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Conserved domains on  [gi|1907163535|ref|XP_036021034|]
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serine dehydratase-like isoform X2 [Mus musculus]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 20-274 7.45e-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: 325.02  E-value: 7.45e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  20 GGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVW-DEANVKAQELATRD-GWVNVSPFDHPLIWE 97
Cdd:cd06448    59 GGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  98 GHASLVRELKESLGT--PPGAVVLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAK 175
Cdd:cd06448   139 GHSSMVDEIAQQLQSqeKVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVAT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 176 SLGAKTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgRLSSALASVVVI 255
Cdd:cd06448   219 SLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVV 297

                         250
                  ....*....|....*....
gi 1907163535 256 VCGGNNISSQQLQELKIQL 274
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 ...
 20-274 7.45e-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: 325.02  E-value: 7.45e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  20 GGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVW-DEANVKAQELATRD-GWVNVSPFDHPLIWE 97
Cdd:cd06448    59 GGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  98 GHASLVRELKESLGT--PPGAVVLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAK 175
Cdd:cd06448   139 GHSSMVDEIAQQLQSqeKVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVAT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 176 SLGAKTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgRLSSALASVVVI 255
Cdd:cd06448   219 SLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVV 297

                         250
                  ....*....|....*....
gi 1907163535 256 VCGGNNISSQQLQELKIQL 274
Cdd:cd06448   298 VCGGSNITLEQLKEYKKQL 316
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 8-261 3.30e-46

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: 157.51  E-value: 3.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535   8 VAFSDwldinqqgGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNV 87
Cdd:COG1171    76 VAASA--------GNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFV 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  88 SPFDHPLIWEGHASLVRELKESLGTPpgavvlavggggllagvTAGLLEVG------------WQHVP---IVAMETRGA 152
Cdd:COG1171   148 HPFDDPDVIAGQGTIALEILEQLPDL-----------------DAVFVPVGgggliagvaaalKALSPdirVIGVEPEGA 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 153 HSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKEC--EVLSevVEDREAVSAVQRFLDDERMLVEPACGAALAA 230
Cdd:COG1171   211 AAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEILRDLvdDIVT--VSEDEIAAAMRLLLERTKIVVEPAGAAALAA 288

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907163535 231 IYSGilwRLQAEGRlssalaSVVVIVCGGNN 261
Cdd:COG1171   289 LLAG---KERLKGK------RVVVVLSGGNI 310
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 20-258 1.72e-42

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: 147.07  E-value: 1.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  20 GGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELA-TRDGWVNVSPFDHPLIWEG 98
Cdd:pfam00291  63 SGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  99 HASLVRELKESLGTPPGAVVLAVGGGGLLAGVTAGLLEvGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLG 178
Cdd:pfam00291 143 YGTIGLEILEQLGGDPDAVVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLG 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 179 AK-TVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIysgilwRLQAEGRLSSAlASVVVIVC 257
Cdd:pfam00291 222 VGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL------KLALAGELKGG-DRVVVVLT 294


                  .
gi 1907163535 258 G 258
Cdd:pfam00291 295 G 295
PRK08246 PRK08246
serine/threonine dehydratase;
20-260 1.01e-31

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 119.29  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  20 GGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGH 99
Cdd:PRK08246   76 GGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 100 ASLVRELKESLGTPPGAVVLAVGGGGLlagvtAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGA 179
Cdd:PRK08246  156 GTLGLEIEEQAPGVDTVLVAVGGGGLI-----AGIAAWFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGA 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 180 KTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgrlssalaSVVVIVCGG 259
Cdd:PRK08246  231 RRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGA 302


                  .
gi 1907163535 260 N 260
Cdd:PRK08246  303 N 303
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 21-260 4.12e-26

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: 105.21  E-value: 4.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHA 100
Cdd:TIGR01127  57 GNHAQGVAYAAKKFGIKAVIVMPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 101 SLVRELKESLGTPPGAVVLAVGGGGLLAGVTA--GLLEvgwqHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLG 178
Cdd:TIGR01127 137 TIGLEIMEDIPDVDTVIVPVGGGGLISGVASAakQINP----NVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 179 AKTVAARTLECAKEC--EVLSevVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssalaSVVVIV 256
Cdd:TIGR01127 213 VKKPGDLTFNIIKEYvdDVVT--VDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQ---KVDVKGK------KIAVVL 281


