|
Name |
Accession |
Description |
Interval |
E-value |
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
10-320 |
1.11e-154 |
|
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: 435.96 E-value: 1.11e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 10 KTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIV 86
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 87 VPSTTPALTIERLKNEGATVKVVGELL-DEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWE--KPGAI 163
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 164 ALSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFS 243
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229462819 244 EVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEgNLRTPLPSLVVIVCGGSNISLAQLRALKEQL 320
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
5-304 |
6.47e-56 |
|
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: 183.67 E-value: 6.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 5 EPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRwAKQGCA--HFVCSSAGNAGMAAAYAARQLGVP 82
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEGgkTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 83 ATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGA 162
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 163 IALSVGGGGLLCGVVQGLQEvGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVK-TVGAQALKLFQEHPI 241
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229462819 242 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVysHVIQKLQLEGNLRTplpslVVIVCG 304
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL--KLALAGELKGGDRV-----VVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
6-318 |
4.22e-52 |
|
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: 174.45 E-value: 4.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 6 PLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRW-AKQGCAHFVCSSagnagmaaayaaRQLGVPAT 84
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLsEEERARGVVAASagnhaqgvayaaRLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLwekP---- 160
Cdd:COG1171 100 IVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQL---Pdlda 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 161 -----------GAIALSvggggllcgvvqgLQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 229
Cdd:COG1171 176 vfvpvggggliAGVAAA-------------LKALSP-DIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 230 AQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHviqKLQLEGnlRTplpsLVVIVCGGsNIS 309
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKG--KR----VVVVLSGG-NID 311
|
....*....
gi 229462819 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 |
3.62e-31 |
|
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: 122.15 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGViAASAGNHAQGVAFSAARLGLKALIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSV 167
Cdd:TIGR01124 96 PETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEK-GLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFVPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 168 GGGGLLCGVVQGLQEVgWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHpIFSEVIS 247
Cdd:TIGR01124 175 GGGGLAAGVAALIKQL-MPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQY-LDDIVTV 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229462819 248 DQEAV-AAIEKFVDDEKILVEPACGAALAAVYSHVIQKlQLEGNlrtplpSLVVIVCgGSNISLAQLRALKEQ 319
Cdd:TIGR01124 253 DTDEVcAAIKDLFEDTRAVAEPAGALALAGLKKYVALH-GIRGQ------TLVAILS-GANMNFHRLRYVSER 317
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
9-319 |
2.49e-28 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 114.51 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGViTASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELketLWEKPGAIALSv 167
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 168 ggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQA 232
Cdd:PRK12483 191 ------------FVPVGGGgliagiaayvkyvrpEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 233 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKlQLEGnlRTplpslVVIVCGGSNISL 310
Cdd:PRK12483 259 FELCRHY--VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAERE-GIEG--QT-----LVAIDSGANVNF 328
|
....*....
gi 229462819 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 ... |
10-320 |
1.11e-154 |
|
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: 435.96 E-value: 1.11e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 10 KTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIV 86
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 87 VPSTTPALTIERLKNEGATVKVVGELL-DEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWE--KPGAI 163
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 164 ALSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFS 243
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229462819 244 EVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEgNLRTPLPSLVVIVCGGSNISLAQLRALKEQL 320
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
5-304 |
6.47e-56 |
|
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: 183.67 E-value: 6.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 5 EPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRwAKQGCA--HFVCSSAGNAGMAAAYAARQLGVP 82
Cdd:pfam00291 2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEGgkTVVEASSGNHGRALAAAAARLGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 83 ATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGA 162
Cdd:pfam00291 81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 163 IALSVGGGGLLCGVVQGLQEvGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVK-TVGAQALKLFQEHPI 241
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229462819 242 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVysHVIQKLQLEGNLRTplpslVVIVCG 304
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL--KLALAGELKGGDRV-----VVVLTG 295
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
6-318 |
4.22e-52 |
|
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: 174.45 E-value: 4.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 6 PLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRW-AKQGCAHFVCSSagnagmaaayaaRQLGVPAT 84
Cdd:COG1171 20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLsEEERARGVVAASagnhaqgvayaaRLLGIPAT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLwekP---- 160
Cdd:COG1171 100 IVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQL---Pdlda 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 161 -----------GAIALSvggggllcgvvqgLQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 229
Cdd:COG1171 176 vfvpvggggliAGVAAA-------------LKALSP-DIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 230 AQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHviqKLQLEGnlRTplpsLVVIVCGGsNIS 309
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKG--KR----VVVVLSGG-NID 311
|
....*....
