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Conserved domains on  [gi|1343962496|ref|XP_020561718|]
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L-serine dehydratase/L-threonine deaminase isoform X2 [Oryzias latipes]

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) ...
 11-260 3.46e-100

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 cd06448:

Pssm-ID: 444852  Cd Length: 316  Bit Score: 294.98  E-value: 3.46e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIGHFCKTAL------------------------------------- 53
Cdd:cd06448     2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAkqglnecvhvvcssggnaglaaayaarklgvpctivv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  54 ---------------------------NESIEFGMQLVANNPGWIFISPFDDPLIWEGHSSLVMELAVDLEE--KPGAIV 104
Cdd:cd06448    82 pestkprvveklrdegatvvvhgkvwwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAIV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 105 VSVGGGGLLNGVVEGLRRVNWADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSE 184
Cdd:cd06448   162 CSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496 185 VVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGKLAeELGPVVVVVCGGNNISMEELRKLKKKL 260
Cdd:cd06448   242 VVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLLT-PLDNVVVVVCGGSNITLEQLKEYKKQL 316
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 11-260 3.46e-100

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: 294.98  E-value: 3.46e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIGHFCKTAL------------------------------------- 53
Cdd:cd06448     2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAkqglnecvhvvcssggnaglaaayaarklgvpctivv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  54 ---------------------------NESIEFGMQLVANNPGWIFISPFDDPLIWEGHSSLVMELAVDLEE--KPGAIV 104
Cdd:cd06448    82 pestkprvveklrdegatvvvhgkvwwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAIV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 105 VSVGGGGLLNGVVEGLRRVNWADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSE 184
Cdd:cd06448   162 CSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496 185 VVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGKLAeELGPVVVVVCGGNNISMEELRKLKKKL 260
Cdd:cd06448   242 VVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLLT-PLDNVVVVVCGGSNITLEQLKEYKKQL 316
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 11-230 9.33e-35

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: 126.27  E-value: 9.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIG-------------------------------------------- 46
Cdd:pfam00291   8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALnlllrlkegeggktvveassgnhgralaaaaarlglkvtivvpe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  47 -----------------HFCKTALNESIEFGMQLVANNPGWIFISPFDDPLIWEGHSSLVMELAVDLEEKPGAIVVSVGG 109
Cdd:pfam00291  88 dappgklllmralgaevVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPVGG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 110 GGLLNGVVEGLRRvNWADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGL-VRVSAQTMKLVGEHTVFSEVVSD 188
Cdd:pfam00291 168 GGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgDEPGALALDLLDEYVGEVVTVSD 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1343962496 189 QEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGK 230
Cdd:pfam00291 247 EEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR 288
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 5-257 1.70e-28

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: 110.51  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496   5 KPLHVATPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG--------------IG------------------------ 46
Cdd:COG1171    19 AGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaynalaslseeeraRGvvaasagnhaqgvayaarllgipa 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  47 -----------------------HFCKTALNESIEFGMQLVANNpGWIFISPFDDPLIWEGHSSLVMELAVDLEEkPGAI 103
Cdd:COG1171    99 tivmpetapavkvaatraygaevVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQLPD-LDAV 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 104 VVSVggggllngvveG-----------LRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQT 172
Cdd:COG1171   177 FVPV-----------GgggliagvaaaLKALS-PDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 173 MKLVGEHTVFSEVVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHiirKLQSEGKlaeelgPVVVVVCGGnNISMEE 252
Cdd:COG1171   245 FEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------RVVVVLSGG-NIDPDR 314


                  ....*
gi 1343962496 253 LRKLK 257
Cdd:COG1171   315 LAEIL 319
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 11-246 7.32e-13

