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Conserved domains on  [gi|943672297|ref|WP_055499123|]
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pyridoxal-phosphate dependent enzyme [Streptomyces albus]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 5-325 1.76e-136

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 PRK07048:

Pssm-ID: 444852 [Multi-domain]  Cd Length: 321  Bit Score: 389.76  E-value: 1.76e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   5 TTTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSS 84
Cdd:PRK07048   1 SDLLLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  85 GNHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQG 164
Cdd:PRK07048  81 GNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 165 TAALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTP 244
Cdd:PRK07048 161 TAAKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 245 GAVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGLERFMEVMG 324
Cdd:PRK07048 241 GNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLS 320


                 .
gi 943672297 325 E 325
Cdd:PRK07048 321 G 321
 
Name Accession Description Interval E-value
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
5-325 1.76e-136

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 389.76  E-value: 1.76e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   5 TTTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSS 84
Cdd:PRK07048   1 SDLLLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  85 GNHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQG 164
Cdd:PRK07048  81 GNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 165 TAALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTP 244
Cdd:PRK07048 161 TAAKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 245 GAVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGLERFMEVMG 324
Cdd:PRK07048 241 GNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLS 320


                 .
gi 943672297 325 E 325
Cdd:PRK07048 321 G 321
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 12-314 1.15e-122

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: 354.10  E-value: 1.15e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  12 LDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAV 91
Cdd:cd01562    1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  92 ALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALELL 171
Cdd:cd01562   81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 172 EETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPGAVTFAI 251
Cdd:cd01562  161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 943672297 252 NQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNI 314
Cdd:cd01562  241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNI 303
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 6-325 1.85e-121

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: 352.03  E-value: 1.85e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   6 TTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSG 85
Cdd:COG1171    2 TALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  86 NHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGT 165
Cdd:COG1171   82 NHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 166 AALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPG 245
Cdd:COG1171  162 IALEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 246 AVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGLERFMEVMGE 325
Cdd:COG1171  242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEILER 321
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 29-316 2.74e-79

threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130197 [Multi-domain]  Cd Length: 380  Bit Score: 246.20  E-value: 2.74e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   29 TPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVMPA 108
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  109 DAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALELLEETGELDALLVPVGGGG 188
Cdd:TIGR01127  81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  189 LAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPGAVTFAINQRLLDGVLVVGDDELR 268
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 943672297  269 TAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGL 316
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDL 288
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 22-284 7.32e-58

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: 188.29  E-value: 7.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   22 IEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTS 101
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  102 AVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAE-RGLTLIPPYDHPRTIAGQGTAAL-ELLEETGELDA 179
Cdd:pfam00291  81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLeILEQLGGDPDA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  180 LLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADAL-TATTPGAVTFAINQRLLDG 258
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLgVGDEPGALALDLLDEYVGE 240

                         250       260
                  ....*....|....*....|....*.
gi 943672297  259 VLVVGDDELRTAMRFALERLKMLVEP 284
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEP 266
 
Name Accession Description Interval E-value
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
5-325 1.76e-136

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 389.76  E-value: 1.76e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   5 TTTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSS 84
Cdd:PRK07048   1 SDLLLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  85 GNHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQG 164
Cdd:PRK07048  81 GNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 165 TAALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTP 244
Cdd:PRK07048 161 TAAKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 245 GAVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGLERFMEVMG 324
Cdd:PRK07048 241 GNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLS 320


                 .
gi 943672297 325 E 325
Cdd:PRK07048 321 G 321
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 12-314 1.15e-122

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: 354.10  E-value: 1.15e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  12 LDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAV 91
Cdd:cd01562    1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  92 ALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALELL 171
Cdd:cd01562   81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 172 EETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPGAVTFAI 251
Cdd:cd01562  161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 943672297 252 NQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNI 314
Cdd:cd01562  241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNI 303
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 6-325 1.85e-121

