NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1383482565|ref|NP_001349671|]
View 

serine racemase isoform 2 [Mus musculus]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 5-297 2.18e-138

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.


The actual alignment was detected with superfamily member PLN02970:

Pssm-ID: 444852 [Multi-domain]  Cd Length: 328  Bit Score: 394.43  E-value: 2.18e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   5 YCISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEekpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  85 GNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 165 TIALEVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGVKSSI 219
Cdd:PLN02970  164 TIALEFLEQvpeldviivpisggglisgialaakAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGLRASL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 220 GLNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSP--EVKNVCIVLSGGNVDLTSL 297
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLGVL 322
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
 5-297 2.18e-138

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 394.43  E-value: 2.18e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   5 YCISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEekpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  85 GNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 165 TIALEVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGVKSSI 219
Cdd:PLN02970  164 TIALEFLEQvpeldviivpisggglisgialaakAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGLRASL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 220 GLNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSP--EVKNVCIVLSGGNVDLTSL 297
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLGVL 322
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-293 1.23e-120

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: 348.32  E-value: 1.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   9 FADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHG 88
Cdd:cd01562     1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSL---SEEERAKGVVAASAGNHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562    78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 169 EVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLN 222
Cdd:cd01562   158 EILEQvpdldavfvpvggggliagiatavkALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVD-TIADGLAvKRPGEL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1383482565 223 TWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQtvsPEVKNVCIVLSGGNVD 293
Cdd:cd01562   237 TFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 7-300 4.78e-106

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: 312.36  E-value: 4.78e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:COG1171     6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASL---SEEERARGVVAASAGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTI 166
Cdd:COG1171    83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 167 ALEVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVK-SSIG 220
Cdd:COG1171   163 ALEILEQlpdldavfvpvggggliagvaaalkALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 221 LNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQtvsPEVKNVCIVLSGGNVDLTSLNWV 300
Cdd:COG1171   242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSGGNIDPDRLAEI 318
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 19-289 3.06e-71

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: 222.57  E-value: 3.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  19 IQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtpEEKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  99 GIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEG-ILVHPNQEPAVIAGQGTIALEVLNQ---- 173
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQlggd 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 174 ----------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GLNTWPIIRD 229
Cdd:pfam00291 158 pdavvvpvggggliagiarglkELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDE 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 230 LVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSPEvKNVCIVLSG 289
Cdd:pfam00291 237 YVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-DRVVVVLTG 295
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 26-300 6.65e-62

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: 201.13  E-value: 6.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 106 VPQTAPNCKKLAIQAYGASIV-YCDPSDESREKVTqRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQ----------- 173
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYAFAT-SLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDipdvdtvivpv 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 174 -----------ALK---PSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLNTWPIIRDLVDDVFTVT 238
Cdd:TIGR01127 157 gggglisgvasAAKqinPNVKVIGVEAEGAPSMYESLREGKIKAVESVR-TIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1383482565 239 EDEIKYATQLVWGRMKLLIEPTAGVALAAVLSqhfQTVSPEVKNVCIVLSGGNVDLTSLNWV 300
Cdd:TIGR01127 236 EEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGKKIAVVLSGGNIDLNLLNKI 294
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
 5-297 2.18e-138

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 394.43  E-value: 2.18e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   5 YCISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEekpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  85 GNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 165 TIALEVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGVKSSI 219
Cdd:PLN02970  164 TIALEFLEQvpeldviivpisggglisgialaakAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGLRASL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 220 GLNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSP--EVKNVCIVLSGGNVDLTSL 297
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLGVL 322
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-293 1.23e-120

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: 348.32  E-value: 1.23e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   9 FADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHG 88
Cdd:cd01562     1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSL---SEEERAKGVVAASAGNHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562    78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 169 EVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLN 222
Cdd:cd01562   158 EILEQvpdldavfvpvggggliagiatavkALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVD-TIADGLAvKRPGEL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1383482565 223 TWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQtvsPEVKNVCIVLSGGNVD 293
Cdd:cd01562   237 TFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 7-300 4.78e-106

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: 312.36  E-value: 4.78e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:COG1171     6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASL---SEEERARGVVAASAGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTI 166
Cdd:COG1171    83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 167 ALEVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVK-SSIG 220
Cdd:COG1171   163 ALEILEQlpdldavfvpvggggliagvaaalkALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 221 LNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQtvsPEVKNVCIVLSGGNVDLTSLNWV 300
Cdd:COG1171   242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSGGNIDPDRLAEI 318
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
7-295 3.44e-95

