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Conserved domains on  [gi|1958669157|ref|XP_038945528|]
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serine dehydratase-like isoform X1 [Rattus norvegicus]

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) ...
 22-276 1.60e-112

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: 326.95  E-value: 1.60e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVW-DEANVRAQELATRD-GWVNVSPFDHPLIWE 99
Cdd:cd06448    59 GGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 100 GNASLVRELKESLRT--PPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVAR 177
Cdd:cd06448   139 GHSSMVDEIAQQLQSqeKVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVAT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 178 SLGAKTVAARTLECAKECEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSGILGRLQTEGRLSPaLDSVVVI 257
Cdd:cd06448   219 SLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLLTP-LDNVVVV 297

                         250
                  ....*....|....*....
gi 1958669157 258 VCGGNNISSQQLQELKTQL 276
Cdd:cd06448   298 VCGGSNITLEQLKEYKKQL 316
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 22-276 1.60e-112

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: 326.95  E-value: 1.60e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVW-DEANVRAQELATRD-GWVNVSPFDHPLIWE 99
Cdd:cd06448    59 GGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 100 GNASLVRELKESLRT--PPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVAR 177
Cdd:cd06448   139 GHSSMVDEIAQQLQSqeKVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVAT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 178 SLGAKTVAARTLECAKECEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSGILGRLQTEGRLSPaLDSVVVI 257
Cdd:cd06448   219 SLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLLTP-LDNVVVV 297

                         250
                  ....*....|....*....
gi 1958669157 258 VCGGNNISSQQLQELKTQL 276
Cdd:cd06448   298 VCGGSNITLEQLKEYKKQL 316
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 22-263 3.30e-44

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: 152.50  E-value: 3.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGN 101
Cdd:COG1171    80 AGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQ 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 102 ASLVRELKESLRTP-----PgavvlavggggllagvvaglleVG------------WQHVP---IVAMETRGAHSFNAAL 161
Cdd:COG1171   160 GTIALEILEQLPDLdavfvP----------------------VGgggliagvaaalKALSPdirVIGVEPEGAAAMYRSL 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 162 LAGRLVTLPDITSVARSLGAKTVAARTLECAKEC--EVLSevVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSgilG 239
Cdd:COG1171   218 AAGEPVTLPGVDTIADGLAVGRPGELTFEILRDLvdDIVT--VSEDEIAAAMRLLLERTKIVVEPAGAAALAALLA---G 292

                         250       260
                  ....*....|....*....|....
gi 1958669157 240 RLQTEGRlspaldSVVVIVCGGNN 263
Cdd:COG1171   293 KERLKGK------RVVVVLSGGNI 310
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 22-260 1.77e-38

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: 136.67  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELA-TRDGWVNVSPFDHPLIWEG 100
Cdd:pfam00291  63 SGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 101 NASLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEvGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLG 180
Cdd:pfam00291 143 YGTIGLEILEQLGGDPDAVVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLG 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 181 AK-TVAARTLECAKECEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVysgilgRLQTEGRLSPAlDSVVVIVC 259
Cdd:pfam00291 222 VGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL------KLALAGELKGG-DRVVVVLT 294


                  .
gi 1958669157 260 G 260
Cdd:pfam00291 295 G 295
PRK08246 PRK08246
serine/threonine dehydratase;
22-262 9.67e-31

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 116.59  E-value: 9.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGN 101
Cdd:PRK08246   76 GGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 102 ASLVRELKESLRTPPGAVVLavggggllagvvaglleVG----------W--QHVPIVAMETRGAHSFNAALLAGRLVTL 169
Cdd:PRK08246  156 GTLGLEIEEQAPGVDTVLVA-----------------VGgggliagiaaWfeGRARVVAVEPEGAPTLHAALAAGEPVDV 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 170 PDITSVARSLGAKTVAARTLECAKECEVLSEVVEDrEAVRAVQRFLDDE-RMLVEPACGAALAAVYSgilgrlqteGRLS 248
Cdd:PRK08246  219 PVSGIAADSLGARRVGEIAFALARAHVVTSVLVSD-EAIIAARRALWEElRLAVEPGAATALAALLS---------GAYV 288

