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Conserved domains on  [gi|517597650|ref|WP_018767858|]
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MULTISPECIES: bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB [Bacillus]

Protein Classification

threonine/serine dehydratase( domain architecture ID 10793105)

serine/threonine dehydratase deaminates L-threonine or L-serine to form 2-oxobutanoate or pyruvate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
1-330 0e+00

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


:

Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 532.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   1 MINKNLPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIAC 80
Cdd:PRK08638   2 HITYDLPVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVAC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  81 SAGNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAG 160
Cdd:PRK08638  82 SAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 161 QGTIGLDILDDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVK 240
Cdd:PRK08638 162 QGTIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 241 IPGDLTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVDLKRIS 320
Cdd:PRK08638 242 RPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVDLSRVS 321
                        330
                 ....*....|
gi 517597650 321 SVCEHFFVAN 330
Cdd:PRK08638 322 QITGHVVAAD 331
 
Name Accession Description Interval E-value
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
1-330 0e+00

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 532.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   1 MINKNLPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIAC 80
Cdd:PRK08638   2 HITYDLPVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVAC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  81 SAGNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAG 160
Cdd:PRK08638  82 SAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 161 QGTIGLDILDDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVK 240
Cdd:PRK08638 162 QGTIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 241 IPGDLTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVDLKRIS 320
Cdd:PRK08638 242 RPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVDLSRVS 321
                        330
                 ....*....|
gi 517597650 321 SVCEHFFVAN 330
Cdd:PRK08638 322 QITGHVVAAD 331
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
10-315 1.04e-142

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: 405.33  E-value: 1.04e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  10 IGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGV 89
Cdd:cd01562    1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  90 ALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDIL 169
Cdd:cd01562   81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 170 DDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEI 249
Cdd:cd01562  161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517597650 250 VKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQytKGKKVVAVISGGNVD 315
Cdd:cd01562  241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL--KGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
6-329 7.66e-134

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: 383.62  E-value: 7.66e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   6 LPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNH 85
Cdd:COG1171    4 LMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  86 AQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIG 165
Cdd:COG1171   84 AQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 166 LDILDDMWDVDTVivpiggggiisgiAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDL 245
Cdd:COG1171  164 LEILEQLPDLDAVfvpvggggliagvAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGEL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 246 TFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVE----------GAGALATaallagkvdqytKGKKVVAVISGGNVD 315
Cdd:COG1171  244 TFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEpagaaalaalLAGKERL------------KGKRVVVVLSGGNID 311
                        330
                 ....*....|....
gi 517597650 316 LKRISSVCEHFFVA 329
Cdd:COG1171  312 PDRLAEILERGLVG 325
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
27-322 1.34e-112

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: 331.71  E-value: 1.34e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   27 TPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALSSHLLGIKSKIVMPI 106
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  107 SAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDILDDMWDVDTVIVPIGGGG 186
Cdd:TIGR01127  81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  187 IISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEIVKELVDDIVTVSEEELE 266
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 517597650  267 VAMKDLLQRGKAVVEGAGALATAALLAGKVDQytKGKKVVAVISGGNVDLKRISSV 322
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDV--KGKKIAVVLSGGNIDLNLLNKI 294
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
20-311 6.47e-70

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: 219.87  E-value: 6.47e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   20 LSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALSSHLLGIK 99
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  100 SKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGE-TYLHPYDDVEVMAGQGTIGLDILDDMW-DVDT 177
Cdd:pfam00291  81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLGgDPDA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  178 VIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKI-PGDLTFEIVKELVDD 256
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDePGALALDLLDEYVGE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 517597650  257 IVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISG 311
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
1-330 0e+00

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 532.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   1 MINKNLPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIAC 80
Cdd:PRK08638   2 HITYDLPVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVAC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  81 SAGNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAG 160
Cdd:PRK08638  82 SAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 161 QGTIGLDILDDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVK 240
Cdd:PRK08638 162 QGTIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 241 IPGDLTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVDLKRIS 320
Cdd:PRK08638 242 RPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAIISGGNVDLSRVS 321
                        330
                 ....*....|
gi 517597650 321 SVCEHFFVAN 330
Cdd:PRK08638 322 QITGHVVAAD 331
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
10-315 1.04e-142

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: 405.33  E-value: 1.04e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  10 IGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGV 89
Cdd:cd01562    1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  90 ALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDIL 169
Cdd:cd01562   81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 170 DDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEI 249
Cdd:cd01562  161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517597650 250 VKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQytKGKKVVAVISGGNVD 315
Cdd:cd01562  241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL--KGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
6-329 7.66e-134

