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Conserved domains on  [gi|52783414|sp|Q8VBT2|]
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RecName: Full=L-serine dehydratase/L-threonine deaminase; Short=SDH; AltName: Full=L-serine deaminase; AltName: Full=L-threonine dehydratase; Short=TDH

Protein Classification

serine/threonine dehydratase family protein( domain architecture ID 10157824)

serine/threonine dehydratase family protein such as L-serine dehydratase/L-threonine deaminase, a pyridoxal-5'-phosphate (PLP)-dependent enzyme that catalyzes dehydration of L-Ser/Thr to yield pyruvate/ketobutyrate and ammonia

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
10-320 4.15e-157

Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.


:

Pssm-ID: 107209  Cd Length: 316  Bit Score: 442.12  E-value: 4.15e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQG---CRHFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:cd06448   1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  87 VPNTTPALTIERLKNEGATVEVVGEML-DEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL--SAKPGAI 163
Cdd:cd06448  81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLqsQEKVDAI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 164 VLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFS 243
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52783414 244 EVISDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgRLQTPLASLVVIVCGGSNISLAQLQALKVQL 320
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
10-320 4.15e-157

Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.


Pssm-ID: 107209  Cd Length: 316  Bit Score: 442.12  E-value: 4.15e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQG---CRHFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:cd06448   1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  87 VPNTTPALTIERLKNEGATVEVVGEML-DEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL--SAKPGAI 163
Cdd:cd06448  81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLqsQEKVDAI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 164 VLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFS 243
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52783414 244 EVISDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgRLQTPLASLVVIVCGGSNISLAQLQALKVQL 320
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
10-304 8.93e-67

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 425586 [Multi-domain]  Cd Length: 295  Bit Score: 211.40  E-value: 8.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCkMKAKQGC--RHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:pfam00291   7 PTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLL-LRLKEGEggKTVVEASSGNHGRALAAAAARLGLKVTIVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 167
Cdd:pfam00291  86 PEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   168 GGGGLLCGVVQGLREvGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGV-NTVGAQTLKLFYEHPIFSEVI 246
Cdd:pfam00291 166 GGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgFEPGALALDLLDEYVGEVVTV 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414   247 SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEGRlqtplasLVVIVCG 304
Cdd:pfam00291 245 SDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR-------VVVVLTG 295
IlvA COG1171
Threonine dehydratase [Amino acid transport and metabolism];
2-316 1.20e-58

Threonine dehydratase [Amino acid transport and metabolism];


Pssm-ID: 224092 [Multi-domain]  Cd Length: 347  Bit Score: 192.05  E-value: 1.20e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQgcRHFVCSSAGNAGMATAY 74
Cdd:COG1171  14 AAAARLKgvvNPTPLQRSPSLSERLGAEIYLKRENLQPVGSFKIRGaynkLSSLSEEEERA--AGVIAASAGNHAQGVAY 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  75 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:COG1171  92 AAKRLGIKATIVMPETTPKIKVDATRGYGAEVILHGDNFDDAYAAAEELAEEE-GLTFVPPFDDPDVIAGQGTIALEILE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 155 TLSAKPGAIVLSVGGGGLLCGVVQGLREVGWeDVPIIAMETFGAHSFHAAIKEGKL-VTLPKITSVAKALGVNTVGAQTL 233
Cdd:COG1171 171 QLPDLPDAVFVPVGGGGLISGIATALKALSP-EIKVIGVEPEGAPSMYASLKAGKIvVVLPDVGTIADGLAVKRPGDLTF 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 234 KLFYEHPifSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgrlqtplaSLVVIVCGGsNISLA 311
Cdd:COG1171 250 EILRELV--DDIVlvDEDEICAAMRDLFERTKIIAEPAGALALAALLAGKIEPLQGK--------TVVVILSGG-NIDFE 318

                ....*
gi 52783414 312 QLQAL 316
Cdd:COG1171 319 RLAEV 323
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
11-310 7.94e-38

threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130197 [Multi-domain]  Cd Length: 380  Bit Score: 138.34  E-value: 7.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLckmKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    87 VPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSaKPGAIVLS 166
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEE-GRVFVHPFDDEFVMAGQGTIGLEIMEDIP-DVDTVIVP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   167 VGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVI 246
Cdd:TIGR01127 156 VGGGGLISGVASAAKQIN-PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTV 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52783414   247 SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVcrlQDEGRlqtplaSLVVIVCGGsNISL 310
Cdd:TIGR01127 235 DEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKV---DVKGK------KIAVVLSGG-NIDL 288
PRK08639 PRK08639
threonine dehydratase; Validated
2-307 1.84e-32

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 124.53  E-value: 1.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHL-CKMKAKQGCRHFVCSSAGNAGMATAYAAR 77
Cdd:PRK08639  14 KAAKRLKdvvPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   78 RLGIPATIVVPNTTPALTIERLK---NEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PRK08639  94 HLGIPGVIFMPVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  155 TLS--AKPGAIVLSVGGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQT 232
Cdd:PRK08639 173 QLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414  233 LKLFYEHPifSEVIS-DQEAVSA--LEKFvDDEKILVEPACGAALAAVysrvvcrlqDEGRLQTPLASLVVIVCGGSN 307
Cdd:PRK08639 252 FEILKDVV--DDVVLvPEGAVCTtiLELY-NKEGIVAEPAGALSIAAL---------ELYKDEIKGKTVVCVISGGNN 317
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
10-320 4.15e-157

Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.