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 284.60  E-value: 3.44e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK07048    6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQF---SPEQRRAGVVTFSSGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTI 166
Cdd:PRK07048   83 HAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 167 ALEVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADGVKS-SIG 220
Cdd:PRK07048  163 AKELFEEvgpldalfvclggggllsgcalaarALSPGCKVYGVEPEAGNDGQQSFRSGEIV-HIDTPRTIADGAQTqHLG 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1383482565 221 LNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSqhfQTVSPEVKNVCIVLSGGNVDLT 295
Cdd:PRK07048  242 NYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALR---GKVPLKGKRVGVIISGGNVDLA 313
PRK06608 PRK06608
serine/threonine dehydratase;
8-298 1.31e-76

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 237.75  E-value: 1.31e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   8 SFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDtpEEKPKAVVTHSSGNH 87
Cdd:PRK06608    6 NPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQ--GKLPDKIVAYSTGNH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  88 GQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGIlvHPNQEPAVIAGQGTIA 167
Cdd:PRK06608   84 GQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEEQGFYYI--HPSDSDSTIAGAGTLC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 168 LEVLNQ--------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVKS-SIG 220
Cdd:PRK06608  162 YEALQQlgfspdaifascgggglisgtylakeLISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSPNTIADGLKTlSVS 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383482565 221 LNTWPIIRDLvDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSPevKNVCIVLSGGNVDLTSLN 298
Cdd:PRK06608  242 ARTFEYLKKL-DDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKP--QKLLVILSGGNIDPILYN 316
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 19-289 3.06e-71

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: 222.57  E-value: 3.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  19 IQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtpEEKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  99 GIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEG-ILVHPNQEPAVIAGQGTIALEVLNQ---- 173
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQlggd 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 174 ----------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GLNTWPIIRD 229
Cdd:pfam00291 158 pdavvvpvggggliagiarglkELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDE 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 230 LVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSPEvKNVCIVLSG 289
Cdd:pfam00291 237 YVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-DRVVVVLTG 295
PRK06815 PRK06815
threonine/serine dehydratase;
9-297 8.10e-64

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 204.16  E-value: 8.10e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   9 FADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHG 88
Cdd:PRK06815    4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLL---NEAQRQQGVITASSGNHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:PRK06815   81 QGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 169 EVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GL 221
Cdd:PRK06815  161 ELVEQqpdldavfvavgggglisgiatylkTLSPKTEIIGCWPANSPSLYTSLEAGEIVE-VAEQPTLSDGTAGGVepGA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383482565 222 NTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQhfqtvSPEV--KNVCIVLSGGNVDLTSL 297
Cdd:PRK06815  240 ITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKL-----APRYqgKKVAVVLCGKNIVLEKY 312
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 26-300 6.65e-62

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: 201.13  E-value: 6.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 106 VPQTAPNCKKLAIQAYGASIV-YCDPSDESREKVTqRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQ----------- 173
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYAFAT-SLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDipdvdtvivpv 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 174 -----------ALK---PSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLNTWPIIRDLVDDVFTVT 238
Cdd:TIGR01127 157 gggglisgvasAAKqinPNVKVIGVEAEGAPSMYESLREGKIKAVESVR-TIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1383482565 239 EDEIKYATQLVWGRMKLLIEPTAGVALAAVLSqhfQTVSPEVKNVCIVLSGGNVDLTSLNWV 300
Cdd:TIGR01127 236 EEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGKKIAVVLSGGNIDLNLLNKI 294
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
7-295 2.51e-61

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 198.04  E-value: 2.51e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK08638    9 VAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSL---TDAEKRKGVVACSAGN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YCDPSDESREKVTQRImqETEG-ILVHPNQEPAVIAGQG 164
Cdd:PRK08638   86 HAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVlHGDNFNDTIAKVEEIV--EEEGrTFIPPYDDPKVIAGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 165 TIALEVLNQ----------------------ALK---PSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVKSSI 219
Cdd:PRK08638  164 TIGLEILEDlwdvdtvivpiggggliagiavALKsinPTIHIIGVQSENVHGMAASFYAGEITTHRTTG-TLADGCDVSR 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383482565 220 -GLNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSPEVKNVCIVlSGGNVDLT 295
Cdd:PRK08638  243 pGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAII-SGGNVDLS 318
PRK07334 PRK07334
threonine dehydratase; Provisional
 7-293 6.76e-56