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: 352.03  E-value: 1.85e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   6 TTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSG 85
Cdd:COG1171    2 TALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  86 NHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGT 165
Cdd:COG1171   82 NHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 166 AALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPG 245
Cdd:COG1171  162 IALEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 246 AVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGLERFMEVMGE 325
Cdd:COG1171  242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEILER 321
PLN02970 PLN02970
serine racemase
 10-322 8.37e-106

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 312.38  E-value: 8.37e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  10 LTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQ 89
Cdd:PLN02970   9 ADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  90 AVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALE 169
Cdd:PLN02970  89 ALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 170 LLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTpGAVTF 249
Cdd:PLN02970 169 FLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRASL-GDLTW 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 943672297 250 AINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPA-----RVGVIISGGNIGLERFMEV 322
Cdd:PLN02970 248 PVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkgckNVGIVLSGGNVDLGVLWES 325
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
5-324 1.26e-80

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 248.11  E-value: 1.26e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   5 TTTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSS 84
Cdd:PRK08638   4 TYDLPVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  85 GNHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQG 164
Cdd:PRK08638  84 GNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 165 TAALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTP 244
Cdd:PRK08638 164 TIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 245 GAVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPL--PARVGVIISGGNIGLERFMEV 322
Cdd:PRK08638 244 GNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYiqNKKVVAIISGGNVDLSRVSQI 323


                 ..
gi 943672297 323 MG 324
Cdd:PRK08638 324 TG 325
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 29-316 2.74e-79

threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130197 [Multi-domain]  Cd Length: 380  Bit Score: 246.20  E-value: 2.74e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   29 TPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVMPA 108
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  109 DAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALELLEETGELDALLVPVGGGG 188
Cdd:TIGR01127  81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  189 LAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPGAVTFAINQRLLDGVLVVGDDELR 268
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 943672297  269 TAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGL 316
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDL 288
PRK07334 PRK07334
threonine dehydratase; Provisional
 6-314 8.04e-75

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 235.56  E-value: 8.04e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   6 TTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSG 85
Cdd:PRK07334   1 AGLMVTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  86 NHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTY-DRYTENReAIGEKIAAERGLTLIPPYDHPRTIAGQG 164
Cdd:PRK07334  81 NHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHgETLDEAR-AHARELAEEEGLTFVHPYDDPAVIAGQG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 165 TAALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGER-VGGEvprTIADALTATT 243
Cdd:PRK07334 160 TVALEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKGVALpCGGS---TIAEGIAVKQ 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 943672297 244 PGAVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNI 314
Cdd:PRK07334 237 PGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNI 307
PRK06815 PRK06815
threonine/serine dehydratase;
12-323 3.83e-74

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 231.12  E-value: 3.83e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  12 LDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAV 91
Cdd:PRK06815   4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  92 ALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALELL 171
Cdd:PRK06815  84 ALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 172 EETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADAlTA--TTPGAVTF 249
Cdd:PRK06815 164 EQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDG-TAggVEPGAITF 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 943672297 250 AINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGLERFMEVM 323
Cdd:PRK06815 243 PLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKYLEAV 316
eutB PRK07476
threonine dehydratase; Provisional
 10-325 1.22e-70

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 222.15  E-value: 1.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  10 LTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQ 89
Cdd:PRK07476   1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  90 AVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALE 169
Cdd:PRK07476  81 ALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 170 LLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATT--PGAV 247
Cdd:PRK07476 161 ILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADSLGGGIglDNRY 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 943672297 248 TFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGLERFMEVMGE 325
Cdd:PRK07476 241 TFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELHRRIING 318
ilvA_2Cterm TIGR01124
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ...
 16-284 3.93e-60

threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130194 [Multi-domain]  Cd Length: 499  Bit Score: 199.96  E-value: 3.93e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   16 RAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAVALAA 95
Cdd:TIGR01124   5 AILTARVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   96 REFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALE-LLEET 174
Cdd:TIGR01124  85 ARLGLKALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEiLRQVA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  175 GELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPGAVTFAINQR 254
Cdd:TIGR01124 165 NPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQ 244