Pssm-ID: 107209  Cd Length: 316  Bit Score: 442.12  E-value: 4.15e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQG---CRHFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:cd06448   1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  87 VPNTTPALTIERLKNEGATVEVVGEML-DEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL--SAKPGAI 163
Cdd:cd06448  81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLqsQEKVDAI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 164 VLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFS 243
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52783414 244 EVISDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgRLQTPLASLVVIVCGGSNISLAQLQALKVQL 320
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
10-304 8.93e-67

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 425586 [Multi-domain]  Cd Length: 295  Bit Score: 211.40  E-value: 8.93e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCkMKAKQGC--RHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:pfam00291   7 PTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLL-LRLKEGEggKTVVEASSGNHGRALAAAAARLGLKVTIVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 167
Cdd:pfam00291  86 PEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   168 GGGGLLCGVVQGLREvGWEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGV-NTVGAQTLKLFYEHPIFSEVI 246
Cdd:pfam00291 166 GGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgFEPGALALDLLDEYVGEVVTV 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414   247 SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEGRlqtplasLVVIVCG 304
Cdd:pfam00291 245 SDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR-------VVVVLTG 295
IlvA COG1171
Threonine dehydratase [Amino acid transport and metabolism];
2-316 1.20e-58

Threonine dehydratase [Amino acid transport and metabolism];


Pssm-ID: 224092 [Multi-domain]  Cd Length: 347  Bit Score: 192.05  E-value: 1.20e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQgcRHFVCSSAGNAGMATAY 74
Cdd:COG1171  14 AAAARLKgvvNPTPLQRSPSLSERLGAEIYLKRENLQPVGSFKIRGaynkLSSLSEEEERA--AGVIAASAGNHAQGVAY 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  75 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:COG1171  92 AAKRLGIKATIVMPETTPKIKVDATRGYGAEVILHGDNFDDAYAAAEELAEEE-GLTFVPPFDDPDVIAGQGTIALEILE 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 155 TLSAKPGAIVLSVGGGGLLCGVVQGLREVGWeDVPIIAMETFGAHSFHAAIKEGKL-VTLPKITSVAKALGVNTVGAQTL 233
Cdd:COG1171 171 QLPDLPDAVFVPVGGGGLISGIATALKALSP-EIKVIGVEPEGAPSMYASLKAGKIvVVLPDVGTIADGLAVKRPGDLTF 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 234 KLFYEHPifSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgrlqtplaSLVVIVCGGsNISLA 311
Cdd:COG1171 250 EILRELV--DDIVlvDEDEICAAMRDLFERTKIIAEPAGALALAALLAGKIEPLQGK--------TVVVILSGG-NIDFE 318

                ....*
gi 52783414 312 QLQAL 316
Cdd:COG1171 319 RLAEV 323
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
2-308 3.89e-55

Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.


Pssm-ID: 107205 [Multi-domain]  Cd Length: 304  Bit Score: 181.53  E-value: 3.89e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGcrhFVCSSAGNAGMATAY 74
Cdd:cd01562   6 AAAARIKpvvRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  75 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:cd01562  83 AAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 155 TLsAKPGAIvlsvggggllcgvvqgLREVG---------------WEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSV 219
Cdd:cd01562 162 QV-PDLDAV----------------FVPVGgggliagiatavkalSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTI 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 220 AKALGVNTVGAQTLKLFYEHPifSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVysrvvcrlqDEGRLQTPLAS 297
Cdd:cd01562 225 ADGLAVKRPGELTFEIIRKLV--DDVVtvSEDEIAAAMLLLFEREKLVAEPAGALALAAL---------LSGKLDLKGKK 293
                       330
                ....*....|.
gi 52783414 298 LVVIVCGGsNI 308
Cdd:cd01562 294 VVVVLSGG-NI 303
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
11-305 8.44e-55

