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Conserved domains on  [gi|2462556829|ref|XP_054172850|]
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serine racemase isoform X1 [Homo sapiens]

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) ...
 5-320 1.51e-154

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: 436.42  E-value: 1.51e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   5 YCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  85 GNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 165 TIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI 244
Cdd:PLN02970  164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIIT-LPVTNTIADGLRASL 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 245 GLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSP--EVKNICIVLSGGNVDLT 320
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLG 320
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
 5-320 1.51e-154

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 436.42  E-value: 1.51e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   5 YCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  85 GNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 165 TIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI 244
Cdd:PLN02970  164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIIT-LPVTNTIADGLRASL 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 245 GLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSP--EVKNICIVLSGGNVDLT 320
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLG 320
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-318 2.48e-142

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: 404.56  E-value: 2.48e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   9 FADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGNHG 88
Cdd:cd01562     1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSE---EERAKGVVAASAGNHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  89 QALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562    78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 169 EVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVK-SSIGLN 247
Cdd:cd01562   158 EILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVT-LPEVDTIADGLAvKRPGEL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462556829 248 TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQtvsPEVKNICIVLSGGNVD 318
Cdd:cd01562   237 TFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 7-320 1.63e-122

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: 355.11  E-value: 1.63e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGN 86
Cdd:COG1171     6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERAR---GVVAASAGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTI 166
Cdd:COG1171    83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 167 ALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVK-SSIG 245
Cdd:COG1171   163 ALEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462556829 246 LNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQtvsPEVKNICIVLSGGNVDLT 320
Cdd:COG1171   242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSGGNIDPD 313
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 19-314 1.20e-86

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: 262.63  E-value: 1.20e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  19 IRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  99 GIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEG-IMVHPNQEPAVIAGQGTIALEVLNQV-PL 176
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLgGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 177 VDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI--GLNTWPIIRD 254
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDE 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 255 LVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEvKNICIVLSG 314
Cdd:pfam00291 237 YVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-DRVVVVLTG 295
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 26-321 3.49e-79

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: 246.58  E-value: 3.49e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpdALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 106 VPQTAPDCKKLAIQAYGASIV-YCEPSDESREnVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPV 184
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYA-FATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 185 GGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVK-SSIGLNTWPIIRDLVDDIFTVT 263
Cdd:TIGR01127 157 GGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIK-AVESVRTIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 264 EDEIKCATQLVWERMKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVLSGGNVDLTS 321
Cdd:TIGR01127 236 EEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGKKIAVVLSGGNIDLNL 290
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
 5-320 1.51e-154

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 436.42  E-value: 1.51e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   5 YCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSS 84
Cdd:PLN02970    7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  85 GNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQG 164
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 165 TIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI 244
Cdd:PLN02970  164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIIT-LPVTNTIADGLRASL 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 245 GLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSP--EVKNICIVLSGGNVDLT 320
Cdd:PLN02970  243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLG 320
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-318 2.48e-142

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: 404.56  E-value: 2.48e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   9 FADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGNHG 88
Cdd:cd01562     1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSE---EERAKGVVAASAGNHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  89 QALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562    78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 169 EVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVK-SSIGLN 247
Cdd:cd01562   158 EILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVT-LPEVDTIADGLAvKRPGEL 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462556829 248 TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQtvsPEVKNICIVLSGGNVD 318
Cdd:cd01562   237 TFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 7-320 1.63e-122

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: 355.11  E-value: 1.63e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGN 86
Cdd:COG1171     6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERAR---GVVAASAGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTI 166
Cdd:COG1171    83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 167 ALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVK-SSIG 245
Cdd:COG1171   163 ALEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462556829 246 LNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQtvsPEVKNICIVLSGGNVDLT 320
Cdd:COG1171   242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSGGNIDPD 313
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
7-320 2.10e-109

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 321.58  E-value: 2.10e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGN 86
Cdd:PRK07048    6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSP---EQRRAGVVTFSSGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTI 166
Cdd:PRK07048   83 HAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 167 ALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVKS-SIG 245
Cdd:PRK07048  163 AKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIV-HIDTPRTIADGAQTqHLG 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462556829 246 LNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVLSGGNVDLT 320
Cdd:PRK07048  242 NYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALR---GKVPLKGKRVGVIISGGNVDLA 313
PRK06608 PRK06608
serine/threonine dehydratase;
8-318 6.03e-88

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 267.79  E-value: 6.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   8 SFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDalERKPKAVVTHSSGNH 87
Cdd:PRK06608    6 NPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQ--GKLPDKIVAYSTGNH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  88 GQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKrvTEETEGIMVHPNQEPAVIAGQGTIA 167
Cdd:PRK06608   84 GQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKE--DEEQGFYYIHPSDSDSTIAGAGTLC 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 168 LEVLNQVPL-VDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKS-SIG 245
Cdd:PRK06608  162 YEALQQLGFsPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSPNTIADGLKTlSVS 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462556829 246 LNTWPIIRDLvDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPevKNICIVLSGGNVD 318
Cdd:PRK06608  242 ARTFEYLKKL-DDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKP--QKLLVILSGGNID 311
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 19-314 1.20e-86

