362
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
19-276 |
8.37e-08 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 53.07 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 19 LSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG--CAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTpalTI 96
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGprVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGN---SV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 97 ErlKNE-----GATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIwEGHASIVKELKEALwekpgaialsvgggg 171
Cdd:PRK06110 107 E--KNAamralGAELIEHGEDFQAAREEAARLAAER-GLHMVPSFHPDLV-RGVATYALELFRAV--------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 172 llcgvvQGLQEV------GWGDVPVIA--------METFGAHSFHAAT-----TAGKLVSLPKITSVAKALGVKTVGAQA 232
Cdd:PRK06110 168 ------PDLDVVyvpigmGSGICGAIAardalglkTRIVGVVSAHAPAyalsfEAGRVVTTPVATTLADGMACRTPDPEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 302563349 233 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAA 276
Cdd:PRK06110 242 LEVIRAG--ADRIVrvTDDEVAAAMRAYFTDTHNVAEGAGAAALAA 285
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
10-303 |
2.81e-07 |
|
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: 50.98 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 10 RTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH------------------FVCssagnagma 71
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKpgttiieptsgntgiglaMVA--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 72 aayaaRQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDE----AFELAKALAKNNPGWVYIPPFDDPLIWEGH-A 146
Cdd:cd01561 73 -----AAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLNQFENPANPEAHyE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 147 SIVKELKEALwekPGAIalsvggggllcgvvqglqevgwgDVPVIAMETFGahsfhaaTTAGklvslpkitsVAKAL--- 223
Cdd:cd01561 148 TTAPEIWEQL---DGKV-----------------------DAFVAGVGTGG-------TITG----------VARYLkek 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 224 --GVKTVGAQALK--LFQEHPIFS---------------------EV--ISDQEAVAAIEKFVDDEKILVEPACGAALAA 276
Cdd:cd01561 185 npNVRIVGVDPVGsvLFSGGPPGPhkiegigagfipenldrslidEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVAA 264
|
330 340
....*....|....*....|....*..
gi 302563349 277 VYshviqKLQREgnlqAPLPSLVVIVC 303
Cdd:cd01561 265 AL-----KLAKR----LGPGKTIVTIL 282
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
10-277 |
7.61e-04 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 40.84 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 10 RTPIRDSMALSKVAGTS-VYLKMDSAQPSGSFKIRGIGHFCKRWAKQG--------CAHFVCSsagnagmaAAYAARQLG 80
Cdd:PRK06381 15 GTPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGysgitvgtCGNYGAS--------IAYFARLYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 81 VPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFD--DPLIWEGHASIVKELKEALWE 158
Cdd:PRK06381 87 LKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKEN-GIYDANPGSvnSVVDIEAYSAIAYEIYEALGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 159 KPGAIAlsvggggllcgvvqglqevgwgdVPVIAMETFGA--HSFHAATTAGKLVSLPKI----TS----VAKAL--GVK 226
Cdd:PRK06381 166 VPDAVA-----------------------VPVGNGTTLAGiyHGFRRLYDRGKTSRMPRMigvsTSggnqIVESFkrGSS 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302563349 227 TVGAQALKLFQEHPIFSEVIS-----DQEAVAAIEK-------FVDDE-----KILVE-------PACGAALAAV 277
Cdd:PRK06381 223 EVVDLEVDEIRETAVNEPLVSyrsfdGDNALEAIYDshgyafgFSDDEmvkyaELLRRmeglnalPASASALAAL 297
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
8-154 |
2.24e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 39.42 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 8 HVRTPIRDSMALSKvagtSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK08329 59 HLTPPITPTVKRSI----KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFV 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302563349 88 PSTTPALTIERLKNEGATVKVVG----ELLDEAFELAKalaknNPGWVYIPPFDDPLIWEGHASIVKELKE 154
Cdd:PRK08329 135 SYNASKEKISLLSRLGAELHFVEgdrmEVHEEAVKFSK-----RNNIPYVSHWLNPYFLEGTKTIAYEIYE 200
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
19-303 |
2.33e-03 |
|
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: 39.26 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 19 LSKVAGTSVYLKMDSAQPSGSFKIR-----------------------------GIGhfckrwakqgcahfvcssagnag 69
Cdd:COG0031 22 LSPGPGAEIYAKLESFNPGGSVKDRialsmiedaekrgllkpggtiveatsgntGIG----------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 70 maAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVV--GELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGH-A 146
Cdd:COG0031 79 --LAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTpgAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHyE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 147 SIVKELKEALWEKPGA-------------IAlsvggggllcgvvQGLQEVgWGDVPVIAMETFGAHSFHAATTAGKLVS- 212
Cdd:COG0031 157 TTGPEIWEQTDGKVDAfvagvgtggtitgVG-------------RYLKER-NPDIKIVAVEPEGSPLLSGGEPGPHKIEg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302563349 213 -----LPKItsvakalgvktvgaqalklFQEHPIfSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAvyshVIQKL 285
Cdd:COG0031 223 igagfVPKI-------------------LDPSLI-DEVItvSDEEAFAMARRLAREEGILVGISSGAAVAA----ALRLA 278
|
330
....*....|....*...
gi 302563349 286 QREGnlqaPLPSLVVIVC 303
Cdd:COG0031 279 KRLG----PGKTIVTILP 292
|
|
| |