                  ....
gi 1907163535 257 CGGN 260
Cdd:TIGR01127 282 SGGN 285
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 20-274 7.45e-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: 325.02  E-value: 7.45e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  20 GGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVW-DEANVKAQELATRD-GWVNVSPFDHPLIWE 97
Cdd:cd06448    59 GGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  98 GHASLVRELKESLGT--PPGAVVLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAK 175
Cdd:cd06448   139 GHSSMVDEIAQQLQSqeKVDAIVCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVAT 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 176 SLGAKTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgRLSSALASVVVI 255
Cdd:cd06448   219 SLGAKTVSSQALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVV 297

                         250
                  ....*....|....*....
gi 1907163535 256 VCGGNNISSQQLQELKIQL 274
Cdd:cd06448   298 VCGGSNITLEQLKEYKKQL 316
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 8-261 3.30e-46

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: 157.51  E-value: 3.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535   8 VAFSDwldinqqgGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNV 87
Cdd:COG1171    76 VAASA--------GNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFV 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  88 SPFDHPLIWEGHASLVRELKESLGTPpgavvlavggggllagvTAGLLEVG------------WQHVP---IVAMETRGA 152
Cdd:COG1171   148 HPFDDPDVIAGQGTIALEILEQLPDL-----------------DAVFVPVGgggliagvaaalKALSPdirVIGVEPEGA 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 153 HSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKEC--EVLSevVEDREAVSAVQRFLDDERMLVEPACGAALAA 230
Cdd:COG1171   211 AAMYRSLAAGEPVTLPGVDTIADGLAVGRPGELTFEILRDLvdDIVT--VSEDEIAAAMRLLLERTKIVVEPAGAAALAA 288

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907163535 231 IYSGilwRLQAEGRlssalaSVVVIVCGGNN 261
Cdd:COG1171   289 LLAG---KERLKGK------RVVVVLSGGNI 310
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 20-258 1.72e-42

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: 147.07  E-value: 1.72e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  20 GGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELA-TRDGWVNVSPFDHPLIWEG 98
Cdd:pfam00291  63 SGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEG 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  99 HASLVRELKESLGTPPGAVVLAVGGGGLLAGVTAGLLEvGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLG 178
Cdd:pfam00291 143 YGTIGLEILEQLGGDPDAVVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLG 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 179 AK-TVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIysgilwRLQAEGRLSSAlASVVVIVC 257
Cdd:pfam00291 222 VGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL------KLALAGELKGG-DRVVVVLT 294


                  .
gi 1907163535 258 G 258
Cdd:pfam00291 295 G 295
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 21-261 1.98e-40

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: 141.86  E-value: 1.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHA 100
Cdd:cd01562    74 GNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQG 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 101 SLVRELKESLGTPpgavvlavggggllagvTAGLLEVG---------------WQHVPIVAMETRGAHSFNSALQAGRPV 165
Cdd:cd01562   154 TIGLEILEQVPDL-----------------DAVFVPVGgggliagiatavkalSPNTKVIGVEPEGAPAMAQSLAAGKPV 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 166 TLPDITSVAKSLGAKTVAARTLECAKEC--EVLSevVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEG 243
Cdd:cd01562   217 TLPEVDTIADGLAVKRPGELTFEIIRKLvdDVVT--VSEDEIAAAMLLLFEREKLVAEPAGALALAALLSG---KLDLKG 291

                         250
                  ....*....|....*...
gi 1907163535 244 RlssalaSVVVIVCGGNN 261
Cdd:cd01562   292 K------KVVVVLSGGNI 303
PRK08246 PRK08246
serine/threonine dehydratase;
20-260 1.01e-31

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 119.29  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  20 GGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGH 99
Cdd:PRK08246   76 GGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGA 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 100 ASLVRELKESLGTPPGAVVLAVGGGGLlagvtAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGA 179
Cdd:PRK08246  156 GTLGLEIEEQAPGVDTVLVAVGGGGLI-----AGIAAWFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGA 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 180 KTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgrlssalaSVVVIVCGG 259
Cdd:PRK08246  231 RRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGA 302