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 186.25  E-value: 6.76e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK07334    5 VTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLL---TEEERARGVIAMSAGN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YCDPSDESREkvTQRIMQETEG-ILVHPNQEPAVIAGQG 164
Cdd:PRK07334   82 HAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVlHGETLDEARA--HARELAEEEGlTFVHPYDDPAVIAGQG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 165 TIALEVLN-------------------------QALKPSVKVYAAEPSNADDCYQsKLKGELTPNLHppETIADG--VKs 217
Cdd:PRK07334  160 TVALEMLEdapdldtlvvpigggglisgmataaKALKPDIEIIGVQTELYPSMYA-AIKGVALPCGG--STIAEGiaVK- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 218 SIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVwgrmkLLIEPT----AGVA-LAAVLS--QHFQTvspevKNVCIVLSGG 290
Cdd:PRK07334  236 QPGQLTLEIVRRLVDDILLVSEADIEQAVSLL-----LEIEKTvvegAGAAgLAALLAypERFRG-----RKVGLVLSGG 305


                  ...
gi 1383482565 291 NVD 293
Cdd:PRK07334  306 NID 308
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 26-290 1.08e-52

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: 173.08  E-value: 1.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDtpEEKPKAVVTH-SSGNHGQALTYAAKLEGIPAYI 104
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEE--GKLPKGVIIEsTGGNTGIALAAAAARLGLKCTI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 105 VVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEG-ILVHPNQEPAVIAGQGTIALEVLNQ---------- 173
Cdd:cd00640    79 VMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGTIGLEILEQlggqkpdavv 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 174 -----------------ALKPSVKVYAAEPsnaddcyqsklkgeltpnlhppetiadgvkssiglntwpiirdlvdDVFT 236
Cdd:cd00640   159 vpvggggniagiaralkELLPNVKVIGVEP----------------------------------------------EVVT 192

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1383482565 237 VTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTvsPEVKNVCIVLSGG 290
Cdd:cd00640   193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL--GKGKTVVVILTGG 244
eutB PRK07476
threonine dehydratase; Provisional
 7-294 6.20e-52

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 173.61  E-value: 6.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK07476    1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSL---SAQERARGVVTASTGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPS-DESREKVtQRIMQETEGILVHPNQEPAVIAGQGT 165
Cdd:PRK07476   78 HGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSqDDAQAEV-ERLVREEGLTMVPPFDDPRIIAGQGT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 166 IALEVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGeltpnlHP-----PETIADGV 215
Cdd:PRK07476  157 IGLEILEAlpdvatvlvplsggglasgvaaavkAIRPAIRVIGVSMERGAAMHASLAAG------RPvqveeVPTLADSL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 216 KSSIGLN---TWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSqhfQTVSPEVKNVCIVLSGGNV 292
Cdd:PRK07476  231 GGGIGLDnryTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLA---GKIAARDGPIVVVVSGANI 307


                  ..
gi 1383482565 293 DL 294
Cdd:PRK07476  308 DM 309
PRK08246 PRK08246
serine/threonine dehydratase;
7-298 7.90e-51

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 170.52  E-value: 7.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVLTSSIlNQIAGRNLFFKCELFQKTGSFKIRGALNAIRglipdTPEEKPKAVVTHSSGN 86
Cdd:PRK08246    5 ITRSDVRAAAQRIAPHIRRTPVLEADG-AGFGPAPVWLKLEHLQHTGSFKARGAFNRLL-----AAPVPAAGVVAASGGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTI 166
Cdd:PRK08246   79 AGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 167 ALEVLNQALKPS----------------------VKVYAAEPSNADDCYQSKLKGEltpnlhPPETIADGVKSS------ 218
Cdd:PRK08246  159 GLEIEEQAPGVDtvlvavggggliagiaawfegrARVVAVEPEGAPTLHAALAAGE------PVDVPVSGIAADslgarr 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 219 IGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTVSPEvkNVCIVLSGGNVDLTSLN 298
Cdd:PRK08246  233 VGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--RVAVVLCGANTDPATLA 310
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
39-305 1.06e-40

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 147.98  E-value: 1.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  39 GRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAI 118
Cdd:PRK09224   34 GNQVLLKREDLQPVFSFKLRGAYNKMAQL---TEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 119 QAYGASIV-YCDPSDESREKvTQRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQ------------------------ 173
Cdd:PRK09224  111 RAFGGEVVlHGDSFDEAYAH-AIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQhphpldavfvpvggggliagvaay 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 174 --ALKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADG--VKsSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLV 249
Cdd:PRK09224  190 ikQLRPEIKVIGVEPEDSACLKAALEAGERV-DLPQVGLFADGvaVK-RIGEETFRLCQEYVDDVITVDTDEICAAIKDV 267