gi 229462819 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 |
4.68e-48 |
|
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: 163.43 E-value: 4.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVPAT 84
Cdd:cd01562 16 RRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEkPGAIa 164
Cdd:cd01562 93 IVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILEQVPD-LDAV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 165 lsvggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 229
Cdd:cd01562 170 ---------------FVPVGGGgliagiatavkalspNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 230 AQALKLFQEHPifSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHviqKLQLEGNlrtplpSLVVIVCGGsN 307
Cdd:cd01562 235 ELTFEIIRKLV--DDVVtvSEDEIAAAMLLLFEREKLVAEPAGALALAALLSG---KLDLKGK------KVVVVLSGG-N 302
|
.
gi 229462819 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 |
1.62e-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: 1.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 11 TPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG---CAHFVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETL-WEKPGAIals 166
Cdd:cd00640 81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 167 vggggllcgvvqglqevgwgdvpVIAMETFGAhsfhaattagklvslpkITSVAKAL-----GVKTVGAQAlklfqehpi 241
Cdd:cd00640 158 -----------------------VVPVGGGGN-----------------IAGIARALkellpNVKVIGVEP--------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229462819 242 FSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEgnlrtplpSLVVIVCGG 305
Cdd:cd00640 189 EVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGK--------TVVVILTGG 244
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
9-319 |
3.62e-31 |
|
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: 122.15 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:TIGR01124 16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGViAASAGNHAQGVAFSAARLGLKALIVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSV 167
Cdd:TIGR01124 96 PETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEK-GLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFVPV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 168 GGGGLLCGVVQGLQEVgWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHpIFSEVIS 247
Cdd:TIGR01124 175 GGGGLAAGVAALIKQL-MPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQY-LDDIVTV 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229462819 248 DQEAV-AAIEKFVDDEKILVEPACGAALAAVYSHVIQKlQLEGNlrtplpSLVVIVCgGSNISLAQLRALKEQ 319
Cdd:TIGR01124 253 DTDEVcAAIKDLFEDTRAVAEPAGALALAGLKKYVALH-GIRGQ------TLVAILS-GANMNFHRLRYVSER 317
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
9-319 |
2.49e-28 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 114.51 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK12483 36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGViTASAGNHAQGVALAAARLGVKAVIVM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELketLWEKPGAIALSv 167
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 168 ggggllcgvvqgLQEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQA 232
Cdd:PRK12483 191 ------------FVPVGGGgliagiaayvkyvrpEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 233 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKlQLEGnlRTplpslVVIVCGGSNISL 310
Cdd:PRK12483 259 FELCRHY--VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAERE-GIEG--QT-----LVAIDSGANVNF 328
|
....*....
gi 229462819 311 AQLRALKEQ 319
Cdd:PRK12483 329 DRLRHVAER 337
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
9-307 |
5.70e-26 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 106.81 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHF-CKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK08639 24 PETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACRHLGIPGVIFM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 88 PSTTPALTIERLK---NEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEKP---- 160
Cdd:PRK08639 104 PVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILEQLEKEGspdy 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 161 --------GAIALSVGGggllcgvvqgLQEVGWgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQA 232
Cdd:PRK08639 183 vfvpvgggGLISGVTTY----------LKERSP-KTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229462819 233 LKLFQEHPifSEVIS-DQEAV-AAIEKFVDDEKILVEPACGAALAAVYSHviqKLQLEGnlrtplpSLVVIVCGGSN 307
Cdd:PRK08639 252 FEILKDVV--DDVVLvPEGAVcTTILELYNKEGIVAEPAGALSIAALELY---KDEIKG-------KTVVCVISGGN 316
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
9-314 |
1.80e-25 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 106.38 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCahfVCSSAGNAGMAAAYAARQLGVPAT 84
Cdd:PRK09224 19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIA 164
Cdd:PRK09224 96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 165 LSvggggllcgvvqglqeVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVG 229
Cdd:PRK09224 175 VP----------------VGGGgliagvaayikqlrpEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 230 AQALKLFQEHpiFSEVI---SDqEAVAAIEKFVDDEKILVEPAcGA-ALAAVYSHViQKLQLEGNlrtplpSLVVIVCgG 305
Cdd:PRK09224 239 EETFRLCQEY--VDDVItvdTD-EICAAIKDVFEDTRSIAEPA-GAlALAGLKKYV-AQHGIEGE------TLVAILS-G 306
|
....*....