                         250
                  ....*....|....*
gi 1958669157 249 PALDS-VVVIVCGGN 262
Cdd:PRK08246  289 PAPGErVAVVLCGAN 303
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 23-262 2.28e-25

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: 103.29  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:TIGR01127  57 GNHAQGVAYAAKKFGIKAVIVMPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVgwQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLGAK 182
Cdd:TIGR01127 137 TIGLEIMEDIPDVDTVIVPVGGGGLISGVASAAKQIN--PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVK 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 183 TVAARTLECAKEC--EVLSevVEDREAVRAVQRFLDDERMLVEPACGAALAAVYsgilgrlqtEGRLSPALDSVVVIVCG 260
Cdd:TIGR01127 215 KPGDLTFNIIKEYvdDVVT--VDEEEIANAIYLLLERHKILAEGAGAAGVAALL---------EQKVDVKGKKIAVVLSG 283


                  ..
gi 1958669157 261 GN 262
Cdd:TIGR01127 284 GN 285
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 22-276 1.60e-112

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: 326.95  E-value: 1.60e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVW-DEANVRAQELATRD-GWVNVSPFDHPLIWE 99
Cdd:cd06448    59 GGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 100 GNASLVRELKESLRT--PPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVAR 177
Cdd:cd06448   139 GHSSMVDEIAQQLQSqeKVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVAT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 178 SLGAKTVAARTLECAKECEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSGILGRLQTEGRLSPaLDSVVVI 257
Cdd:cd06448   219 SLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLLTP-LDNVVVV 297

                         250
                  ....*....|....*....
gi 1958669157 258 VCGGNNISSQQLQELKTQL 276
Cdd:cd06448   298 VCGGSNITLEQLKEYKKQL 316
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 22-263 3.30e-44

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: 152.50  E-value: 3.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGN 101
Cdd:COG1171    80 AGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQ 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 102 ASLVRELKESLRTP-----PgavvlavggggllagvvaglleVG------------WQHVP---IVAMETRGAHSFNAAL 161
Cdd:COG1171   160 GTIALEILEQLPDLdavfvP----------------------VGgggliagvaaalKALSPdirVIGVEPEGAAAMYRSL 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 162 LAGRLVTLPDITSVARSLGAKTVAARTLECAKEC--EVLSevVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSgilG 239
Cdd:COG1171   218 AAGEPVTLPGVDTIADGLAVGRPGELTFEILRDLvdDIVT--VSEDEIAAAMRLLLERTKIVVEPAGAAALAALLA---G 292

                         250       260
                  ....*....|....*....|....
gi 1958669157 240 RLQTEGRlspaldSVVVIVCGGNN 263
Cdd:COG1171   293 KERLKGK------RVVVVLSGGNI 310
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 22-260 1.77e-38

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: 136.67  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELA-TRDGWVNVSPFDHPLIWEG 100
Cdd:pfam00291  63 SGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 101 NASLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEvGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLG 180
Cdd:pfam00291 143 YGTIGLEILEQLGGDPDAVVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLG 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 181 AK-TVAARTLECAKECEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVysgilgRLQTEGRLSPAlDSVVVIVC 259
Cdd:pfam00291 222 VGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL------KLALAGELKGG-DRVVVVLT 294


                  .
gi 1958669157 260 G 260
Cdd:pfam00291 295 G 295
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 23-263 1.40e-37

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: 134.54  E-value: 1.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:cd01562    74 GNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLRTP------------------------PgavvlavggggllagvvagllevgwqHVPIVAMETRGAHSFN 158
Cdd:cd01562   154 TIGLEILEQVPDLdavfvpvggggliagiatavkalsP--------------------------NTKVIGVEPEGAPAMA 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 159 AALLAGRLVTLPDITSVARSLGAKTVAARTLECAKEC--EVLSevVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSg 236
Cdd:cd01562   208 QSLAAGKPVTLPEVDTIADGLAVKRPGELTFEIIRKLvdDVVT--VSEDEIAAAMLLLFEREKLVAEPAGALALAALLS- 284