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: 67.46  E-value: 7.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG----IGHFC-------------------------KTALNESI---- 57
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANLSedqrqrgvvaasagnhaqgvayaakKFGIKAVIvmpe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  58 -----------EFGMQLV----------------ANNPGWIFISPFDDPLIWEGHSSLVMELAVDLeEKPGAIVVSVGGG 110
Cdd:TIGR01127  81 sappskvkatkSYGAEVIlhgddydeayafatslAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDI-PDVDTVIVPVGGG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 111 GLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVSDQE 190
Cdd:TIGR01127 160 GLISGVASAAKQIN-PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496 191 AVRAVDHFVDDEKILVEPACGAALSAVYShiiRKLQSEGKlaeelgPVVVVVCGGN 246
Cdd:TIGR01127 239 IANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGK------KIAVVLSGGN 285
PRK08246 PRK08246
serine/threonine dehydratase;
11-219 9.74e-11

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 60.74  E-value: 9.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQsLALTKLAGTSVYIKLESSQPTGSFKIRG---------------------------------IGHFCKTALNESI 57
Cdd:PRK08246   24 TPVLE-ADGAGFGPAPVWLKLEHLQHTGSFKARGafnrllaapvpaagvvaasggnaglavayaaaaLGVPATVFVPETA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  58 ---------EFGMQLV----------------ANNPGWIFISPFDDPLIWEGHSSLVMELavdLEEKPG--AIVVSVG-- 108
Cdd:PRK08246  103 ppakvarlrALGAEVVvvgaeyadaleaaqafAAETGALLCHAYDQPEVLAGAGTLGLEI---EEQAPGvdTVLVAVGgg 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 109 -GGGLLNGVVEGLRRVnwadvpiVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVS 187
Cdd:PRK08246  180 gLIAGIAAWFEGRARV-------VAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVS 252

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1343962496 188 DQEAVRAVDHFVDDEKILVEPACGAALSAVYS 219
Cdd:PRK08246  253 DEAIIAARRALWEELRLAVEPGAATALAALLS 284
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 11-260 3.46e-100

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: 294.98  E-value: 3.46e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIGHFCKTAL------------------------------------- 53
Cdd:cd06448     2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAkqglnecvhvvcssggnaglaaayaarklgvpctivv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  54 ---------------------------NESIEFGMQLVANNPGWIFISPFDDPLIWEGHSSLVMELAVDLEE--KPGAIV 104
Cdd:cd06448    82 pestkprvveklrdegatvvvhgkvwwEADNYLREELAENDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAIV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 105 VSVGGGGLLNGVVEGLRRVNWADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSE 184
Cdd:cd06448   162 CSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKSE 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496 185 VVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGKLAeELGPVVVVVCGGNNISMEELRKLKKKL 260
Cdd:cd06448   242 VVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLLT-PLDNVVVVVCGGSNITLEQLKEYKKQL 316
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 11-230 9.33e-35

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: 126.27  E-value: 9.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIG-------------------------------------------- 46
Cdd:pfam00291   8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALnlllrlkegeggktvveassgnhgralaaaaarlglkvtivvpe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  47 -----------------HFCKTALNESIEFGMQLVANNPGWIFISPFDDPLIWEGHSSLVMELAVDLEEKPGAIVVSVGG 109
Cdd:pfam00291  88 dappgklllmralgaevVLVGGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVPVGG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 110 GGLLNGVVEGLRRvNWADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGL-VRVSAQTMKLVGEHTVFSEVVSD 188
Cdd:pfam00291 168 GGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVgDEPGALALDLLDEYVGEVVTVSD 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1343962496 189 QEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGK 230
Cdd:pfam00291 247 EEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR 288
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 5-257 1.70e-28