gi 229462819 306 SNISLAQLR 314
Cdd:PRK09224 307 ANMNFDRLR 315
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
27-305 |
5.27e-24 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 99.64 E-value: 5.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 27 VYLKMDSAQPSGSFKIRGIGHFCkRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATV 106
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNRL-LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 107 KVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEKP---------GAIAlsvggggllcgvv 177
Cdd:PRK08246 118 VVVGAEYADALEAAQAFAAET-GALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDtvlvavgggGLIA------------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 178 qGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEK 257
Cdd:PRK08246 184 -GIAAWFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDEAIIAARRA 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 229462819 258 FVDDEKILVEPACGAALAAVYShviqklqleGNLRtPLPS--LVVIVCGG 305
Cdd:PRK08246 263 LWEELRLAVEPGAATALAALLS---------GAYV-PAPGerVAVVLCGA 302
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
9-318 |
1.69e-23 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 100.77 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFV-CSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGViCSSAGNHAQGVALSAQRLGCDAVIAM 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSV 167
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEE-GRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 168 GGGGLLCGVVQGLQEVGwGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVIS 247
Cdd:PLN02550 267 GGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 229462819 248 DQEAVAAIEKFVDDEKILVEPACGAALAAVYSHViQKLQLEGnlrtplpSLVVIVCGGSNISLAQLRALKE 318
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALAGAEAYC-KYYGLKD-------ENVVAITSGANMNFDRLRIVTE 408
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
9-316 |
8.15e-23 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 96.57 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH-FVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK07476 18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARgVVTASTGNHGRALAYAARALGIRATICM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 88 PSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEKP------- 160
Cdd:PRK07476 98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREE-GLTMVPPFDDPRIIAGQGTIGLEILEALPDVAtvlvpls 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 161 --GAIALSVGGGGLLCGVVQglqevgwgdVPVIAMETfGAhSFHAATTAGKLVSLPKITSVAKALGvktvGAQAL----- 233
Cdd:PRK07476 177 ggGLASGVAAAVKAIRPAIR---------VIGVSMER-GA-AMHASLAAGRPVQVEEVPTLADSLG----GGIGLdnryt 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 234 -KLFQEhpIFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviqklqLEGNLRTPLPSLVVIVCGGsNISL 310
Cdd:PRK07476 242 fAMCRA--LLDDVVllDEAEIAAGIRHAYREERLVVEGAGAVGIAAL---------LAGKIAARDGPIVVVVSGA-NIDM 309
|
....*.
gi 229462819 311 AQLRAL 316
Cdd:PRK07476 310 ELHRRI 315
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
11-315 |
2.70e-21 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 92.45 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 11 TPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVPATIV 86
Cdd:PRK06815 21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAAKLAGIPVTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 87 VPSTTPALTIERLKNEGATVKVVGELLDEAfELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLwEKPGAIALS 166
Cdd:PRK06815 98 APEQASAIKLDAIRALGAEVRLYGGDALNA-ELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ-PDLDAVFVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 167 VGGGGLLCGVVQGLQEVGwGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAK--ALGVKTvGAQALKLFQEHPIFSE 244
Cdd:PRK06815 176 VGGGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgtAGGVEP-GAITFPLCQQLIDQKV 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 229462819 245 VISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviqkLQLEGNLRTplPSLVVIVCgGSNISLAQLRA 315
Cdd:PRK06815 254 LVSEEEIKEAMRLIAETDRWLIEGAAGVALAAA-------LKLAPRYQG--KKVAVVLC-GKNIVLEKYLE 314
|
|
| PLN02970 |
PLN02970 |
serine racemase |
10-313 |
1.49e-19 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 87.43 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 10 KTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCahfVCSSAGNAGMAAAYAARQLGVPATI 85
Cdd:PLN02970 27 RTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 86 VVPSTTPALTIERLKNEGATVkVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETL--------- 156
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGII-TWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVpeldviivp 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 157 WEKPGAIAlsvggggLLCGVVQGLQEvgwgDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKtVGAQALKLF 236
Cdd:PLN02970 183 ISGGGLIS-------GIALAAKAIKP----SIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS-LGDLTWPVV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 237 QEhpIFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQ-KLQLEGNLRtplpsLVVIVCGGsNISLAQL 313
Cdd:PLN02970 251 RD--LVDDVItvDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRsNPAWKGCKN-----VGIVLSGG-NVDLGVL 322
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
9-280 |