                  .
gi 1907163535 260 N 260
Cdd:PRK08246  303 N 303
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 20-259 1.14e-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: 114.53  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  20 GGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELA-TRDGWVNVSPFDHPLIWEG 98
Cdd:cd00640    58 GGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAeEDPGAYYVNQFDNPANIAG 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  99 HASLVRELKEslgtppgavvlavggggllagvtagllEVGWQHVPIVAMETRGAHSFN---SALQAGRPVTlpditsvak 175
Cdd:cd00640   138 QGTIGLEILE---------------------------QLGGQKPDAVVVPVGGGGNIAgiaRALKELLPNV--------- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 176 slgaKTVAArtlecakecEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILwRLQAEGRlssalasVVVI 255
Cdd:cd00640   182 ----KVIGV---------EPEVVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAK-KLGKGKT-------VVVI 240


                  ....
gi 1907163535 256 VCGG 259
Cdd:cd00640   241 LTGG 244
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 21-260 4.12e-26

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: 105.21  E-value: 4.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHA 100
Cdd:TIGR01127  57 GNHAQGVAYAAKKFGIKAVIVMPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 101 SLVRELKESLGTPPGAVVLAVGGGGLLAGVTA--GLLEvgwqHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLG 178
Cdd:TIGR01127 137 TIGLEIMEDIPDVDTVIVPVGGGGLISGVASAakQINP----NVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 179 AKTVAARTLECAKEC--EVLSevVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssalaSVVVIV 256
Cdd:TIGR01127 213 VKKPGDLTFNIIKEYvdDVVT--VDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQ---KVDVKGK------KIAVVL 281


                  ....
gi 1907163535 257 CGGN 260
Cdd:TIGR01127 282 SGGN 285
PRK08639 PRK08639
threonine dehydratase; Validated
 28-271 3.59e-18

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 83.32  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  28 AYSARKLGIPVTIVLPEGT---SVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVR 104
Cdd:PRK08639   89 AYACRHLGIPGVIFMPVTTpqqKIDQVRFFGGEFVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAV 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 105 ELKESLGTPPGAVVLAVGGGGllagvtAGLL--------EVGWQhVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKS 176
Cdd:PRK08639  169 EILEQLEKEGSPDYVFVPVGG------GGLIsgvttylkERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDG 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 177 LGAKTVAARTLECAKecEVLSEVV---EDReAVSAVQRFLDDERMLVEPAcGA----ALAAIYSGIlwrlqaEGRlssal 249
Cdd:PRK08639  242 AAVARVGDLTFEILK--DVVDDVVlvpEGA-VCTTILELYNKEGIVAEPA-GAlsiaALELYKDEI------KGK----- 306

                         250       260
                  ....*....|....*....|...
gi 1907163535 250 aSVVVIVCGGNN-ISsqQLQELK 271
Cdd:PRK08639  307 -TVVCVISGGNNdIE--RMPEIK 326
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
28-260 4.33e-18

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 83.65  E-value: 4.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  28 AYSARKLGIPVTIVLPEGT---SVQVVRRLegeGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVR 104
Cdd:PRK09224   84 ALSAARLGIKAVIVMPVTTpdiKVDAVRAF---GGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAM 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 105 ELKESLGTPPGAVVLAVGGGGLLAGVTAGLLEVgWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAA 184
Cdd:PRK09224  161 EILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQL-RPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGE 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 185 RTLECAKecEVLSEVVE-DREAV-SAVQRFLDDERMLVEPAcGA-ALAAI--YSGilwRLQAEGRlssalaSVVVIVCGG 259
Cdd:PRK09224  240 ETFRLCQ--EYVDDVITvDTDEIcAAIKDVFEDTRSIAEPA-GAlALAGLkkYVA---QHGIEGE------TLVAILSGA 307


                  .
gi 1907163535 260 N 260
Cdd:PRK09224  308 N 308
eutB PRK07476
threonine dehydratase; Provisional
 21-260 2.76e-15