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 178.86  E-value: 8.44e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKM---KAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:cd00640   1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLaeeEGKLPKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL-SAKPGAIvls 166
Cdd:cd00640  81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV--- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 167 vggggllcgvvqglrevgwedvpIIAMETFGAHS-FHAAIKEGKLvtLPKItsvakalgvntVGAQTlklfyehpiFSEV 245
Cdd:cd00640 158 -----------------------VVPVGGGGNIAgIARALKELLP--NVKV-----------IGVEP---------EVVT 192
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 246 ISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGrlqTPLASLVVIVCGG 305
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAAL-----KLAKKL---GKGKTVVVILTGG 244
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
11-310 7.94e-38

threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130197 [Multi-domain]  Cd Length: 380  Bit Score: 138.34  E-value: 7.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLckmKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    87 VPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSaKPGAIVLS 166
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEE-GRVFVHPFDDEFVMAGQGTIGLEIMEDIP-DVDTVIVP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   167 VGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVI 246
Cdd:TIGR01127 156 VGGGGLISGVASAAKQIN-PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTV 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52783414   247 SDQEAVSALEKFVDDEKILVEPACGAALAAVYSRVVcrlQDEGRlqtplaSLVVIVCGGsNISL 310
Cdd:TIGR01127 235 DEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKV---DVKGK------KIAVVLSGG-NIDL 288
PRK08639 PRK08639
threonine dehydratase; Validated
2-307 1.84e-32

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 124.53  E-value: 1.84e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHL-CKMKAKQGCRHFVCSSAGNAGMATAYAAR 77
Cdd:PRK08639  14 KAAKRLKdvvPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAiSQLSDEELAAGVVCASAGNHAQGVAYACR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   78 RLGIPATIVVPNTTPALTIERLK---NEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PRK08639  94 HLGIPGVIFMPVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEET-GATFIPPFDDPDVIAGQGTVAVEILE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  155 TLS--AKPGAIVLSVGGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQT 232
Cdd:PRK08639 173 QLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLT 251
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414  233 LKLFYEHPifSEVIS-DQEAVSA--LEKFvDDEKILVEPACGAALAAVysrvvcrlqDEGRLQTPLASLVVIVCGGSN 307
Cdd:PRK08639 252 FEILKDVV--DDVVLvPEGAVCTtiLELY-NKEGIVAEPAGALSIAAL---------ELYKDEIKGKTVVCVISGGNN 317
PRK12483 PRK12483
threonine dehydratase; Reviewed
9-321 2.51e-32

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 125.68  E-value: 2.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    9 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:PRK12483  36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAyNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELketLSAKPGAIVLS- 166
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEE-GLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGPLDAIf 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  167 -----VGGGGLLCGVVQGLRevgwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHpi 241
Cdd:PRK12483 192 vpvggGGLIAGIAAYVKYVR----PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHY-- 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  242 FSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVySRVVCRLQDEGRlqtplaSLVVIVcGGSNISLAQLQ--ALK 317
Cdd:PRK12483 266 VDEVVtvSTDELCAAIKDIYDDTRSITEPAGALAVAGI-KKYAEREGIEGQ------TLVAID-SGANVNFDRLRhvAER 337

                 ....
gi 52783414  318 VQLG 321
Cdd:PRK12483 338 AELG 341
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
9-304 1.76e-30

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 120.24  E-value: 1.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    9 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCrhfVCSSAGNAGMATAYAARRLGIPAT 84
Cdd:PRK09224  19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARGV---ITASAGNHAQGVALSAARLGIKAV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   85 IVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIV 164
Cdd:PRK09224  96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  165 LSvggggllcgvvqglreVG---------------WEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVG 229
Cdd:PRK09224 175 VP----------------VGgggliagvaayikqlRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIG 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414  230 AQTLKLFYEHpiFSEVIS-DQEAVSALEKFV-DDEKILVEPAcGA-ALAAVySRVVCRLQDEGRlqtplaSLVVIVCG 304
Cdd:PRK09224 239 EETFRLCQEY--VDDVITvDTDEICAAIKDVfEDTRSIAEPA-GAlALAGL-KKYVAQHGIEGE------TLVAILSG 306
PRK07334 PRK07334
threonine dehydratase; Provisional
1-277 2.45e-30

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 118.46  E-value: 2.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    1 MAAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAA 76
Cdd:PRK07334  11 RAAAARLAgqvLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGaLNKLLLLTEEERARGVIAMSAGNHAQGVAYHA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   77 RRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELketL 156
Cdd:PRK07334  91 QRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVALEM---L 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  157 SAKP------------GAIvlsvgggGLLCGVVQGLRevgwEDVPIIAMETFGAHSFHAAIKEgklVTLPKITS-VAKAL 223
Cdd:PRK07334 167 EDAPdldtlvvpigggGLI-------SGMATAAKALK----PDIEIIGVQTELYPSMYAAIKG---VALPCGGStIAEGI 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 52783414  224 GVNTVGAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAV 277
Cdd:PRK07334 233 AVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAAL 286
PRK08246 PRK08246
serine/threonine dehydratase;
22-305 7.17e-30

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 115.44  E-value: 7.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   22 LAGTSVFLKMDSSQPSGSFKIRGIGHLCkMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKN 101
Cdd:PRK08246  34 FGPAPVWLKLEHLQHTGSFKARGAFNRL-LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  102 EGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLsAKPGAIvlsvggggllcgvvqgLR 181
Cdd:PRK08246 113 LGAEVVVVGAEYADALEAAQAFAAET-GALLCHAYDQPEVLAGAGTLGLEIEEQA-PGVDTV----------------LV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  182 EVG-----------WED-VPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQ 249
Cdd:PRK08246 175 AVGgggliagiaawFEGrARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVSDE 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414  250 EAVSALEKFVDDEKILVEPACGAALAAVYSRVVCRLQDEgrlqtplaSLVVIVCGG 305
Cdd:PRK08246 255 AIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGA 302
PRK06815 PRK06815
threonine/serine dehydratase;
11-315 1.35e-29

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 114.79  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGH-LCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPN 89
Cdd:PRK06815  21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNkLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYAPE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   90 TTPALTIERLKNEGATVEVVG-EMLDEAIQVAKALEKNnpGWVYISPFDDPLIWEGHTSLVKELKETLsAKPGAIVLSVG 168
Cdd:PRK06815 101 QASAIKLDAIRALGAEVRLYGgDALNAELAARRAAEQQ--GKVYISPYNDPQVIAGQGTIGMELVEQQ-PDLDAVFVAVG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  169 GGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAK--ALGVNTvGAQTLKLFYEHPIFSEVI 246
Cdd:PRK06815 178 GGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgtAGGVEP-GAITFPLCQQLIDQKVLV 255
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52783414  247 SDQEAVSALEKFVDDEKILVEPACGAALAAvYSRVVCRLQdeGRlqtplaSLVVIVCgGSNISLAQLQA 315
Cdd:PRK06815 256 SEEEIKEAMRLIAETDRWLIEGAAGVALAA-ALKLAPRYQ--GK------KVAVVLC-GKNIVLEKYLE 314
eutB PRK07476
threonine dehydratase; Provisional
9-156 6.75e-29

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 113.14  E-value: 6.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    9 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGH-LCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:PRK07476  18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNaLLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICM 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52783414   88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETL 156
Cdd:PRK07476  98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREE-GLTMVPPFDDPRIIAGQGTIGLEILEAL 165
PLN02550 PLN02550
threonine dehydratase
9-314 1.07e-28

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 116.17  E-value: 1.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    9 VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:PLN02550 108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAyNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAM 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   88 PNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLSV 167
Cdd:PLN02550 188 PVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEE-GRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  168 GGGGLLCGVVQGLREVGWEdVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVIS 247
Cdd:PLN02550 267 GGGGLIAGIAAYVKRVRPE-VKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVS 345
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  248 DQEAVSALEKFVDDEKILVEPACGAALAAvySRVVCR---LQDEGrlqtplaslVVIVCGGSNISLAQLQ 314
Cdd:PLN02550 346 RDAICASIKDMFEEKRSILEPAGALALAG--AEAYCKyygLKDEN---------VVAITSGANMNFDRLR 404
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
11-304 1.07e-26

Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.


Pssm-ID: 107206 [Multi-domain]  Cd Length: 324  Bit Score: 107.29  E-value: 1.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  11 TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGighlckM-----KAKQ-GCRHFVCSSAGNAGMATAYAARRLGIPA 83
Cdd:cd01563  23 TPLVRAPRLGErLGGKNLYVKDEGLNPTGSFKDRG------MtvavsKAKElGVKAVACASTGNTSASLAAYAARAGIKC 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  84 TIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpgWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGA 162
Cdd:cd01563  97 VVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN--WIYLSNSLNPYRLEGQKTIAFEIAEQLGWEvPDY 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 163 IVLSVGGGGLLCGVVQG---LREVGW-EDVP-IIAMETFGAHSFHAAIKEGKLVTLP--KITSVAKALGV-NTVGA-QTL 233
Cdd:cd01563 175 VVVPVGNGGNITAIWKGfkeLKELGLiDRLPrMVGVQAEGAAPIVRAFKEGKDDIEPveNPETIATAIRIgNPASGpKAL 254
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52783414 234 KLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGRLQTPlASLVVIVCG 304
Cdd:cd01563 255 RAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLK-----KLREEGIIDKG-ERVVVVLTG 319
PLN02970 PLN02970
serine racemase
10-313 1.13e-24

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 101.68  E-value: 1.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGCrhfVCSSAGNAGMATAYAARRLGIPATI 85
Cdd:PLN02970  27 RTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKGV---VTHSSGNHAAALALAAKLRGIPAYI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   86 VVPNTTPALTIERLKNEGATVeVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLsakPG--AI 163
Cdd:PLN02970 104 VVPKNAPACKVDAVIRYGGII-TWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQV---PEldVI 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  164 VLSVGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVnTVGAQTLklfyehPIFS 243
Cdd:PLN02970 180 IVPISGGGLISGIALAAKAIK-PSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRA-SLGDLTW------PVVR 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  244 E------VISDQEAVSALEKFVDDEKILVEPACGAALAAVYSrvvcrlqdEGRLQTPLAS----LVVIVCGGsNISLAQL 313
Cdd:PLN02970 252 DlvddviTVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALS--------DSFRSNPAWKgcknVGIVLSGG-NVDLGVL 322
PRK06608 PRK06608
serine/threonine dehydratase;
10-316 1.76e-24

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 101.39  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGI-GHLCKMKaKQGCR--HFVCSSAGNAGMATAYAARRLGIPATIV 86
Cdd:PRK06608  23 LTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVlNHLLELK-EQGKLpdKIVAYSTGNHGQAVAYASKLFGIKTRIY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   87 VPNTTPALTIERLKNEGATVEVVgEMLDEAIQvaKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETLSAKPGAIVLS 166
Cdd:PRK06608 102 LPLNTSKVKQQAALYYGGEVILT-NTRQEAEE--KAKEDEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIFAS 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  167 VGGGGLLCGVVQGLREVGwEDVPIIAMETFGAHSFHAAIKEGKLVTLPKI-TSVAKALGVNTVGAQTLKL------FYEH 239
Cdd:PRK06608 179 CGGGGLISGTYLAKELIS-PTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYlkklddFYLV 257
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52783414  240 PIFSEVISDQEAVSALekfvddeKILVEPACGAALAAVYSRVvcrlqdegRLQTPLASLVVIVCGGsNISLAQLQAL 316
Cdd:PRK06608 258 EEYEIYYWTAWLTHLL-------KVICEPSSAINMVAVVNWL--------KTQSKPQKLLVILSGG-NIDPILYNEL 318
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
2-156 9.31e-21

bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 90.95  E-value: 9.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    2 AAQESLH---VKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG----IGHLCKMKAKQGcrhFVCSSAGNAGMATAY 74
Cdd:PRK08638  16 EAKQRLAgriRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVAL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   75 AARRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:PRK08638  93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILE 171

                 ..
gi 52783414  155 TL 156
Cdd:PRK08638 172 DL 173
PRK08813 PRK08813
threonine dehydratase; Provisional
27-276 4.99e-20

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 89.30  E-value: 4.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   27 VFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNEGAT 105
Cdd:PRK08813  50 VWLKLENLQRTGSYKVRGaLNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  106 VEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKetlSAKPGAIVLSVGGGGLLCGVVQGLREVGw 185
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIELA---AHAPDVVIVPIGGGGLASGVALALKSQG- 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  186 edVPIIAMETFGAHSFHAAIKeGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKIL 265
Cdd:PRK08813 205 --VRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVI 281
                        250
                 ....*....|.
gi 52783414  266 VEPACGAALAA 276
Cdd:PRK08813 282 AEGAGALALAA 292
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
10-154 1.30e-19

ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.


Pssm-ID: 132036 [Multi-domain]  Cd Length: 317  Bit Score: 87.60  E-value: 1.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVP 88
Cdd:TIGR02991  19 ETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGaTNAVLSLSDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMS 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414    89 NTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE 154
Cdd:TIGR02991  99 ELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADR-GLTMLPPFDHPDIVAGQGTLGLEVVE 163
PRK08197 PRK08197
threonine synthase; Validated
11-304 9.31e-19

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 85.82  E-value: 9.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   11 TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMA-TAYAArRLGIPATIVVP 88
Cdd:PRK08197  80 TPLLPLPRLGKaLGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAwAAYAA-RAGIRATIFMP 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   89 NTTPALTIERLKNEGATVEVV-GEMLDEAIQVAKALEKNnpGWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGAIVLS 166
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVdGLISDAGKIVAEAVAEY--GWFDVSTLKEPYRIEGKKTMGLELAEQLGWRlPDVILYP 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  167 VGGGGLLCGVVQGLRE---VGW--EDVP-IIAMETFG----AHSFHAAIKEGKL----VTLPKITSVAKALGVNTVgaqt 232
Cdd:PRK08197 237 TGGGVGLIGIWKAFDEleaLGWigGKRPrLVAVQAEGcapiVKAWEEGKEESEFwedaHTVAFGIRVPKALGDFLV---- 312
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52783414  233 LKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcRLQDEGRLQtPLASLVVIVCG 304
Cdd:PRK08197 313 LDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAAAR-----QLRESGWLK-GDERVVLFNTG 378
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
2-316 5.74e-18

threo-3-hydroxy-L-aspartate ammonia-lyase;


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 82.76  E-value: 5.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    2 AAQESL----HvKTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQGCRHFVCSSAGNAGMATAYAA 76
Cdd:PRK07048  13 AAAARLagvaH-RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaYNALSQFSPEQRRAGVVTFSSGNHAQAIALSA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   77 RRLGIPATIVVPNTTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKE-- 154
Cdd:PRK07048  92 RLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEER-GLTLIPPYDHPHVIAGQGTAAKELFEev 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  155 ----TLSAKPGAIVLSVGGGGLLCGVVQGLREVGWEdvPIIAMEtfGAHSFHAaikeGKLVTLPKITSVAKalgvntvGA 230
Cdd:PRK07048 171 gpldALFVCLGGGGLLSGCALAARALSPGCKVYGVE--PEAGND--GQQSFRS----GEIVHIDTPRTIAD-------GA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  231 QTLKL-FYEHPIFSE------VISDQEAVSALEKFVDDEKILVEPACGAALAAVYsrvvcrlqdEGRLQTPLASLVVIVC 303
Cdd:PRK07048 236 QTQHLgNYTFPIIRRlvddivTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAAL---------RGKVPLKGKRVGVIIS 306
                        330
                 ....*....|...
gi 52783414  304 GGsNISLAQLQAL 316
Cdd:PRK07048 307 GG-NVDLARFAAL 318
PRK05638 PRK05638
threonine synthase; Validated
11-276 2.73e-17

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 82.17  E-value: 2.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   11 TPLRDSMALSKLaGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNT 90
Cdd:PRK05638  67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   91 TPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSakPGAIVLSVGGG 170
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLN-GLYNVTPEYNIIGLEGQKTIAFELWEEIN--PTHVIVPTGSG 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  171 GLLCGVVQGLREV----GWEDVP-IIAMETFGAHSFHAAIkegklVTLPKITSVAKALGvntvgaqtlkLFYEHPIFSE- 244
Cdd:PRK05638 223 SYLYSIYKGFKELleigVIEEIPkLIAVQTERCNPIASEI-----LGNKTKCNETKALG----------LYVKNPVMKEy 287
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 52783414  245 ------------VISDQEAVSALEKFVDDEKILVEPACGAALAA 276
Cdd:PRK05638 288 vseaikesggtaVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPA 331
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
10-290 4.10e-17

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 79.87  E-value: 4.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  10 KTPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGC----RHFVCSSAGNAGMATAYAARRLGIPATI 85
Cdd:cd01561   2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFII 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  86 VVPNTTPALTIERLKNEGATVEVVGEMLDE----AIQVAKALEKNNPGWVYISPFDDPLIWEGH-TSLVKELKETLSAKP 160
Cdd:cd01561  82 VMPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAETPNAFWLNQFENPANPEAHyETTAPEIWEQLDGKV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 161 GAIVLSVGGGGLLCGVVQGLREVgWEDVPIIAMETFGAHSF-----HAAIKEGklvtlpkitsvakaLGVNTVGAqtlkl 235
Cdd:cd01561 162 DAFVAGVGTGGTITGVARYLKEK-NPNVRIVGVDPVGSVLFsggppGPHKIEG--------------IGAGFIPE----- 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414 236 FYEHPIFSEV--ISDQEAVSALEKFVDDEKILVEPACGAALAAVY---------SRVVCRLQDEGR 290
Cdd:cd01561 222 NLDRSLIDEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALklakrlgpgKTIVTILPDSGE 287
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism];
11-303 3.89e-15

Cysteine synthase [Amino acid transport and metabolism];


Pssm-ID: 223110 [Multi-domain]  Cd Length: 300  Bit Score: 74.49  E-value: 3.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIRgIGH------LCKMKAKQGcRHFVCSSAGNAGMATAYAARRLGIPAT 84
Cdd:COG0031  12 TPLVRLNRLSPGTGVEIYAKLESFNPGGSVKDR-IALymiedaEKRGLLKPG-GTIVEATSGNTGIALAMVAAAKGYRLI 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  85 IVVPNTTPALTIERLKNEGATVEVV---GEMLDEAIQVAKALEKNNPGWVYISP-FDDPLIWEGH-TSLVKELKETLSAK 159
Cdd:COG0031  90 IVMPETMSQERRKLLRALGAEVILTpgaPGNMKGAIERAKELAAEIPGYAVWLNqFENPANPEAHyETTGPEIWQQTDGK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 160 PGAIVLSVGGGGLLCGVVQGLREVgWEDVPIIAMETFGAHSFHAAIKEGKLvtlpkitsvaKALGVNTVgaqTLKLFYEH 239
Cdd:COG0031 170 VDAFVAGVGTGGTITGVARYLKER-NPNVRIVAVDPEGSVLLSGGEGPHKI----------EGIGAGFV---PENLDLDL 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52783414 240 PIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVysRVVCRLQDEGrlqtplASLVVIVC 303
Cdd:COG0031 236 IDEVIRVSDEEAIATARRLAREEGLLVGISSGAALAAA--LKLAKELPAG------KTIVTILP 291
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism];
11-276 6.34e-14

Threonine synthase [Amino acid transport and metabolism];


Pssm-ID: 223572 [Multi-domain]  Cd Length: 411  Bit Score: 71.97  E-value: 6.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  11 TPLRDSMALS---KLAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:COG0498  77 TPLYKAPALAaplGVLNDNLYVKELGHNPTGSFKDRGMTVLVSLAKELGAKTILCASSGNTGASAAAYAARAGLKVFVLY 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  88 PNT-TPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFDDPLIWEGHTSLVKELKETLSAK------- 159
Cdd:COG0498 157 PKGkVSPGKLAQMLTLGAHVIAVDGNFDDAQELVKEAANRE-GLLSAVNSINPYRLEGQKTYAFEIAEQLGWKapdhvvv 235
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414 160 P----GAIVLSVGGGGLlcgvvqgLREVGW-EDVP-IIAMETFGAHSFHAAIKEGKLVtlPKITSVAKALGVNTVGAQTL 233
Cdd:COG0498 236 PvgngGNLLAIYKGFKE-------GLPIGKiDKAPnMNGVQAEGFSPGVYAWKEGRET--PETIAPAMDIGNPSNWERAL 306
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 52783414 234 KLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAA 276
Cdd:COG0498 307 FALRESGGLAVAVSDEEILEAIKLLAEREGILIEPHSAVAVAA 349
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
4-294 1.01e-12

threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 67.79  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414     4 QESLHVK-TPLRDSMALSK-LAGTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGI 81
Cdd:TIGR00260  15 LVDLGEGvTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    82 PATIVVPNTtpalTIERLK-----NEGATVEVVGEMLDEAIQVAKALEKNNPGWVYISPFDDPLIWEGHTSLVKELKETL 156
Cdd:TIGR00260  95 KVVVLYPAG----KISLGKlaqalGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSANSIPYRLEGQKTYAFEAVEQL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   157 SAK-PGAIVLSVGGGGLLCGVVQG---LREVGWEDVPI-IAMETFGAHSF-HAAIKEGKLVTLPKITSVAKALGV-NTV- 228
Cdd:TIGR00260 171 GWEaPDKVVVPVPNSGNFGAIWKGfkeKKMLGLDSLPVkRGIQAEGAADIvRAFLEGGQWEPIETPETLSTAMDIgNPAn 250
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52783414   229 GAQTLKLFYEHPIFSEVISDQEAVSALEKFVDDEKILVEPACGAALAAVY-----------SRVVCRLQDEGrLQTP 294
Cdd:TIGR00260 251 WPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLklvekgtadpaERVVCALTGNG-LKDP 326
PRK06110 PRK06110
threonine dehydratase;
19-313 1.87e-10

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 60.78  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   19 LSKLAGTSVFLKMDSSQPSGSFKIRG-IGHLCKMKAKQ-GCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTpalTI 96
Cdd:PRK06110  30 LAERLGCEVWVKHENHTPTGAFKVRGgLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGN---SV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   97 ErlKNE-----GATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFddpliwegHTSLVKELK----ETLSAKP------- 160
Cdd:PRK06110 107 E--KNAamralGAELIEHGEDFQAAREEAARLAAER-GLHMVPSF--------HPDLVRGVAtyalELFRAVPdldvvyv 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  161 ---------GAIVLSvggggllcgvvqglREVGWeDVPIIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALGVNTVGAQ 231
Cdd:PRK06110 176 pigmgsgicGAIAAR--------------DALGL-KTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  232 TLKLFYEHpiFSEVI--SDQEAVSALEKFVDDEKILVEPACGAALAAVysrvvcrLQDEGRLQtplASLVVIVCGGSNIS 309
Cdd:PRK06110 241 ALEVIRAG--ADRIVrvTDDEVAAAMRAYFTDTHNVAEGAGAAALAAA-------LQERERLA---GKRVGLVLSGGNID 308

                 ....
gi 52783414  310 LAQL 313
Cdd:PRK06110 309 RAVF 312
PRK06450 PRK06450
threonine synthase; Validated
24-276 2.88e-10

