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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

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 3.28e-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: 294246  Cd Length: 316  Bit Score: 294.98  E-value: 3.28e-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 3.28e-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: 3.28e-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 6.65e-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: 395228 [Multi-domain]  Cd Length: 295  Bit Score: 126.65  E-value: 6.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIG-------------------------------------------- 46
Cdd:pfam00291   8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALnlllrlkegeggktvveassgnhgralaaaaarlglkctivvpe 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-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVSDTIADGLGVgDEPGALALDLLDEYVGEVVTVSD 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1343962496 189 QEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGK 230
Cdd:pfam00291 247 EEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR 288
IlvA COG1171
Threonine dehydratase [Amino acid transport and metabolism];
11-247 1.06e-28

Threonine dehydratase [Amino acid transport and metabolism];


Pssm-ID: 224092  Cd Length: 347  Bit Score: 111.54  E-value: 1.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGI---------------GHFCKTALN--------------------- 54
Cdd:COG1171    26 TPLQRSPSLSERLGAEIYLKRENLQPVGSFKIRGAynklsslseeeeraaGVIAASAGNhaqgvayaakrlgikativmp 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  55 --------------------------ESIEFGMQLVANNpGWIFISPFDDPLIWEGHSSLVMELAVDLEEKPGAIVVSVG 108
Cdd:COG1171   106 ettpkikvdatrgygaevilhgdnfdDAYAAAEELAEEE-GLTFVPPFDDPDVIAGQGTIALEILEQLPDLPDAVFVPVG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 109 GGGLLNGVVEGLRRVNWaDVPIVAVETYGAHSLNAAMKAGKL-VTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVS 187
Cdd:COG1171   185 GGGLISGIATALKALSP-EIKVIGVEPEGAPSMYASLKAGKIvVVLPDVGTIADGLAVKRPGDLTFEILRELVDDIVLVD 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 188 DQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGKLAeelgpvvvVVCGGNN 247
Cdd:COG1171   264 EDEICAAMRDLFERTKIIAEPAGALALAALLAGKIEPLQGKTVVV--------ILSGGNI 315
PRK08198 PRK08198
threonine dehydratase; Provisional
11-246 6.66e-16

threonine dehydratase; Provisional


Pssm-ID: 236182 [Multi-domain]  Cd Length: 404  Bit Score: 76.34  E-value: 6.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG---------------------------------------------- 44
Cdd:PRK08198   23 TPLEYSRTLSELTGAEVYLKCENLQRTGSFKIRGaynkiaslseeerargvvaasagnhaqgvayaasllgikativmpe 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  45 -------------------IGHFCKTALNESIEFgmqlvANNPGWIFISPFDDPLIWEGHSSLVMELavdLEEKPG--AI 103
Cdd:PRK08198  103 taplskvkatrsygaevvlHGDVYDEALAKAQEL-----AEETGATFVHPFDDPDVIAGQGTIGLEI---LEDLPDvdTV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 104 VVSVggggllngvveG-----------LRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQT 172
Cdd:PRK08198  175 VVPI-----------GggglisgvataVKALR-PEVRVIGVQAEGAPAMPESLAAGRPVELESVDTIADGIAVKRPGDLT 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496 173 MKLVGEHTvfSEV--VSDQEAVRAVDHFVDDEKILVEPACGAALSAVYShiirklqseGKLAEELGPVVVVVCGGN 246
Cdd:PRK08198  243 FEIIRELV--DDVvtVSDEEIARAILLLLERAKLVVEGAGAVSVAALLS---------GKLDVKGKKVVAVLSGGN 307
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
11-260 3.28e-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: 3.28e-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 6.65e-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: 395228 [Multi-domain]  Cd Length: 295  Bit Score: 126.65  E-value: 6.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGIG-------------------------------------------- 46
Cdd:pfam00291   8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALnlllrlkegeggktvveassgnhgralaaaaarlglkctivvpe 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-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVSDTIADGLGVgDEPGALALDLLDEYVGEVVTVSD 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1343962496 189 QEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGK 230
Cdd:pfam00291 247 EEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDR 288
IlvA COG1171
Threonine dehydratase [Amino acid transport and metabolism];
11-247 1.06e-28

Threonine dehydratase [Amino acid transport and metabolism];