                         250       260
                  ....*....|....*....|....*..
gi 1958669157 237 ilGRLQTEGRlspaldSVVVIVCGGNN 263
Cdd:cd01562   285 --GKLDLKGK------KVVVVLSGGNI 303
PRK08246 PRK08246
serine/threonine dehydratase;
22-262 9.67e-31

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 116.59  E-value: 9.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGN 101
Cdd:PRK08246   76 GGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 102 ASLVRELKESLRTPPGAVVLavggggllagvvaglleVG----------W--QHVPIVAMETRGAHSFNAALLAGRLVTL 169
Cdd:PRK08246  156 GTLGLEIEEQAPGVDTVLVA-----------------VGgggliagiaaWfeGRARVVAVEPEGAPTLHAALAAGEPVDV 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 170 PDITSVARSLGAKTVAARTLECAKECEVLSEVVEDrEAVRAVQRFLDDE-RMLVEPACGAALAAVYSgilgrlqteGRLS 248
Cdd:PRK08246  219 PVSGIAADSLGARRVGEIAFALARAHVVTSVLVSD-EAIIAARRALWEElRLAVEPGAATALAALLS---------GAYV 288

                         250
                  ....*....|....*
gi 1958669157 249 PALDS-VVVIVCGGN 262
Cdd:PRK08246  289 PAPGErVAVVLCGAN 303
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 22-261 5.93e-30

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: 112.99  E-value: 5.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  22 GGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELA-TRDGWVNVSPFDHPLIWEG 100
Cdd:cd00640    58 GGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAeEDPGAYYVNQFDNPANIAG 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 101 NASLVRELKEslrtppgavvlavggggllagvvagllEVGWQHVP--IVAMETRGAHsfnAALLAGRLVTLPDITSVArs 178
Cdd:cd00640   138 QGTIGLEILE---------------------------QLGGQKPDavVVPVGGGGNI---AGIARALKELLPNVKVIG-- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 179 lgaktvaartlecakeCEVLSEVVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSGIlgrlqtegRLSPALDSVVVIV 258
Cdd:cd00640   186 ----------------VEPEVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLA--------KKLGKGKTVVVIL 241


                  ...
gi 1958669157 259 CGG 261
Cdd:cd00640   242 TGG 244
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 23-262 2.28e-25

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: 103.29  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:TIGR01127  57 GNHAQGVAYAAKKFGIKAVIVMPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVgwQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLGAK 182
Cdd:TIGR01127 137 TIGLEIMEDIPDVDTVIVPVGGGGLISGVASAAKQIN--PNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVK 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 183 TVAARTLECAKEC--EVLSevVEDREAVRAVQRFLDDERMLVEPACGAALAAVYsgilgrlqtEGRLSPALDSVVVIVCG 260
Cdd:TIGR01127 215 KPGDLTFNIIKEYvdDVVT--VDEEEIANAIYLLLERHKILAEGAGAAGVAALL---------EQKVDVKGKKIAVVLSG 283


                  ..
gi 1958669157 261 GN 262
Cdd:TIGR01127 284 GN 285
PRK08639 PRK08639
threonine dehydratase; Validated
 30-273 1.20e-16

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 79.08  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  30 AYSAQKLGIPVTIVLPESTSKQ---VVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNASLVR 106
Cdd:PRK08639   89 AYACRHLGIPGVIFMPVTTPQQkidQVRFFGGEFVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAV 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 107 ELKESLRTPPGAVVLAVGgggllagvvaglleVGW------------QHVP---IVAMETRGAHSFNAALLAGRLVTLPD 171
Cdd:PRK08639  169 EILEQLEKEGSPDYVFVP--------------VGGgglisgvttylkERSPktkIIGVEPAGAASMKAALEAGKPVTLEK 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 172 I------TSVARslgaktVAARTLECAKecEVLSEVV---EDREAVrAVQRFLDDERMLVEPAcGA----ALAAVYSGIL 238
Cdd:PRK08639  235 IdkfvdgAAVAR------VGDLTFEILK--DVVDDVVlvpEGAVCT-TILELYNKEGIVAEPA-GAlsiaALELYKDEIK 304

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958669157 239 GRlqtegrlspaldSVVVIVCGGNN-ISsqQLQELK 273
Cdd:PRK08639  305 GK------------TVVCVISGGNNdIE--RMPEIK 326
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
30-262 1.73e-14