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 74.23  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPE---GTSVQVVRRLegeGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWE 97
Cdd:PRK07476   76 GNHGRALAYAARALGIRATICMSRlvpANKVDAIRAL---GAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIA 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  98 GHASLVRELKESL-----------GTPPGAVVLAVGGGGLLAGVTAGllevgwqhvpiVAMEtRGAhSFNSALQAGRPVT 166
Cdd:PRK07476  153 GQGTIGLEILEALpdvatvlvplsGGGLASGVAAAVKAIRPAIRVIG-----------VSME-RGA-AMHASLAAGRPVQ 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 167 LPDITSVAKSLGAKTVAARTLECAKECEVLSEVV--EDREAVSAVQRFLDDERMLVEPACGAALAAIYsgilwrlqaEGR 244
Cdd:PRK07476  220 VEEVPTLADSLGGGIGLDNRYTFAMCRALLDDVVllDEAEIAAGIRHAYREERLVVEGAGAVGIAALL---------AGK 290

                         250
                  ....*....|....*.
gi 1907163535 245 LSSALASVVVIVCGGN 260
Cdd:PRK07476  291 IAARDGPIVVVVSGAN 306
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 21-258 2.10e-14

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: 71.86  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIA-AAYSARKlGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELAtRDGWVNVSPFDHPLIWEGH 99
Cdd:cd01563    79 GNTSASlAAYAARA-GIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELA-EENWIYLSNSLNPYRLEGQ 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 100 ASLVRELKESLGTP-PGAVVLAVGGGGLLAGVTAG---LLEVGW-QHVP-IVAMETRGA----HSFNSALQAGRPVTLPD 169
Cdd:cd01563   157 KTIAFEIAEQLGWEvPDYVVVPVGNGGNITAIWKGfkeLKELGLiDRLPrMVGVQAEGAapivRAFKEGKDDIEPVENPE 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 170 itSVAKSL--GAKTVAARTLECAKECEVLSEVVEDREAVSAvQRFLD-DERMLVEPACGAALAAiysgiLWRLQAEGRLS 246
Cdd:cd01563   237 --TIATAIriGNPASGPKALRAVRESGGTAVAVSDEEILEA-QKLLArTEGIFVEPASAASLAG-----LKKLREEGIID 308

                         250
                  ....*....|..
gi 1907163535 247 SAlASVVVIVCG 258
Cdd:cd01563   309 KG-ERVVVVLTG 319
PRK07334 PRK07334
threonine dehydratase; Provisional
 21-260 4.93e-14

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 71.46  E-value: 4.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHA 100
Cdd:PRK07334   80 GNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 101 SLVRELKESLGTppgavVLAVGGGGLLAGVTAGLLEVGWQHVP---IVAMETRgahSFNSALQAGRPVTLPDITS-VAKS 176
Cdd:PRK07334  160 TVALEMLEDAPD-----LDTLVVPIGGGGLISGMATAAKALKPdieIIGVQTE---LYPSMYAAIKGVALPCGGStIAEG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 177 LGAKTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIysgilwrLQAEGRLssALASVVVIV 256
Cdd:PRK07334  232 IAVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAAL-------LAYPERF--RGRKVGLVL 302


                  ....
gi 1907163535 257 CGGN 260
Cdd:PRK07334  303 SGGN 306
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 21-260 1.90e-13

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: 69.11  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHA 100
Cdd:TIGR02991  76 GNHGRALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQG 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 101 SLVRELKESLGTPPGAVVLAVGGGGLLAGVTAGLLEVGWQHVPIVAMEtRGAhSFNSALQAGRPVTLPDITSVAKSLGAK 180
Cdd:TIGR02991 156 TLGLEVVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSME-RGA-AMKASLQAGRPVLVAELPTLADSLGGG 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 181 TVAARTLECAKECEVLSEVV--EDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssalasVVVIVCG 258
Cdd:TIGR02991 234 IGLDNRVTFAMCKALLDEIVlvSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAG---KIKNPGP-------CAVIVSG 303


                  ..
gi 1907163535 259 GN 260
Cdd:TIGR02991 304 RN 305
PRK12483 PRK12483
threonine dehydratase; Reviewed
 16-231 7.09e-13