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1383482565 250 WGRMKLLIEPTAGVALAAvLSQHFQTVSPEVKNVCIVLSGGNVDLTSLNWVgqAER 305
Cdd:PRK09224  268 FEDTRSIAEPAGALALAG-LKKYVAQHGIEGETLVAILSGANMNFDRLRYV--AER 320
PRK12483 PRK12483
threonine dehydratase; Reviewed
 26-305 2.52e-37

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 139.16  E-value: 2.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:PRK12483   38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARL---PAEQLARGVITASAGNHAQGVALAAARLGVKAVIV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 106 VPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQ------------ 173
Cdd:PRK12483  115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQhpgpldaifvpv 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 174 --------------ALKPSVKVYAAEPSNAdDCYQSKLKGELTPNLHPPETIADGVK-SSIGLNTWPIIRDLVDDVFTVT 238
Cdd:PRK12483  195 ggggliagiaayvkYVRPEIKVIGVEPDDS-NCLQAALAAGERVVLGQVGLFADGVAvAQIGEHTFELCRHYVDEVVTVS 273

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383482565 239 EDEIKYATQLVWGRMKLLIEPTAGVALAAvLSQHFQTVSPEVKNVCIVLSGGNVDLTSLNWVgqAER 305
Cdd:PRK12483  274 TDELCAAIKDIYDDTRSITEPAGALAVAG-IKKYAEREGIEGQTLVAIDSGANVNFDRLRHV--AER 337
PRK08639 PRK08639
threonine dehydratase; Validated
 7-293 4.31e-37

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 136.86  E-value: 4.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK08639    7 VSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQL---SDEELAAGVVCASAGN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGAS----IVYCDPSDESrEKVTQRIMQETEGILVHPNQEPAVIAG 162
Cdd:PRK08639   84 HAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEfveiVLVGDTFDDS-AAAAQEYAEETGATFIPPFDDPDVIAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 163 QGTIALEVLNQA-------------------------LK---PSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADG 214
Cdd:PRK08639  163 QGTVAVEILEQLekegspdyvfvpvgggglisgvttyLKersPKTKIIGVEPAGAASMKAALEAGKPVT-LEKIDKFVDG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 215 --VKsSIGLNTWPIIRDLVDDVFTVTEDEIkYATQLvwgrmKLL------IEPtAGVALAAVLSQHFQTVspEVKNVCIV 286
Cdd:PRK08639  242 aaVA-RVGDLTFEILKDVVDDVVLVPEGAV-CTTIL-----ELYnkegivAEP-AGALSIAALELYKDEI--KGKTVVCV 311


                  ....*..
gi 1383482565 287 LSGGNVD 293
Cdd:PRK08639  312 ISGGNND 318
PRK06110 PRK06110
threonine dehydratase;
8-306 8.57e-29

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 112.78  E-value: 8.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   8 SFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEekPKAVVTHSSGNH 87
Cdd:PRK06110    4 TLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPR--VRGVISATRGNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  88 GQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YCDPSDESREKVTQRimQETEGILVHPNQEPAVIAGQGTI 166
Cdd:PRK06110   82 GQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIeHGEDFQAAREEAARL--AAERGLHMVPSFHPDLVRGVATY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 167 ALEVLNQ-------------------------ALKPSVKVYAAEPSNADDCYQSKLKGEL--TPNlhpPETIADGVKSSI 219
Cdd:PRK06110  160 ALELFRAvpdldvvyvpigmgsgicgaiaardALGLKTRIVGVVSAHAPAYALSFEAGRVvtTPV---ATTLADGMACRT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 220 GL-NTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQTvspEVKNVCIVLSGGNVDLTSLN 298
Cdd:PRK06110  237 PDpEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERERL---AGKRVGLVLSGGNIDRAVFA 313


                  ....*....
gi 1383482565 299 -WVGQAERP 306
Cdd:PRK06110  314 rVLAGAAAE 322
PRK08813 PRK08813
threonine dehydratase; Provisional
 7-308 4.84e-28

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 111.26  E-value: 4.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565   7 ISFADVEKAHINIQDSIHLTPVltssilnQIAGR-NLFFKCELFQKTGSFKIRGALNA-IRGLipDTPEEKPkaVVTHSS 84
Cdd:PRK08813   21 VSVADVLAAQARLRRYLSPTPL-------HYAERfGVWLKLENLQRTGSYKVRGALNAlLAGL--ERGDERP--VICASA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  85 GNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQG 164
Cdd:PRK08813   90 GNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 165 TIALEVLNQ--------------------ALKPS-VKVYAAEPSNADDCYQSkLKGELTpNLHPPETIADGVKSSI-GLN 222
Cdd:PRK08813  170 TVGIELAAHapdvvivpigggglasgvalALKSQgVRVVGAQVEGVDSMARA-IRGDLR-EIAPVATLADGVKVKIpGFL 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 223 TWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAvlsqhFQTVSPEVKnvCIVLSGGNVDLTSLNWVGQ 302
Cdd:PRK08813  248 TRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAA-----GRRVSGKRK--CAVVSGGNIDATVLATLLS 320


