|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
27-336 |
1.36e-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: 431.34 E-value: 1.36e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 27 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELL-DEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWE--KPGAIA 180
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 181 LSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSE 260
Cdd:cd06448 162 CSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966974738 261 VISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREgNLQAPLPSLVVIVCGGSNISLAQLRALKEQL 336
Cdd:cd06448 242 VVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
21-320 |
1.34e-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: 183.28 E-value: 1.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 21 EPLHVRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRwAKQGCA--HFVCSSAGNAGMAAAYAARQLGVP 98
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEGgkTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 99 ATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGA 178
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 179 IALSVGGGGLLCGVVQGLQEvGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVK-TVGAQALKLFQEHPI 257
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966974738 258 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCG 320
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR-------VVVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
22-334 |
5.99e-51 |
|
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: 172.14 E-value: 5.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 22 PLHVRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRW-AKQGCAHFVCSSagnagmaaayaaRQLGVPAT 100
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLsEEERARGVVAASagnhaqgvayaaRLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 101 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALwekP---- 176
Cdd:COG1171 100 IVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQL---Pdlda 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 177 -----------GAIALSvggggllcgvvqgLQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 245
Cdd:COG1171 176 vfvpvggggliAGVAAA-------------LKALSP-DIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 246 AQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHviqKLQREGNlqaplpSLVVIVCGGsNIS 325
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------RVVVVLSGG-NID 311
|
....*....
gi 966974738 326 LAQLRALKE 334
Cdd:COG1171 312 PDRLAEILE 320
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
25-335 |
2.20e-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: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGViAASAGNHAQGVAFSAARLGLKALIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIALSV 183
Cdd:TIGR01124 96 PETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEK-GLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFVPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 184 GGGGLLCGVVQGLQEVgWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHpIFSEVIS 263
Cdd:TIGR01124 175 GGGGLAAGVAALIKQL-MPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQY-LDDIVTV 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966974738 264 DQEAV-AAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCgGSNISLAQLRALKEQ 335
Cdd:TIGR01124 253 DTDEVcAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQT-------LVAILS-GANMNFHRLRYVSER 317
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
25-335 |
4.93e-28 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 114.12 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGViTASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELkeaLWEKPGAIALSv 183
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 184 ggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQA 248
Cdd:PRK12483 191 ------------FVPVGGGgliagiaayvkyvrpEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 249 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHViqklQREGNLQAPLpslvVIVCGGSNISL 326
Cdd:PRK12483 259 FELCRHY--VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYA----EREGIEGQTL----VAIDSGANVNF 328
|
....*....
gi 966974738 327 AQLRALKEQ 335
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 ... |
27-336 |
1.36e-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: 431.34 E-value: 1.36e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 27 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELL-DEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWE--KPGAIA 180
Cdd:cd06448 82 PESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 181 LSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSE 260
Cdd:cd06448 162 CSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966974738 261 VISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREgNLQAPLPSLVVIVCGGSNISLAQLRALKEQL 336
Cdd:cd06448 242 VVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
21-320 |
1.34e-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: 183.28 E-value: 1.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 21 EPLHVRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRwAKQGCA--HFVCSSAGNAGMAAAYAARQLGVP 98
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEGgkTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 99 ATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGA 178
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 179 IALSVGGGGLLCGVVQGLQEvGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVK-TVGAQALKLFQEHPI 257
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966974738 258 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCG 320
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR-------VVVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
22-334 |
5.99e-51 |
|
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: 172.14 E-value: 5.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 22 PLHVRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRW-AKQGCAHFVCSSagnagmaaayaaRQLGVPAT 100
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLsEEERARGVVAASagnhaqgvayaaRLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 101 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALwekP---- 176
Cdd:COG1171 100 IVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQL---Pdlda 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 177 -----------GAIALSvggggllcgvvqgLQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 245
Cdd:COG1171 176 vfvpvggggliAGVAAA-------------LKALSP-DIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 246 AQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHviqKLQREGNlqaplpSLVVIVCGGsNIS 325
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------RVVVVLSGG-NID 311
|
....*....
gi 966974738 326 LAQLRALKE 334
Cdd:COG1171 312 PDRLAEILE 320
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
25-324 |
3.36e-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: 161.50 E-value: 3.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVPAT 100
Cdd:cd01562 16 RRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 101 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEkPGAIa 180
Cdd:cd01562 93 IVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILEQVPD-LDAV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 181 lsvggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 245
Cdd:cd01562 170 ---------------FVPVGGGgliagiatavkalspNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 246 AQALKLFQEHPifSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQRegnlqaplpSLVVIVCGGsN 323
Cdd:cd01562 235 ELTFEIIRKLV--DDVVtvSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGK---------KVVVVLSGG-N 302
|
.