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: 383.62  E-value: 7.66e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   6 LPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNH 85
Cdd:COG1171    4 LMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  86 AQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIG 165
Cdd:COG1171   84 AQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 166 LDILDDMWDVDTVivpiggggiisgiAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDL 245
Cdd:COG1171  164 LEILEQLPDLDAVfvpvggggliagvAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGEL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 246 TFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVE----------GAGALATaallagkvdqytKGKKVVAVISGGNVD 315
Cdd:COG1171  244 TFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEpagaaalaalLAGKERL------------KGKRVVVVLSGGNID 311
                        330
                 ....*....|....
gi 517597650 316 LKRISSVCEHFFVA 329
Cdd:COG1171  312 PDRLAEILERGLVG 325
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
27-322 1.34e-112

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: 331.71  E-value: 1.34e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   27 TPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALSSHLLGIKSKIVMPI 106
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  107 SAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDILDDMWDVDTVIVPIGGGG 186
Cdd:TIGR01127  81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  187 IISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEIVKELVDDIVTVSEEELE 266
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 517597650  267 VAMKDLLQRGKAVVEGAGALATAALLAGKVDQytKGKKVVAVISGGNVDLKRISSV 322
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDV--KGKKIAVVLSGGNIDLNLLNKI 294
PRK07334 PRK07334
threonine dehydratase; Provisional
6-324 1.11e-96

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 291.80  E-value: 1.11e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   6 LPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNH 85
Cdd:PRK07334   3 LMVTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  86 AQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIG 165
Cdd:PRK07334  83 AQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 166 LDILDDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASydvgkiVSHYEAP----TIADGCAVKI 241
Cdd:PRK07334 163 LEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAA------IKGVALPcggsTIAEGIAVKQ 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 242 PGDLTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKvdQYTKGKKVVAVISGGNVDLKRISS 321
Cdd:PRK07334 237 PGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYP--ERFRGRKVGLVLSGGNIDTRLLAN 314

                 ...
gi 517597650 322 VCE 324
Cdd:PRK07334 315 VLL 317
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
24-324 5.11e-91

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 280.49  E-value: 5.11e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  24 ARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALSSHLLGIKSKIV 103
Cdd:PRK09224  18 AQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 104 MPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDILDDMWD-VDTVIVPI 182
Cdd:PRK09224  98 MPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAVFVPV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 183 GGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEIVKELVDDIVTVSE 262
Cdd:PRK09224 178 GGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDT 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517597650 263 EELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVDLKRISSVCE 324
Cdd:PRK09224 258 DEICAAIKDVFEDTRSIAEPAGALALAGLKKYVAQHGIEGETLVAILSGANMNFDRLRYVAE 319
ilvA_2Cterm TIGR01124
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ...
24-324 7.42e-91

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: 280.08  E-value: 7.42e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   24 ARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALSSHLLGIKSKIV 103
Cdd:TIGR01124  15 AQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGLKALIV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  104 MPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDIL-DDMWDVDTVIVPI 182
Cdd:TIGR01124  95 MPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILrQVANPLDAVFVPV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  183 GGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEIVKELVDDIVTVSE 262
Cdd:TIGR01124 175 GGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDIVTVDT 254
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517597650  263 EELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVDLKRISSVCE 324
Cdd:TIGR01124 255 DEVCAAIKDLFEDTRAVAEPAGALALAGLKKYVALHGIRGQTLVAILSGANMNFHRLRYVSE 316
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
6-321 3.25e-86

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 262.26  E-value: 3.25e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   6 LPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNH 85
Cdd:PRK07048   4 LLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  86 AQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIG 165
Cdd:PRK07048  84 AQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 166 LDILDDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVsHYEAP-TIADGCAVKIPGD 244
Cdd:PRK07048 164 KELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIV-HIDTPrTIADGAQTQHLGN 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517597650 245 LTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDqyTKGKKVVAVISGGNVDLKRISS 321
Cdd:PRK07048 243 YTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVP--LKGKRVGVIISGGNVDLARFAA 317
PRK06815 PRK06815
threonine/serine dehydratase;
13-323 1.18e-85

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 260.78  E-value: 1.18e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  13 IKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALS 92
Cdd:PRK06815   7 ILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  93 SHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDILDDM 172
Cdd:PRK06815  87 AKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 173 WDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKI-PGDLTFEIVK 251
Cdd:PRK06815 167 PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAGGVePGAITFPLCQ 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517597650 252 ELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKvDQYtKGKKVVAVISGGNVDLKRISSVC 323
Cdd:PRK06815 247 QLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLA-PRY-QGKKVAVVLCGKNIVLEKYLEAV 316
PRK08639 PRK08639
threonine dehydratase; Validated
3-330 2.99e-84