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 72.86  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  30 AYSAQKLGIPVTIVLPESTSK---QVVRRLegeGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNASLVR 106
Cdd:PRK09224   84 ALSAARLGIKAVIVMPVTTPDikvDAVRAF---GGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAM 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 107 ELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVgWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLGAKTVAA 186
Cdd:PRK09224  161 EILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQL-RPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGE 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 187 RTLECAKecEVLSEVVE-DREAV-RAVQRFLDDERMLVEPAcGA-ALAAV--YsgiLGRLQTEGRlspaldSVVVIVCGG 261
Cdd:PRK09224  240 ETFRLCQ--EYVDDVITvDTDEIcAAIKDVFEDTRSIAEPA-GAlALAGLkkY---VAQHGIEGE------TLVAILSGA 307


                  .
gi 1958669157 262 N 262
Cdd:PRK09224  308 N 308
PRK07334 PRK07334
threonine dehydratase; Provisional
 23-110 5.33e-14

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 71.08  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:PRK07334   80 GNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQG 159


                  ....*...
gi 1958669157 103 SLVRELKE 110
Cdd:PRK07334  160 TVALEMLE 167
PRK12483 PRK12483
threonine dehydratase; Reviewed
 18-253 2.15e-13

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 69.83  E-value: 2.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  18 INQQGGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLI 97
Cdd:PRK12483   89 ITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDV 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  98 WEGNASLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVGwQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVAR 177
Cdd:PRK12483  169 IAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVR-PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFAD 247

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958669157 178 SLGAKTVAARTLECAKecEVLSEV--VEDREAVRAVQRFLDDERMLVEPACGAALAAVySGILGRLQTEGRLSPALDS 253
Cdd:PRK12483  248 GVAVAQIGEHTFELCR--HYVDEVvtVSTDELCAAIKDIYDDTRSITEPAGALAVAGI-KKYAEREGIEGQTLVAIDS 322
eutB PRK07476
threonine dehydratase; Provisional
 23-262 5.71e-13

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 67.68  E-value: 5.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:PRK07476   76 GNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQG 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLrtppgavvlavggggllagvvaglLEVGWQHVPI------------------------VAMEtRGAhSFN 158
Cdd:PRK07476  156 TIGLEILEAL------------------------PDVATVLVPLsggglasgvaaavkairpairvigVSME-RGA-AMH 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 159 AALLAGRLVTLPDITSVARSLGAKTVAARTLECAKECEVLSEVV--EDREAVRAVQRFLDDERMLVEPACGAALAAVYsg 236
Cdd:PRK07476  210 ASLAAGRPVQVEEVPTLADSLGGGIGLDNRYTFAMCRALLDDVVllDEAEIAAGIRHAYREERLVVEGAGAVGIAALL-- 287

                         250       260
                  ....*....|....*....|....*.
gi 1958669157 237 ilgrlqtEGRLSPALDSVVVIVCGGN 262
Cdd:PRK07476  288 -------AGKIAARDGPIVVVVSGAN 306
PLN02550 PLN02550
threonine dehydratase
 18-262 1.34e-12

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 67.64  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  18 INQQGGNAGIAAAYSAQKLGIPVTIVLPESTSK---QVVRRLegeGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDH 94
Cdd:PLN02550  161 ICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEikwQSVERL---GATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDH 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  95 PLIWEGNASLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVGwQHVPIVAMETRGAHSFNAALLAGRLVTLPDITS 174
Cdd:PLN02550  238 PDVIAGQGTVGMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGG 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 175 VARSLGAKTVAARTLECAKECeVLSEVVEDREAV-RAVQRFLDDERMLVEPACGAALAAV-----YSGILGrlqtegrls 248
Cdd:PLN02550  317 FADGVAVKEVGEETFRLCREL-VDGVVLVSRDAIcASIKDMFEEKRSILEPAGALALAGAeayckYYGLKD--------- 386

                         250
                  ....*....|....
gi 1958669157 249 palDSVVVIVCGGN 262
Cdd:PLN02550  387 ---ENVVAITSGAN 397
PLN02970 PLN02970
serine racemase
 23-262 1.24e-11

