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Conserved domains on  [gi|1720366294|ref|XP_030101905|]
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serine racemase isoform X1 [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

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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) ...
 5-267 5.95e-121

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: 349.36  E-value: 5.95e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   5 YCISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEekpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  85 GNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 165 TIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGVKSSI 244
Cdd:PLN02970  164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGLRASL 242

                         250       260
                  ....*....|....*....|...
gi 1720366294 245 GLNTWPIIRDLVDDVFTVTEDEI 267
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEI 265
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
 5-267 5.95e-121

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 349.36  E-value: 5.95e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   5 YCISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEekpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  85 GNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 165 TIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGVKSSI 244
Cdd:PLN02970  164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGLRASL 242

                         250       260
                  ....*....|....*....|...
gi 1720366294 245 GLNTWPIIRDLVDDVFTVTEDEI 267
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEI 265
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-269 2.28e-105

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: 309.03  E-value: 2.28e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   9 FADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHG 88
Cdd:cd01562     1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSL---SEEERAKGVVAASAGNHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562    78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 169 EVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLN 247
Cdd:cd01562   158 EILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVD-TIADGLAvKRPGEL 236

                         250       260
                  ....*....|....*....|..
gi 1720366294 248 TWPIIRDLVDDVFTVTEDEIKV 269
Cdd:cd01562   237 TFEIIRKLVDDVVTVSEDEIAA 258
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 7-267 3.69e-93

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: 278.84  E-value: 3.69e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:COG1171     6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASL---SEEERARGVVAASAGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTI 166
Cdd:COG1171    83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 167 ALEVLNQVPLVDALvvpvggggmvagIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVK-SSIG 245
Cdd:COG1171   163 ALEILEQLPDLDAVfvpvggggliagVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241

                         250       260
                  ....*....|....*....|..
gi 1720366294 246 LNTWPIIRDLVDDVFTVTEDEI 267
Cdd:COG1171   242 ELTFEILRDLVDDIVTVSEDEI 263
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 19-268 1.83e-62

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: 199.07  E-value: 1.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  19 IQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtpEEKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  99 GIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEG-ILVHPNQEPAVIAGQGTIALEVLNQV-PL 176
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLgGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 177 VDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GLNTWPIIRD 254
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDE 236

                         250
                  ....*....|....
gi 1720366294 255 LVDDVFTVTEDEIK 268
Cdd:pfam00291 237 YVGEVVTVSDEEAL 250
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 26-267 6.15e-53

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: 177.24  E-value: 6.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 106 VPQTAPNCKKLAIQAYGASIV-YCDPSDESREKVTqRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPV 184
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYAFAT-SLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 185 GGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLNTWPIIRDLVDDVFTVT 263
Cdd:TIGR01127 157 GGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVR-TIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235


                  ....
gi 1720366294 264 EDEI 267
Cdd:TIGR01127 236 EEEI 239
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
 5-267 5.95e-121

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 349.36  E-value: 5.95e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   5 YCISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEekpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  85 GNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 165 TIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGVKSSI 244
Cdd:PLN02970  164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGLRASL 242

                         250       260
                  ....*....|....*....|...
gi 1720366294 245 GLNTWPIIRDLVDDVFTVTEDEI 267
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEI 265
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-269 2.28e-105

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: 309.03  E-value: 2.28e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   9 FADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHG 88
Cdd:cd01562     1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSL---SEEERAKGVVAASAGNHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562    78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 169 EVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLN 247
Cdd:cd01562   158 EILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVD-TIADGLAvKRPGEL 236

                         250       260
                  ....*....|....*....|..
gi 1720366294 248 TWPIIRDLVDDVFTVTEDEIKV 269
Cdd:cd01562   237 TFEIIRKLVDDVVTVSEDEIAA 258
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 7-267 3.69e-93

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: 278.84  E-value: 3.69e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:COG1171     6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASL---SEEERARGVVAASAGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTI 166
Cdd:COG1171    83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 167 ALEVLNQVPLVDALvvpvggggmvagIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVK-SSIG 245
Cdd:COG1171   163 ALEILEQLPDLDAVfvpvggggliagVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241