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 260.51  E-value: 2.99e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   3 NKNLPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSA 82
Cdd:PRK08639   2 TVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  83 GNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGS---EVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMA 159
Cdd:PRK08639  82 GNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 160 GQGTIGLDILDDM---WDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADG 236
Cdd:PRK08639 162 GQGTVAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 237 CAVKIPGDLTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKvdQYTKGKKVVAVISGGNVDL 316
Cdd:PRK08639 242 AAVARVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYK--DEIKGKTVVCVISGGNNDI 319
                        330       340
                 ....*....|....*....|...
gi 517597650 317 KRISSVCE---------HFFVAN 330
Cdd:PRK08639 320 ERMPEIKErsliyeglkHYFIVN 342
PLN02970 PLN02970
serine racemase
1-319 2.95e-82

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 252.29  E-value: 2.95e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   1 MINKNLPLNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIAC 80
Cdd:PLN02970   2 AASEKYAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  81 SAGNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAG 160
Cdd:PLN02970  82 SSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 161 QGTIGLDILDDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVK 240
Cdd:PLN02970 162 QGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 241 IpGDLTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKV---DQYTKGKKVVAVISGGNVDLK 317
Cdd:PLN02970 242 L-GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFrsnPAWKGCKNVGIVLSGGNVDLG 320

                 ..
gi 517597650 318 RI 319
Cdd:PLN02970 321 VL 322
eutB PRK07476
threonine dehydratase; Provisional
8-317 1.68e-78

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 242.56  E-value: 1.68e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   8 LNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQ 87
Cdd:PRK07476   1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  88 GVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLD 167
Cdd:PRK07476  81 ALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 168 ILDDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIAD--GCAVKIPGDL 245
Cdd:PRK07476 161 ILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADslGGGIGLDNRY 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517597650 246 TFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDqyTKGKKVVAVISGGNVDLK 317
Cdd:PRK07476 241 TFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIA--ARDGPIVVVVSGANIDME 310
PRK12483 PRK12483
threonine dehydratase; Reviewed
24-324 3.51e-78

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 248.17  E-value: 3.51e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  24 ARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALSSHLLGIKSKIV 103
Cdd:PRK12483  35 ARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 104 MPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDIL-DDMWDVDTVIVPI 182
Cdd:PRK12483 115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILrQHPGPLDAIFVPV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 183 GGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEIVKELVDDIVTVSE 262
Cdd:PRK12483 195 GGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVDEVVTVST 274
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517597650 263 EELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVDLKRISSVCE 324
Cdd:PRK12483 275 DELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGIEGQTLVAIDSGANVNFDRLRHVAE 336
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
20-311 6.47e-70

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: 219.87  E-value: 6.47e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   20 LSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALSSHLLGIK 99
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  100 SKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGE-TYLHPYDDVEVMAGQGTIGLDILDDMW-DVDT 177
Cdd:pfam00291  81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLGgDPDA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  178 VIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKI-PGDLTFEIVKELVDD 256
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDePGALALDLLDEYVGE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 517597650  257 IVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISG 311
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGDRVVVVLTG 295
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
8-319 8.01e-66

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: 210.09  E-value: 8.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650    8 LNIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQ 87
Cdd:TIGR02991   1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   88 GVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLD 167
Cdd:TIGR02991  81 ALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  168 ILDDMWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIAD--GCAVKIPGDL 245
Cdd:TIGR02991 161 VVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517597650  246 TFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDqyTKGKKVVaVISGGNVDL---KRI 319
Cdd:TIGR02991 241 TFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIK--NPGPCAV-IVSGRNIDMdlhKRI 314
PRK08246 PRK08246
serine/threonine dehydratase;
12-281 9.01e-56

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 183.62  E-value: 9.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  12 DIKKAQQILSGNARKTPLVKSfYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKIsnLTDEEKAHGVIACSAGNHAQGVAL 91
Cdd:PRK08246   9 DVRAAAQRIAPHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  92 SSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDILDD 171
Cdd:PRK08246  86 AAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 172 MWDVDTVivpiggggiisgiAVA----------LKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKI 241
Cdd:PRK08246 166 APGVDTV-------------LVAvggggliagiAAWFEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARR 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 517597650 242 PGDLTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVE 281
Cdd:PRK08246 233 VGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVE 272
PLN02550 PLN02550
threonine dehydratase
18-324 2.19e-55