                         250       260       270
                  ....*....|....*....|....*....|
gi 943672297  255 LLDGVLVVGDDELRTAMRFALERLKMLVEP 284
Cdd:TIGR01124 245 YLDDIVTVDTDEVCAAIKDLFEDTRAVAEP 274
PRK08639 PRK08639
threonine dehydratase; Validated
 5-323 6.64e-58

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 192.33  E-value: 6.64e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   5 TTTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSS 84
Cdd:PRK08639   2 TVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  85 GNHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIV-------TYDR-YTENREaigekIAAERGLTLIPPYDH 156
Cdd:PRK08639  82 GNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFVeivlvgdTFDDsAAAAQE-----YAEETGATFIPPFDD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 157 PRTIAGQGTAAL---ELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPR 233
Cdd:PRK08639 157 PDVIAGQGTVAVeilEQLEKEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKID 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 234 TIADALTATTPGAVTFAINQRLLDGVLVVGDDELRTAMrfalerLKML------VEPGGAAGLAALLADRVDPLPARVGV 307
Cdd:PRK08639 237 KFVDGAAVARVGDLTFEILKDVVDDVVLVPEGAVCTTI------LELYnkegivAEPAGALSIAALELYKDEIKGKTVVC 310

                        330
                 ....*....|....*.
gi 943672297 308 IISGGNIGLERFMEVM 323
Cdd:PRK08639 311 VISGGNNDIERMPEIK 326
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 22-284 7.32e-58

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: 188.29  E-value: 7.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   22 IEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTS 101
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  102 AVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAE-RGLTLIPPYDHPRTIAGQGTAAL-ELLEETGELDA 179
Cdd:pfam00291  81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLeILEQLGGDPDA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  180 LLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADAL-TATTPGAVTFAINQRLLDG 258
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLgVGDEPGALALDLLDEYVGE 240

                         250       260
                  ....*....|....*....|....*.
gi 943672297  259 VLVVGDDELRTAMRFALERLKMLVEP 284
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEP 266
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
20-284 3.82e-56

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 189.58  E-value: 3.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  20 ARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAVALAAREFG 99
Cdd:PRK09224  12 ARVYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 100 TSAVIVMPADAPTAKLDATAGYGAEIVTY-DRYTE-NREAIgeKIAAERGLTLIPPYDHPRTIAGQGTAAL-ELLEETGE 176
Cdd:PRK09224  92 IKAVIVMPVTTPDIKVDAVRAFGGEVVLHgDSFDEaYAHAI--ELAEEEGLTFIHPFDDPDVIAGQGTIAMeILQQHPHP 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 177 LDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVggEVPRT--IADALTATTPGAVTFAINQR 254
Cdd:PRK09224 170 LDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERV--DLPQVglFADGVAVKRIGEETFRLCQE 247

                        250       260       270
                 ....*....|....*....|....*....|
gi 943672297 255 LLDGVLVVGDDELRTAMRFALERLKMLVEP 284
Cdd:PRK09224 248 YVDDVITVDTDEICAAIKDVFEDTRSIAEP 277
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 10-323 4.32e-55

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: 181.97  E-value: 4.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   10 LTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQ 89
Cdd:TIGR02991   1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   90 AVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALE 169
Cdd:TIGR02991  81 ALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  170 LLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATT--PGAV 247
Cdd:TIGR02991 161 VVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLGGGIglDNRV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 943672297  248 TFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDpLPARVGVIISGGNIGLERFMEVM 323
Cdd:TIGR02991 241 TFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIK-NPGPCAVIVSGRNIDMDLHKRII 315
PRK12483 PRK12483
threonine dehydratase; Reviewed
 3-284 9.40e-54

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 183.84  E-value: 9.40e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   3 DETTTPSLTLDDV--RAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVV 80
Cdd:PRK12483  10 TTIAPRAALLADYlrKILAARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  81 ACSSGNHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTI 160
Cdd:PRK12483  90 TASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 161 AGQGT-AALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVggEVPR--TIAD 237
Cdd:PRK12483 170 AGQGTvAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERV--VLGQvgLFAD 247