gi 966974738 324 I 324
Cdd:cd01562 303 I 303
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
27-321 |
6.34e-47 |
|
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: 159.22 E-value: 6.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 27 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEAL-WEKPGAIals 182
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 183 vggggllcgvvqglqevgwgdvpVIAMETFGAhsfhaattagklvslpkITSVAKAL-----GVKTVGAQAlklfqehpi 257
Cdd:cd00640 158 -----------------------VVPVGGGGN-----------------IAGIARALkellpNVKVIGVEP--------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966974738 258 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYshviqKLQREGNLQAPlpsLVVIVCGG 321
Cdd:cd00640 189 EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAAL-----KLAKKLGKGKT---VVVILTGG 244
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
25-335 |
2.20e-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: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGViAASAGNHAQGVAFSAARLGLKALIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIALSV 183
Cdd:TIGR01124 96 PETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEK-GLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFVPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 184 GGGGLLCGVVQGLQEVgWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHpIFSEVIS 263
Cdd:TIGR01124 175 GGGGLAAGVAALIKQL-MPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQY-LDDIVTV 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966974738 264 DQEAV-AAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCgGSNISLAQLRALKEQ 335
Cdd:TIGR01124 253 DTDEVcAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQT-------LVAILS-GANMNFHRLRYVSER 317
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
25-335 |
4.93e-28 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 114.12 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGViTASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELkeaLWEKPGAIALSv 183
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 184 ggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQA 248
Cdd:PRK12483 191 ------------FVPVGGGgliagiaayvkyvrpEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 249 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHViqklQREGNLQAPLpslvVIVCGGSNISL 326
Cdd:PRK12483 259 FELCRHY--VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYA----EREGIEGQTL----VAIDSGANVNF 328
|
....*....
gi 966974738 327 AQLRALKEQ 335
Cdd:PRK12483 329 DRLRHVAER 337
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
25-323 |
7.20e-25 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 104.12 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHF-CKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:PRK08639 24 PETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACRHLGIPGVIFM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLK---NEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKP---- 176
Cdd:PRK08639 104 PVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILEQLEKEGspdy 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 177 --------GAIAlsvggggllcgvvqG----LQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTV 244
Cdd:PRK08639 183 vfvpvgggGLIS--------------GvttyLKERSP-KTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 245 GAQALKLFQEHPifSEVIS-DQEAV-AAIEKFVDDEKILVEPAcGA----ALAAVYSHVIQKlqregnlqaplpSLVVIV 318
Cdd:PRK08639 248 GDLTFEILKDVV--DDVVLvPEGAVcTTILELYNKEGIVAEPA-GAlsiaALELYKDEIKGK------------TVVCVI 312
|
....*
gi 966974738 319 CGGSN 323
Cdd:PRK08639 313 SGGNN 317
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
25-330 |
2.86e-24 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 103.29 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCahfVCSSAGNAGMAAAYAARQLGVPAT 100
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 101 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIA 180
Cdd:PRK09224 96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 181 LSvggggllcgvvqglqeVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 245
Cdd:PRK09224 175 VP----------------VGGGgliagvaayikqlrpEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 246 AQALKLFQEHpiFSEVI---SDqEAVAAIEKFVDDEKILVEPAcGA-ALAAVYSHVIQ-KLQREgnlqaplpSLVVIVCg 320
Cdd:PRK09224 239 EETFRLCQEY--VDDVItvdTD-EICAAIKDVFEDTRSIAEPA-GAlALAGLKKYVAQhGIEGE--------TLVAILS- 305
|
330
....*....|
gi 966974738 321 GSNISLAQLR 330
Cdd:PRK09224 306 GANMNFDRLR 315
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
24-321 |
5.91e-24 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 100.03 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 24 HVR-TPI--RDSMALSKVAgtsVYLKMDSAQPSGSFKIRGIGHFCkRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPAT 100
Cdd:PRK08246 20 HIRrTPVleADGAGFGPAP---VWLKLEHLQHTGSFKARGAFNRL-LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPAT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 101 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKP---- 176