3.61e-19 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 87.26 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 9 VKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIghfCKRWAK-------------------QGCAHfvcssagnag 69
Cdd:PRK07334 22 LRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGA---LNKLLLlteeerargviamsagnhaQGVAY---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 70 maaayAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIV 149
Cdd:PRK07334 89 -----HAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 150 KELketLWEKP------------GAIAlsvggggllcgvvqGLQEVGWG---DVPVIAMETfgaHSFHAATTAGKLVSLP 214
Cdd:PRK07334 163 LEM---LEDAPdldtlvvpigggGLIS--------------GMATAAKAlkpDIEIIGVQT---ELYPSMYAAIKGVALP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 229462819 215 KITS-VAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSH 280
Cdd:PRK07334 223 CGGStIAEGIAVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAY 289
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
10-320 |
1.47e-18 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 84.79 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 10 KTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGcahFVCSSAGNAGMAAAYAARQLGVPATI 85
Cdd:PRK08638 27 KTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGIDGKV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 86 VVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIAl 165
Cdd:PRK08638 104 VMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILEDLWDVDTVIV- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 166 svggggllcgvvqglqEVGWG---------------DVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGA 230
Cdd:PRK08638 182 ----------------PIGGGgliagiavalksinpTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 231 QALKLFQEhpIFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLqLEGNlrtplpSLVVIVCGGsNI 308
Cdd:PRK08638 246 LTYEIVRE--LVDDIVlvSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQY-IQNK------KVVAIISGG-NV 315
|
330
....*....|..
gi 229462819 309 SLAQLRALKEQL 320
Cdd:PRK08638 316 DLSRVSQITGHV 327
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
11-304 |
1.68e-17 |
|
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: 81.49 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 11 TPIRDSMALSKMAGT-SVYLKMDSAQPSGSFKIRG----IGHfckrwAKQ-GCAHFVCSSAGNAGMAAAYAARQLGVPAT 84
Cdd:cd01563 23 TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGmtvaVSK-----AKElGVKAVACASTGNTSASLAAYAARAGIKCV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 85 IVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpgWVYIPPFDDPLIWEGHASIVKELKETL-WEKPGAI 163
Cdd:cd01563 98 VFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN--WIYLSNSLNPYRLEGQKTIAFEIAEQLgWEVPDYV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 164 ALSVGGGGLLCGVVQG---LQEVGWGD-VP-VIAMETFGAHSFHAATTAGK--LVSLPKITSVAKAL--GVKTVGAQALK 234
Cdd:cd01563 176 VVPVGNGGNITAIWKGfkeLKELGLIDrLPrMVGVQAEGAAPIVRAFKEGKddIEPVENPETIATAIriGNPASGPKALR 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 235 LFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVyshviQKLQLEGNLRTPlPSLVVIVCG 304
Cdd:cd01563 256 AVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGL-----KKLREEGIIDKG-ERVVVVLTG 319
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
10-163 |
3.40e-14 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 72.11 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 10 KTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGC--AHFVCSSAGNAGMAAAYAARQLGVPATIVV 87
Cdd:PRK06608 23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlpDKIVAYSTGNHGQAVAYASKLFGIKTRIYL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229462819 88 PSTTPALTIERLKNEGATVKVVgELLDEAFElaKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAI 163
Cdd:PRK06608 103 PLNTSKVKQQAALYYGGEVILT-NTRQEAEE--KAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAI 175
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
10-154 |
1.39e-12 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 67.35 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 10 KTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRG----IGHFCKRWAKQGCAHFvcsSAGNAGMAAAYAARQLGVPATI 85
Cdd:PRK07048 24 RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAGVVTF---SSGNHAQAIALSARLLGIPATI 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229462819 86 VVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKE 154
Cdd:PRK07048 101 VMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER-GLTLIPPYDHPHVIAGQGTAAKELFE 168
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
27-276 |
2.32e-12 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 66.96 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 27 VYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH-FVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGAT 105
Cdd:PRK08813 50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERpVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 106 VKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKEtlwEKPGAIALSVGGGGLLCGVVQGLQEVGw 185
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIELAA---HAPDVVIVPIGGGGLASGVALALKSQG- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 186 gdVPVIAMETFGAHSFhAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKIL 265
Cdd:PRK08813 205 --VRVVGAQVEGVDSM-ARAIRGDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVI 281
|
250
....*....|.