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 943672297 238 ALTATTPGAVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEP 284
Cdd:PRK12483 248 GVAVAQIGEHTFELCRHYVDEVVTVSTDELCAAIKDIYDDTRSITEP 294
PRK08246 PRK08246
serine/threonine dehydratase;
6-314 5.09e-53

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 176.30  E-value: 5.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   6 TTPSLTLDDVRAAAARIEGAVHRTPVVRSRTLDrLVGAEVHLKCENLQRIGAFKFRGAYNWLvqLTPEQRQRGVVACSSG 85
Cdd:PRK08246   1 AHAMITRSDVRAAAQRIAPHIRRTPVLEADGAG-FGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  86 NHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIV-TYDRYTENREAiGEKIAAERGLTLIPPYDHPRTIAGQG 164
Cdd:PRK08246  78 NAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVvVGAEYADALEA-AQAFAAETGALLCHAYDQPEVLAGAG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 165 TAALELLEETGELDALLVPVGGGGLAAGcatVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTP 244
Cdd:PRK08246 157 TLGLEIEEQAPGVDTVLVAVGGGGLIAG---IAAWFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRV 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 943672297 245 GAVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPA-RVGVIISGGNI 314
Cdd:PRK08246 234 GEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGeRVAVVLCGANT 304
PRK06608 PRK06608
serine/threonine dehydratase;
8-314 9.66e-53

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 176.50  E-value: 9.66e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   8 PSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTpEQRQR--GVVACSSG 85
Cdd:PRK06608   3 LLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELK-EQGKLpdKIVAYSTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  86 NHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIgeKIAAERGLTLIPPYDHPRTIAGQGT 165
Cdd:PRK06608  82 NHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKA--KEDEEQGFYYIHPSDSDSTIAGAGT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 166 AALEL-LEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVG-GEVPRTIADALTATT 243
Cdd:PRK06608 160 LCYEAlQQLGFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRlNYSPNTIADGLKTLS 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 943672297 244 PGAVTFAINQRLLDGVLVvgdDELRTA--MRFALERLKMLVEPGGAAGLAALladrVDPL-----PARVGVIISGGNI 314
Cdd:PRK06608 240 VSARTFEYLKKLDDFYLV---EEYEIYywTAWLTHLLKVICEPSSAINMVAV----VNWLktqskPQKLLVILSGGNI 310
PLN02550 PLN02550
threonine dehydratase
 29-284 1.42e-45

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 163.17  E-value: 1.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  29 TPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVMPA 108
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMPV 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 109 DAPTAKLDATAGYGAEIVTY-DRYTENrEAIGEKIAAERGLTLIPPYDHPRTIAGQGTAALELLEETGE-LDALLVPVGG 186
Cdd:PLN02550 190 TTPEIKWQSVERLGATVVLVgDSYDEA-QAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGpLHAIFVPVGG 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 187 GGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPGAVTFAINQRLLDGVLVVGDDE 266
Cdd:PLN02550 269 GGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSRDA 348

                        250
                 ....*....|....*...
gi 943672297 267 LRTAMRFALERLKMLVEP 284
Cdd:PLN02550 349 ICASIKDMFEEKRSILEP 366
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 29-284 5.24e-42

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: 145.74  E-value: 5.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  29 TPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRG--VVACSSGNHAQAVALAAREFGTSAVIVM 106
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 107 PADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAER-GLTLIPPYDHPRTIAGQGTAAL--ELLEETGELDALLVP 183
Cdd:cd00640   81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLeiLEQLGGQKPDAVVVP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 184 VGGGGLAAGCATVAKSLHPGMRVLGVEPEagddtarslaagervggevprtiadaltattpgavtfainqrlldgVLVVG 263
Cdd:cd00640  161 VGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------------------VVTVS 194

                        250       260
                 ....*....|....*....|.
gi 943672297 264 DDELRTAMRFALERLKMLVEP 284
Cdd:cd00640  195 DEEALEAIRLLAREEGILVEP 215
PRK06110 PRK06110
threonine dehydratase;
8-324 6.06e-38