Cdd:PRK08246 96 VFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAET-GALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDtvlv 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 177 -----GAIAlsvggggllcgvvqGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKL 251
Cdd:PRK08246 175 avgggGLIA--------------GIAAWFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFAL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 252 FQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKlqregnlqAPLPSLVVIVCGG 321
Cdd:PRK08246 241 ARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVP--------APGERVAVVLCGA 302
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
25-172 |
8.77e-23 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 96.96 E-value: 8.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH-FVCSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARgVVTASTGNHGRALAYAARALGIRATICM 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEAL 172
Cdd:PRK07476 98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREE-GLTMVPPFDDPRIIAGQGTIGLEILEAL 165
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
25-334 |
1.15e-22 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 98.84 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGViCSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 104 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIALSV 183
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEE-GRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 184 GGGGLLCGVVQGLQEVGwGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVIS 263
Cdd:PLN02550 267 GGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966974738 264 DQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpslVVIVCGGSNISLAQLRALKE 334
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDEN--------VVAITSGANMNFDRLRIVTE 408
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
24-331 |
3.49e-20 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 89.37 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 24 HVR-TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVP 98
Cdd:PRK06815 17 QVRvTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAAKLAGIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 99 ATIVVPSTTPALTIERLKNEGATVKVVGELLDEAfELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALwEKPGA 178
Cdd:PRK06815 94 VTVYAPEQASAIKLDAIRALGAEVRLYGGDALNA-ELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ-PDLDA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 179 IALSVGGGGLLCGVVQGLQEVGwGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAK--ALGVKTvGAQALKLFQEHP 256
Cdd:PRK06815 172 VFVAVGGGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgtAGGVEP-GAITFPLCQQLI 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966974738 257 IFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAvyshvIQKLQREGNLQaplpSLVVIVCgGSNISLAQLRA 331
Cdd:PRK06815 250 DQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAA-----ALKLAPRYQGK----KVAVVLC-GKNIVLEKYLE 314
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
25-296 |
5.36e-20 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 89.95 E-value: 5.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 25 VRTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIghfCKRWAK-------------------QGCAHfvcssagnag 85
Cdd:PRK07334 22 LRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGA---LNKLLLlteeerargviamsagnhaQGVAY---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 86 maaayAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIV 165
Cdd:PRK07334 89 -----HAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 166 KELKEALwekP------------GAIAlsvggggllcgvvqGLQEVGWG---DVPVIAMETfgaHSFHAATTAGKLVSLP 230
Cdd:PRK07334 163 LEMLEDA---PdldtlvvpigggGLIS--------------GMATAAKAlkpDIEIIGVQT---ELYPSMYAAIKGVALP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966974738 231 KITS-VAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSH 296
Cdd:PRK07334 223 CGGStIAEGIAVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAY 289
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
26-336 |
5.63e-19 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 86.33 E-value: 5.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 26 RTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVPATI 101
Cdd:PRK08638 27 KTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGIDGKV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 102 VVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIAl 181
Cdd:PRK08638 104 VMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTVIV- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 182 svggggllcgvvqglqEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGA 246
Cdd:PRK08638 182 ----------------PIGGGgliagiavalksinpTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 247 QALKLFQEhpIFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQREGNlqaplpsLVVIVCGGsNI 324
Cdd:PRK08638 246 LTYEIVRE--LVDDIVlvSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKK-------VVAIISGG-NV 315
|
330
....*....|..