Pssm-ID: 224092  Cd Length: 347  Bit Score: 111.54  E-value: 1.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRGI---------------GHFCKTALN--------------------- 54
Cdd:COG1171    26 TPLQRSPSLSERLGAEIYLKRENLQPVGSFKIRGAynklsslseeeeraaGVIAASAGNhaqgvayaakrlgikativmp 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  55 --------------------------ESIEFGMQLVANNpGWIFISPFDDPLIWEGHSSLVMELAVDLEEKPGAIVVSVG 108
Cdd:COG1171   106 ettpkikvdatrgygaevilhgdnfdDAYAAAEELAEEE-GLTFVPPFDDPDVIAGQGTIALEILEQLPDLPDAVFVPVG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 109 GGGLLNGVVEGLRRVNWaDVPIVAVETYGAHSLNAAMKAGKL-VTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVS 187
Cdd:COG1171   185 GGGLISGIATALKALSP-EIKVIGVEPEGAPSMYASLKAGKIvVVLPDVGTIADGLAVKRPGDLTFEILRELVDDIVLVD 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 188 DQEAVRAVDHFVDDEKILVEPACGAALSAVYSHIIRKLQSEGKLAeelgpvvvVVCGGNN 247
Cdd:COG1171   264 EDEICAAMRDLFERTKIIAEPAGALALAALLAGKIEPLQGKTVVV--------ILSGGNI 315
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
11-247 7.87e-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  Cd Length: 304  Bit Score: 97.56  E-value: 7.87e-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 3.02e-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: 3.02e-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
PRK08198 PRK08198
threonine dehydratase; Provisional
11-246 6.66e-16

threonine dehydratase; Provisional


Pssm-ID: 236182 [Multi-domain]  Cd Length: 404  Bit Score: 76.34  E-value: 6.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG---------------------------------------------- 44
Cdd:PRK08198   23 TPLEYSRTLSELTGAEVYLKCENLQRTGSFKIRGaynkiaslseeerargvvaasagnhaqgvayaasllgikativmpe 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  45 -------------------IGHFCKTALNESIEFgmqlvANNPGWIFISPFDDPLIWEGHSSLVMELavdLEEKPG--AI 103
Cdd:PRK08198  103 taplskvkatrsygaevvlHGDVYDEALAKAQEL-----AEETGATFVHPFDDPDVIAGQGTIGLEI---LEDLPDvdTV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 104 VVSVggggllngvveG-----------LRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQT 172
Cdd:PRK08198  175 VVPI-----------GggglisgvataVKALR-PEVRVIGVQAEGAPAMPESLAAGRPVELESVDTIADGIAVKRPGDLT 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496 173 MKLVGEHTvfSEV--VSDQEAVRAVDHFVDDEKILVEPACGAALSAVYShiirklqseGKLAEELGPVVVVVCGGN 246
Cdd:PRK08198  243 FEIIRELV--DDVvtVSDEEIARAILLLLERAKLVVEGAGAVSVAALLS---------GKLDVKGKKVVAVLSGGN 307
PRK08246 PRK08246
serine/threonine dehydratase;
11-219 9.22e-11

serine/threonine dehydratase;


Pssm-ID: 181319  Cd Length: 310  Bit Score: 60.74  E-value: 9.22e-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 9.55e-11

threonine/serine dehydratase;


Pssm-ID: 180709  Cd Length: 317  Bit Score: 60.86  E-value: 9.55e-11
                          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 1.72e-10

serine racemase


Pssm-ID: 215524  Cd Length: 328  Bit Score: 60.08  E-value: 1.72e-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 2.49e-09

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 57.11  E-value: 2.49e-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 1.79e-07

threonine dehydratase; Provisional


Pssm-ID: 236025  Cd Length: 322  Bit Score: 51.12  E-value: 1.79e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG 44
Cdd:PRK07476   20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRG 53
PRK08639 PRK08639
threonine dehydratase; Validated
72-156 4.31e-07

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 50.19  E-value: 4.31e-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
PRK08526 PRK08526
threonine dehydratase; Provisional
11-246 4.56e-07

threonine dehydratase; Provisional


Pssm-ID: 181457 [Multi-domain]  Cd Length: 403  Bit Score: 50.10  E-value: 4.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG--------------IGHFCKTALNESI-------EFGMQLV----- 64
Cdd:PRK08526   21 TPFAYAPFLSKISGAEVYLKKENLQITGAYKIRGaynkianlseeqkqHGVIAASAGNHAQgvaisakKFGIKAVivmpe 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  65 ----------------------------------ANNPGWIFISPFDDPLIWEGHSSLVMELaVDLEEKPGAIVVSVGGG 110
Cdd:PRK08526  101 atpllkvsgtkalgaevilkgdnydeayafaleyAKENNLTFIHPFEDEEVMAGQGTIALEM-LDEISDLDMVVVPVGGG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 111 GLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVSDQE 190
Cdd:PRK08526  180 GLISGIASAAKQIN-PNIKIIGVGAKGAPAMYESFHAKKIINSKSVRTIADGIAVRDASPINLAIILECVDDFVQVDDEE 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1343962496 191 AVRAVDHFVDDEKILVEPAcGAALSAVYSHIIRKLQSEGKLAEELGpvvvvvcGGN 246
Cdd:PRK08526  259 IANAILFLLEKQKIVVEGA-GAASVAALLHQKIDLKKGKKIGVVLS-------GGN 306
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
11-224 1.70e-06