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 189.75  E-value: 2.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  18 QILSGN----ARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGNHAQGVALSS 93
Cdd:PLN02550  97 NILSAKvydvAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSA 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  94 HLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDILDDMW 173
Cdd:PLN02550 177 QRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQ 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 174 D-VDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEIVKE 252
Cdd:PLN02550 257 GpLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRE 336
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517597650 253 LVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVDLKRISSVCE 324
Cdd:PLN02550 337 LVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGLKDENVVAITSGANMNFDRLRIVTE 408
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
27-312 6.34e-52

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: 171.54  E-value: 6.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  27 TPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEK-AHGVIACSA-GNHAQGVALSSHLLGIKSKIVM 104
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKlPKGVIIESTgGNTGIALAAAAARLGLKCTIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 105 PISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGE-TYLHPYDDVEVMAGQGTIGLDILDDMWD--VDTVIVP 181
Cdd:cd00640   81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGTIGLEILEQLGGqkPDAVVVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 182 IGGGGIISGIAVALKSFNPSINIIGVQAdnvhgmkasydvgkivshyeaptiadgcavkipgdltfeivkelvdDIVTVS 261
Cdd:cd00640  161 VGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVTVS 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517597650 262 EEELEVAMKDLLQRGKAVVEGAGALATAALLAGKvDQYTKGKKVVAVISGG 312
Cdd:cd00640  195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLA-KKLGKGKTVVVILTGG 244
PRK08813 PRK08813
threonine dehydratase; Provisional
5-315 3.05e-51

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 173.27  E-value: 3.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   5 NLPLNIGDIKKAQQILSGNARKTPLvksfYLTSKTGgeIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHGVIACSAGN 84
Cdd:PRK08813  18 DVAVSVADVLAAQARLRRYLSPTPL----HYAERFG--VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  85 HAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTI 164
Cdd:PRK08813  92 HAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 165 GLDILDDMWDVdtVIVPIGGGGIISGIAVALKSfnPSINIIGVQADNVHGMkASYDVGKIVSHYEAPTIADGCAVKIPGD 244
Cdd:PRK08813 172 GIELAAHAPDV--VIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSM-ARAIRGDLREIAPVATLADGVKVKIPGF 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517597650 245 LTFEIVKELVDDIVTVSEEELEVAMKDLlqrgkaVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVD 315
Cdd:PRK08813 247 LTRRLCSSLLDDVVIVREAELRETLVRL------ALEEHVIAEGAGALALAAGRRVSGKRKCAVVSGGNID 311
PRK06608 PRK06608
serine/threonine dehydratase;
5-315 3.83e-50

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 169.95  E-value: 3.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   5 NLPL-NIGDIKKAQQILSGNARKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEK-AHGVIACSA 82
Cdd:PRK06608   1 NLLLqNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKlPDKIVAYST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  83 GNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHgDTFDDAKAKCEEiIQETGETYLHPYDDVEVMAGQG 162
Cdd:PRK06608  81 GNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILT-NTRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 163 TIGLDILDDM-WDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAP-TIADGCAVK 240
Cdd:PRK06608 159 TLCYEALQQLgFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSPnTIADGLKTL 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517597650 241 IPGDLTFEIVKELvDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQyTKGKKVVAVISGGNVD 315
Cdd:PRK06608 239 SVSARTFEYLKKL-DDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQ-SKPQKLLVILSGGNID 311
PRK06110 PRK06110
threonine dehydratase;
35-322 2.21e-33

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 125.49  E-value: 2.21e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  35 LTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEE-KAHGVIACSAGNHAQGVALSSHLLGIKSKIVMPISAPQAKV 113
Cdd:PRK06110  30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 114 DATRGYGSEVILHGDTFDDAKAKCEEIIQETGetyLH--PYDDVEVMAGQGTIGLDILDDMWDVDTVIVPIGGGGIISGI 191
Cdd:PRK06110 110 AAMRALGAELIEHGEDFQAAREEAARLAAERG---LHmvPSFHPDLVRGVATYALELFRAVPDLDVVYVPIGMGSGICGA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 192 AVALKSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGDLTFEIVKELVDDIVTVSEEELEVAMKD 271
Cdd:PRK06110 187 IAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRA 266
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517597650 272 LLQRGKAVVEGAGALATAALLAGKVDQytKGKKVVAVISGGNVDLKRISSV 322
Cdd:PRK06110 267 YFTDTHNVAEGAGAAALAAALQERERL--AGKRVGLVLSGGNIDRAVFARV 315
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
26-281 1.79e-24