gi 966974738 325 SLAQLRALKEQL 336
Cdd:PRK08638 316 DLSRVSQITGHV 327
|
|
| PLN02970 |
PLN02970 |
serine racemase |
26-329 |
8.83e-19 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 85.50 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 26 RTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCahfVCSSAGNAGMAAAYAARQLGVPATI 101
Cdd:PLN02970 27 RTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 102 VVPSTTPALTIERLKNEGATVkVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEAL--------- 172
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGII-TWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVpeldviivp 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 173 WEKPGAIAlsvggggLLCGVVQGLQEvgwgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKtVGAQALKLF 252
Cdd:PLN02970 183 ISGGGLIS-------GIALAAKAIKP----SIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS-LGDLTWPVV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 253 QEhpIFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKlqregNLQAPLPSLV-VIVCGGsNISLAQL 329
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 ... |
27-320 |
4.91e-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: 83.41 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 27 TPIRDSMALSKVAGT-SVYLKMDSAQPSGSFKIRG----IGHfckrwAKQ-GCAHFVCSSAGNAGMAAAYAARQLGVPAT 100
Cdd:cd01563 23 TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGmtvaVSK-----AKElGVKAVACASTGNTSASLAAYAARAGIKCV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 101 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpgWVYIPPFDDPLIWEGHASIVKELKEAL-WEKPGAI 179
Cdd:cd01563 98 VFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN--WIYLSNSLNPYRLEGQKTIAFEIAEQLgWEVPDYV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 180 ALSVGGGGLLCGVVQG---LQEVGWGD-VP-VIAMETFGAHSFHAATTAGK--LVSLPKITSVAKAL--GVKTVGAQALK 250
Cdd:cd01563 176 VVPVGNGGNITAIWKGfkeLKELGLIDrLPrMVGVQAEGAAPIVRAFKEGKddIEPVENPETIATAIriGNPASGPKALR 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 251 LFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviQKLQREGNLqAPLPSLVVIVCG 320
Cdd:cd01563 256 AVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGL-----KKLREEGII-DKGERVVVVLTG 319
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
27-335 |
7.84e-14 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 71.34 E-value: 7.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 27 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGC--AHFVCSSAGNAGMAAAYAARQLGVPATIVVP 104
Cdd:PRK06608 24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYSTGNHGQAVAYASKLFGIKTRIYLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 105 STTPALTIERLKNEGATVKVVgELLDEAFElaKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEALWEKPGAIALS-- 182
Cdd:PRK06608 104 LNTSKVKQQAALYYGGEVILT-NTRQEAEE--KAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFAScg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 183 -VGGGGLLCGVVQGLQEvgwgDVPVIAMETFGAHSFHAATTAGKLVSLPKI-TSVAKALGVKTVGAQALKLFQEHPIFSE 260
Cdd:PRK06608 181 gGGLISGTYLAKELISP----TSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYLKKLDDFYL 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966974738 261 ViSDQEAVAAIEKFVDDEKILVEPACGAALAAvyshVIQKLQRegnlQAPLPSLVVIVCGGsNISLAQLRALKEQ 335
Cdd:PRK06608 257 V-EEYEIYYWTAWLTHLLKVICEPSSAINMVA----VVNWLKT----QSKPQKLLVILSGG-NIDPILYNELWKE 321
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
26-332 |
5.80e-13 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 68.51 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 26 RTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCAHFvcsSAGNAGMAAAYAARQLGVPATI 101
Cdd:PRK07048 24 RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAGVVTF---SSGNHAQAIALSARLLGIPATI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 102 VVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELkealwekpgaial 181
Cdd:PRK07048 101 VMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER-GLTLIPPYDHPHVIAGQGTAAKEL------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 182 svggggllcgvvqgLQEVGWGDV-------------------------PVIAMETF----GAHSFHaattAGKLVSLPKI 232
Cdd:PRK07048 167 --------------FEEVGPLDAlfvclggggllsgcalaaralspgcKVYGVEPEagndGQQSFR----SGEIVHIDTP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 233 TSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviqklqREGNLQAPLP 312
Cdd:PRK07048 229 RTIADGAQTQHLGNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAA---------LRGKVPLKGK 299
|
330 340
....*....|....*....|
gi 966974738 313 SLVVIVCGGsNISLAQLRAL 332
Cdd:PRK07048 300 RVGVIISGG-NVDLARFAAL 318
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
43-292 |
4.60e-12 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 66.19 E-value: 4.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 43 VYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH-FVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGAT 121
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERpVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 122 VKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEalwEKPGAIALSVGGGGLLCGVVQGLQEVGw 201
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIELAA---HAPDVVIVPIGGGGLASGVALALKSQG- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 202 gdVPVIAMETFGAHSFhAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKIL 281
Cdd:PRK08813 205 --VRVVGAQVEGVDSM-ARAIRGDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVI 281
|
250
....*....|.
gi 966974738 282 VEPACGAALAA 292
Cdd:PRK08813 282 AEGAGALALAA 292
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
3-308 |
4.66e-09 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 57.32 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 3 SQREPEPW--SQLLLVMmsgEPLHV------RTPIRDSMALSKVAG-TSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGC 73
Cdd:PRK08197 51 AGRPANLWryHELLPVR---DPEHIvslgegMTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 74 AHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKAlAKNNPGWVYIPPFD 153
Cdd:PRK08197 128 KHLAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAE-AVAEYGWFDVSTLK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 154 DPLIWEGHASIVKELKEAL-WEKPGAI---ALSVGGGGLLCGVVQGLQEVGW--GDVP-VIAMETFGAHSFHAATTAGKL 226
Cdd:PRK08197 207 EPYRIEGKKTMGLELAEQLgWRLPDVIlypTGGGVGLIGIWKAFDELEALGWigGKRPrLVAVQAEGCAPIVKAWEEGKE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 227 VSLPKITSVAKALGV---KTVGAQ-ALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviQKLQ 302
Cdd:PRK08197 287 ESEFWEDAHTVAFGIrvpKALGDFlVLDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAA-----RQLR 361
|
....*.