                         250       260
                  ....*....|....*....|..
gi 1720366294 246 LNTWPIIRDLVDDVFTVTEDEI 267
Cdd:COG1171   242 ELTFEILRDLVDDIVTVSEDEI 263
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
7-267 4.29e-83

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 253.02  E-value: 4.29e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK07048    6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQF---SPEQRRAGVVTFSSGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTI 166
Cdd:PRK07048   83 HAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 167 ALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADGVKS-SIG 245
Cdd:PRK07048  163 AKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIV-HIDTPRTIADGAQTqHLG 241

                         250       260
                  ....*....|....*....|..
gi 1720366294 246 LNTWPIIRDLVDDVFTVTEDEI 267
Cdd:PRK07048  242 NYTFPIIRRLVDDIVTVSDAEL 263
PRK06608 PRK06608
serine/threonine dehydratase;
8-267 2.09e-66

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 210.78  E-value: 2.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   8 SFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDtpEEKPKAVVTHSSGNH 87
Cdd:PRK06608    6 NPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQ--GKLPDKIVAYSTGNH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  88 GQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGIlvHPNQEPAVIAGQGTIA 167
Cdd:PRK06608   84 GQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEEQGFYYI--HPSDSDSTIAGAGTLC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 168 LEVLNQVPL-VDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVKS-SIG 245
Cdd:PRK06608  162 YEALQQLGFsPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSPNTIADGLKTlSVS 241

                         250       260
                  ....*....|....*....|..
gi 1720366294 246 LNTWPIIRDLvDDVFTVTEDEI 267
Cdd:PRK06608  242 ARTFEYLKKL-DDFYLVEEYEI 262
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 19-268 1.83e-62

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: 199.07  E-value: 1.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  19 IQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtpEEKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  99 GIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEG-ILVHPNQEPAVIAGQGTIALEVLNQV-PL 176
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLgGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 177 VDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GLNTWPIIRD 254
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDE 236

                         250
                  ....*....|....
gi 1720366294 255 LVDDVFTVTEDEIK 268
Cdd:pfam00291 237 YVGEVVTVSDEEAL 250
PRK06815 PRK06815
threonine/serine dehydratase;
9-268 1.01e-59

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 192.99  E-value: 1.01e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   9 FADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHG 88
Cdd:PRK06815    4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLL---NEAQRQQGVITASSGNHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:PRK06815   81 QGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 169 EVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GL 246
Cdd:PRK06815  161 ELVEQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVE-VAEQPTLSDGTAGGVepGA 239

                         250       260
                  ....*....|....*....|..
gi 1720366294 247 NTWPIIRDLVDDVFTVTEDEIK 268
Cdd:PRK06815  240 ITFPLCQQLIDQKVLVSEEEIK 261
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
7-269 2.36e-56

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 184.55  E-value: 2.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK08638    9 VAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSL---TDAEKRKGVVACSAGN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YCDPSDESREKVTQRImqETEG-ILVHPNQEPAVIAGQG 164
Cdd:PRK08638   86 HAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVlHGDNFNDTIAKVEEIV--EEEGrTFIPPYDDPKVIAGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 165 TIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVKSSI 244
Cdd:PRK08638  164 TIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTG-TLADGCDVSR 242

                         250       260
                  ....*....|....*....|....*.
gi 1720366294 245 -GLNTWPIIRDLVDDVFTVTEDEIKV 269
Cdd:PRK08638  243 pGNLTYEIVRELVDDIVLVSEDEIRN 268
PRK07334 PRK07334
threonine dehydratase; Provisional
 7-267 1.11e-54

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 182.40  E-value: 1.11e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK07334    5 VTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLL---TEEERARGVIAMSAGN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YCDPSDESREkvTQRIMQETEG-ILVHPNQEPAVIAGQG 164
Cdd:PRK07334   82 HAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVlHGETLDEARA--HARELAEEEGlTFVHPYDDPAVIAGQG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 165 TIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQsKLKGELTPNLHppETIADG--VKs 242
Cdd:PRK07334  160 TVALEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYA-AIKGVALPCGG--STIAEGiaVK- 235