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 68.28  E-value: 7.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  16 INQQGGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLI 95
Cdd:PRK12483   89 ITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDV 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  96 WEGHASLVRELKESLGTPPGAVVLAVGGGGLLAGVTAGLLEVGwQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAK 175
Cdd:PRK12483  169 IAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVR-PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFAD 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907163535 176 SLGAKTVAARTLECAKecEVLSEV--VEDREAVSAVQRFLDDERMLVEPACGAALAAI 231
Cdd:PRK12483  248 GVAVAQIGEHTFELCR--HYVDEVvtVSTDELCAAIKDIYDDTRSITEPAGALAVAGI 303
PRK06815 PRK06815
threonine/serine dehydratase;
21-269 1.28e-12

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 66.64  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTS---VQVVRRLegeGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWE 97
Cdd:PRK06815   77 GNHGQGVALAAKLAGIPVTVYAPEQASaikLDAIRAL---GAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  98 GHASLVRELKESLgtPPGAVVLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAK-S 176
Cdd:PRK06815  154 GQGTIGMELVEQQ--PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgT 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 177 LGAKTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAiysgiLWRLQAE--GRlssalaSVVV 254
Cdd:PRK06815  232 AGGVEPGAITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAA-----ALKLAPRyqGK------KVAV 300

                         250
                  ....*....|....*
gi 1907163535 255 IVCGGnNISSQQLQE 269
Cdd:PRK06815  301 VLCGK-NIVLEKYLE 314
PRK06110 PRK06110
threonine dehydratase;
21-260 1.64e-12

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 66.56  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFdHPLIWEGHA 100
Cdd:PRK06110   79 GNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 101 SLVRELKESLgTPPGAVVLAVGGGGLLAGVTAGLLEVGWQhVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAK 180
Cdd:PRK06110  158 TYALELFRAV-PDLDVVYVPIGMGSGICGAIAARDALGLK-TRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACR 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 181 TVAARTLECAKECevLSEV--VEDREAVSAVQRFLDDERMLVEPACGAALAAIysgilwrLQAEGRLssALASVVVIVCG 258
Cdd:PRK06110  236 TPDPEALEVIRAG--ADRIvrVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAA-------LQERERL--AGKRVGLVLSG 304


                  ..
gi 1907163535 259 GN 260
Cdd:PRK06110  305 GN 306
PLN02550 PLN02550
threonine dehydratase
 16-229 4.32e-12

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 65.71  E-value: 4.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  16 INQQGGNAGIAAAYSARKLGIPVTIVLPEGT---SVQVVRRLegeGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDH 92
Cdd:PLN02550  161 ICSSAGNHAQGVALSAQRLGCDAVIAMPVTTpeiKWQSVERL---GATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDH 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  93 PLIWEGHASLVRELKESLGTPPGAVVLAVGGGGLLAGVTAGLLEVGwQHVPIVAMETRGAHSFNSALQAGRPVTLPDITS 172
Cdd:PLN02550  238 PDVIAGQGTVGMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGG 316

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907163535 173 VAKSLGAKTVAARTLECAKECeVLSEVVEDREAV-SAVQRFLDDERMLVEPACGAALA 229
Cdd:PLN02550  317 FADGVAVKEVGEETFRLCREL-VDGVVLVSRDAIcASIKDMFEEKRSILEPAGALALA 373
PLN02970 PLN02970
serine racemase
 21-260 1.92e-11

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 63.16  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVqltgkVWDEANV-----KAQELATRDGWVNVSPFDHPLI 95
Cdd:PLN02970   84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGII-----TWCEPTVesreaVAARVQQETGAVLIHPYNDGRV 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  96 WEGHASLVRELKESLgtPPGAVVLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAK 175
Cdd:PLN02970  159 ISGQGTIALEFLEQV--PELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIAD 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 176 SLGAKtVAARTLECAKecEVLSEV--VEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGiLWRLQAEGRLSSalaSVV 253
Cdd:PLN02970  237 GLRAS-LGDLTWPVVR--DLVDDVitVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSD-SFRSNPAWKGCK---NVG 309


                  ....*..
gi 1907163535 254 VIVCGGN 260
Cdd:PLN02970  310 IVLSGGN 316
PRK06608 PRK06608
serine/threonine dehydratase;
21-270 7.90e-11