gi 966974738 303 REGNLQ 308
Cdd:PRK08197 362 ESGWLK 367
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
26-293 |
6.80e-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: 56.62 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 26 RTPIRDSMALSK-VAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVP 104
Cdd:TIGR00260 22 VTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 105 STtpalTIERLK-----NEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKEAL-WEKPGA 178
Cdd:TIGR00260 102 AG----KISLGKlaqalGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLEGQKTYAFEAVEQLgWEAPDK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 179 IALSVGGGGLLCGVVQGLQE---VGWGDVPV-IAMETFGAHSFHAATTAGKLV---SLPKITSVAKALGVKTVGAQALKL 251
Cdd:TIGR00260 178 VVVPVPNSGNFGAIWKGFKEkkmLGLDSLPVkRGIQAEGAADIVRAFLEGGQWepiETPETLSTAMDIGNPANWPRALEA 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 966974738 252 FQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAV 293
Cdd:TIGR00260 258 FRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAAL 299
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
27-322 |
1.12e-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: 55.98 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 27 TPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSS-------------AGnagmaaayaar 93
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASsgngsaalaayaaRA----------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 94 qlGVPATIVVPST-TPALTIERLKNEGATVKVVGELLDEAFELAKALAKN---------NPG------------------ 145
Cdd:COG0498 136 --GIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADeglyavnsiNPArlegqktyafeiaeqlgr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 146 ---WVYIPP--FDDPL-IWEGhasivkeLKEalwekpgaialsvggggllcgvvqgLQEVGWGD-VP-VIAMETFGAHSF 217
Cdd:COG0498 214 vpdWVVVPTgnGGNILaGYKA-------FKE-------------------------LKELGLIDrLPrLIAVQATGCNPI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 218 HAATTAGKLVSLPK-ITSVAKALGV-KTV-GAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVy 294
Cdd:COG0498 262 LTAFETGRDEYEPErPETIAPSMDIgNPSnGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGL- 340
|
330 340
....*....|....*....|....*...
gi 966974738 295 shviQKLQREGNLQAPLPslVVIVCGGS 322
Cdd:COG0498 341 ----RKLREEGEIDPDEP--VVVLSTGH 362
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
27-292 |
1.34e-08 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 55.97 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 27 TPIRDSMALSKVaGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPST 106
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 107 TPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEALweKPGAIALSVGGG 186
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN-GLYNVTPEYNIIGLEGQKTIAFELWEEI--NPTHVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 187 GLLCGVVQG---LQEVGWGD-VP-VIAMETfgahsFHAATTAGKLVSLPKITSVAKALGV----KTVGAQALKLFQEHPI 257
Cdd:PRK05638 223 SYLYSIYKGfkeLLEIGVIEeIPkLIAVQT-----ERCNPIASEILGNKTKCNETKALGLyvknPVMKEYVSEAIKESGG 297
|
250 260 270
....*....|....*....|....*....|....*
gi 966974738 258 FSEVISDQEAVAAiEKFVDDEKILVEPACGAALAA 292
Cdd:PRK05638 298 TAVVVNEEEIMAG-EKLLAKEGIFAELSSAVVMPA 331
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
35-292 |
6.44e-08 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 53.46 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 35 LSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG--CAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTpalTI 112
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGprVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGN---SV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 113 ErlKNE-----GATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIwEGHASIVKELKEALwekpgaialsvgggg 187
Cdd:PRK06110 107 E--KNAamralGAELIEHGEDFQAAREEAARLAAER-GLHMVPSFHPDLV-RGVATYALELFRAV--------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 188 llcgvvQGLQEV------GWGDVPVIA--------METFGAHSFHAAT-----TAGKLVSLPKITSVAKALGVKTVGAQA 248
Cdd:PRK06110 168 ------PDLDVVyvpigmGSGICGAIAardalglkTRIVGVVSAHAPAyalsfEAGRVVTTPVATTLADGMACRTPDPEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 966974738 249 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAA 292
Cdd:PRK06110 242 LEVIRAG--ADRIVrvTDDEVAAAMRAYFTDTHNVAEGAGAAALAA 285
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
26-319 |
1.91e-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: 51.75 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 26 RTPIRDSMALSKVAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH------------------FVCssagnagma 87
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKpgttiieptsgntgiglaMVA--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 88 aayaaRQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDE----AFELAKALAKNNPGWVYIPPFDDPLIWEGH-A 162
Cdd:cd01561 73 -----AAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLNQFENPANPEAHyE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 163 SIVKELKEALwekPGAIalsvggggllcgvvqglqevgwgDVPVIAMETFGahsfhaaTTAGklvslpkitsVAKAL--- 239
Cdd:cd01561 148 TTAPEIWEQL---DGKV-----------------------DAFVAGVGTGG-------TITG----------VARYLkek 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 240 --GVKTVGAQALK--LFQEHPIFS---------------------EV--ISDQEAVAAIEKFVDDEKILVEPACGAALAA 292
Cdd:cd01561 185 npNVRIVGVDPVGsvLFSGGPPGPhkiegigagfipenldrslidEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVAA 264
|
330 340
....*....|....*....|....*..