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: 262.63  E-value: 1.20e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  19 IRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  99 GIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEG-IMVHPNQEPAVIAGQGTIALEVLNQV-PL 176
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLgGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 177 VDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI--GLNTWPIIRD 254
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDE 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 255 LVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEvKNICIVLSG 314
Cdd:pfam00291 237 YVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-DRVVVVLTG 295
PRK06815 PRK06815
threonine/serine dehydratase;
9-319 3.38e-83

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 254.62  E-value: 3.38e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   9 FADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGNHG 88
Cdd:PRK06815    4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQ---GVITASSGNHG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  89 QALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIAL 168
Cdd:PRK06815   81 QGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 169 EVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI--GL 246
Cdd:PRK06815  161 ELVEQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVE-VAEQPTLSDGTAGGVepGA 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462556829 247 NTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQhfqtvSPEV--KNICIVLSGGNVDL 319
Cdd:PRK06815  240 ITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKL-----APRYqgKKVAVVLCGKNIVL 309
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 26-321 3.49e-79

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: 246.58  E-value: 3.49e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpdALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 106 VPQTAPDCKKLAIQAYGASIV-YCEPSDESREnVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPV 184
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYA-FATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 185 GGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVK-SSIGLNTWPIIRDLVDDIFTVT 263
Cdd:TIGR01127 157 GGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIK-AVESVRTIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 264 EDEIKCATQLVWERMKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVLSGGNVDLTS 321
Cdd:TIGR01127 236 EEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGKKIAVVLSGGNIDLNL 290
PRK07334 PRK07334
threonine dehydratase; Provisional
 7-318 3.40e-74

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 234.40  E-value: 3.40e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGN 86
Cdd:PRK07334    5 VTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTE---EERARGVIAMSAGN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIV-YCEPSDESREnVAKRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:PRK07334   82 HAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVlHGETLDEARA-HARELAEEEGLTFVHPYDDPAVIAGQGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQsKLKGKLMPNlyPPETIADG--VKsS 243
Cdd:PRK07334  161 VALEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYA-AIKGVALPC--GGSTIAEGiaVK-Q 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462556829 244 IGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLS--QHFQTvspevKNICIVLSGGNVD 318
Cdd:PRK07334  237 PGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAypERFRG-----RKVGLVLSGGNID 308
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
7-324 1.97e-73

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 230.39  E-value: 1.97e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGN 86
Cdd:PRK08638    9 VAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTD---AEKRKGVVACSAGN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIV-YCEPSDESRENVAKRVTEETEgIMVHPNQEPAVIAGQGT 165
Cdd:PRK08638   86 HAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVlHGDNFNDTIAKVEEIVEEEGR-TFIPPYDDPKVIAGQGT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVKSSI- 244
Cdd:PRK08638  165 IGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEIT-THRTTGTLADGCDVSRp 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 245 GLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVlSGGNVDLT--SS 322
Cdd:PRK08638  244 GNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAII-SGGNVDLSrvSQ 322


                  ..
gi 2462556829 323 IT 324
Cdd:PRK08638  323 IT 324
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 26-315 6.15e-72

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: 223.16  E-value: 6.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpDALERKPKAVVTH-SSGNHGQALTYAAKLEGIPAYI 104
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLA--EEEGKLPKGVIIEsTGGNTGIALAAAAARLGLKCTI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 105 VVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEG-IMVHPNQEPAVIAGQGTIALEVLNQVP--LVDALV 181
Cdd:cd00640    79 VMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGTIGLEILEQLGgqKPDAVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 182 VPVGGGGMLAGIAITVKALKPSVKVYAAEPsnaddcyqsklkgklmpnlyppetiadgvkssiglntwpiirdlvdDIFT 261
Cdd:cd00640   159 VPVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVT 192

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462556829 262 VTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTvsPEVKNICIVLSGG 315
Cdd:cd00640   193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL--GKGKTVVVILTGG 244
eutB PRK07476
threonine dehydratase; Provisional
 7-319 1.81e-70

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 222.15  E-value: 1.81e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGN 86
Cdd:PRK07476    1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERAR---GVVTASTGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPS-DESRENVAkRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:PRK07476   78 HGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSqDDAQAEVE-RLVREEGLTMVPPFDDPRIIAGQGT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKlmP-NLYPPETIADGVKSSI 244
Cdd:PRK07476  157 IGLEILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGR--PvQVEEVPTLADSLGGGI 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 245 GLN---TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVLSGGNVDL 319
Cdd:PRK07476  235 GLDnryTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLA---GKIAARDGPIVVVVSGANIDM 309
PRK08246 PRK08246
serine/threonine dehydratase;
7-321 2.50e-62