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: 101.22  E-value: 1.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  26 KTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDE---EKAHgVIACSAGNHAQGVALSSHLLGIKSKI 102
Cdd:cd06448    1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQglnECVH-VVCSSGGNAGLAAAYAARKLGVPCTI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 103 VMPISAPQAKVDATRGYGSEVILHGDT-FDDAKAKCEEII-QETGETYLHPYDDVEVMAGQGTIGLDILDDMWDVDTViv 180
Cdd:cd06448   80 VVPESTKPRVVEKLRDEGATVVVHGKVwWEADNYLREELAeNDPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSQEKV-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 181 piggggiisgIAVAL----------------KSFNPSINIIGVQADNVHGMKASYDVGKIVSHYEAPTIADGCAVKIPGD 244
Cdd:cd06448  158 ----------DAIVCsvggggllngivqgleRNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSS 227
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 517597650 245 LTFEIVKELVDDIVTVSEEELEVAMKDLLQRGKAVVE 281
Cdd:cd06448  228 QALEYAQEHNIKSEVVSDRDAVQACLRFADDERILVE 264
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
27-272 2.36e-18

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: 84.18  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  27 TPLVKSFYLTSKTGG-EIHLKLENMQLTGSFKFRGAFNKISNLTdEEKAHGVIACSAGNHAQGVALSSHLLGIKSKIVMP 105
Cdd:cd01563   23 TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGMTVAVSKAK-ELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 106 ISAPQAKVDATRGYGSEVI-LHGDtFDDAKAKCEEIIQETG---ETYLHPYDdVEvmaGQGTIGLDILDDM-WDV-DTVI 179
Cdd:cd01563  102 AGKALGKLAQALAYGATVLaVEGN-FDDALRLVRELAEENWiylSNSLNPYR-LE---GQKTIAFEIAEQLgWEVpDYVV 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 180 VPIGGGGIISGIAVALKSF--------NPSIniIGVQADNVHGMKASYDVGK--IVSHYEAPTIADGCAVKIP--GDLTF 247
Cdd:cd01563  177 VPVGNGGNITAIWKGFKELkelglidrLPRM--VGVQAEGAAPIVRAFKEGKddIEPVENPETIATAIRIGNPasGPKAL 254
                        250       260
                 ....*....|....*....|....*
gi 517597650 248 EIVKELVDDIVTVSEEELEVAMKDL 272
Cdd:cd01563  255 RAVRESGGTAVAVSDEEILEAQKLL 279
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
26-275 5.01e-18

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: 82.56  E-value: 5.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  26 KTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEEKAHG---VIACSAGNHAQGVALSSHLLGIKSKI 102
Cdd:cd01561    2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPgttIIEPTSGNTGIGLAMVAAAKGYRFII 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 103 VMPISAPQAKVDATRGYGSEVIL----HGDTFDDAKAKCEEIIQETGETY-LHPYD-DVEVMAGQGTIGLDILDDM-WDV 175
Cdd:cd01561   82 VMPETMSEEKRKLLRALGAEVILtpeaEADGMKGAIAKARELAAETPNAFwLNQFEnPANPEAHYETTAPEIWEQLdGKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 176 DTVivpiggggiisgiaVA--------------LKSFNPSINIIGVQADNvhgmKASYDVGKIVSHyeaptiadgcavKI 241
Cdd:cd01561  162 DAF--------------VAgvgtggtitgvaryLKEKNPNVRIVGVDPVG----SVLFSGGPPGPH------------KI 211
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 517597650 242 PG---DLTFEIVK-ELVDDIVTVSEEELEVAMKDLLQR 275
Cdd:cd01561  212 EGigaGFIPENLDrSLIDEVVRVSDEEAFAMARRLARE 249
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
27-275 3.32e-14

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: 72.00  E-value: 3.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  27 TPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKIsnlTDEEKA------HGVIACSAGNHAQGVALSSHLLGIKS 100
Cdd:COG0031   14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMI---EDAEKRgllkpgGTIVEATSGNTGIGLAMVAAAKGYRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 101 KIVMPISAPQAKVDATRGYGSEVIL--HGDTFDDAKAKCEEIIQETGETYlhpyddvevMAGQ-----------GTIGLD 167
Cdd:COG0031   91 ILVMPETMSKERRALLRAYGAEVVLtpGAEGMKGAIDKAEELAAETPGAF---------WPNQfenpanpeahyETTGPE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 168 ILDDMW-DVDTVivpiggggiisgiaVA--------------LKSFNPSINIIGVQADNvhgmKASYDVGKIVSHyeapt 232
Cdd:COG0031  162 IWEQTDgKVDAF--------------VAgvgtggtitgvgryLKERNPDIKIVAVEPEG----SPLLSGGEPGPH----- 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 517597650 233 iadgcavKIPGdLTFEIV-----KELVDDIVTVSEEELEVAMKDLLQR 275
Cdd:COG0031  219 -------KIEG-IGAGFVpkildPSLIDEVITVSDEEAFAMARRLARE 258
PRK05638 PRK05638
threonine synthase; Validated
27-311 6.35e-12