gi 966974738 293 VYshviqKLQREgnlqAPLPSLVVIVC 319
Cdd:cd01561 265 AL-----KLAKR----LGPGKTIVTIL 282
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
26-293 |
8.46e-04 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 40.84 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 26 RTPIRDSMALSKVAGTS-VYLKMDSAQPSGSFKIRGIGHFCKRWAKQG--------CAHFVCSsagnagmaAAYAARQLG 96
Cdd:PRK06381 15 GTPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGysgitvgtCGNYGAS--------IAYFARLYG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 97 VPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFD--DPLIWEGHASIVKELKEALWE 174
Cdd:PRK06381 87 LKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKEN-GIYDANPGSvnSVVDIEAYSAIAYEIYEALGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 175 KPGAIAlsvggggllcgvvqglqevgwgdVPVIAMETFGA--HSFHAATTAGKLVSLPKI----TS----VAKAL--GVK 242
Cdd:PRK06381 166 VPDAVA-----------------------VPVGNGTTLAGiyHGFRRLYDRGKTSRMPRMigvsTSggnqIVESFkrGSS 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966974738 243 TVGAQALKLFQEHPIFSEVIS-----DQEAVAAIEK-------FVDDE-----KILVE-------PACGAALAAV 293
Cdd:PRK06381 223 EVVDLEVDEIRETAVNEPLVSyrsfdGDNALEAIYDshgyafgFSDDEmvkyaELLRRmeglnalPASASALAAL 297
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
35-319 |
1.64e-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: 39.65 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 35 LSKVAGTSVYLKMDSAQPSGSFKIR-----------------------------GIGhfckrwakqgcahfvcssagnag 85
Cdd:COG0031 22 LSPGPGAEIYAKLESFNPGGSVKDRialsmiedaekrgllkpggtiveatsgntGIG----------------------- 78
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 86 maAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVV--GELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGH-A 162
Cdd:COG0031 79 --LAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTpgAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHyE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 163 SIVKELKEALWEKPGA-------------IAlsvggggllcgvvQGLQEVgWGDVPVIAMETFGAHSFHAATTAGKLVS- 228
Cdd:COG0031 157 TTGPEIWEQTDGKVDAfvagvgtggtitgVG-------------RYLKER-NPDIKIVAVEPEGSPLLSGGEPGPHKIEg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 229 -----LPKItsvakalgvktvgaqalklFQEHPIfSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAvyshVIQKL 301
Cdd:COG0031 223 igagfVPKI-------------------LDPSLI-DEVItvSDEEAFAMARRLAREEGILVGISSGAAVAA----ALRLA 278
|
330
....*....|....*...
gi 966974738 302 QREGnlqaPLPSLVVIVC 319
Cdd:COG0031 279 KRLG----PGKTIVTILP 292
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|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
24-170 |
2.48e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 39.42 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966974738 24 HVRTPIRDSMALSKvagtSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVV 103
Cdd:PRK08329 59 HLTPPITPTVKRSI----KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFV 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966974738 104 PSTTPALTIERLKNEGATVKVVG----ELLDEAFELAKalaknNPGWVYIPPFDDPLIWEGHASIVKELKE 170
Cdd:PRK08329 135 SYNASKEKISLLSRLGAELHFVEgdrmEVHEEAVKFSK-----RNNIPYVSHWLNPYFLEGTKTIAYEIYE 200
|
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