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 63.93  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVqltgkVWDEANVR-----AQELATRDGWVNVSPFDHPLI 97
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGII-----TWCEPTVEsreavAARVQQETGAVLIHPYNDGRV 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  98 WEGNASLVRELKESLrtPPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVAR 177
Cdd:PLN02970  159 ISGQGTIALEFLEQV--PELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIAD 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 178 SLGAKtVAARTLECAKecEVLSEV--VEDREAVRAVQRFLDDERMLVEPACGAALAAVysgilgrLQTEGRLSPALDS-- 253
Cdd:PLN02970  237 GLRAS-LGDLTWPVVR--DLVDDVitVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAA-------LSDSFRSNPAWKGck 306

                         250
                  ....*....|
gi 1958669157 254 -VVVIVCGGN 262
Cdd:PLN02970  307 nVGIVLSGGN 316
PRK06815 PRK06815
threonine/serine dehydratase;
23-271 1.98e-11

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 63.17  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:PRK06815   77 GNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQG 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLrtPPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLV------TLPDITSVA 176
Cdd:PRK06815  157 TIGMELVEQQ--PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVevaeqpTLSDGTAGG 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 177 RSLGAKTVA-ARTLecakeceVLSEVVEDREAVRAVQRF-LDDERMLVEPACGAALAAvYSGILGRLQteGRlspaldSV 254
Cdd:PRK06815  235 VEPGAITFPlCQQL-------IDQKVLVSEEEIKEAMRLiAETDRWLIEGAAGVALAA-ALKLAPRYQ--GK------KV 298

                         250
                  ....*....|....*..
gi 1958669157 255 VVIVCGGnNISSQQLQE 271
Cdd:PRK06815  299 AVVLCGK-NIVLEKYLE 314
PRK06608 PRK06608
serine/threonine dehydratase;
23-272 2.49e-11

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 63.25  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTgKVWDEANVRAQElATRDGWVNVSPFDHPLIWEGNA 102
Cdd:PRK06608   81 GNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILT-NTRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAG 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVGWQhVPIVAMETRGAHSFNAALLAGRLVTLPDI-TSVARSLGA 181
Cdd:PRK06608  159 TLCYEALQQLGFSPDAIFASCGGGGLISGTYLAKELISPT-SLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKT 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 182 KTVAARTLECAKECEVLSEvVEDREAVRAVQRFLDDERMLVEPACGAALAAVYSGILGRLQTEgrlspaldSVVVIVCGG 261
Cdd:PRK06608  238 LSVSARTFEYLKKLDDFYL-VEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKPQ--------KLLVILSGG 308

                         250
                  ....*....|.
gi 1958669157 262 nNISSQQLQEL 272
Cdd:PRK06608  309 -NIDPILYNEL 318
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 23-262 1.39e-10

ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.


Pssm-ID: 132036 [Multi-domain]  Cd Length: 317  Bit Score: 60.64  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:TIGR02991  76 GNHGRALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQG 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLRTPPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMEtRGAhSFNAALLAGRLVTLPDITSVARSLGAK 182
Cdd:TIGR02991 156 TLGLEVVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSME-RGA-AMKASLQAGRPVLVAELPTLADSLGGG 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 183 TVAARTLECAKECEVLSEVV--EDREAVRAVQRFLDDERMLVEPACGAALAAVysgILGRLQTEGRlspaldsVVVIVCG 260
Cdd:TIGR02991 234 IGLDNRVTFAMCKALLDEIVlvSEAEIAAGIRHAYAEEREIVEGAGAVGIAAL---LAGKIKNPGP-------CAVIVSG 303


                  ..
gi 1958669157 261 GN 262
Cdd:TIGR02991 304 RN 305
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 23-260 3.23e-10