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 65.99  E-value: 6.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  27 TPLVKSfYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTDEeKAHGVIACSAGNHAQGVALSSHLLGIKSKIVMPI 106
Cdd:PRK05638  67 TPLIRA-RISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPY-AANGFIVASDGNAAASVAAYSARAGKEAFVVVPR 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 107 SAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGETYLHPYDDVEVMAGQGTIGLDILDDMWDVDTVIVPIGGGG 186
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINPTHVIVPTGSGSY 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 187 IISGiavaLKSFNPSINI---------IGVQADN-------VHGMKASYDvgkivshyeaPTIADGCAVKIP--GDLTFE 248
Cdd:PRK05638 225 LYSI----YKGFKELLEIgvieeipklIAVQTERcnpiaseILGNKTKCN----------ETKALGLYVKNPvmKEYVSE 290
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517597650 249 IVKELVDDIVTVSEEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISG 311
Cdd:PRK05638 291 AIKESGGTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTG 353
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
27-275 2.35e-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: 64.07  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  27 TPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAF---NKIsnltdeeKAHG--VIAC-SAGNHAQGVALSSHLLGIKS 100
Cdd:COG0498   67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQvavSLA-------LERGakTIVCaSSGNGSAALAAYAARAGIEV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 101 KIVMPIS-APQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGeTYL----HPYddveVMAGQGTIGLDILDDMWDV 175
Cdd:COG0498  140 FVFVPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEG-LYAvnsiNPA----RLEGQKTYAFEIAEQLGRV 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 176 -DTVIVPIGGGGIISGIAVALKSFNPS--IN----IIGVQADNVHGMKASYDVGKIVSHYEAP-TIADGCAVKIPGDLtF 247
Cdd:COG0498  215 pDWVVVPTGNGGNILAGYKAFKELKELglIDrlprLIAVQATGCNPILTAFETGRDEYEPERPeTIAPSMDIGNPSNG-E 293
                        250       260       270
                 ....*....|....*....|....*....|.
gi 517597650 248 EIVKELVD---DIVTVSEEELEVAMKDLLQR 275
Cdd:COG0498  294 RALFALREsggTAVAVSDEEILEAIRLLARR 324
PRK08197 PRK08197
threonine synthase; Validated
13-175 1.04e-10

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 62.33  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  13 IKKAQQILSGNARKTPLVKSFYLTSKTG-GEIHLKLENMQLTGSFKFRGAFNKISnltdEEKAHGV--IAC-SAGNHAQG 88
Cdd:PRK08197  66 VRDPEHIVSLGEGMTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVS----RAKELGVkhLAMpTNGNAGAA 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  89 VALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETG----ETYLHPYdDVEvmaGQGTI 164
Cdd:PRK08197 142 WAAYAARAGIRATIFMPADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGwfdvSTLKEPY-RIE---GKKTM 217
                        170
                 ....*....|..
gi 517597650 165 GLDILDDM-WDV 175
Cdd:PRK08197 218 GLELAEQLgWRL 229
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
8-172 1.36e-10

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 61.82  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   8 LNIGDIKKAQQILSG--NARKTPLVKSFYLTSKTG-GEIHLKLENMQL-TGSFKFRGA-----------FNK------IS 66
Cdd:PRK08206  24 LSQEEAKKARAFHQSfpGYAPTPLVALPDLAAELGvGSILVKDESYRFgLNAFKALGGayavarllaekLGLdiselsFE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  67 NLTDEEK----AHGVIAC-SAGNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDTFDD--------A 133
Cdd:PRK08206 104 ELTSGEVreklGDITFATaTDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDsvrlaaqeA 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 517597650 134 KAKCEEIIQET---GetylhpYDDV--EVMAGQGTIGLDILDDM 172
Cdd:PRK08206 184 QENGWVVVQDTaweG------YEEIptWIMQGYGTMADEAVEQL 221
PRK08329 PRK08329
threonine synthase; Validated
36-316 1.75e-09