                  ....*.
gi 1383482565 303 AERPAP 308
Cdd:PRK08813  321 EVRPRP 326
PLN02550 PLN02550
threonine dehydratase
 24-300 1.28e-27

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 112.71  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  24 HLTPVLTSSI--------------LNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQ 89
Cdd:PLN02550   94 YLTNILSAKVydvaiesplqlakkLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKL---PKEQLDKGVICSSAGNHAQ 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  90 ALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYC-DPSDESREKVTQRIMQETEgILVHPNQEPAVIAGQGTIAL 168
Cdd:PLN02550  171 GVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVgDSYDEAQAYAKQRALEEGR-TFIPPFDHPDVIAGQGTVGM 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 169 EVLNQA--------------------------LKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADGVK-SSIGL 221
Cdd:PLN02550  250 EIVRQHqgplhaifvpvggggliagiaayvkrVRPEVKIIGVEPSDANAMALSLHHGERV-MLDQVGGFADGVAvKEVGE 328

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1383482565 222 NTWPIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVlSQHFQTVSPEVKNVCIVLSGGNVDLTSLNWV 300
Cdd:PLN02550  329 ETFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGA-EAYCKYYGLKDENVVAITSGANMNFDRLRIV 406
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 26-269 2.14e-25

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: 102.59  E-value: 2.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLI-PDTpeekpkAVVTHSSGNHGQALTYAAKLEG 99
Cdd:cd01561     3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIedaekRGLLkPGT------TIIEPTSGNTGIGLAMVAAAKG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 100 IPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSD----ESREKVTQRIMQETEGIlVHPNQ--EPA--------------- 158
Cdd:cd01561    77 YRFIIVMPETMSEEKRKLLRALGAEVILTPEAEadgmKGAIAKARELAAETPNA-FWLNQfeNPAnpeahyettapeiwe 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 159 --------VIAGQGT------IAlEVLnQALKPSVKVYAAEPSNADdcyqsklkgeLTPNLHPPETIADGvkssIGLNTW 224
Cdd:cd01561   156 qldgkvdaFVAGVGTggtitgVA-RYL-KEKNPNVRIVGVDPVGSV----------LFSGGPPGPHKIEG----IGAGFI 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1383482565 225 PII--RDLVDDVFTVTEDE-IKYATQLVwGRMKLLIEPTAGVALAAVL 269
Cdd:cd01561   220 PENldRSLIDEVVRVSDEEaFAMARRLA-REEGLLVGGSSGAAVAAAL 266
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 26-291 1.13e-23

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: 98.53  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIpDTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:cd06448     2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSA-KQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 106 VPQTAPNCKKLAIQAYGASIV-----YCDPSDESREKVTQRimqETEGILVHPNQEPAVIAGQGTIALEVLnQALKP--- 177
Cdd:cd06448    81 VPESTKPRVVEKLRDEGATVVvhgkvWWEADNYLREELAEN---DPGPVYVHPFDDPLIWEGHSSMVDEIA-QQLQSqek 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 178 ---------------------------SVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSS-IGLNTW----- 224
Cdd:cd06448   157 vdaivcsvggggllngivqglerngwgDIPVVAVETEGAHSLNASLKAGKLVT-LPKITSVATSLGAKtVSSQALeyaqe 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1383482565 225 -PIIRDLVDD------VFTVTEDEikyatqlvwgrmKLLIEPTAGVALAAVLSQHFQTVSPEVK-----NVCIVLSGGN 291
Cdd:cd06448   236 hNIKSEVVSDrdavqaCLRFADDE------------RILVEPACGAALAVVYSGKILDLQLEVLltpldNVVVVVCGGS 302
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 26-269 1.73e-23