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 200.95  E-value: 2.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSIlNQLTGRNLFFKCELFQKTGSFKIRGALNAVRS-LVPDAlerkpkAVVTHSSG 85
Cdd:PRK08246    5 ITRSDVRAAAQRIAPHIRRTPVLEADG-AGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAaPVPAA------GVVAASGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  86 NHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:PRK08246   78 NAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAitvKALKPSVKVYAAEPSNADDCYQSKLKGKlmpnlyPPETIADGVKSS-- 243
Cdd:PRK08246  158 LGLEIEEQAPGVDTVLVAVGGGGLIAGIA---AWFEGRARVVAVEPEGAPTLHAALAAGE------PVDVPVSGIAADsl 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 244 ----IGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEvkNICIVLSGGNVDL 319
Cdd:PRK08246  229 garrVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--RVAVVLCGANTDP 306


                  ..
gi 2462556829 320 TS 321
Cdd:PRK08246  307 AT 308
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 7-319 1.24e-57

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: 188.91  E-value: 1.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpDALERKpKAVVTHSSGN 86
Cdd:TIGR02991   1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSL--SDTQRA-AGVVAASTGN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASI-VYCEPSDESRENVaKRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:TIGR02991  78 HGRALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVrIVGRSQDDAQEEV-ERLVADRGLTMLPPFDHPDIVAGQGT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKlmPNLYPPE-TIADGVKSSI 244
Cdd:TIGR02991 157 LGLEVVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGR--PVLVAELpTLADSLGGGI 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 245 GLN---TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPevknICIVLSGGNVDL 319
Cdd:TIGR02991 235 GLDnrvTFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPGP----CAVIVSGRNIDM 308
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
26-317 8.82e-55

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 186.50  E-value: 8.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:PRK09224   21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLAR---GVITASAGNHAQGVALSAARLGIKAVIV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 106 VPQTAPDCKKLAIQAYGASIV-YCEPSDESRENvAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVP-LVDALVVP 183
Cdd:PRK09224   98 MPVTTPDIKVDAVRAFGGEVVlHGDSFDEAYAH-AIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPhPLDAVFVP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 184 VGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKlmpnlypPETI------ADG--VKsSIGLNTWPIIRDL 255
Cdd:PRK09224  177 VGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGE-------RVDLpqvglfADGvaVK-RIGEETFRLCQEY 248

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462556829 256 VDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAvLSQHFQTVSPEVKNICIVLSGGNV 317
Cdd:PRK09224  249 VDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAG-LKKYVAQHGIEGETLVAILSGANM 309
PRK12483 PRK12483
threonine dehydratase; Reviewed
 26-318 1.32e-54

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 186.54  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:PRK12483   38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLAR---GVITASAGNHAQGVALAAARLGVKAVIV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 106 VPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVP-LVDALVVPV 184
Cdd:PRK12483  115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPgPLDAIFVPV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 185 GGGGMLAGIAITVKALKPSVKVYAAEPSNAdDCYQSKLKGKLMPNLYPPETIADGVK-SSIGLNTWPIIRDLVDDIFTVT 263
Cdd:PRK12483  195 GGGGLIAGIAAYVKYVRPEIKVIGVEPDDS-NCLQAALAAGERVVLGQVGLFADGVAvAQIGEHTFELCRHYVDEVVTVS 273

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462556829 264 EDEIKCATQLVWERMKLLIEPTAGVGVAAvLSQHFQTVSPEVKNICIVLSGGNVD 318
Cdd:PRK12483  274 TDELCAAIKDIYDDTRSITEPAGALAVAG-IKKYAEREGIEGQTLVAIDSGANVN 327
PRK08639 PRK08639
threonine dehydratase; Validated
 7-318 3.05e-53

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 180.39  E-value: 3.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSSGN 86
Cdd:PRK08639    7 VSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELA---AGVVCASAGN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGAS----IVYCEPSDESrENVAKRVTEETEGIMVHPNQEPAVIAG 162
Cdd:PRK08639   84 HAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEfveiVLVGDTFDDS-AAAAQEYAEETGATFIPPFDDPDVIAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 163 QGTIALEVLNQV---PLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKL--MPNLyppETIA 237
Cdd:PRK08639  163 QGTVAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPvtLEKI---DKFV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 238 DG--VKsSIGLNTWPIIRDLVDDIFTVTEDEIkCATQLvwermKLL------IEPtAGVGVAAVLSQHFQTVspEVKNIC 309
Cdd:PRK08639  240 DGaaVA-RVGDLTFEILKDVVDDVVLVPEGAV-CTTIL-----ELYnkegivAEP-AGALSIAALELYKDEI--KGKTVV 309


                  ....*....
gi 2462556829 310 IVLSGGNVD 318
Cdd:PRK08639  310 CVISGGNND 318
PLN02550 PLN02550
threonine dehydratase
 24-318 1.02e-40