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 58.30  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  36 TSKTGGEIHLKLENMQLTGSFKFRGAFNKISNLTdEEKAHGVIACSAGNHAQGVALSSHLLGIKSKIVMPISAPQAKVDA 115
Cdd:PRK08329  67 TVKRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLK-EEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 116 TRGYGSEV-ILHGDTFDDAKaKCEEIIQETGETY----LHPYddveVMAGQGTIGLDILDDMWDVDTVIVPIGGGGIISG 190
Cdd:PRK08329 146 LSRLGAELhFVEGDRMEVHE-EAVKFSKRNNIPYvshwLNPY----FLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLG 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 191 IAVALKSF------NPSINIIGVQADNVHGM-KASYDVGKivshyeaptIADGCAVKIPG--DLTFEIVKELVDDIVTVS 261
Cdd:PRK08329 221 IWKGFKELhemgeiSKMPKLVAVQAEGYESLcKRSKSENK---------LADGIAIPEPPrkEEMLRALEESNGFCISVG 291
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517597650 262 EEELEVAMKDLLQRGKAVVEGAGALATAALLAGKVDQYTKGKKVVAVISGGNVDL 316
Cdd:PRK08329 292 EEETRAALHWLRRMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLKN 346
cysM PRK11761
cysteine synthase CysM;
22-272 4.97e-08

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 53.34  E-value: 4.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  22 GNarkTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKISnltdEEKAHGVI--------ACSaGNhaQGVALS- 92
Cdd:PRK11761  11 GN---TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIV----QAEKRGEIkpgdtlieATS-GN--TGIALAm 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  93 -SHLLGIKSKIVMPISAPQAKVDATRGYGSEVIL-------------------HG-----DTF---DDAKAKCE----EI 140
Cdd:PRK11761  81 iAAIKGYRMKLIMPENMSQERRAAMRAYGAELILvpkeqgmegardlalqmqaEGegkvlDQFanpDNPLAHYEttgpEI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 141 IQETGETYLHpydDVEVMAGQGTIgldilddmwdvdtvivpiggggiiSGIAVALKSFNPSINIIGVQadnvhgmkasyd 220
Cdd:PRK11761 161 WRQTEGRITH---FVSSMGTTGTI------------------------MGVSRYLKEQNPAVQIVGLQ------------ 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517597650 221 vgkivshyeaPtiADGCAvkIPGdltfeIVK------------ELVDDIVTVSEEELEVAMKDL 272
Cdd:PRK11761 202 ----------P--EEGSS--IPG-----IRRwpeeylpkifdaSRVDRVLDVSQQEAENTMRRL 246
PRK06450 PRK06450
threonine synthase; Validated
27-276 5.44e-08

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 53.59  E-value: 5.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  27 TPLVKsfyltsktGGEIHLKLENMQLTGSFKFRGAFNKISNLTDeeKAHGVIA-CSAGNHAQGVALSSHLLGIKSKIVMP 105
Cdd:PRK06450  59 TPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAE--KGIKQISeDSSGNAGASIAAYGAAAGIEVKIFVP 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 106 ISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEeiiqETGETY----LHPyddvEVMAGQGTIGLDILDDM-WDV-DTVI 179
Cdd:PRK06450 129 ETASGGKLKQIESYGAEVVRVRGSREDVAKAAE----NSGYYYashvLQP----QFRDGIRTLAYEIAKDLdWKIpNYVF 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 180 VPIGGGGIISGIAVALKS-FNPSI-----NIIGVQADNVHGMKA-----SYDVGKIVShyeapTIADGCAVKIPGdLTFE 248
Cdd:PRK06450 201 IPVSAGTLLLGVYSGFKHlLDSGVisempKIVAVQTEQVSPLCAkfkgiSYTPPDKVT-----SIADALVSTRPF-LLDY 274
                        250       260       270
                 ....*....|....*....|....*....|
gi 517597650 249 IVKEL--VDDIVTVSEEELEVAMKDLLQRG 276
Cdd:PRK06450 275 MVKALseYGECIVVSDNEIVEAWKELAKKG 304
PRK10717 PRK10717
cysteine synthase A; Provisional
27-125 2.03e-07

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 51.79  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  27 TPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAFNKIsnlTDEE-----KAHGVIA-CSAGNHAQGVALSSHLLGIKS 100
Cdd:PRK10717  14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNII---WDAEkrgllKPGGTIVeGTAGNTGIGLALVAAARGYKT 90
                         90       100
                 ....*....|....*....|....*
gi 517597650 101 KIVMPISAPQAKVDATRGYGSEVIL 125
Cdd:PRK10717  91 VIVMPETQSQEKKDLLRALGAELVL 115
PRK06381 PRK06381
threonine synthase; Validated
27-175 5.12e-07