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 137.43  E-value: 6.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   8 PSLTLDDVRAAAARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQ-RGVVACSSGN 86
Cdd:PRK06110   1 MMFTLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRvRGVISATRGN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  87 HAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTY-DRYTENREAIGEkIAAERGLTLIPPYdHPRTIAGQGT 165
Cdd:PRK06110  81 HGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHgEDFQAAREEAAR-LAAERGLHMVPSF-HPDLVRGVAT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 166 AALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPG 245
Cdd:PRK06110 159 YALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPD 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 943672297 246 AVTFAINQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAAGLAALLADRVDPLPARVGVIISGGNIGLERFMEVMG 324
Cdd:PRK06110 239 PEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVFARVLA 317
PRK08813 PRK08813
threonine dehydratase; Provisional
 9-276 4.12e-33

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 125.12  E-value: 4.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   9 SLTLDDVRAAAARIEGAVHRTPVVRSRTLDrlvgaeVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVACSSGNHA 88
Cdd:PRK08813  20 AVSVADVLAAQARLRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  89 QAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAAl 168
Cdd:PRK08813  94 QGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVG- 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 169 eLLEETGELDALLVPVGGGGLAAGCATVAKSlhPGMRVLGVEPEAGDDTARSLAAGERVGGEVPrTIADALTATTPGAVT 248
Cdd:PRK08813 173 -IELAAHAPDVVIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARAIRGDLREIAPVA-TLADGVKVKIPGFLT 248

                        250       260
                 ....*....|....*....|....*....
gi 943672297 249 FAINQRLLDGVLVVGDDELR-TAMRFALE 276
Cdd:PRK08813 249 RRLCSSLLDDVVIVREAELReTLVRLALE 277
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 29-284 1.63e-22

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: 95.44  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  29 TPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQLT--PEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVM 106
Cdd:cd06448    2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAkqGLNECVHVVCSSGGNAGLAAAYAARKLGVPCTIVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 107 PADAPTAKLDATAGYGAE-IVTYDRYTENREAIGEKIAA-ERGLTLIPPYDHPRTIAGQGT---AALELLEETGELDALL 181
Cdd:cd06448   82 PESTKPRVVEKLRDEGATvVVHGKVWWEADNYLREELAEnDPGPVYVHPFDDPLIWEGHSSmvdEIAQQLQSQEKVDAIV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 182 VPVGGGGLAAGcatVAKSL--HPGMR--VLGVEPEAGDDTARSLAAGERVGGEVPRTIADALTATTPGAVTFAINQRLLD 257
Cdd:cd06448  162 CSVGGGGLLNG---IVQGLerNGWGDipVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNI 238

                        250       260
                 ....*....|....*....|....*...
gi 943672297 258 GVLVVGD-DELRTAMRFALERlKMLVEP 284
Cdd:cd06448  239 KSEVVSDrDAVQACLRFADDE-RILVEP 265
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 29-284 2.43e-13

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: 69.54  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  29 TPVVRSRTL-DRLVGAEVHLKCENLQRIGAFKFRGAYnWLVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVMP 107
Cdd:cd01563   23 TPLVRAPRLgERLGGKNLYVKDEGLNPTGSFKDRGMT-VAVSKAKELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 108 ADAPTAKLDATAGYGAEIV----TYDRYTEnreaIGEKIAAERGLTLIpPYDHPRTIAGQGTAA--LELLEETGELDALL 181
Cdd:cd01563  102 AGKALGKLAQALAYGATVLavegNFDDALR----LVRELAEENWIYLS-NSLNPYRLEGQKTIAfeIAEQLGWEVPDYVV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 182 VPVGGGGLAAGCATVAKSLH--------PgmRVLGVEPEAGDDTARSLAAG----ERVggEVPRTIADALTATTPGAVTF 249
Cdd:cd01563  177 VPVGNGGNITAIWKGFKELKelglidrlP--RMVGVQAEGAAPIVRAFKEGkddiEPV--ENPETIATAIRIGNPASGPK 252