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: 110.51  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496   5 KPLHVATPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG--------------IG------------------------ 46
Cdd:COG1171    19 AGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaynalaslseeeraRGvvaasagnhaqgvayaarllgipa 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  47 -----------------------HFCKTALNESIEFGMQLVANNpGWIFISPFDDPLIWEGHSSLVMELAVDLEEkPGAI 103
Cdd:COG1171    99 tivmpetapavkvaatraygaevVLHGDTYDDAEAAAAELAEEE-GATFVHPFDDPDVIAGQGTIALEILEQLPD-LDAV 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 104 VVSVggggllngvveG-----------LRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQT 172
Cdd:COG1171   177 FVPV-----------GgggliagvaaaLKALS-PDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 173 MKLVGEHTVFSEVVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHiirKLQSEGKlaeelgPVVVVVCGGnNISMEE 252
Cdd:COG1171   245 FEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------RVVVVLSGG-NIDPDR 314


                  ....*
gi 1343962496 253 LRKLK 257
Cdd:COG1171   315 LAEIL 319
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 11-247 8.31e-24

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: 97.56  E-value: 8.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG-----------------IGH-------------------------- 47
Cdd:cd01562    18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkllslseeerakgvVAAsagnhaqgvayaakllgipativmpe 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  48 ------------------FCKTALNESIEFGMQLVANNpGWIFISPFDDPLIWEGHSSLVMELAVDLEEkPGAIVVSVgg 109
Cdd:cd01562    98 tapaakvdatraygaevvLYGEDFDEAEAKARELAEEE-GLTFIHPFDDPDVIAGQGTIGLEILEQVPD-LDAVFVPV-- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 110 ggllngvveG-----------LRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGE 178
Cdd:cd01562   174 ---------GgggliagiataVKALS-PNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEIIRK 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343962496 179 H---TVfseVVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHiirKLQSEGKlaeelgPVVVVVCGGNN 247
Cdd:cd01562   244 LvddVV---TVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSG---KLDLKGK------KVVVVLSGGNI 303
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 11-223 3.19e-20

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: 86.41  E-value: 3.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIGHFCKTA-------------------------------------- 52
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAeeegklpkgviiestggntgialaaaaarlglkctivm 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  53 -------------------------LNESIEFGMQLVANNPGWIFISPFDDPLIWEGHSSLVMELAVDLEE-KPGAIVVS 106
Cdd:cd00640    81 pegaspekvaqmralgaevvlvpgdFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLGGqKPDAVVVP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 107 VGGGGLLNGVVEGLRRVNWaDVPIVAVETYgahslnaamkagklvtlpaitsvattlglvrvsaqtmklvgehtvfSEVV 186
Cdd:cd00640   161 VGGGGNIAGIARALKELLP-NVKVIGVEPE----------------------------------------------VVTV 193

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1343962496 187 SDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIR 223
Cdd:cd00640   194 SDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKK 230
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 11-246 7.32e-13

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: 67.46  E-value: 7.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG----IGHFC-------------------------KTALNESI---- 57
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANLSedqrqrgvvaasagnhaqgvayaakKFGIKAVIvmpe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  58 -----------EFGMQLV----------------ANNPGWIFISPFDDPLIWEGHSSLVMELAVDLeEKPGAIVVSVGGG 110
Cdd:TIGR01127  81 sappskvkatkSYGAEVIlhgddydeayafatslAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDI-PDVDTVIVPVGGG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 111 GLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVSDQE 190
Cdd:TIGR01127 160 GLISGVASAAKQIN-PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496 191 AVRAVDHFVDDEKILVEPACGAALSAVYShiiRKLQSEGKlaeelgPVVVVVCGGN 246
Cdd:TIGR01127 239 IANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGK------KIAVVLSGGN 285
PRK08246 PRK08246
serine/threonine dehydratase;
11-219 9.74e-11

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 60.74  E-value: 9.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQsLALTKLAGTSVYIKLESSQPTGSFKIRG---------------------------------IGHFCKTALNESI 57
Cdd:PRK08246   24 TPVLE-ADGAGFGPAPVWLKLEHLQHTGSFKARGafnrllaapvpaagvvaasggnaglavayaaaaLGVPATVFVPETA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  58 ---------EFGMQLV----------------ANNPGWIFISPFDDPLIWEGHSSLVMELavdLEEKPG--AIVVSVG-- 108
Cdd:PRK08246  103 ppakvarlrALGAEVVvvgaeyadaleaaqafAAETGALLCHAYDQPEVLAGAGTLGLEI---EEQAPGvdTVLVAVGgg 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 109 -GGGLLNGVVEGLRRVnwadvpiVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVS 187
Cdd:PRK08246  180 gLIAGIAAWFEGRARV-------VAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFALARAHVVTSVLVS 252

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1343962496 188 DQEAVRAVDHFVDDEKILVEPACGAALSAVYS 219
Cdd:PRK08246  253 DEAIIAARRALWEELRLAVEPGAATALAALLS 284
PRK06815 PRK06815
threonine/serine dehydratase;
11-255 1.01e-10

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 60.86  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGI--------GHFCK----TALN------------------------ 54
Cdd:PRK06815   21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGAsnklrllnEAQRQqgviTASSgnhgqgvalaaklagipvtvyape 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  55 -------ESI-EFGMQLV----------------ANNPGWIFISPFDDPLIWEGHSSLVMELAvdlEEKPG--AIVVSVG 108
Cdd:PRK06815  101 qasaiklDAIrALGAEVRlyggdalnaelaarraAEQQGKVYISPYNDPQVIAGQGTIGMELV---EQQPDldAVFVAVG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 109 GGGLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVAT-TLGLVRVSAQTMKLVGEHTVFSEVVS 187
Cdd:PRK06815  178 GGGLISGIATYLKTLS-PKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgTAGGVEPGAITFPLCQQLIDQKVLVS 256

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343962496 188 DQEAVRAVDHFVDDEKILVEPACGAALSAVYshiirklqsegKLAEEL-GPVVVVVCGGNNISMEELRK 255
Cdd:PRK06815  257 EEEIKEAMRLIAETDRWLIEGAAGVALAAAL-----------KLAPRYqGKKVAVVLCGKNIVLEKYLE 314
PLN02970 PLN02970
serine racemase
 11-246 1.81e-10

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 60.08  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG---------------------------------------------- 44
Cdd:PLN02970   28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaifslsddqaekgvvthssgnhaaalalaaklrgipayivvpk 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  45 ---------------IGHFCKtALNESIEFGMQLVANNPGWIFISPFDDPLIWEGHSSLVMELavdLEEKPG--AIVVSV 107
Cdd:PLN02970  108 napackvdaviryggIITWCE-PTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEF---LEQVPEldVIIVPI 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 108 GGGGLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVA----TTLG-----LVRvsaqtmKLVGE 178
Cdd:PLN02970  184 SGGGLISGIALAAKAIK-PSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIAdglrASLGdltwpVVR------DLVDD 256

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343962496 179 htVFseVVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKlqseGKLAEELGPVVVVVCGGN 246
Cdd:PLN02970  257 --VI--TVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRS----NPAWKGCKNVGIVLSGGN 316
PRK12483 PRK12483
threonine dehydratase; Reviewed
 11-223 2.63e-09

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 57.11  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGI--------------GHFCKTALN---------------------- 54
Cdd:PRK12483   38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAynkmarlpaeqlarGVITASAGNhaqgvalaaarlgvkavivmpr 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  55 ---------------ESIEFG---------MQLVANNPGWIFISPFDDPLIWEGHSSLVMELavdLEEKPG---AIVVSV 107
Cdd:PRK12483  118 ttpqlkvdgvrahggEVVLHGesfpdalahALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEI---LRQHPGpldAIFVPV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 108 GGGGLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVS 187
Cdd:PRK12483  195 GGGGLIAGIAAYVKYVR-PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVDEVVTVS 273

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1343962496 188 DQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIR 223
Cdd:PRK12483  274 TDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAER 309
eutB PRK07476
threonine dehydratase; Provisional
 11-44 1.89e-07