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: 59.53  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELAtRDGWVNVSPFDHPLIWEGNA 102
Cdd:cd01563    79 GNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELA-EENWIYLSNSLNPYRLEGQK 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESL--RTP-----PgavVLAVGGGGLLAGVVAGLLEVGW-QHVP-IVAMETRGAHSFNAALLAGRLVTLP--D 171
Cdd:cd01563   158 TIAFEIAEQLgwEVPdyvvvP---VGNGGNITAIWKGFKELKELGLiDRLPrMVGVQAEGAAPIVRAFKEGKDDIEPveN 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 172 ITSVARSL--GAKTVAARTLECAKECEVLSEVVEDREAVRAvQRFLD-DERMLVEPACGAALAAvysgiLGRLQTEGRLS 248
Cdd:cd01563   235 PETIATAIriGNPASGPKALRAVRESGGTAVAVSDEEILEA-QKLLArTEGIFVEPASAASLAG-----LKKLREEGIID 308

                         250
                  ....*....|..
gi 1958669157 249 PAlDSVVVIVCG 260
Cdd:cd01563   309 KG-ERVVVVLTG 319
PRK06110 PRK06110
threonine dehydratase;
23-262 6.15e-10

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 58.85  E-value: 6.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFdHPLIWEGNA 102
Cdd:PRK06110   79 GNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLrtPPGAVVLAVGGGGLLAGVVAGLLEVGWQHVPIVAMETRGAHSFNAALLAGRLVTLPDITSVARSLGAK 182
Cdd:PRK06110  158 TYALELFRAV--PDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACR 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 183 TVAARTLECAKECevLSEV--VEDREAVRAVQRFLDDERMLVEPACGAALAAVysgilgrLQTEGRLspALDSVVVIVCG 260
Cdd:PRK06110  236 TPDPEALEVIRAG--ADRIvrVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAA-------LQERERL--AGKRVGLVLSG 304


                  ..
gi 1958669157 261 GN 262
Cdd:PRK06110  305 GN 306
PRK06381 PRK06381
threonine synthase; Validated
 23-116 3.57e-09

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 56.64  E-value: 3.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFD-HPLI-WEG 100
Cdd:PRK06381   72 GNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSvNSVVdIEA 151

                          90
                  ....*....|....*.
gi 1958669157 101 NASLVRELKESLRTPP 116
Cdd:PRK06381  152 YSAIAYEIYEALGDVP 167
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
23-262 8.62e-09

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 55.51  E-value: 8.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:PRK08638   84 GNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQG 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 103 SLVRELKESLrtppgavvlavggggllagvvaglLEVGWQHVP----------------------IVAMETRGAHSFNAA 160
Cdd:PRK08638  164 TIGLEILEDL------------------------WDVDTVIVPiggggliagiavalksinptihIIGVQSENVHGMAAS 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 161 LLAGRLV------TLPDITSVARSlGAKTVaartlecakecEVLSEVVED------REAVRAVQRFLDDERMLVEPACGA 228
Cdd:PRK08638  220 FYAGEITthrttgTLADGCDVSRP-GNLTY-----------EIVRELVDDivlvseDEIRNAMKDLIQRNKVVTEGAGAL 287

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958669157 229 ALAAVYSGILGRLqTEGRlspaldSVVVIVCGGN 262
Cdd:PRK08638  288 ATAALLSGKLDQY-IQNK------KVVAIISGGN 314
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
23-110 8.79e-09

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 55.41  E-value: 8.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGNA 102
Cdd:PRK07048   81 GNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQG 160


                  ....*...
gi 1958669157 103 SLVRELKE 110
Cdd:PRK07048  161 TAAKELFE 168
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 23-260 1.11e-07

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: 52.12  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIA-AAYSAqKLGIPVTIVLPES-TSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFdHPL---- 96
Cdd:COG0498   122 GNGSAAlAAYAA-RAGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPArleg 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  97 -------IWE-------------GNASLV-------RELKEslrtppgavvlavggggllagvvaglleVGW-QHVP-IV 147
Cdd:COG0498   200 qktyafeIAEqlgrvpdwvvvptGNGGNIlagykafKELKE----------------------------LGLiDRLPrLI 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 148 AMETRGAHSFNAALLAGRLVTLPDitsvarslGAKTVA-----------ARTLECAKECEVLSEVVEDREAVRAVQRFLD 216
Cdd:COG0498   252 AVQATGCNPILTAFETGRDEYEPE--------RPETIApsmdignpsngERALFALRESGGTAVAVSDEEILEAIRLLAR 323