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 943672297 250 AIN-QRLLDGVLV-VGDDELRTAMRFALERLKMLVEP 284
Cdd:cd01563  253 ALRaVRESGGTAVaVSDEEILEAQKLLARTEGIFVEP 289
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 29-167 1.54e-11

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: 64.45  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  29 TPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAynwlvQLTPE---QRQRGVVAC-SSGNHAQAVALAAREFGTSAVI 104
Cdd:COG0498   67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAM-----QVAVSlalERGAKTIVCaSSGNGSAALAAYAARAGIEVFV 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 943672297 105 VMPAD-APTAKLDATAGYGAEIV----TYDRytenREAIGEKIAAERGLTLIPPYdHPRTIAGQGTAA 167
Cdd:COG0498  142 FVPEGkVSPGQLAQMLTYGAHVIavdgNFDD----AQRLVKELAADEGLYAVNSI-NPARLEGQKTYA 204
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 28-126 1.35e-09

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: 58.29  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  28 RTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQ------LTPEQRqrgVVACSSGNHAQAVALAAREFGTS 101
Cdd:cd01561    2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDaekrglLKPGTT---IIEPTSGNTGIGLAMVAAAKGYR 78

                         90       100
                 ....*....|....*....|....*
gi 943672297 102 AVIVMPADAPTAKLDATAGYGAEIV 126
Cdd:cd01561   79 FIIVMPETMSEEKRKLLRALGAEVI 103
PRK08329 PRK08329
threonine synthase; Validated
 29-184 1.99e-08

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 54.83  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  29 TPVVRsrtldrlVGAEVHLKCENLQRIGAFKFRGAYNWLVQLTpEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVMPA 108
Cdd:PRK08329  65 TPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKLK-EEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSY 136

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 943672297 109 DAPTAKLDATAGYGAEI--VTYDRYTENREAIgeKIAAERGLTLIPPYDHPRTIAGQGTAALELLEETGELDALLVPV 184
Cdd:PRK08329 137 NASKEKISLLSRLGAELhfVEGDRMEVHEEAV--KFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPV 212
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 79-151 1.19e-07

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 52.57  E-value: 1.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 943672297  79 VVACSS-GNHAQAVALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIV----TYDRYTenREAIgeKIAAERGLTLI 151
Cdd:PRK08206 118 TFATATdGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIitdgNYDDSV--RLAA--QEAQENGWVVV 191
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 19-126 3.53e-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: 50.82  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  19 AARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQ------LTPEQRqrgVVACSSGNHAQAVA 92
Cdd:COG0031    4 YDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDaekrglLKPGGT---IVEATSGNTGIGLA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 943672297  93 LAAREFGTSAVIVMPADAPTAKLDATAGYGAEIV 126
Cdd:COG0031   81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVV 114
PRK05638 PRK05638
threonine synthase; Validated
 29-167 5.11e-07

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 50.97  E-value: 5.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  29 TPVVRSRTLDRLvGAEVHLKCENLQRIGAFKFRGAYNWLVQLTPEQRQRGVVAcSSGNHAQAVALAAREFGTSAVIVMPA 108
Cdd:PRK05638  67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVA-SDGNAAASVAAYSARAGKEAFVVVPR 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 943672297 109 DAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLTLIPPYDHPRTIAGQGTAA 167
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIA 203
PRK06381 PRK06381
threonine synthase; Validated
 28-155 3.08e-06

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 48.16  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  28 RTPVVRSRTLDRLVG-AEVHLKCENLQRIGAFKFRGAYNWlVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVM 106
Cdd:PRK06381  15 GTPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAH-VRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFI 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 943672297 107 PADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGLtlippYD 155
Cdd:PRK06381  94 PRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGI-----YD 137
cysM PRK11761
cysteine synthase CysM;
22-126 4.56e-06