                         250       260
                  ....*....|....*....|....*
gi 1720366294 243 SIGLNTWPIIRDLVDDVFTVTEDEI 267
Cdd:PRK07334  236 QPGQLTLEIVRRLVDDILLVSEADI 260
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 26-267 6.15e-53

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: 177.24  E-value: 6.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 106 VPQTAPNCKKLAIQAYGASIV-YCDPSDESREKVTqRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPV 184
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYAFAT-SLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 185 GGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLNTWPIIRDLVDDVFTVT 263
Cdd:TIGR01127 157 GGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVR-TIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235


                  ....
gi 1720366294 264 EDEI 267
Cdd:TIGR01127 236 EEEI 239
eutB PRK07476
threonine dehydratase; Provisional
 7-267 5.07e-51

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 170.53  E-value: 5.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK07476    1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSL---SAQERARGVVTASTGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPS-DESREKVtQRIMQETEGILVHPNQEPAVIAGQGT 165
Cdd:PRK07476   78 HGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSqDDAQAEV-ERLVREEGLTMVPPFDDPRIIAGQGT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 166 IALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGeltpnlHP-----PETIADGV 240
Cdd:PRK07476  157 IGLEILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAG------RPvqveeVPTLADSL 230

                         250       260       270
                  ....*....|....*....|....*....|
gi 1720366294 241 KSSIGLN---TWPIIRDLVDDVFTVTEDEI 267
Cdd:PRK07476  231 GGGIGLDnryTFAMCRALLDDVVLLDEAEI 260
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 26-211 2.80e-45

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: 153.44  E-value: 2.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDtpEEKPKAVVTH-SSGNHGQALTYAAKLEGIPAYI 104
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEE--GKLPKGVIIEsTGGNTGIALAAAAARLGLKCTI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 105 VVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEG-ILVHPNQEPAVIAGQGTIALEVLNQVP--LVDALv 181
Cdd:cd00640    79 VMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGTIGLEILEQLGgqKPDAV- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720366294 182 vpvggggmvagIA-------IT-----IKALKPSVKVYAAEP 211
Cdd:cd00640   158 -----------VVpvggggnIAgiaraLKELLPNVKVIGVEP 188
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 7-275 3.50e-43

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: 150.00  E-value: 3.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:TIGR02991   1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSL---SDTQRAAGVVAASTGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASI-VYCDPSDESREKVtQRIMQETEGILVHPNQEPAVIAGQGT 165
Cdd:TIGR02991  78 HGRALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVrIVGRSQDDAQEEV-ERLVADRGLTMLPPFDHPDIVAGQGT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 166 IALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSkLKGELTPNLHPPETIADGVKSSIG 245
Cdd:TIGR02991 157 LGLEVVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKAS-LQAGRPVLVAELPTLADSLGGGIG 235

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720366294 246 LN---TWPIIRDLVDDVFTVTEDEIKVPCCQGS 275
Cdd:TIGR02991 236 LDnrvTFAMCKALLDEIVLVSEAEIAAGIRHAY 268
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
39-267 3.29e-41

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 148.75  E-value: 3.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  39 GRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAI 118
Cdd:PRK09224   34 GNQVLLKREDLQPVFSFKLRGAYNKMAQL---TEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 119 QAYGASIV-YCDPSDESREKvTQRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQVP-LVDALVVPVGGGGMVAGIAIT 196
Cdd:PRK09224  111 RAFGGEVVlHGDSFDEAYAH-AIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPhPLDAVFVPVGGGGLIAGVAAY 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366294 197 IKALKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADG--VKsSIGLNTWPIIRDLVDDVFTVTEDEI 267
Cdd:PRK09224  190 IKQLRPEIKVIGVEPEDSACLKAALEAGERV-DLPQVGLFADGvaVK-RIGEETFRLCQEYVDDVITVDTDEI 260
PRK08246 PRK08246
serine/threonine dehydratase;
7-267 1.86e-39