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958669157 217 DERMLVEPACGAALAAvysgiLGRLQTEGRLSPAlDSVVVIVCG 260
Cdd:COG0498   324 REGIFVEPATAVAVAG-----LRKLREEGEIDPD-EPVVVLSTG 361
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 23-259 1.73e-07

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


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 51.20  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKV--WDEANVRAQELA--TRDGWV-----NVS-PF 92
Cdd:COG0031    73 GNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAaeTPGAFWpnqfeNPAnPE 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  93 DH-----PLIWE---GNAS-LV-------------RELKESlrtppgavvlavggggllagvvagllevgWQHVPIVAME 150
Cdd:COG0031   153 AHyettgPEIWEqtdGKVDaFVagvgtggtitgvgRYLKER-----------------------------NPDIKIVAVE 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157 151 TRGAHSFNAALLAGRLVtlpditsvaRSLGAKTVAArTLecakECEVLSEV--VEDREAVRAVQRFLDDERMLVEPACGA 228
Cdd:COG0031   204 PEGSPLLSGGEPGPHKI---------EGIGAGFVPK-IL----DPSLIDEVitVSDEEAFAMARRLAREEGILVGISSGA 269

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958669157 229 ALAAVysgilgrLQTEGRLSPAlDSVVVIVC 259
Cdd:COG0031   270 AVAAA-------LRLAKRLGPG-KTIVTILP 292
PRK08813 PRK08813
threonine dehydratase; Provisional
 18-108 1.10e-06

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 49.24  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  18 INQQGGNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLI 97
Cdd:PRK08813   85 ICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDV 164

                          90
                  ....*....|.
gi 1958669157  98 WEGNASLVREL 108
Cdd:PRK08813  165 IAGQGTVGIEL 175
PRK05638 PRK05638
threonine synthase; Validated
 10-112 1.34e-06

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 49.04  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  10 VVFSDWLDINQQG------GNAGIA-AAYSAqKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELAT 82
Cdd:PRK05638  102 VAVSYGLPYAANGfivasdGNAAASvAAYSA-RAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELAR 180

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958669157  83 RDGWVNVSPFDHPLIWEGNASLVRELKESL 112
Cdd:PRK05638  181 LNGLYNVTPEYNIIGLEGQKTIAFELWEEI 210
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 23-99 3.14e-06

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: 47.51  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLT---GKVWDEANV-RAQELA-TRDGWVNVSPFDHPLI 97
Cdd:cd01561    62 GNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVILTpeaEADGMKGAIaKARELAaETPNAFWLNQFENPAN 141


                  ..
gi 1958669157  98 WE 99
Cdd:cd01561   142 PE 143
PRK08197 PRK08197
threonine synthase; Validated
 23-112 7.85e-05

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 43.45  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIA-AAYSAqKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEANVRAQELATRDGWVNVSPFDHPLIWEGN 101
Cdd:PRK08197  136 GNAGAAwAAYAA-RAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGK 214

                          90
                  ....*....|.
gi 1958669157 102 ASLVRELKESL 112
Cdd:PRK08197  215 KTMGLELAEQL 225
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 23-90 1.27e-04

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 42.94  E-value: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958669157  23 GNAGIAAAYSAQKLGIPVTIVLPESTSKQVVRRLEGEGAEVQLTGKVWDEAnVR-AQELATRDGWVNVS 90
Cdd:PRK08206  125 GNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDS-VRlAAQEAQENGWVVVQ 192
PRK06450 PRK06450
threonine synthase; Validated
 23-112 9.99e-04

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 40.10  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958669157  23 GNAGIA-AAYSAQKlGIPVTIVLPESTSKQVVRRLEGEGAEV-QLTGKVWDeanvrAQELATRDGWVNVSPFDHPLIWEG 100
Cdd:PRK06450  106 GNAGASiAAYGAAA-GIEVKIFVPETASGGKLKQIESYGAEVvRVRGSRED-----VAKAAENSGYYYASHVLQPQFRDG 179

                          90
                  ....*....|..
gi 1958669157 101 NASLVRELKESL 112
Cdd:PRK06450  180 IRTLAYEIAKDL 191
 
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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