gi 229462819 266 VEPACGAALAA 276
Cdd:PRK08813 282 AEGAGALALAA 292
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
11-306 |
4.54e-09 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 57.13 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 11 TPIRDSMALSKMaGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPST 90
Cdd:PRK05638 67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 91 TPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIWEGHASIVKELKETLweKPGAIALSVGGG 170
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN-GLYNVTPEYNIIGLEGQKTIAFELWEEI--NPTHVIVPTGSG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 171 GLLCGVVQG---LQEVGWGD-VP-VIAMETfgahsFHAATTAGKLVSLPKITSVAKALGV----KTVGAQALKLFQEHPI 241
Cdd:PRK05638 223 SYLYSIYKGfkeLLEIGVIEeIPkLIAVQT-----ERCNPIASEILGNKTKCNETKALGLyvknPVMKEYVSEAIKESGG 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 229462819 242 FSEVISDQEAVAAiEKFVDDEKILVEPACGAALAAVyshviqkLQLEGNLRTPLPSLVVIVCGGS 306
Cdd:PRK05638 298 TAVVVNEEEIMAG-EKLLAKEGIFAELSSAVVMPAL-------LKLGEEGYIEKGDKVVLVVTGS 354
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
11-277 |
1.60e-08 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 55.39 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 11 TPIRDSMALSKMAG-TSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPS 89
Cdd:PRK08197 80 TPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 90 TTPALTIERLKNEGATVKVVGELLDEAFELAKAlAKNNPGWVYIPPFDDPLIWEGHASIVKELKETL-WEKPGAI---AL 165
Cdd:PRK08197 160 DAPEITRLECALAGAELYLVDGLISDAGKIVAE-AVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLgWRLPDVIlypTG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 166 SVGGGGLLCGVVQGLQEVGW--GDVP-VIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGV---KTVGAQ-ALKLFQE 238
Cdd:PRK08197 239 GGVGLIGIWKAFDELEALGWigGKRPrLVAVQAEGCAPIVKAWEEGKEESEFWEDAHTVAFGIrvpKALGDFlVLDAVRE 318
|
250 260 270
....*....|....*....|....*....|....*....
gi 229462819 239 HPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAV 277
Cdd:PRK08197 319 TGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAA 357
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
11-306 |
5.61e-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: 53.67 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 11 TPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSS-------------AGnagmaaayaar 77
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASsgngsaalaayaaRA----------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 78 qlGVPATIVVPST-TPALTIERLKNEGATVKVVGELLDEAFELAKALAKN---------NPG------------------ 129
Cdd:COG0498 136 --GIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADeglyavnsiNPArlegqktyafeiaeqlgr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 130 ---WVYIPP--FDDPL-IWEGhasivkeLKEtlwekpgaialsvggggllcgvvqgLQEVGWGD-VP-VIAMETFGAHSF 201
Cdd:COG0498 214 vpdWVVVPTgnGGNILaGYKA-------FKE-------------------------LKELGLIDrLPrLIAVQATGCNPI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 202 HAATTAGKLVSLPK-ITSVAKALGV-KTV-GAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVy 278
Cdd:COG0498 262 LTAFETGRDEYEPErPETIAPSMDIgNPSnGERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGL- 340
|
330 340
....*....|....*....|....*...
gi 229462819 279 shviQKLQLEGNLRTPLPslVVIVCGGS 306
Cdd:COG0498 341 ----RKLREEGEIDPDEP--VVVLSTGH 362
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
19-314 |
9.50e-08 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 52.69 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 19 LSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQG--CAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTpalTI 96
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGprVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGN---SV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 97 ErlKNE-----GATVKVVGELLDEAFELAKALAKNNpGWVYIPPFDDPLIwEGHASIVKELKETLwekpgaialsvgggg 171
Cdd:PRK06110 107 E--KNAamralGAELIEHGEDFQAAREEAARLAAER-GLHMVPSFHPDLV-RGVATYALELFRAV--------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 172 llcgvvQGLQEV------GWGDVPVIA--------METFGAHSFHAAT-----TAGKLVSLPKITSVAKALGVKTVGAQA 232
Cdd:PRK06110 168 ------PDLDVVyvpigmGSGICGAIAardalglkTRIVGVVSAHAPAyalsfEAGRVVTTPVATTLADGMACRTPDPEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 233 LKLFQEHpiFSEVI--SDQEAVAAIEKFVDDEKILVEPACGAALAAVYShviQKLQLEGnLRtplpslVVIVCGGSNISL 310
Cdd:PRK06110 242 LEVIRAG--ADRIVrvTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQ---ERERLAG-KR------VGLVLSGGNIDR 309
|
....
gi 229462819 311 AQLR 314
Cdd:PRK06110 310 AVFA 313
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
11-277 |
9.93e-08 |
|
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: 52.77 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 11 TPIRDSMALSKMAG-TSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPS 89
Cdd:TIGR00260 23 TPLFRAPALAANVGiKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 90 TtpalTIERLK-----NEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETL-WEKPGAI 163
Cdd:TIGR00260 103 G----KISLGKlaqalGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLEGQKTYAFEAVEQLgWEAPDKV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 164 ALSVGGGGLLCGVVQGLQE---VGWGDVPV-IAMETFGAHSFHAATTAGKLV---SLPKITSVAKALGVKTVGAQALKLF 236
Cdd:TIGR00260 179 VVPVPNSGNFGAIWKGFKEkkmLGLDSLPVkRGIQAEGAADIVRAFLEGGQWepiETPETLSTAMDIGNPANWPRALEAF 258
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 229462819 237 QEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAV 277
Cdd:TIGR00260 259 RRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAAL 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
10-277 |
8.78e-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: 49.82 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 10 KTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAH------------------FVCssagnagma 71
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKpgttiieptsgntgiglaMVA--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 72 aayaaRQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDE----AFELAKALAKNNPGWVYIPPFDDPLIWEGH-- 145
Cdd:cd01561 73 -----AAKGYRFIIVMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLNQFENPANPEAHye 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 146 ---ASIVKELKETLwekpgaialsvggggllcgvvqglqevgwgDVPVIAMETFGahsfhaaTTAGklvslpkitsVAKA 222
Cdd:cd01561 148 ttaPEIWEQLDGKV------------------------------DAFVAGVGTGG-------TITG----------VARY 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 223 L-----GVKTVGAQALK--LFQEHPIFS---------------------EV--ISDQEAVAAIEKFVDDEKILVEPACGA 272
Cdd:cd01561 181 LkeknpNVRIVGVDPVGsvLFSGGPPGPhkiegigagfipenldrslidEVvrVSDEEAFAMARRLAREEGLLVGGSSGA 260
|
....*
gi 229462819 273 ALAAV 277
Cdd:cd01561 261 AVAAA 265
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
24-154 |
2.89e-03 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 39.04 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 24 GTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEG 103
Cdd:PRK08329 71 SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLG 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 229462819 104 ATVKVVG----ELLDEAFELAKalaknNPGWVYIPPFDDPLIWEGHASIVKELKE 154
Cdd:PRK08329 151 AELHFVEgdrmEVHEEAVKFSK-----RNNIPYVSHWLNPYFLEGTKTIAYEIYE 200
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
11-277 |
7.53e-03 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 37.76 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 11 TPIRDSMALSKMAGTS-VYLKMDSAQPSGSFKIRGIGHFCKRWAKQG--------CAHFVCSsagnagmaAAYAARQLGV 81
Cdd:PRK06381 16 TPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGysgitvgtCGNYGAS--------IAYFARLYGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 82 PATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNpGWVYIPPFD--DPLIWEGHASIVKELKETLWEK 159
Cdd:PRK06381 88 KAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKEN-GIYDANPGSvnSVVDIEAYSAIAYEIYEALGDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229462819 160 PGAIAlsvggggllcgvvqglqevgwgdVPVIAMETFGA--HSFHAATTAGKLVSLPKI----TS----VAKAL--GVKT 227
Cdd:PRK06381 167 PDAVA-----------------------VPVGNGTTLAGiyHGFRRLYDRGKTSRMPRMigvsTSggnqIVESFkrGSSE 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229462819 228 VGAQALKLFQEHPIFSEVIS-----DQEAVAAIEK-------FVDDE-----KILVE-------PACGAALAAV 277
Cdd:PRK06381 224 VVDLEVDEIRETAVNEPLVSyrsfdGDNALEAIYDshgyafgFSDDEmvkyaELLRRmeglnalPASASALAAL 297
|
|
| |