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 61.71  E-value: 7.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTgKVWDEANVKAQElATRDGWVNVSPFDHPLIWEGHA 100
Cdd:PRK06608   81 GNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILT-NTRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAG 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 101 SLVRELKESLGTPPGAVVLAVGGGgllagvtaGLL-------EVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDI-TS 172
Cdd:PRK06608  159 TLCYEALQQLGFSPDAIFASCGGG--------GLIsgtylakELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNT 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 173 VAKSLGAKTVAARTLECAKECEVLSEvVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSgilWrLQAEgrlsSALASV 252
Cdd:PRK06608  231 IADGLKTLSVSARTFEYLKKLDDFYL-VEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVN---W-LKTQ----SKPQKL 301

                         250
                  ....*....|....*...
gi 1907163535 253 VVIVCGGnNISSQQLQEL 270
Cdd:PRK06608  302 LVILSGG-NIDPILYNEL 318
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
8-111 3.34e-10

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 59.65  E-value: 3.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535   8 VAFSDwldinqqgGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNV 87
Cdd:PRK07048   76 VTFSS--------GNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLI 147

                          90       100
                  ....*....|....*....|....
gi 1907163535  88 SPFDHPLIWEGHASLVRELKESLG 111
Cdd:PRK07048  148 PPYDHPHVIAGQGTAAKELFEEVG 171
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 21-258 2.01e-09

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: 57.52  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIA-AAYSARKlGIPVTIVLPEG-TSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFdHPLIWEG 98
Cdd:COG0498   122 GNGSAAlAAYAARA-GIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEG 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  99 HASLVRELKESLGTPPgavvlavggggllagvTAG------LLEVGW-QHVP-IVAMETRGAHSFNSALQAGRPVTLPDi 170
Cdd:COG0498   200 QKTYAFEIAEQLGRVPdwvvvpt---gnggniLAGykafkeLKELGLiDRLPrLIAVQATGCNPILTAFETGRDEYEPE- 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 171 tsvakslGAKTVA-----------ARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAiysgiLWRL 239
Cdd:COG0498   276 -------RPETIApsmdignpsngERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAG-----LRKL 343

                         250
                  ....*....|....*....
gi 1907163535 240 QAEGRLSSAlASVVVIVCG 258
Cdd:COG0498   344 REEGEIDPD-EPVVVLSTG 361
PRK06381 PRK06381
threonine synthase; Validated
 21-114 3.34e-09

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 56.64  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFD-HPLI-WEG 98
Cdd:PRK06381   72 GNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSvNSVVdIEA 151

                          90
                  ....*....|....*.
gi 1907163535  99 HASLVRELKESLGTPP 114
Cdd:PRK06381  152 YSAIAYEIYEALGDVP 167
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
21-110 1.16e-08

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 55.13  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHA 100
Cdd:PRK08638   84 GNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQG 163

                          90
                  ....*....|
gi 1907163535 101 SLVRELKESL 110
Cdd:PRK08638  164 TIGLEILEDL 173
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 21-230 4.47e-08

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: 52.90  E-value: 4.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLT---GKVWDEANV-KAQELA-TRDGWVNVSPFDHPLI 95
Cdd:cd01561    62 GNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVILTpeaEADGMKGAIaKARELAaETPNAFWLNQFENPAN 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  96 WEGH-----ASLVRELKESL----------GTppgavvlavggggllagvTAGLLEVGWQHVP---IVAMETRGAHSFNS 157
Cdd:cd01561   142 PEAHyettaPEIWEQLDGKVdafvagvgtgGT------------------ITGVARYLKEKNPnvrIVGVDPVGSVLFSG 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 158 ALQAGRPVT------LPDITsvakslgaktvaartlecakECEVLSEV--VEDREAVSAVQRFLDDERMLVEPACGAALA 229
Cdd:cd01561   204 GPPGPHKIEgigagfIPENL--------------------DRSLIDEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVA 263


                  .
gi 1907163535 230 A 230
Cdd:cd01561   264 A 264
PRK08813 PRK08813
threonine dehydratase; Provisional
 16-106 1.28e-07

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 51.94  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  16 INQQGGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLI 95
Cdd:PRK08813   85 ICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDV 164