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 51.12  E-value: 1.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG 44
Cdd:PRK07476   20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRG 53
PRK08639 PRK08639
threonine dehydratase; Validated
 72-156 4.55e-07

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 50.19  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  72 FISPFDDPLIWEGHSSLVMELAVDLEE--KPGAIVVSVGGGGLLNGVVEGLRRVNWaDVPIVAVETYGAHSLNAAMKAGK 149
Cdd:PRK08639  150 FIPPFDDPDVIAGQGTVAVEILEQLEKegSPDYVFVPVGGGGLISGVTTYLKERSP-KTKIIGVEPAGAASMKAALEAGK 228


                  ....*..
gi 1343962496 150 LVTLPAI 156
Cdd:PRK08639  229 PVTLEKI 235
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
11-224 1.79e-06

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 48.19  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG----IGHFC------------------------------------K 50
Cdd:PRK08638   28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTdaekrkgvvacsagnhaqgvalscallgidgkvvmpK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  51 TA---------------------LNESIEFGMQLVANNpGWIFISPFDDPLIWEGHSSLVMELAVDLEEKpGAIVVSVGG 109
Cdd:PRK08638  108 GApkskvaatcgygaevvlhgdnFNDTIAKVEEIVEEE-GRTFIPPYDDPKVIAGQGTIGLEILEDLWDV-DTVIVPIGG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 110 GGLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLV------TLPAITSVAT----TLGLVRvsaqtmKLVGEH 179
Cdd:PRK08638  186 GGLIAGIAVALKSIN-PTIHIIGVQSENVHGMAASFYAGEITthrttgTLADGCDVSRpgnlTYEIVR------ELVDDI 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1343962496 180 TvfseVVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRK 224
Cdd:PRK08638  259 V----LVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQ 299
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
61-212 5.72e-06

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 47.06  E-value: 5.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  61 MQLVANNpGWIFISPFDDPLIWEGHSSLVMELAVDLEEKPGAIVVSVggggllngvveG-----------LRRVnWADVP 129
Cdd:PRK09224  132 IELAEEE-GLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVFVPV-----------GgggliagvaayIKQL-RPEIK 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 130 IVAVETYGAHSLNAAMKAGKLVTLPaitsvatTLGL----VRVsaqtmKLVGEHTvF-------SEVVS-DQEAVRAV-- 195
Cdd:PRK09224  199 VIGVEPEDSACLKAALEAGERVDLP-------QVGLfadgVAV-----KRIGEET-FrlcqeyvDDVITvDTDEICAAik 265

                         170
                  ....*....|....*..
gi 1343962496 196 DHFVDDEKILvEPAcGA 212
Cdd:PRK09224  266 DVFEDTRSIA-EPA-GA 280
PLN02550 PLN02550
threonine dehydratase
 9-215 5.98e-06

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 47.22  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496   9 VATPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGI--------------GHFCKTALN-------------------- 54
Cdd:PLN02550  108 IESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAynmmaklpkeqldkGVICSSAGNhaqgvalsaqrlgcdaviam 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  55 ---------ESIE-FGMQLV----------------ANNPGWIFISPFDDPLIWEGHSSLVMELAVDLEEKPGAIVVSVG 108
Cdd:PLN02550  188 pvttpeikwQSVErLGATVVlvgdsydeaqayakqrALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPVG 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 109 GGGLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVSD 188
Cdd:PLN02550  268 GGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSR 346

                         250       260
                  ....*....|....*....|....*..
gi 1343962496 189 QEAVRAVDHFVDDEKILVEPACGAALS 215
Cdd:PLN02550  347 DAICASIKDMFEEKRSILEPAGALALA 373
PRK07334 PRK07334
threonine dehydratase; Provisional
 9-220 1.02e-05