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: 99.12  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAGRNLFFKcELFQ-KTGSFKIRG---ALNAIRglipdtpEEKPKAVVTHSSGNHGQAL-TYAAKlEGI 100
Cdd:COG0498    67 TPLVKAPRLADELGKNLYVK-EEGHnPTGSFKDRAmqvAVSLAL-------ERGAKTIVCASSGNGSAALaAYAAR-AGI 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 101 PAYIVVPQT-APNCKKLAIQAYGASIVYCDPS-DEsREKVTQRIMQETEGILVHpNQEPAVIAGQGTIALEVLNQALKP- 177
Cdd:COG0498   138 EVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNfDD-AQRLVKELAADEGLYAVN-SINPARLEGQKTYAFEIAEQLGRVp 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 178 ---SV----------------------------KVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVksSIG--LNTW 224
Cdd:COG0498   216 dwvVVptgnggnilagykafkelkelglidrlpRLIAVQATGCNPILTAFETGRDEYEPERPETIAPSM--DIGnpSNGE 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1383482565 225 PIIRDLVD---DVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVL 269
Cdd:COG0498   294 RALFALREsggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLR 341
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 26-286 5.22e-21

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: 91.12  E-value: 5.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAG-RNLFFKCELFQKTGSFKIRGALNAIRGLIpdtpEEKPKAVVTHSSGNHGQAL-TYAAKlEGIPAY 103
Cdd:cd01563    23 TPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVSKAK----ELGVKAVACASTGNTSASLaAYAAR-AGIKCV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 104 IVVPQTAPNCKKLAIQAYGASIVycdPSDESRE---KVTQRIMQETEGILVHpNQEPAVIAGQGTIALEVLNQ------- 173
Cdd:cd01563    98 VFLPAGKALGKLAQALAYGATVL---AVEGNFDdalRLVRELAEENWIYLSN-SLNPYRLEGQKTIAFEIAEQlgwevpd 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 174 --------------------ALKPS------VKVYAAEPSNADDCYQSKLKG--ELTPNLHpPETIADGVKssIGlN--T 223
Cdd:cd01563   174 yvvvpvgnggnitaiwkgfkELKELglidrlPRMVGVQAEGAAPIVRAFKEGkdDIEPVEN-PETIATAIR--IG-NpaS 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383482565 224 WPIIRDLVD----DVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQ-TVSPEVKNVCIV 286
Cdd:cd01563   250 GPKALRAVResggTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgIIDKGERVVVVL 317
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 18-269 1.83e-20

Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 89.34  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  18 NIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLI-PDTPeekpkaVVTHSSGNHGQAL 91
Cdd:COG0031     6 SILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIedaekRGLLkPGGT------IVEATSGNTGIGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  92 TYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSD--ESREKVTQRIMQETEGIlVHPNQ-------------- 155
Cdd:COG0031    80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEgmKGAIDKAEELAAETPGA-FWPNQfenpanpeahyett 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 156 ----------EP-AVIAGQGT------IAlevlnQALK---PSVKVYAAEPSNAddcyqSKLKGElTPNLHPPETIADGV 215
Cdd:COG0031   159 gpeiweqtdgKVdAFVAGVGTggtitgVG-----RYLKernPDIKIVAVEPEGS-----PLLSGG-EPGPHKIEGIGAGF 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1383482565 216 KSSIglntwpIIRDLVDDVFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVL 269
Cdd:COG0031   228 VPKI------LDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAAL 275
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 33-293 6.62e-15

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: 73.96  E-value: 6.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  33 ILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIpdtpEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPN 112
Cdd:TIGR00260  31 LAANVGIKNLYVKELGHNPTLSFKDRGMAVALTKAL----ELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKIS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 113 CKKLAIQ-AYGASIVYCDPS-DESREKVTQrIMQETEGILVHP-NQEPAVIAGQGTIALEV---LNQALKPSVKV----- 181
Cdd:TIGR00260 107 LGKLAQAlGYNAEVVAIDGNfDDAQRLVKQ-LFEDKPALGLNSaNSIPYRLEGQKTYAFEAveqLGWEAPDKVVVpvpns 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 182 ------------------------YAAEPSNADDCYQSKLK-GELTPNLHpPETIA---DGVKSSIGLNTWPIIRDLVDD 233
Cdd:TIGR00260 186 gnfgaiwkgfkekkmlgldslpvkRGIQAEGAADIVRAFLEgGQWEPIET-PETLStamDIGNPANWPRALEAFRRSNGY 264

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1383482565 234 VFTVTEDEIKYATQLVWGRMKLLIEPTAGVALAAVLSQHFQ-TVSPEVKNVCIVLSGGNVD 293
Cdd:TIGR00260 265 AEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKgTADPAERVVCALTGNGLKD 325
PRK08329 PRK08329
threonine synthase; Validated
 24-294 1.08e-13