                          90
                  ....*....|.
gi 1907163535  96 WEGHASLVREL 106
Cdd:PRK08813  165 IAGQGTVGIEL 175
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 21-99 1.58e-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: 51.59  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKV--WDEANVKAQELA-TRDGWVNVSPFDHPLIWE 97
Cdd:COG0031    73 GNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAaETPGAFWPNQFENPANPE 152


                  ..
gi 1907163535  98 GH 99
Cdd:COG0031   153 AH 154
PRK05638 PRK05638
threonine synthase; Validated
 8-259 1.24e-06

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 49.04  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535   8 VAFSDWLDINQQG------GNAGIA-AAYSARKlGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELAT 80
Cdd:PRK05638  102 VAVSYGLPYAANGfivasdGNAAASvAAYSARA-GKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELAR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  81 RDGWVNVSPFDHPLIWEGHASLVRELKESLGtpPGAVVLAVGGGGLLAGVTAG---LLEVG-WQHVP-IVAMETRGAHSF 155
Cdd:PRK05638  181 LNGLYNVTPEYNIIGLEGQKTIAFELWEEIN--PTHVIVPTGSGSYLYSIYKGfkeLLEIGvIEEIPkLIAVQTERCNPI 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 156 NSALQAgrpvtLPDITSVAKSLG-------AKTVAARTLECAKEcevlSEVVEDREAVSAVQRFLDDERMLVEPACGAAL 228
Cdd:PRK05638  259 ASEILG-----NKTKCNETKALGlyvknpvMKEYVSEAIKESGG----TAVVVNEEEIMAGEKLLAKEGIFAELSSAVVM 329

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907163535 229 AAiysgiLWRLQAEGRLSSALASVVVIVCGG 259
Cdd:PRK05638  330 PA-----LLKLGEEGYIEKGDKVVLVVTGSG 355
PRK08197 PRK08197
threonine synthase; Validated
 21-258 1.30e-06

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 48.84  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIA-AAYSARKlGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGH 99
Cdd:PRK08197  136 GNAGAAwAAYAARA-GIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGK 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 100 ASLVRELKESLG--TP-----PgavvlavggggllagvTAG-------------LLEVGW--QHVP-IVAMETRGAHSFN 156
Cdd:PRK08197  215 KTMGLELAEQLGwrLPdvilyP----------------TGGgvgligiwkafdeLEALGWigGKRPrLVAVQAEGCAPIV 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535 157 SALQAGR--------PVTLPDITSVAKSLGAKTVaartLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAAL 228
Cdd:PRK08197  279 KAWEEGKeesefwedAHTVAFGIRVPKALGDFLV----LDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATF 354

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907163535 229 AAiysgiLWRLQAEGRLSSAlASVVVIVCG 258
Cdd:PRK08197  355 AA-----ARQLRESGWLKGD-ERVVLFNTG 378
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 21-88 6.41e-05

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 43.71  E-value: 6.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907163535  21 GNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVS 88
Cdd:PRK08206  125 GNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVQ 192
PRK06450 PRK06450
threonine synthase; Validated
 21-230 8.53e-04

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 40.10  E-value: 8.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  21 GNAGIA-AAYSARKlGIPVTIVLPEGTSVQVVRRLEGEGAEV-QLTGKVWDeanvkAQELATRDGWVNVSPFDHPLIWEG 98
Cdd:PRK06450  106 GNAGASiAAYGAAA-GIEVKIFVPETASGGKLKQIESYGAEVvRVRGSRED-----VAKAAENSGYYYASHVLQPQFRDG 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907163535  99 HASLVRELKESLGT-PPgavvlavggGGLLAGVTAG--LLEV--GWQH---------VP-IVAMETRGAHSFNSALQaGR 163
Cdd:PRK06450  180 IRTLAYEIAKDLDWkIP---------NYVFIPVSAGtlLLGVysGFKHlldsgviseMPkIVAVQTEQVSPLCAKFK-GI 249

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907163535 164 PVTLPD-ITSVAKSLgaktVAARTLECAKECEVLSE-----VVEDREAVSAvQRFLDDERMLVEPACGAALAA 230
Cdd:PRK06450  250 SYTPPDkVTSIADAL----VSTRPFLLDYMVKALSEygeciVVSDNEIVEA-WKELAKKGLLVEYSSATVYAA 317
 
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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