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 46.04  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496   9 VATPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGI----------------------GH------------------- 47
Cdd:PRK07334   22 LRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGAlnkllllteeerargviamsagNHaqgvayhaqrlgipativm 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  48 -----FCKTA---------------LNESIEFGMQLVANNpGWIFISPFDDPLIWEGHSSLVMELavdLEEKPG--AIVV 105
Cdd:PRK07334  102 prftpTVKVErtrgfgaevvlhgetLDEARAHARELAEEE-GLTFVHPYDDPAVIAGQGTVALEM---LEDAPDldTLVV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 106 SVGGGGLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAgklVTLPAITS-VATTLGLVRVSAQTMKLVGEHTVFSE 184
Cdd:PRK07334  178 PIGGGGLISGMATAAKALK-PDIEIIGVQTELYPSMYAAIKG---VALPCGGStIAEGIAVKQPGQLTLEIVRRLVDDIL 253

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1343962496 185 VVSDQEAVRAVDHFVDDEKILVEPACGAALSAVYSH 220
Cdd:PRK07334  254 LVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAY 289
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 11-237 2.08e-05

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: 44.81  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIR-----------------------------GIG--HFC---------- 49
Cdd:cd01561     3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRialymiedaekrgllkpgttiieptsgntGIGlaMVAaakgyrfiiv 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  50 ---------------------------KTALNESIEFGMQLVANNPGWIFISPFDDPLIWEGH-SSLVMELAVDLEEKPG 101
Cdd:cd01561    83 mpetmseekrkllralgaeviltpeaeADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHyETTAPEIWEQLDGKVD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 102 AIVVSVGGGGLLNGVVEGLRRVNWaDVPIVAVETYGAhSLNAAMKAGklvtlPAITsvaTTLGLVRVSAqtmklVGEHTV 181
Cdd:cd01561   163 AFVAGVGTGGTITGVARYLKEKNP-NVRIVGVDPVGS-VLFSGGPPG-----PHKI---EGIGAGFIPE-----NLDRSL 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1343962496 182 FSEV--VSDQEAVRAVDHFVDDEKILVEPACGAALSAVYshiirklqsegKLAEELGP 237
Cdd:cd01561   228 IDEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVAAAL-----------KLAKRLGP 274
PRK06608 PRK06608
serine/threonine dehydratase;
11-69 1.39e-03

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 39.37  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIghfCKT--ALNESIEFGMQLVANNPG 69
Cdd:PRK06608   24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGV---LNHllELKEQGKLPDKIVAYSTG 81
PRK08813 PRK08813
threonine dehydratase; Provisional
 41-216 1.70e-03

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 39.22  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  41 KIRGIGHFCKT------ALNESIEFGMQLVANNpGWIFISPFDDPLIWEGHSSLVMELAVdleEKPGAIVVSVGGGGLLN 114
Cdd:PRK08813  119 KIAGVAHWGATvrqhgnSYDEAYAFARELADQN-GYRFLSAFDDPDVIAGQGTVGIELAA---HAPDVVIVPIGGGGLAS 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 115 GVVEGLRRvnwADVPIVAVETYGAHSLNAAMKAgklvTLPAITSVATTLGLVRVSAQ---TMKLVGEHTVFSEVVSDQEA 191
Cdd:PRK08813  195 GVALALKS---QGVRVVGAQVEGVDSMARAIRG----DLREIAPVATLADGVKVKIPgflTRRLCSSLLDDVVIVREAEL 267

                         170       180
                  ....*....|....*....|....*
gi 1343962496 192 VRAVDHFVDDEKILVEPACGAALSA 216
Cdd:PRK08813  268 RETLVRLALEEHVIAEGAGALALAA 292
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 11-44 1.75e-03

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: 39.03  E-value: 1.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG 44
Cdd:COG0498    67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRA 100
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 11-65 2.90e-03

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: 38.34  E-value: 2.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496  11 TP-VRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIGhfckTALNESIEFGMQLVA 65
Cdd:cd01563    23 TPlVRAPRLGERLGGKNLYVKDEGLNPTGSFKDRGMT----VAVSKAKELGVKAVA 74
 
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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