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 50.47  E-value: 5.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  27 TPLVKSFYLTSKTG-GEIHLKLENMQLTGSFKFRGAFNKISNLTDEeKAHGVIACSAGNHAQGVALSSHLLGIKSKIVMP 105
Cdd:PRK06381  16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVRRAMRL-GYSGITVGTCGNYGASIAYFARLYGLKAVIFIP 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517597650 106 ISAPQAKVDATRGYGSEVILHGDTFDDAKAKCEEIIQETGeTY------LHPYDDVEvmaGQGTIGLDILDDMWDV 175
Cdd:PRK06381  95 RSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENG-IYdanpgsVNSVVDIE---AYSAIAYEIYEALGDV 166
PLN03013 PLN03013
cysteine synthase
8-279 1.38e-05

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 46.31  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   8 LNIGDikKAQQILSgnarKTPLVksfYLTSKTGG---EIHLKLENMQLTGSFKFRGAFnkiSNLTDEEKAHGV------- 77
Cdd:PLN03013 111 LNIAD--NVSQLIG----KTPMV---YLNSIAKGcvaNIAAKLEIMEPCCSVKDRIGY---SMVTDAEQKGFIspgksvl 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  78 IACSAGNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILH--GDTFDDAKAKCEEIIQETGETY-LHPYDD 154
Cdd:PLN03013 179 VEPTSGNTGIGLAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTdpAKGMTGAVQKAEEILKNTPDAYmLQQFDN 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 155 -VEVMAGQGTIGLDILDDM-WDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGV---QADNVHGmkasydvGKIVSHye 229
Cdd:PLN03013 259 pANPKIHYETTGPEIWDDTkGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVeptESDILSG-------GKPGPH-- 329
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 517597650 230 apTIADGCAVKIPGDLTFEIVKELvddIVTVSEEELEVAMKDLLQRGKAV 279
Cdd:PLN03013 330 --KIQGIGAGFIPKNLDQKIMDEV---IAISSEEAIETAKQLALKEGLMV 374
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
4-208 6.83e-05

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 44.18  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650   4 KNLPLNigDIKKAQQILSGnarKTPLVKSFYLTSKTGGEIHLKLENMQLTGSFKFRGAfnkISNLTDEEKAH-------G 76
Cdd:PLN02556  42 KDLPGT--KIKTDASQLIG---KTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPA---LAMIEDAEKKNlitpgktT 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  77 VIACSAGNHAQGVALSSHLLGIKSKIVMPISAPQAKVDATRGYGSEVILHGDT--FDDAKAKCEEIIQETGETY-LHPYD 153
Cdd:PLN02556 114 LIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTkgMGGTVKKAYELLESTPDAFmLQQFS 193
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 517597650 154 D-VEVMAGQGTIGLDILDD-MWDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQ 208
Cdd:PLN02556 194 NpANTQVHFETTGPEIWEDtLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVE 250
PLN02565 PLN02565
cysteine synthase
26-279 2.82e-04

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 42.22  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  26 KTPLVksfYLTSKTGG---EIHLKLENMQLTGSFKFRGAFNKISNLtdEEKA------HGVIACSAGNHAQGVALSSHLL 96
Cdd:PLN02565  15 KTPLV---YLNNVVDGcvaRIAAKLEMMEPCSSVKDRIGYSMITDA--EEKGlikpgeSVLIEPTSGNTGIGLAFMAAAK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650  97 GIKSKIVMPISAPQAKVDATRGYGSEVILHGDT--FDDAKAKCEEIIQETGETYL--------HP---YDDVEVMAGQGT 163
Cdd:PLN02565  90 GYKLIITMPASMSLERRIILLAFGAELVLTDPAkgMKGAVQKAEEILAKTPNSYIlqqfenpaNPkihYETTGPEIWKGT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517597650 164 IGldilddmwDVDTVIVPIGGGGIISGIAVALKSFNPSINIIGVQADNvhgmKASYDVGKIVSHyeapTIADGCAVKIPG 243
Cdd:PLN02565 170 GG--------KVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVE----SAVLSGGKPGPH----KIQGIGAGFIPG 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 517597650 244 DLTFeivkELVDDIVTVSEEE-LEVAMKDLLQRGKAV 279
Cdd:PLN02565 234 VLDV----DLLDEVVQVSSDEaIETAKLLALKEGLLV 266
 
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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