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 70.63  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  24 HLTPVLTSSILNqiaGRNLFFKCELFQKTGSFKIRGALNAIRGLipdtPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAY 103
Cdd:PRK08329   59 HLTPPITPTVKR---SIKVYFKLDYLQPTGSFKDRGTYVTVAKL----KEEGINEVVIDSSGNAALSLALYSLSEGIKVH 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 104 IVVPQTAPNCKKLAIQAYGASIVYCdpsDESREKVTQRIMQ--ETEGIL-VHPNQEPAVIAGQGTIALEVLNQALKPSvk 180
Cdd:PRK08329  132 VFVSYNASKEKISLLSRLGAELHFV---EGDRMEVHEEAVKfsKRNNIPyVSHWLNPYFLEGTKTIAYEIYEQIGVPD-- 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 181 vYAAEPSNADDCYQSKLKG--EL--------TPNL---------------HPPETIADGvkssIGLNTWP-------IIR 228
Cdd:PRK08329  207 -YAFVPVGSGTLFLGIWKGfkELhemgeiskMPKLvavqaegyeslckrsKSENKLADG----IAIPEPPrkeemlrALE 281

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383482565 229 DLVDDVFTVTEDEIKYAtqLVW-GRMKLLIEPTAGVALAAVLSQHFQTVSPEVKNVCIVLSGGNVDL 294
Cdd:PRK08329  282 ESNGFCISVGEEETRAA--LHWlRRMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLKN 346
PRK05638 PRK05638
threonine synthase; Validated
 26-289 4.10e-13

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 69.46  E-value: 4.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIaGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtpeEKPKAVVTHSSGNHGQALT-YAAKlEGIPAYI 104
Cdd:PRK05638   67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLP----YAANGFIVASDGNAAASVAaYSAR-AGKEAFV 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 105 VVPQTAPNCKKLAIQAYGAS-IVYCDPSDESREKVTQRimQETEGIL-VHPNQEPAVIAGQGTIALEVLNQALKPSVKVY 182
Cdd:PRK05638  141 VVPRKVDKGKLIQMIAFGAKiIRYGESVDEAIEYAEEL--ARLNGLYnVTPEYNIIGLEGQKTIAFELWEEINPTHVIVP 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 183 AAEPSNADDCYQS--------------KLKGELTPNLHPPETIADGVKS------SIGLNTW-PIIRDLVDDVF------ 235
Cdd:PRK05638  219 TGSGSYLYSIYKGfkelleigvieeipKLIAVQTERCNPIASEILGNKTkcnetkALGLYVKnPVMKEYVSEAIkesggt 298

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1383482565 236 --TVTEDEIKYATQLVwgrMK--LLIEPTAGVALAAVLSQHFQTVSPEVKNVCIVLSG 289
Cdd:PRK05638  299 avVVNEEEIMAGEKLL---AKegIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTG 353
PRK06450 PRK06450
threonine synthase; Validated
 37-289 5.90e-12

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 65.53  E-value: 5.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  37 IAGRNLFFKCELFQKTGSFKIRGAlnaiRGLIPDTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKL 116
Cdd:PRK06450   62 IKKGNIWFKLDFLNPTGSYKDRGS----VTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 117 AIQAYGASIVYCdpsDESREKVtQRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQ-ALKPSVKVY------------- 182
Cdd:PRK06450  138 QIESYGAEVVRV---RGSREDV-AKAAENSGYYYASHVLQPQFRDGIRTLAYEIAKDlDWKIPNYVFipvsagtlllgvy 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 183 -------------------AAEPSNADDCYqSKLKGEltpNLHPPE---TIADGVKSsiglnTWPIIRDLVDDVF----- 235
Cdd:PRK06450  214 sgfkhlldsgvisempkivAVQTEQVSPLC-AKFKGI---SYTPPDkvtSIADALVS-----TRPFLLDYMVKALseyge 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1383482565 236 --TVTEDEIKYATQLVwGRMKLLIEPTAGVALAAvlsqhFQTVSPEvkNVCIVLSG 289
Cdd:PRK06450  285 ciVVSDNEIVEAWKEL-AKKGLLVEYSSATVYAA-----YKKYSVN--DSVLVLTG 332
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 53-262 1.56e-10

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 61.43  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  53 GSFKIRGALNAIRGLIPD---------------TPEEKPKA----VVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNC 113
Cdd:PRK08206   74 NAFKALGGAYAVARLLAEklgldiselsfeeltSGEVREKLgditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 114 KKLAIQAYGASIVYCDPS-DES-REkvTQRIMQETEGILVhpnQEPA----------VIAGQGTIALEVLNQ----ALKP 177
Cdd:PRK08206  154 RVDAIRALGAECIITDGNyDDSvRL--AAQEAQENGWVVV---QDTAwegyeeiptwIMQGYGTMADEAVEQlkemGVPP 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565 178 S-------------------VKVYAA--------EPSNADDCYQSKLKGELTPNLHPPETI----ADGVKSSIGlntWPI 226
Cdd:PRK08206  229 ThvflqagvgslagavlgyfAEVYGEqrphfvvvEPDQADCLYQSAVDGKPVAVTGDMDTImaglACGEPNPLA---WEI 305