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 150.46  E-value: 1.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  24 HLTPVLTSSI--------------LNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSSGNHGQ 89
Cdd:PLN02550   94 YLTNILSAKVydvaiesplqlakkLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLD---KGVICSSAGNHAQ 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  90 ALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALE 169
Cdd:PLN02550  171 GVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGME 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 170 VLNQVP-LVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVK-SSIGLN 247
Cdd:PLN02550  251 IVRQHQgPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERV-MLDQVGGFADGVAvKEVGEE 329

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462556829 248 TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVlSQHFQTVSPEVKNICIVLSGGNVD 318
Cdd:PLN02550  330 TFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGA-EAYCKYYGLKDENVVAITSGANMN 399
PRK08813 PRK08813
threonine dehydratase; Provisional
 7-320 2.09e-38

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 139.76  E-value: 2.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   7 ISFADVEKAHINIRDSIHLTPVLTSSILNqltgrnLFFKCELFQKTGSFKIRGALNAVRSlvpdALER-KPKAVVTHSSG 85
Cdd:PRK08813   21 VSVADVLAAQARLRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLA----GLERgDERPVICASAG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  86 NHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:PRK08813   91 NHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 166 IALEVLNQVPlvDALVVPVGGGGMLAGIAITVKAlkPSVKVYAAEPSNADDCYQSkLKGKLMpNLYPPETIADGVKSSI- 244
Cdd:PRK08813  171 VGIELAAHAP--DVVIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARA-IRGDLR-EIAPVATLADGVKVKIp 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462556829 245 GLNTWPIIRDLVDDIFTVTEDEIK-CATQLVWERmKLLIEPTAGVGVAAvlsqhFQTVSPEVKniCIVLSGGNVDLT 320
Cdd:PRK08813  245 GFLTRRLCSSLLDDVVIVREAELReTLVRLALEE-HVIAEGAGALALAA-----GRRVSGKRK--CAVVSGGNIDAT 313
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 9-294 5.34e-37

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: 136.87  E-value: 5.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   9 FADVEKAhINIRDSIhlTPVLTSSILNQLTGRNLFFKcELFQ-KTGSFKIRGAlnAVrsLVPDALERKPKAVVTHSSGNH 87
Cdd:COG0498    53 FDDEEKA-VSLGEGG--TPLVKAPRLADELGKNLYVK-EEGHnPTGSFKDRAM--QV--AVSLALERGAKTIVCASSGNG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  88 GQAL-TYAAKlEGIPAYIVVPQT-APDCKKLAIQAYGASIVYCEPS-DEsRENVAKRVTEETEGIMVHpNQEPAVIAGQG 164
Cdd:COG0498   125 SAALaAYAAR-AGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNfDD-AQRLVKELAADEGLYAVN-SINPARLEGQK 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 165 TIALEV---LNQVPlvDALVVPVGGGGMLAGIAitvKALK-----------PsvKVYAAEPSNADDCYQSKLKGKLMPNL 230
Cdd:COG0498   202 TYAFEIaeqLGRVP--DWVVVPTGNGGNILAGY---KAFKelkelglidrlP--RLIAVQATGCNPILTAFETGRDEYEP 274

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462556829 231 YPPETIADGVksSIG--LNTWPIIRDLVD---DIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVL 294
Cdd:COG0498   275 ERPETIAPSM--DIGnpSNGERALFALREsggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLR 341
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 26-312 6.75e-37

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: 134.18  E-value: 6.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRslvpDALER---KPKA-VVTHSSGNHGQALTYAAKLEGIP 101
Cdd:cd01561     3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIE----DAEKRgllKPGTtIIEPTSGNTGIGLAMVAAAKGYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 102 AYIVVPQTAPDCKKLAIQAYGASIVYCEPSD----ESRENVAKRVTEETEGImVHPNQ--EPA-VIAGQGTIALEVLNQV 174
Cdd:cd01561    79 FIIVMPETMSEEKRKLLRALGAEVILTPEAEadgmKGAIAKARELAAETPNA-FWLNQfeNPAnPEAHYETTAPEIWEQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 175 P-LVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADdcyqsklkgkLMPNLYPPETIADGvkssIGLNTWPII- 252
Cdd:cd01561   158 DgKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSV----------LFSGGPPGPHKIEG----IGAGFIPENl 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462556829 253 -RDLVDDIFTVTEDE-IKCATQLVwERMKLLIEPTAGVGVAAVLsqHFQTVSPEVKNICIVL 312
Cdd:cd01561   224 dRSLIDEVVRVSDEEaFAMARRLA-REEGLLVGGSSGAAVAAAL--KLAKRLGPGKTIVTIL 282
PRK06110 PRK06110
threonine dehydratase;
8-332 1.38e-36

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 133.97  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829   8 SFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVpdALERKPKAVVTHSSGNH 87
Cdd:PRK06110    4 TLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLA--RRGPRVRGVISATRGNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  88 GQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIV-YCEPSDESRENvAKRVTEETEGIMVhPNQEPAVIAGQGTI 166
Cdd:PRK06110   82 GQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIeHGEDFQAAREE-AARLAAERGLHMV-PSFHPDLVRGVATY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 167 ALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNlypP--ETIADGVKSSI 244
Cdd:PRK06110  160 ALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTT---PvaTTLADGMACRT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 245 GL-NTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTvspEVKNICIVLSGGNVDLTSSI 323
Cdd:PRK06110  237 PDpEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERERL---AGKRVGLVLSGGNIDRAVFA 313