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 140.09  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSIlNQIAGRNLFFKCELFQKTGSFKIRGALNAIRglipdTPEEKPKAVVTHSSGN 86
Cdd:PRK08246    5 ITRSDVRAAAQRIAPHIRRTPVLEADG-AGFGPAPVWLKLEHLQHTGSFKARGAFNRLL-----AAPVPAAGVVAASGGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-----YCDPSDESREKVtqrimQETEGILVHPNQEPAVIA 161
Cdd:PRK08246   79 AGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVvvgaeYADALEAAQAFA-----AETGALLCHAYDQPEVLA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 162 GQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAitiKALKPSVKVYAAEPsnaddcyqsklkgELTPNLH-------PPE 234
Cdd:PRK08246  154 GAGTLGLEIEEQAPGVDTVLVAVGGGGLIAGIA---AWFEGRARVVAVEP-------------EGAPTLHaalaagePVD 217

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1720366294 235 TIADGVKSS------IGLNTWPIIRDLVDDVFTVTEDEI 267
Cdd:PRK08246  218 VPVSGIAADslgarrVGEIAFALARAHVVTSVLVSDEAI 256
PRK12483 PRK12483
threonine dehydratase; Reviewed
 26-267 1.24e-37

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 139.55  E-value: 1.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:PRK12483   38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARL---PAEQLARGVITASAGNHAQGVALAAARLGVKAVIV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 106 VPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQVP-LVDALVVPV 184
Cdd:PRK12483  115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPgPLDAIFVPV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 185 GGGGMVAGIAITIKALKPSVKVYAAEPSNAdDCYQSKLKGELTPNLHPPETIADGVK-SSIGLNTWPIIRDLVDDVFTVT 263
Cdd:PRK12483  195 GGGGLIAGIAAYVKYVRPEIKVIGVEPDDS-NCLQAALAAGERVVLGQVGLFADGVAvAQIGEHTFELCRHYVDEVVTVS 273


                  ....
gi 1720366294 264 EDEI 267
Cdd:PRK12483  274 TDEL 277
PRK08639 PRK08639
threonine dehydratase; Validated
 7-267 1.26e-34

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 129.54  E-value: 1.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGN 86
Cdd:PRK08639    7 VSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQL---SDEELAAGVVCASAGN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGAS----IVYCDPSDESrEKVTQRIMQETEGILVHPNQEPAVIAG 162
Cdd:PRK08639   84 HAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEfveiVLVGDTFDDS-AAAAQEYAEETGATFIPPFDDPDVIAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 163 QGTIALEVLNQV---PLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADG 239
Cdd:PRK08639  163 QGTVAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVT-LEKIDKFVDG 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 1720366294 240 --VKsSIGLNTWPIIRDLVDDVFTVTEDEI 267
Cdd:PRK08639  242 aaVA-RVGDLTFEILKDVVDDVVLVPEGAV 270
PLN02550 PLN02550
threonine dehydratase
 24-267 4.27e-27

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 110.40  E-value: 4.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  24 HLTPVLTSSI--------------LNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTPEEKPKAVVTHSSGNHGQ 89
Cdd:PLN02550   94 YLTNILSAKVydvaiesplqlakkLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKL---PKEQLDKGVICSSAGNHAQ 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  90 ALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYC-DPSDESREKVTQRIMQETEgILVHPNQEPAVIAGQGTIAL 168
Cdd:PLN02550  171 GVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVgDSYDEAQAYAKQRALEEGR-TFIPPFDHPDVIAGQGTVGM 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 169 EVLNQVP-LVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADGVK-SSIGL 246
Cdd:PLN02550  250 EIVRQHQgPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERV-MLDQVGGFADGVAvKEVGE 328

                         250       260
                  ....*....|....*....|.
gi 1720366294 247 NTWPIIRDLVDDVFTVTEDEI 267
Cdd:PLN02550  329 ETFRLCRELVDGVVLVSRDAI 349
PRK08813 PRK08813
threonine dehydratase; Provisional
 7-268 7.42e-25

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 102.01  E-value: 7.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   7 ISFADVEKAHINIQDSIHLTPVltssilnQIAGR-NLFFKCELFQKTGSFKIRGALNA-IRGLipDTPEEKPkaVVTHSS 84
Cdd:PRK08813   21 VSVADVLAAQARLRRYLSPTPL-------HYAERfGVWLKLENLQRTGSYKVRGALNAlLAGL--ERGDERP--VICASA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  85 GNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSDESREKVTQRIMQETEGILVHPNQEPAVIAGQG 164
Cdd:PRK08813   90 GNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 165 TIALEVLNQVPlvDALVVPVGGGGMVAGIAITIKAlkPSVKVYAAEPSNADDCYQSkLKGELTpNLHPPETIADGVKSSI 244
Cdd:PRK08813  170 TVGIELAAHAP--DVVIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARA-IRGDLR-EIAPVATLADGVKVKI 243

                         250       260
                  ....*....|....*....|....*
gi 1720366294 245 -GLNTWPIIRDLVDDVFTVTEDEIK 268
Cdd:PRK08813  244 pGFLTRRLCSSLLDDVVIVREAELR 268
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 26-266 8.10e-24

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: 97.97  E-value: 8.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLI-PDTpeekpkAVVTHSSGNHGQALTYAAKLEG 99
Cdd:cd01561     3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIedaekRGLLkPGT------TIIEPTSGNTGIGLAMVAAAKG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 100 IPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSD----ESREKVTQRIMQETEGIlVHPNQ--EPA-VIAGQGTIALEVLN 172
Cdd:cd01561    77 YRFIIVMPETMSEEKRKLLRALGAEVILTPEAEadgmKGAIAKARELAAETPNA-FWLNQfeNPAnPEAHYETTAPEIWE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 173 QVP-LVDALvvpvggggmvagIA-------IT-----IKALKPSVKVYAAEPSNADdcyqsklkgeLTPNLHPPETIADG 239
Cdd:cd01561   156 QLDgKVDAF------------VAgvgtggtITgvaryLKEKNPNVRIVGVDPVGSV----------LFSGGPPGPHKIEG 213

                         250       260
                  ....*....|....*....|....*....
gi 1720366294 240 vkssIGLNTWPII--RDLVDDVFTVTEDE 266
Cdd:cd01561   214 ----IGAGFIPENldRSLIDEVVRVSDEE 238
PRK06110 PRK06110
threonine dehydratase;
8-267 2.42e-23

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 97.37  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294   8 SFADVEKAHINIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTPEekPKAVVTHSSGNH 87
Cdd:PRK06110    4 TLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPR--VRGVISATRGNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  88 GQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YCDPSDESREKVTQRimQETEGILVHPNQEPAVIAGQGTI 166
Cdd:PRK06110   82 GQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIeHGEDFQAAREEAARL--AAERGLHMVPSFHPDLVRGVATY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 167 ALEVLNQVPLVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNADDCYQSKLKGEL--TPNlhpPETIADGVKSSI 244
Cdd:PRK06110  160 ALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVvtTPV---ATTLADGMACRT 236

                         250       260
                  ....*....|....*....|....
gi 1720366294 245 GL-NTWPIIRDLVDDVFTVTEDEI 267
Cdd:PRK06110  237 PDpEALEVIRAGADRIVRVTDDEV 260
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 26-180 8.56e-21

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: 90.05  E-value: 8.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIpDTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:cd06448     2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSA-KQGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 106 VPQTAPNCKKLAIQAYGASIV-----YCDPSDESREKVTQRimqETEGILVHPNQEPAVIAGQGTIALEVLNQVPL---V 177
Cdd:cd06448    81 VPESTKPRVVEKLRDEGATVVvhgkvWWEADNYLREELAEN---DPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekV 157


                  ...
gi 1720366294 178 DAL 180
Cdd:cd06448   158 DAI 160
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 18-266 8.93e-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: 87.03  E-value: 8.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  18 NIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLI-PDTPeekpkaVVTHSSGNHGQAL 91
Cdd:COG0031     6 SILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIedaekRGLLkPGGT------IVEATSGNTGIGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  92 TYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCDPSD--ESREKVTQRIMQETEGIlVHPNQ--EPA-VIAGQGTI 166
Cdd:COG0031    80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEgmKGAIDKAEELAAETPGA-FWPNQfeNPAnPEAHYETT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 167 ALEVLNQVPL-VDALvvpvggggmvagIA-------IT-----IKALKPSVKVYAAEPSNAddcyqSKLKGElTPNLHPP 233
Cdd:COG0031   159 GPEIWEQTDGkVDAF------------VAgvgtggtITgvgryLKERNPDIKIVAVEPEGS-----PLLSGG-EPGPHKI 220

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720366294 234 ETIADGVKSSIglntwpIIRDLVDDVFTVTEDE 266
Cdd:COG0031   221 EGIGAGFVPKI------LDPSLIDEVITVSDEE 247
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 26-174 4.23e-17

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


Pssm-ID: 107206 [Multi-domain]  Cd Length: 324  Bit Score: 79.94  E-value: 4.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAG-RNLFFKCELFQKTGSFKIRGALNAIRGLIpdtpEEKPKAVVTHSSGNHGQAL-TYAAKlEGIPAY 103
Cdd:cd01563    23 TPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVSKAK----ELGVKAVACASTGNTSASLaAYAAR-AGIKCV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366294 104 IVVPQTAPNCKKLAIQAYGASIVycdPSDESRE---KVTQRIMQETEGILVHpNQEPAVIAGQGTIALEVLNQV 174
Cdd:cd01563    98 VFLPAGKALGKLAQALAYGATVL---AVEGNFDdalRLVRELAEENWIYLSN-SLNPYRLEGQKTIAFEIAEQL 167
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 26-267 9.89e-17

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: 79.47  E-value: 9.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAGRNLFFKcELFQ-KTGSFKIRG---ALNAIRglipdtpEEKPKAVVTHSSGNHGQAL-TYAAKlEGI 100
Cdd:COG0498    67 TPLVKAPRLADELGKNLYVK-EEGHnPTGSFKDRAmqvAVSLAL-------ERGAKTIVCASSGNGSAALaAYAAR-AGI 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 101 PAYIVVPQT-APNCKKLAIQAYGASIVYCDPS-DEsREKVTQRIMQETEGILVHpNQEPAVIAGQGTIALEV---LNQVP 175
Cdd:COG0498   138 EVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNfDD-AQRLVKELAADEGLYAVN-SINPARLEGQKTYAFEIaeqLGRVP 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 176 lvDalvvpvggggmvagiAITI------------KALK-----------PsvKVYAAEPSNADDCYQSKLKGELTPNLHP 232
Cdd:COG0498   216 --D---------------WVVVptgnggnilagyKAFKelkelglidrlP--RLIAVQATGCNPILTAFETGRDEYEPER 276

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1720366294 233 PETIADGVksSIG--LNTWPIIRDLVD---DVFTVTEDEI 267
Cdd:COG0498   277 PETIAPSM--DIGnpSNGERALFALREsggTAVAVSDEEI 314
PRK05638 PRK05638
threonine synthase; Validated
 26-174 6.52e-12

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 65.60  E-value: 6.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIaGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtpeEKPKAVVTHSSGNHGQALT-YAAKlEGIPAYI 104
Cdd:PRK05638   67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLP----YAANGFIVASDGNAAASVAaYSAR-AGKEAFV 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366294 105 VVPQTAPNCKKLAIQAYGAS-IVYCDPSDESREKVTQRimQETEGIL-VHPNQEPAVIAGQGTIALEVLNQV 174
Cdd:PRK05638  141 VVPRKVDKGKLIQMIAFGAKiIRYGESVDEAIEYAEEL--ARLNGLYnVTPEYNIIGLEGQKTIAFELWEEI 210
PRK06450 PRK06450
threonine synthase; Validated
 37-173 6.01e-11

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 62.06  E-value: 6.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  37 IAGRNLFFKCELFQKTGSFKIRGAlnaiRGLIPDTPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKL 116
Cdd:PRK06450   62 IKKGNIWFKLDFLNPTGSYKDRGS----VTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLK 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366294 117 AIQAYGASIVYCdpsDESREKVtQRIMQETEGILVHPNQEPAVIAGQGTIALEVLNQ 173
Cdd:PRK06450  138 QIESYGAEVVRV---RGSREDV-AKAAENSGYYYASHVLQPQFRDGIRTLAYEIAKD 190
PRK08329 PRK08329
threonine synthase; Validated
 24-182 7.25e-11

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 62.15  E-value: 7.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  24 HLTPVLTSSILNqiaGRNLFFKCELFQKTGSFKIRGALNAIRGLipdtPEEKPKAVVTHSSGNHGQALTYAAKLEGIPAY 103
Cdd:PRK08329   59 HLTPPITPTVKR---SIKVYFKLDYLQPTGSFKDRGTYVTVAKL----KEEGINEVVIDSSGNAALSLALYSLSEGIKVH 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 104 IVVPQTAPNCKKLAIQAYGASIVYCDpsdESREKVTQRIMQ--ETEGIL-VHPNQEPAVIAGQGTIALEVLNQVPLVDAL 180
Cdd:PRK08329  132 VFVSYNASKEKISLLSRLGAELHFVE---GDRMEVHEEAVKfsKRNNIPyVSHWLNPYFLEGTKTIAYEIYEQIGVPDYA 208


                  ..
gi 1720366294 181 VV 182
Cdd:PRK08329  209 FV 210
PRK08197 PRK08197
threonine synthase; Validated
 25-173 1.65e-09

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 58.09  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  25 LTPVLTSSIL-NQIAGRNLFFKCELFQKTGSFKIRGALNAI-RGlipdtPEEKPKAVVTHSSGNHGQAL-TYAAKLeGIP 101
Cdd:PRK08197   79 MTPLLPLPRLgKALGIGRLWVKDEGLNPTGSFKARGLAVGVsRA-----KELGVKHLAMPTNGNAGAAWaAYAARA-GIR 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366294 102 AYIVVPQTAPNCKKLAIQAYGASIVYCDP--SDESReKVTQRImqETEGIL-VHPNQEPAVIAGQGTIALEVLNQ 173
Cdd:PRK08197  153 ATIFMPADAPEITRLECALAGAELYLVDGliSDAGK-IVAEAV--AEYGWFdVSTLKEPYRIEGKKTMGLELAEQ 224
PRK06381 PRK06381
threonine synthase; Validated
 26-133 2.15e-09

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 57.41  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAG-RNLFFKCELFQKTGSFKIRGALNAIRGLIpdtpEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYI 104
Cdd:PRK06381   16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRRAM----RLGYSGITVGTCGNYGASIAYFARLYGLKAVI 91

                          90       100
                  ....*....|....*....|....*....
gi 1720366294 105 VVPQTAPNCKKLAIQAYGASIVYCDPSDE 133
Cdd:PRK06381   92 FIPRSYSNSRVKEMEKYGAEIIYVDGKYE 120
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 33-175 1.56e-08

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


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 54.70  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  33 ILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIpdtpEEKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPN 112
Cdd:TIGR00260  31 LAANVGIKNLYVKELGHNPTLSFKDRGMAVALTKAL----ELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKIS 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366294 113 CKKLAIQ-AYGASIVYCDPS-DESREKVTQrIMQETEGILVHP-NQEPAVIAGQGTIALEVLNQVP 175
Cdd:TIGR00260 107 LGKLAQAlGYNAEVVAIDGNfDDAQRLVKQ-LFEDKPALGLNSaNSIPYRLEGQKTYAFEAVEQLG 171
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 53-267 2.33e-08

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 54.50  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  53 GSFKIRGALNAIRGLIPD---------------TPEEKPKA----VVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNC 113
Cdd:PRK08206   74 NAFKALGGAYAVARLLAEklgldiselsfeeltSGEVREKLgditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 114 KKLAIQAYGASIVYCDPS-DES-REkvTQRIMQETEGILVhpnQEPA----------VIAGQGTIALEVLNQVPlvdalv 181
Cdd:PRK08206  154 RVDAIRALGAECIITDGNyDDSvRL--AAQEAQENGWVVV---QDTAwegyeeiptwIMQGYGTMADEAVEQLK------ 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 182 vpvggggmVAGIAIT-------IKALKPSV-----KVYAA--------EPSNADDCYQSKLKGELTPNLHPPETI----A 237
Cdd:PRK08206  223 --------EMGVPPThvflqagVGSLAGAVlgyfaEVYGEqrphfvvvEPDQADCLYQSAVDGKPVAVTGDMDTImaglA 294

                         250       260       270
                  ....*....|....*....|....*....|
gi 1720366294 238 DGVKSSIGlntWPIIRDLVDDVFTVTEDEI 267
Cdd:PRK08206  295 CGEPNPLA---WEILRNCADAFISCPDEVA 321
PRK10717 PRK10717
cysteine synthase A; Provisional
 18-266 5.48e-06

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 47.16  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  18 NIQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLIpdtpeeKP-KAVVTHSSGNHGQAL 91
Cdd:PRK10717    6 DVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIwdaekRGLL------KPgGTIVEGTAGNTGIGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  92 TYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV------YCDPSDesREKVTQRIMQEtegiLVHPNQEPAVIAGQ-- 163
Cdd:PRK10717   80 ALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVlvpaapYANPNN--YVKGAGRLAEE----LVASEPNGAIWANQfd 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294 164 ---------GTIALEVLNQVP-LVDALVVPVGGGGMVAGIAITIKALKPSVKVYAAEPSNAdDCYQSKLKGELTPnlhPP 233
Cdd:PRK10717  154 npanreahyETTGPEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGS-ALYSYYKTGELKA---EG 229

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720366294 234 ETIADGvkssIGLN--TWPIIRDLVDDVFTVTEDE 266
Cdd:PRK10717  230 SSITEG----IGQGriTANLEGAPIDDAIRIPDEE 260
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 26-131 2.18e-04

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 42.25  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLIpdTPEEKpkAVVTHSSGNHGQALTYAAKLEGI 100
Cdd:PLN02556   60 TPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIedaekKNLI--TPGKT--TLIEPTSGNMGISLAFMAAMKGY 135

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720366294 101 PAYIVVPQTAPNCKKLAIQAYGASIVYCDPS 131
Cdd:PLN02556  136 KMILTMPSYTSLERRVTMRAFGAELVLTDPT 166
cysM PRK11761
cysteine synthase CysM;
19-150 2.30e-04

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 42.17  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  19 IQDSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLIpdtpeeKPKAV-VTHSSGNHGQALT 92
Cdd:PRK11761    6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIvqaekRGEI------KPGDTlIEATSGNTGIALA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366294  93 YAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYCdPSDESRE---KVTQRIMQETEGIL 150
Cdd:PRK11761   80 MIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILV-PKEQGMEgarDLALQMQAEGEGKV 139
PLN02356 PLN02356
phosphateglycerate kinase
 21-130 7.07e-04

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 40.74  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  21 DSIHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIpDTPEEKPKAVVTH-SSGNHGQALTYAAKLEG 99
Cdd:PLN02356   49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEAL-ESGQLFPGGVVTEgSAGSTAISLATVAPAYG 127

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720366294 100 IPAYIVVPQTAPNCKKLAIQAYGASIVYCDP 130
Cdd:PLN02356  128 CKCHVVIPDDVAIEKSQILEALGATVERVRP 158
PLN02569 PLN02569
threonine synthase
 36-173 2.85e-03

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 39.03  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366294  36 QIAGRN-LFFKCELFQKTGSFKIRG------ALNAIRGLipdtpeEKP-KAVVTHSSGNHGQALTYAAKLEGIPAYIVVP 107
Cdd:PLN02569  145 EFLGMNdLWVKHCGISHTGSFKDLGmtvlvsQVNRLRKM------AKPvVGVGCASTGDTSAALSAYCAAAGIPSIVFLP 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366294 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.
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