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 60.52  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   24 GTSVFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNEG 103
Cdd:PRK06450  64 KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYG 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  104 ATVEVVGEMLDEaiqVAKALEknNPGWVYISPFDDPLIWEGHTSLVKELKETLSAK-PGAIVLSVGGGGLLCGVVQGLR- 181
Cdd:PRK06450 144 AEVVRVRGSRED---VAKAAE--NSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWKiPNYVFIPVSAGTLLLGVYSGFKh 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  182 --EVG-WEDVP-IIAMETFGAHSFHAAIKEGKLVTLPKITSVAKALgvntVGAQTLKLFYEHPIFSE-----VISDQEAV 252
Cdd:PRK06450 219 llDSGvISEMPkIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADAL----VSTRPFLLDYMVKALSEygeciVVSDNEIV 294
                        250       260
                 ....*....|....*....|....
gi 52783414  253 SAlEKFVDDEKILVEPACGAALAA 276
Cdd:PRK06450 295 EA-WKELAKKGLLVEYSSATVYAA 317
PRK08329 PRK08329
threonine synthase; Validated
24-310 6.53e-09

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 56.37  E-value: 6.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   24 GTSVFLKMDSSQPSGSFKIRGIG-HLCKMKaKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPNTTPALTIERLKNE 102
Cdd:PRK08329  71 SIKVYFKLDYLQPTGSFKDRGTYvTVAKLK-EEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRL 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  103 GATVEVVG----EMLDEAIQVAKaleknNPGWVYISPFDDPLIWEGHTSLVKELKETLSAkPGAIVLSVGGGGLLCGVVQ 178
Cdd:PRK08329 150 GAELHFVEgdrmEVHEEAVKFSK-----RNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGV-PDYAFVPVGSGTLFLGIWK 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414  179 G---LREVG-WEDVP-IIAMETFGAHSF-HAAIKEGKLVTLPKITSVAKAlgvntvgAQTLKLFYEHPIFSEVISDQEAV 252
Cdd:PRK08329 224 GfkeLHEMGeISKMPkLVAVQAEGYESLcKRSKSENKLADGIAIPEPPRK-------EEMLRALEESNGFCISVGEEETR 296
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 52783414  253 SALEKFVdDEKILVEPACGAALAAVYSrvvcrLQDEGRLQTplASLVVIVCGGSNISL 310
Cdd:PRK08329 297 AALHWLR-RMGFLVEPTSAVALAAYWK-----LLEEGLIEG--GSKVLLPLSGSGLKN 346
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
8-134 1.62e-07

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 52.19  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414    8 HVKTPLRDSMALSKLAGT-SVFLKmDSSQPSG--SFKIRG-----IGHLCKM------------------KAKQGCRHFV 61
Cdd:PRK08206  42 YAPTPLVALPDLAAELGVgSILVK-DESYRFGlnAFKALGgayavARLLAEKlgldiselsfeeltsgevREKLGDITFA 120
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414   62 CSSAGNAGMATAYAARRLGIPATIVVPNTTpalTIERLKN---EGATVEVVGEMLDEAIQVAKALEKNNpGWVYIS 134
Cdd:PRK08206 121 TATDGNHGRGVAWAAQQLGQKAVIYMPKGS---SEERVDAiraLGAECIITDGNYDDSVRLAAQEAQEN-GWVVVQ 192
PRK06381 PRK06381
threonine synthase; Validated
11-163 6.49e-07

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 50.09  E-value: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   11 TPLRDSMALSKLAGTS-VFLKMDSSQPSGSFKIRGIGHLCKMKAKQGCRHFVCSSAGNAGMATAYAARRLGIPATIVVPN 89
Cdd:PRK06381  16 TPLLRARKLEEELGLRkIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPR 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52783414   90 TTPALTIERLKNEGATVEVVGEMLDEAIQVAKALEKNNpGWVYISPFD--DPLIWEGHTSLVKELKETLSAKPGAI 163
Cdd:PRK06381  96 SYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKEN-GIYDANPGSvnSVVDIEAYSAIAYEIYEALGDVPDAV 170
PLN02569 PLN02569
threonine synthase
36-106 2.61e-03

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 39.41  E-value: 2.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52783414   36 PSGSFKIRGIGHLCKM-----KAKQGCRHFVCSSAGNAGMA-TAYAARrLGIPATIVVPNTTPALT--IERLKNeGATV 106
Cdd:PLN02569 161 HTGSFKDLGMTVLVSQvnrlrKMAKPVVGVGCASTGDTSAAlSAYCAA-AGIPSIVFLPADKISIAqlVQPIAN-GALV 237
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
11-120 2.77e-03

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 39.41  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52783414   11 TPLRDSMALSKLAGTSVFLKMDSSQPSGSFKIR---GIGHLCKMKAKQgcRHFVCSSAGNAGMATAYAARRLGIPATIVV 87
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINnalGQALLAKRMGKT--RIIAETGAGQHGVATATACALFGLKCTIFM 349
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 52783414   88 PNTT---PALTIERLKNEGATVEVV---GEMLDEAIQVA 120
Cdd:PRK13803 350 GEEDikrQALNVERMKLLGANVIPVlsgSKTLKDAVNEA 388
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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