                  ....*....
gi 2462556829 324 TWVKQAERP 332
Cdd:PRK06110  314 RVLAGAAAE 322
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 26-316 2.39e-34

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: 128.19  E-value: 2.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPkAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:cd06448     2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECV-HVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 106 VPQTAPDCKKLAIQAYGASIV-----YCEPSDESRENVAKRvteETEGIMVHPNQEPAVIAGQGTIALEVLNQVPL---V 177
Cdd:cd06448    81 VPESTKPRVVEKLRDEGATVVvhgkvWWEADNYLREELAEN---DPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 178 DALVVPVGGGGMLAGIaitVKALK----PSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSS-IGLNTW--- 249
Cdd:cd06448   158 DAIVCSVGGGGLLNGI---VQGLErngwGDIPVVAVETEGAHSLNASLKAGKLVT-LPKITSVATSLGAKtVSSQALeya 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462556829 250 ---PIIRDLVDDIFTVTedeikcATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVK-----NICIVLSGGN 316
Cdd:cd06448   234 qehNIKSEVVSDRDAVQ------ACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLltpldNVVVVVCGGS 302
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 26-294 3.80e-33

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: 125.01  E-value: 3.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSIL-NQLTGRNLFFKCELFQKTGSFKIRGALNAVRSlvpdALERKPKAVVTHSSGNHGQAL-TYAAKlEGIPAY 103
Cdd:cd01563    23 TPLVRAPRLgERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSK----AKELGVKAVACASTGNTSASLaAYAAR-AGIKCV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 104 IVVPQTAPDCKKLAIQAYGASIVycePSDESRENVAKRVTEETE--GIMVHPNQEPAVIAGQGTIALEVLNQ----VPlv 177
Cdd:cd01563    98 VFLPAGKALGKLAQALAYGATVL---AVEGNFDDALRLVRELAEenWIYLSNSLNPYRLEGQKTIAFEIAEQlgweVP-- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 178 DALVVPVGGGGMLAGIAITVKALKPS------VKVYAAEPSNADDCYQSKLKGKLMPNLYP-PETIADGVKssIGlN--T 248
Cdd:cd01563   173 DYVVVPVGNGGNITAIWKGFKELKELglidrlPRMVGVQAEGAAPIVRAFKEGKDDIEPVEnPETIATAIR--IG-NpaS 249

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462556829 249 WPIIRDLVD----DIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVL 294
Cdd:cd01563   250 GPKALRAVResggTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLK 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 18-266 2.53e-30

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: 116.69  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  18 NIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRgalnAVRSLVPDALER---KP-KAVVTHSSGNHGQALTY 93
Cdd:COG0031     6 SILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDR----IALSMIEDAEKRgllKPgGTIVEATSGNTGIGLAM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  94 AAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSD--ESRENVAKRVTEETEGiMVHPNQ--EPA-VIAGQGTIAL 168
Cdd:COG0031    82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEgmKGAIDKAEELAAETPG-AFWPNQfeNPAnPEAHYETTGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 169 EVLNQVPL-VDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNA-----DDCYQSKLKGklmpnlyppetiadgvks 242
Cdd:COG0031   161 EIWEQTDGkVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSpllsgGEPGPHKIEG------------------ 222

                         250       260
                  ....*....|....*....|....*.
gi 2462556829 243 sIGLNTWP--IIRDLVDDIFTVTEDE 266
Cdd:COG0031   223 -IGAGFVPkiLDPSLIDEVITVSDEE 247
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 33-318 3.19e-24

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: 100.92  E-value: 3.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  33 ILNQLTGRNLFFKCELFQKTGSFKIRGalnaVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPD 112
Cdd:TIGR00260  31 LAANVGIKNLYVKELGHNPTLSFKDRG----MAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKIS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 113 CKKLAIQ-AYGASIVYCEPSDESRENVAKRVTEETEGIMVHP-NQEPAVIAGQGTIALEVLNQVP--LVDALVVPVGGGG 188
Cdd:TIGR00260 107 LGKLAQAlGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSaNSIPYRLEGQKTYAFEAVEQLGweAPDKVVVPVPNSG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 189 MLAGIAITVKALK-------PsvKVYAAEPSNADDCYQSKLKGKlmpNLYP---PETIA---DGVKSSIGLNTWPIIRDL 255
Cdd:TIGR00260 187 NFGAIWKGFKEKKmlgldslP--VKRGIQAEGAADIVRAFLEGG---QWEPietPETLStamDIGNPANWPRALEAFRRS 261

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462556829 256 VDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQ-TVSPEVKNICIVLSGGNVD 318
Cdd:TIGR00260 262 NGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKgTADPAERVVCALTGNGLKD 325
PRK08329 PRK08329
threonine synthase; Validated
 24-319 2.73e-20

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 90.27  E-value: 2.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  24 HLTPVLTSSILnqlTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpdaLERKPKAVVTHSSGNHGQALTYAAKLEGIPAY 103
Cdd:PRK08329   59 HLTPPITPTVK---RSIKVYFKLDYLQPTGSFKDRGTYVTVAKL----KEEGINEVVIDSSGNAALSLALYSLSEGIKVH 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 104 IVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVP 183
Cdd:PRK08329  132 VFVSYNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 184 VGGGGMLAGIAITVKALK--------PSVKVYAAEPSNAdDCYQSKLKGKL-----MPNlyPP--ETIADGVKSSIGLnt 248
Cdd:PRK08329  212 VGSGTLFLGIWKGFKELHemgeiskmPKLVAVQAEGYES-LCKRSKSENKLadgiaIPE--PPrkEEMLRALEESNGF-- 286

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462556829 249 wpiirdlvddIFTVTEDEIKCAtqLVW-ERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDL 319
Cdd:PRK08329  287 ----------CISVGEEETRAA--LHWlRRMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLKN 346
PRK05638 PRK05638
threonine synthase; Validated
 26-314 1.49e-18

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 86.02  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLtGRNLFFKCELFQKTGSFKIRGALNAVRslvpDALERKPKAVVTHSSGNHGQALT-YAAKlEGIPAYI 104
Cdd:PRK05638   67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVS----YGLPYAANGFIVASDGNAAASVAaYSAR-AGKEAFV 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 105 VVPQTAPDCKKLAIQAYGAS-IVYCEPSDESREnVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQV-PlvDALVV 182
Cdd:PRK05638  141 VVPRKVDKGKLIQMIAFGAKiIRYGESVDEAIE-YAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEInP--THVIV 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 183 PVGGGGMLAGI------AITVKALKPSVKVYAAEPSNADDCYQS------KLKGKLMPNLYppetIADGVKSSIGLNtwp 250
Cdd:PRK05638  218 PTGSGSYLYSIykgfkeLLEIGVIEEIPKLIAVQTERCNPIASEilgnktKCNETKALGLY----VKNPVMKEYVSE--- 290

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462556829 251 IIRDLVDDIFTVTEDEIKCATQLVWERmKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSG 314
Cdd:PRK05638  291 AIKESGGTAVVVNEEEIMAGEKLLAKE-GIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTG 353
PRK10717 PRK10717
cysteine synthase A; Provisional
 18-211 7.31e-17

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 79.91  E-value: 7.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  18 NIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRslvpDALER---KP-KAVVTHSSGNHGQALTY 93
Cdd:PRK10717    6 DVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIW----DAEKRgllKPgGTIVEGTAGNTGIGLAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  94 AAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESREN----VAKRVTEEtegiMVHPNQEPAVIAGQ------ 163
Cdd:PRK10717   82 VAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNnyvkGAGRLAEE----LVASEPNGAIWANQfdnpan 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462556829 164 -----GTIALEVLNQVP-LVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEP 211
Cdd:PRK10717  158 reahyETTGPEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADP 211
PRK06381 PRK06381
threonine synthase; Validated
 26-193 1.70e-16

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 78.98  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVLTSSILNQLTG-RNLFFKCELFQKTGSFKIRGALNAVRslvpDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYI 104
Cdd:PRK06381   16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVR----RAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 105 VVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIA--GQGTIALEVLNQVPLV-DALV 181
Cdd:PRK06381   92 FIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDieAYSAIAYEIYEALGDVpDAVA 171

                         170
                  ....*....|..
gi 2462556829 182 VPVGGGGMLAGI 193
Cdd:PRK06381  172 VPVGNGTTLAGI 183
PRK06450 PRK06450
threonine synthase; Validated
 19-314 8.76e-15

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 74.00  E-value: 8.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  19 IRDSIHLTPVLTSSIlnqlTGRNLFFKCELFQKTGSFKIRGAlnavRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:PRK06450   48 IKHFISLGEGRTPLI----KKGNIWFKLDFLNPTGSYKDRGS----VTLISYLAEKGIKQISEDSSGNAGASIAAYGAAA 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  99 GIPAYIVVPQTAPDCKKLAIQAYGASIVYCEpsdESRENVAKrVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQ----V 174
Cdd:PRK06450  120 GIEVKIFVPETASGGKLKQIESYGAEVVRVR---GSREDVAK-AAENSGYYYASHVLQPQFRDGIRTLAYEIAKDldwkI 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 175 PlvDALVVPVGGGGMLAGIAITVKALKPS------VKVYAAEPSNADDCYqSKLKGKlmpNLYPPE---TIADGVKSsig 245
Cdd:PRK06450  196 P--NYVFIPVSAGTLLLGVYSGFKHLLDSgvisemPKIVAVQTEQVSPLC-AKFKGI---SYTPPDkvtSIADALVS--- 266

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462556829 246 lnTWPIIRDLVDDIF-------TVTEDEIKCAtqlvWE---RMKLLIEPTAGVGVAAvlsqhFQTVSPEvkNICIVLSG 314
Cdd:PRK06450  267 --TRPFLLDYMVKALseygeciVVSDNEIVEA----WKelaKKGLLVEYSSATVYAA-----YKKYSVN--DSVLVLTG 332
PRK08197 PRK08197
threonine synthase; Validated
 25-201 1.08e-14

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 74.27  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  25 LTPVLTSSILNQLTG-RNLFFKCELFQKTGSFKIRGALNAVRSlvpdALERKPKAVVTHSSGNHGQAL-TYAAKLeGIPA 102
Cdd:PRK08197   79 MTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSR----AKELGVKHLAMPTNGNAGAAWaAYAARA-GIRA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 103 YIVVPQTAPDCKKLAIQAYGASIVYCEP--SDESREnVAKRVTEetEGIM-VHPNQEPAVIAGQGTIALEVLNQ----VP 175
Cdd:PRK08197  154 TIFMPADAPEITRLECALAGAELYLVDGliSDAGKI-VAEAVAE--YGWFdVSTLKEPYRIEGKKTMGLELAEQlgwrLP 230

                         170       180
                  ....*....|....*....|....*.
gi 2462556829 176 lvDALVVPVGGGGMLAGIaitVKALK 201
Cdd:PRK08197  231 --DVILYPTGGGVGLIGI---WKAFD 251
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 53-295 1.69e-14

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 73.76  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  53 GSFKIRGALNAV------------RSLVPDAL---ERKPKA----VVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDC 113
Cdd:PRK08206   74 NAFKALGGAYAVarllaeklgldiSELSFEELtsgEVREKLgditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 114 KKLAIQAYGASIV-----YcepsDES-REnvAKRVTEETEGIMVhpnQEPA----------VIAGQGTIALEVLNQVPlv 177
Cdd:PRK08206  154 RVDAIRALGAECIitdgnY----DDSvRL--AAQEAQENGWVVV---QDTAwegyeeiptwIMQGYGTMADEAVEQLK-- 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 178 DALVVP--------VGG--GGMLAGIAITVKALKPSVKVyaAEPSNADDCYQSKLKGKLmpnlyppeTIADGVKSSI--G 245
Cdd:PRK08206  223 EMGVPPthvflqagVGSlaGAVLGYFAEVYGEQRPHFVV--VEPDQADCLYQSAVDGKP--------VAVTGDMDTImaG 292

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 246 LN-------TWPIIRDLVDDIFTVTEDEIKCAtqlvwerMKLLIEPTAG-----------VGVAAVLS 295
Cdd:PRK08206  293 LAcgepnplAWEILRNCADAFISCPDEVAALG-------MRILANPLGGdppivsgesgaVGLGALAA 353
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 18-294 5.57e-10

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 59.97  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  18 NIRDS----IHLTPVLtssILNQLT---GRNLFFKCELFQKTGSFKIRGALnavrSLVPDALERK-----PKAVVTHSSG 85
Cdd:PLN02556   48 KIKTDasqlIGKTPLV---YLNKVTegcGAYIAAKQEMFQPTSSIKDRPAL----AMIEDAEKKNlitpgKTTLIEPTSG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  86 NHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAK--RVTEET-EGIMVHPNQEPA-VIA 161
Cdd:PLN02556  121 NMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKayELLESTpDAFMLQQFSNPAnTQV 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 162 GQGTIALEVL-NQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKlkgklmPNlyPPETIADGV 240
Cdd:PLN02556  201 HFETTGPEIWeDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGK------PG--PHHITGNGV 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462556829 241 kssiGLNTWPIIRDLVDDIFTVT-EDEIKCATQLVWERmKLLIEPTAGVGVAAVL 294
Cdd:PLN02556  273 ----GFKPDILDMDVMEKVLEVSsEDAVNMARELALKE-GLMVGISSGANTVAAL 322
PLN02356 PLN02356
phosphateglycerate kinase
 21-211 8.65e-09

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 56.54  E-value: 8.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  21 DSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNavrsLVPDALERK---PKAVVTH-SSGNHGQALTYAAK 96
Cdd:PLN02356   49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVK----IIEEALESGqlfPGGVVTEgSAGSTAISLATVAP 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  97 LEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEP----------------SDESRENVAKR---------VTEETEGIMV 151
Cdd:PLN02356  125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVRPvsithkdhyvniarrrALEANELASKRrkgsetdgiHLEKTNGCIS 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 152 HPNQEPAVIAG---------------------QGTiALEVLNQVPL-VDALVVPVGGGGMLAGIAITVKALKPSVKVYAA 209
Cdd:PLN02356  205 EEEKENSLFSSsctggffadqfenlanfrahyEGT-GPEIWEQTQGnLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLI 283


                  ..
gi 2462556829 210 EP 211
Cdd:PLN02356  284 DP 285
PLN02569 PLN02569
threonine synthase
 52-192 5.73e-08

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 54.05  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  52 TGSFKIRGALNAVrSLVpDALERKPK---AVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLaIQ--AYGASIV 126
Cdd:PLN02569  162 TGSFKDLGMTVLV-SQV-NRLRKMAKpvvGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISIAQL-VQpiANGALVL 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 127 YCEPSDESRENVAKRVTEETEgIMVHPNQEPAVIAGQGTIALEVLNQ----VPlvDALVVPVGGGGMLAG 192
Cdd:PLN02569  239 SIDTDFDGCMRLIREVTAELP-IYLANSLNSLRLEGQKTAAIEILQQfdweVP--DWVIVPGGNLGNIYA 305
PLN03013 PLN03013
cysteine synthase
 18-294 5.22e-06

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 47.85  E-value: 5.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  18 NIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALnavrSLVPDALERK-----PKAVVTHSSGNHGQALT 92
Cdd:PLN03013  116 NVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGY----SMVTDAEQKGfispgKSVLVEPTSGNTGIGLA 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  93 YAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENV--AKRVTEET-EGIMVHPNQEPAVIAGQ-GTIAL 168
Cdd:PLN03013  192 FIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVqkAEEILKNTpDAYMLQQFDNPANPKIHyETTGP 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 169 EVLNQVP-LVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKlkgklmPNLYPPETIADGVkssIGLN 247
Cdd:PLN03013  272 EIWDDTKgKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGK------PGPHKIQGIGAGF---IPKN 342

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2462556829 248 twpIIRDLVDDIFTVTEDE-IKCATQLVWERmKLLIEPTAGVGVAAVL 294
Cdd:PLN03013  343 ---LDQKIMDEVIAISSEEaIETAKQLALKE-GLMVGISSGAAAAAAI 386
cysM PRK11761
cysteine synthase CysM;
19-150 9.86e-06

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 46.40  E-value: 9.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  19 IRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSlvpdALER---KPKAV-VTHSSGNHGQALTYA 94
Cdd:PRK11761    6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQ----AEKRgeiKPGDTlIEATSGNTGIALAMI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462556829  95 AKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCePSDESRE---NVAKRVTEETEGIM 150
Cdd:PRK11761   82 AAIKGYRMKLIMPENMSQERRAAMRAYGAELILV-PKEQGMEgarDLALQMQAEGEGKV 139
PLN00011 PLN00011
cysteine synthase
 45-323 9.92e-06

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 46.53  E-value: 9.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  45 KCELFQKTGSFKIRGALNAVRSLVPDALERKPKA-VVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGA 123
Cdd:PLN00011   37 KLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKStLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIILRALGA 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 124 SIVYCEPSDESR---ENVAKRVTEETEGIMVHPNQEPAVIAGQ-GTIALEVL-NQVPLVDALVVPVGGGGMLAGIAITVK 198
Cdd:PLN00011  117 EVHLTDQSIGLKgmlEKAEEILSKTPGGYIPQQFENPANPEIHyRTTGPEIWrDSAGKVDILVAGVGTGGTATGVGKFLK 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829 199 ALKPSVKVYAAEPSnaddcyQSKLKGKLMPNLYPPETIADG-VKSSIGLNtwpiirdLVDDIFTVTEDEIKCATQLVWER 277
Cdd:PLN00011  197 EKNKDIKVCVVEPV------ESAVLSGGQPGPHLIQGIGSGiIPFNLDLT-------IVDEIIQVTGEEAIETAKLLALK 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2462556829 278 MKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVL---SGGNVDLTSSI 323
Cdd:PLN00011  264 EGLLVGISSGAAAAAALK---VAKRPENAGKLIVVifpSGGERYLSTKL 309
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 26-206 4.20e-04

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 41.64  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  26 TPVltsSILNQLTgRNLFFKCELFQK----TGSFKIRGalNAVRSL---VPDALERKPKAVVT----HSsgNHGQALTYA 94
Cdd:cd06449     1 TPI---QYLPRLS-EHLGGKVEIYAKrddcNSGLAFGG--NKIRKLeylLPDALAKGADTLVTvggiQS--NHTRQVAAV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462556829  95 AKLEGIPAYIV----VPQTAPDCKK----LAIQAYGASIVYCEPS-----DESRENVAKRVTEE-------TEGIMVHPn 154
Cdd:cd06449    73 AAKLGLKCVLVqenwVPYSDAVYDRvgniLLSRIMGADVRLVSAGfdigiRKSFEEAAEEVEAKggkpyviPAGGSEHP- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462556829 155 qepavIAGQGTI--ALEVLNQVPLV----DALVVPVGGGGMLAGIAITVKALKPSVKV 206
Cdd:cd06449   152 -----LGGLGYVgfVLEIAQQEEELgfkfDSIVVCSVTGSTHAGLSVGLAALGRQRRV 204
 
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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