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


Pssm-ID: 236317  Cd Length: 333  Bit Score: 48.19  E-value: 1.70e-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
PRK06382 PRK06382
threonine dehydratase; Provisional
11-230 4.03e-06

threonine dehydratase; Provisional


Pssm-ID: 180550 [Multi-domain]  Cd Length: 406  Bit Score: 47.19  E-value: 4.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  11 TPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG-IGHFCK-----------TA-------------------------- 52
Cdd:PRK06382   26 TPLIHSTTFGDEYGGDIYFKLENFQKTGSFKSRGaVFKFSKlsedelrngviTAsagnhaqgvayaasingidakivmpe 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  53 ------LNESIEFGMQLV----------------ANNPGWIFISPFDDPLIWEGHSSLVMELAVDLEEKpGAIVVSVGGG 110
Cdd:PRK06382  106 ytipqkVNAVEAYGAHVIltgrdydeahryadkiAMDENRTFIEAFNDRWVISGQGTIGLEIMEDLPDL-DQIIVPVGGG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 111 GLLNGVVEGLRRVNwADVPIVAVETYGAHSLNAAMKAGKLVTLPAITSVATTLGLVRVSAQTMKLVGEHTVFSEVVSDQE 190
Cdd:PRK06382  185 GLISGIALAAKHIN-PNVKIIGIESELSDSMKASLREGKIVAHTSGVSICDGISVKYPGDLTFDIAKNYVDDIVTVTEES 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1343962496 191 AVRAVDHFVDDEKILVEPACGAALSAVYSHiirKLQSEGK 230
Cdd:PRK06382  264 VSKAIYKLFEREKIVAEPSGAVGLAAIMEG---KVDVKGK 300
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
61-212 5.42e-06

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 47.06  E-value: 5.42e-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 5.66e-06

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 47.22  E-value: 5.66e-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 9.67e-06

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 46.04  E-value: 9.67e-06
                          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 1.97e-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  Cd Length: 291  Bit Score: 44.81  E-value: 1.97e-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
PRK07409 PRK07409
threonine synthase; Validated
10-44 6.86e-04

threonine synthase; Validated


Pssm-ID: 236013  Cd Length: 353  Bit Score: 40.18  E-value: 6.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1343962496  10 ATPVRQSLALTKLAGTSVYIKLESSQPTGSFKIRG 44
Cdd:PRK07409   31 NTPLIPAPNLSELLGVEVYVKYEGLNPTGSFKDRG 65
PRK06608 PRK06608
serine/threonine dehydratase;
11-69 1.31e-03

serine/threonine dehydratase;


Pssm-ID: 235842  Cd Length: 338  Bit Score: 39.37  E-value: 1.31e-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 1.61e-03

threonine dehydratase; Provisional


Pssm-ID: 236339  Cd Length: 349  Bit Score: 39.22  E-value: 1.61e-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
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism];
56-237 1.73e-03

Cysteine synthase [Amino acid transport and metabolism];


Pssm-ID: 223110  Cd Length: 300  Bit Score: 39.06  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496  56 SIEFGMQLVANNPGW-IFISPFDDPLIWEGHSSLVM-ELAVDLEEKPGAIVVSVGGGGLLNGVVEGLRRVNwADVPIVAV 133
Cdd:COG0031   124 AIERAKELAAEIPGYaVWLNQFENPANPEAHYETTGpEIWQQTDGKVDAFVAGVGTGGTITGVARYLKERN-PNVRIVAV 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343962496 134 ETYGAHSLNAAMKAGKlvtLPAItsvattlGLVRVSAqtmklVGEHTVFSEV--VSDQEAVRAVDHFVDDEKILVEPACG 211
Cdd:COG0031   203 DPEGSVLLSGGEGPHK---IEGI-------GAGFVPE-----NLDLDLIDEVirVSDEEAIATARRLAREEGLLVGISSG 267
                         170       180
                  ....*....|....*....|....*.
gi 1343962496 212 AALSAVYshiirklqsegKLAEELGP 237
Cdd:COG0031   268 AALAAAL-----------KLAKELPA 282
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
11-65 2.75e-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  Cd Length: 324  Bit Score: 38.34  E-value: 2.75e-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.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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