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 47.56  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  22 IEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNWLVQltPEQRQR-----GVVACSSGNHAQAVALAAR 96
Cdd:PRK11761   6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQ--AEKRGEikpgdTLIEATSGNTGIALAMIAA 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 943672297  97 EFGTSAVIVMPADAPTAKLDATAGYGAEIV 126
Cdd:PRK11761  84 IKGYRMKLIMPENMSQERRAAMRAYGAELI 113
PRK08197 PRK08197
threonine synthase; Validated
 29-272 6.51e-05

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 44.22  E-value: 6.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  29 TPVVRSRTLDRLVGA-EVHLKCENLQRIGAFKFRGAyNWLVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVMP 107
Cdd:PRK08197  80 TPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGL-AVGVSRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMP 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 108 ADAPTAKLDATAGYGAEIVTYDRYTENREAIGEKIAAERGL----TLIPPYdhprTIAGQGTAALELLEET--GELDALL 181
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWfdvsTLKEPY----RIEGKKTMGLELAEQLgwRLPDVIL 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 182 VPVGGgglaagcatvakslhpGMRVLGVEpEAGDDtarsLAAGERVGGEVPRTIA----------DALTATT------PG 245
Cdd:PRK08197 235 YPTGG----------------GVGLIGIW-KAFDE----LEALGWIGGKRPRLVAvqaegcapivKAWEEGKeesefwED 293

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 943672297 246 AVTFAINQR---------LLDGV-------LVVGDDELRTAMR 272
Cdd:PRK08197 294 AHTVAFGIRvpkalgdflVLDAVretggcaIAVSDDAILAAQR 336
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 22-126 1.11e-04

cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273463  Cd Length: 299  Bit Score: 43.04  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   22 IEGAVHRTPVVRsrtLDRLV---GAEVHLKCENLQRIGAFKFRGAYNWLVQltPEQR---QRG--VVACSSGNHAQAVAL 93
Cdd:TIGR01136   1 IEELIGNTPLVR---LNRLApgcDARVLAKLEGFNPSGSVKDRIALSMILD--AEKRgllKPGdtIIEATSGNTGIALAM 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 943672297   94 AAREFGTSAVIVMPADAPTAKLDATAGYGAEIV 126
Cdd:TIGR01136  76 VAAARGYKLILTMPETMSLERRKLLRAYGAELI 108
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 28-276 1.65e-04

cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273465  Cd Length: 298  Bit Score: 42.74  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   28 RTPVVRsrtLDRLVG--AEVHLKCENLQRIGAFKFRGAYNwlvqLTPEQRQRGV-------VACSSGNHAQAVALAAREF 98
Cdd:TIGR01139   7 NTPLVR---LNRIEGcnANVFVKLEGRNPSGSVKDRIALN----MIWDAEKRGLlkpgktiVEPTSGNTGIALAMVAAAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   99 GTSAVIVMPADAPTAKLDATAGYGAEIVTYDRYTENREAI--GEKIAAERGLTLIPP--YDHPRT--IAGQGTAALELLE 172
Cdd:TIGR01139  80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIakAEEIAASTPNSYFMLqqFENPANpeIHRKTTGPEIWRD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  173 ETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPeagddtARS--LAAGERvGgevprtiADALTATTPGAVTFA 250
Cdd:TIGR01139 160 TDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEP------AESpvLSGGKP-G-------PHKIQGIGAGFIPKN 225

                         250       260
                  ....*....|....*....|....*..
gi 943672297  251 INQRLLDGVLVVGDDE-LRTAMRFALE 276
Cdd:TIGR01139 226 LNRSVIDEVITVSDEEaIETARRLAAE 252
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 28-288 2.66e-04

threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 41.98  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297   28 RTPVVRSRTLDRLVGA-EVHLKCENLQRIGAFKFRGaynwLVQLTPEQRQRG--VVAC-SSGNHAQAVALAAREFGTSAV 103
Cdd:TIGR00260  22 VTPLFRAPALAANVGIkNLYVKELGHNPTLSFKDRG----MAVALTKALELGndTVLCaSTGNTGAAAAAYAGKAGLKVV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  104 IVMPADAPTA-KLDATAGYGAEIVTYDRYTENREAIGEKIAAER-GLTLIPPYDHPRTIAGQGTAA--LELLEETGELDA 179
Cdd:TIGR00260  98 VLYPAGKISLgKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKpALGLNSANSIPYRLEGQKTYAfeAVEQLGWEAPDK 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  180 LLVPVGGG-------GLAAGCATVAKSLHPGMRvlGVEPEAGDDTARS-LAAGERVGGEVPRTIADALTATTPGAVTFA- 250
Cdd:TIGR00260 178 VVVPVPNSgnfgaiwKGFKEKKMLGLDSLPVKR--GIQAEGAADIVRAfLEGGQWEPIETPETLSTAMDIGNPANWPRAl 255

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 943672297  251 -INQRLLDGVLVVGDDELRTAMRFALERLKMLVEPGGAA 288
Cdd:TIGR00260 256 eAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAV 294
PLN02356 PLN02356
phosphateglycerate kinase
 25-125 3.14e-04

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 42.29  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  25 AVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAynwlVQLTPEQRQRGVVAC-------SSGNHAQAVALAARE 97
Cdd:PLN02356  50 AIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVA----VKIIEEALESGQLFPggvvtegSAGSTAISLATVAPA 125

                         90       100
                 ....*....|....*....|....*...
gi 943672297  98 FGTSAVIVMPADAPTAKLDATAGYGAEI 125
Cdd:PLN02356 126 YGCKCHVVIPDDVAIEKSQILEALGATV 153
PRK06450 PRK06450
threonine synthase; Validated
 28-146 4.81e-04

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 41.26  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  28 RTPVVRsrtldrlvGAEVHLKCENLQRIGAFKFRGAYNwLVQLTPEQRQRGVVACSSGNHAQAVALAAREFGTSAVIVMP 107
Cdd:PRK06450  58 RTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVT-LISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVP 128

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 943672297 108 ADAPTAKLDATAGYGAEIVtydRYTENREAIgeKIAAER 146
Cdd:PRK06450 129 ETASGGKLKQIESYGAEVV---RVRGSREDV--AKAAEN 162
PRK10717 PRK10717
cysteine synthase A; Provisional
 24-129 4.06e-03

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 38.30  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  24 GAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYnWLVQltpEQRQRG-------VVACSSGNHAQAVALAAR 96
Cdd:PRK10717   9 DTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAAL-NIIW---DAEKRGllkpggtIVEGTAGNTGIGLALVAA 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 943672297  97 EFGTSAVIVMPADAPTAKLDATAGYGAEIVTYD 129
Cdd:PRK10717  85 ARGYKTVIVMPETQSQEKKDLLRALGAELVLVP 117
PLN03013 PLN03013
cysteine synthase
 19-276 7.64e-03

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 37.83  E-value: 7.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  19 AARIEGAVHRTPVVRSRTLDRLVGAEVHLKCENLQRIGAFKFRGAYNwlvqLTPEQRQRG--------VVACSSGNHAQA 90
Cdd:PLN03013 114 ADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYS----MVTDAEQKGfispgksvLVEPTSGNTGIG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297  91 VALAAREFGTSAVIVMPADAPTAKLDATAGYGAEIVTYDrytENREAIGEKIAAERGLTLIP------PYDHPRT--IAG 162
Cdd:PLN03013 190 LAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTD---PAKGMTGAVQKAEEILKNTPdaymlqQFDNPANpkIHY 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943672297 163 QGTAALELLEETGELDALLVPVGGGGLAAGCATVAKSLHPGMRVLGVEPEAGDdtarsLAAGERVGgevPRTIadalTAT 242
Cdd:PLN03013 267 ETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESD-----ILSGGKPG---PHKI----QGI 334

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 943672297 243 TPGAVTFAINQRLLDGVLVVGDDE-LRTAMRFALE 276
Cdd:PLN03013 335 GAGFIPKNLDQKIMDEVIAISSEEaIETAKQLALK 369
 
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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