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1383482565 227 IRDLVDDVFTVTEDEIKYAtqlvwgrMKLLIEPTAG 262
Cdd:PRK08206  306 LRNCADAFISCPDEVAALG-------MRILANPLGG 334
PRK08197 PRK08197
threonine synthase; Validated
 25-173 1.98e-09

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 58.09  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  25 LTPVLTSSIL-NQIAGRNLFFKCELFQKTGSFKIRGALNAI-RGlipdtPEEKPKAVVTHSSGNHGQAL-TYAAKLeGIP 101
Cdd:PRK08197   79 MTPLLPLPRLgKALGIGRLWVKDEGLNPTGSFKARGLAVGVsRA-----KELGVKHLAMPTNGNAGAAWaAYAARA-GIR 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1383482565 102 AYIVVPQTAPNCKKLAIQAYGASIVYCDP--SDESReKVTQRImqETEGIL-VHPNQEPAVIAGQGTIALEVLNQ 173
Cdd:PRK08197  153 ATIFMPADAPEITRLECALAGAELYLVDGliSDAGK-IVAEAV--AEYGWFdVSTLKEPYRIEGKKTMGLELAEQ 224
PRK06381 PRK06381
threonine synthase; Validated
 26-133 2.54e-09

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 57.41  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAG-RNLFFKCELFQKTGSFKIRGALNAIRGLIpdtpEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYI 104
Cdd:PRK06381   16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRRAM----RLGYSGITVGTCGNYGASIAYFARLYGLKAVI 91

                          90       100
                  ....*....|....*....|....*....
gi 1383482565 105 VVPQTAPNCKKLAIQAYGASIVYCDPSDE 133
Cdd:PRK06381   92 FIPRSYSNSRVKEMEKYGAEIIYVDGKYE 120
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 26-131 2.59e-04

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 42.25  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLIpdTPEEKpkAVVTHSSGNHGQALTYAAKLEGI 100
Cdd:PLN02556   60 TPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIedaekKNLI--TPGKT--TLIEPTSGNMGISLAFMAAMKGY 135

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1383482565 101 PAYIVVPQTAPNCKKLAIQAYGASIVYCDPS 131
Cdd:PLN02556  136 KMILTMPSYTSLERRVTMRAFGAELVLTDPT 166
cysM PRK11761
cysteine synthase CysM;
19-150 2.68e-04

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 41.78  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  19 IQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLIpdtpeeKPKAV-VTHSSGNHGQALT 92
Cdd:PRK11761    6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIvqaekRGEI------KPGDTlIEATSGNTGIALA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1383482565  93 YAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCdPSDESRE---KVTQRIMQETEGIL 150
Cdd:PRK11761   80 MIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILV-PKEQGMEgarDLALQMQAEGEGKV 139
PLN02356 PLN02356
phosphateglycerate kinase
 21-130 7.94e-04

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 40.74  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  21 DSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIpDTPEEKPKAVVTH-SSGNHGQALTYAAKLEG 99
Cdd:PLN02356   49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEAL-ESGQLFPGGVVTEgSAGSTAISLATVAPAYG 127

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1383482565 100 IPAYIVVPQTAPNCKKLAIQAYGASIVYCDP 130
Cdd:PLN02356  128 CKCHVVIPDDVAIEKSQILEALGATVERVRP 158
PLN02569 PLN02569
threonine synthase
 36-173 3.19e-03

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 39.03  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383482565  36 QIAGRN-LFFKCELFQKTGSFKIRG------ALNAIRGLipdtpeEKP-KAVVTHSSGNHGQALTYAAKLEGIPAYIVVP 107
Cdd:PLN02569  145 EFLGMNdLWVKHCGISHTGSFKDLGmtvlvsQVNRLRKM------AKPvVGVGCASTGDTSAALSAYCAAAGIPSIVFLP 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383482565 108 QTAPNCKKLaIQ--AYGASIVYCDPSDESREKVTQRIMQETEgILVHPNQEPAVIAGQGTIALEVLNQ 173
Cdd:PLN02569  219 ADKISIAQL-VQpiANGALVLSIDTDFDGCMRLIREVTAELP-IYLANSLNSLRLEGQKTAAIEILQQ 284
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH