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Conserved domains on  [gi|6322631|ref|NP_012704|]
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threo-3-hydroxy-L-aspartate ammonia-lyase SRY1 [Saccharomyces cerevisiae S288C]

Protein Classification

threonine/serine dehydratase( domain architecture ID 10792871)

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
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
4-319 0e+00

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


:

Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 565.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     4 PTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQ 83
Cdd:PRK07048   6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    84 AIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKE 163
Cdd:PRK07048  86 AIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   164 LLEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTF 243
Cdd:PRK07048 166 LFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTF 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322631   244 AIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISG 319
Cdd:PRK07048 246 PIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLSG 321
 
Name Accession Description Interval E-value
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
4-319 0e+00

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 565.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     4 PTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQ 83
Cdd:PRK07048   6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    84 AIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKE 163
Cdd:PRK07048  86 AIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   164 LLEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTF 243
Cdd:PRK07048 166 LFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTF 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322631   244 AIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISG 319
Cdd:PRK07048 246 PIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLSG 321
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 6-309 1.09e-150

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: 424.98  E-value: 1.09e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    6 YGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAI 85
Cdd:cd01562   1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   86 ALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELL 165
Cdd:cd01562  81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  166 EEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAI 245
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631  246 IRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVD 309
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 1-317 3.90e-144

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: 409.43  E-value: 3.90e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    1 MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGN 80
Cdd:COG1171   3 ALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   81 HAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTS 160
Cdd:COG1171  83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  161 AKELLEEVGQLDALFVPlggggllsgsalaaRSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGE 240
Cdd:COG1171 163 ALEILEQLPDLDAVFVPvggggliagvaaalKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGE 242

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631  241 YTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLI 317
Cdd:COG1171 243 LTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEIL 319
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 23-317 1.64e-83

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: 256.98  E-value: 1.64e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    103 DAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGGGG 182
Cdd:TIGR01127  81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    183 LLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQELV 262
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6322631    263 KCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLI 317
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKII 295
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 16-305 2.31e-73

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: 228.35  E-value: 2.31e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     16 IKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVP 95
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     96 ATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAE-HGFALIPPYDHPDVIAGQGTSAKELLEEVGQ-LDA 173
Cdd:pfam00291  81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLGGdPDA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    174 LFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQ-HLGEYTFAIIRENVDD 252
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVGE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6322631    253 ILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELV--GKKVGIILSG 305
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELkgGDRVVVVLTG 295
 
Name Accession Description Interval E-value
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
4-319 0e+00

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 565.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     4 PTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQ 83
Cdd:PRK07048   6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNHAQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    84 AIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKE 163
Cdd:PRK07048  86 AIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   164 LLEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTF 243
Cdd:PRK07048 166 LFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADGAQTQHLGNYTF 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322631   244 AIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISG 319
Cdd:PRK07048 246 PIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARFAALLSG 321
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 6-309 1.09e-150

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: 424.98  E-value: 1.09e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    6 YGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAI 85
Cdd:cd01562   1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   86 ALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELL 165
Cdd:cd01562  81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  166 EEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAI 245
Cdd:cd01562 161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVKRPGELTFEI 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631  246 IRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVD 309
Cdd:cd01562 241 IRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 1-317 3.90e-144

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: 409.43  E-value: 3.90e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    1 MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGN 80
Cdd:COG1171   3 ALMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   81 HAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTS 160
Cdd:COG1171  83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  161 AKELLEEVGQLDALFVPlggggllsgsalaaRSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGE 240
Cdd:COG1171 163 ALEILEQLPDLDAVFVPvggggliagvaaalKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAVGRPGE 242

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631  241 YTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLI 317
Cdd:COG1171 243 LTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAEIL 319
PLN02970 PLN02970
serine racemase
 5-318 1.72e-133

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 382.49  E-value: 1.72e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     5 TYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQA 84
Cdd:PLN02970  10 DLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    85 IALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:PLN02970  90 LALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEF 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   165 LEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQhLGEYTFA 244
Cdd:PLN02970 170 LEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS-LGDLTWP 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322631   245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGAL---LKKEELV--GKKVGIILSGGNVDMKRYATLIS 318
Cdd:PLN02970 249 VVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALsdsFRSNPAWkgCKNVGIVLSGGNVDLGVLWESFS 327
PRK06608 PRK06608
serine/threonine dehydratase;
1-316 2.29e-85

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 260.47  E-value: 2.29e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     1 MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDE-KRSKGVIAFSSG 79
Cdd:PRK06608   2 LLLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQgKLPDKIVAYSTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    80 NHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIgrQLAAEHGFALIPPYDHPDVIAGQGT 159
Cdd:PRK06608  82 NHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKA--KEDEEQGFYYIHPSDSDSTIAGAGT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   160 SAKELLEEVG-QLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHIN-TPKTIADGAQTQH 237
Cdd:PRK06608 160 LCYEALQQLGfSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNySPNTIADGLKTLS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   238 LGEYTFAIIREnVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAG--ALLKKEElVGKKVGIILSGGNVDMKRYAT 315
Cdd:PRK06608 240 VSARTFEYLKK-LDDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAvvNWLKTQS-KPQKLLVILSGGNIDPILYNE 317


                 .
gi 6322631   316 L 316
Cdd:PRK06608 318 L 318
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
5-317 3.04e-85

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 260.05  E-value: 3.04e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     5 TYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQA 84
Cdd:PRK08638  10 AIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    85 IALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:PRK08638  90 VALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEI 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   165 LEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFA 244
Cdd:PRK08638 170 LEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCDVSRPGNLTYE 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322631   245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVE-----PTACLgFAGALlkKEELVGKKVGIILSGGNVDMKRYATLI 317
Cdd:PRK08638 250 IVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEgagalATAAL-LSGKL--DQYIQNKKVVAIISGGNVDLSRVSQIT 324
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 23-317 1.64e-83

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: 256.98  E-value: 1.64e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    103 DAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGGGG 182
Cdd:TIGR01127  81 SAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVGGGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    183 LLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQELV 262
Cdd:TIGR01127 161 LISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTVDEEEIA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6322631    263 KCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLI 317
Cdd:TIGR01127 241 NAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKII 295
PRK07334 PRK07334
threonine dehydratase; Provisional
 5-309 3.77e-79

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 246.73  E-value: 3.77e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     5 TYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQA 84
Cdd:PRK07334   6 TLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    85 IALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:PRK07334  86 VAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEM 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   165 LEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAgNDGQQSFRSGSIVHINTpKTIADGAQTQHLGEYTFA 244
Cdd:PRK07334 166 LEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTEL-YPSMYAAIKGVALPCGG-STIAEGIAVKQPGQLTLE 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322631   245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVD 309
Cdd:PRK07334 244 IVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNID 308
PRK06815 PRK06815
threonine/serine dehydratase;
6-318 2.05e-77

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 239.59  E-value: 2.05e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     6 YGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAI 85
Cdd:PRK06815   4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    86 ALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELL 165
Cdd:PRK06815  84 ALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   166 EEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADG-AQTQHLGEYTFA 244
Cdd:PRK06815 164 EQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGtAGGVEPGAITFP 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631   245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLIS 318
Cdd:PRK06815 244 LCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKYLEAVS 317
ilvA_2Cterm TIGR01124
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ...
 15-312 1.92e-73

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: 235.01  E-value: 1.92e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     15 RIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNV 94
Cdd:TIGR01124  10 RVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFSAARLGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     95 PATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQ-LDA 173
Cdd:TIGR01124  90 KALIVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANpLDA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    174 LFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDI 253
Cdd:TIGR01124 170 VFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRLCQQYLDDI 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322631    254 LTVSDQELVKCMHFLAERMKVVVEPTACLGFAG--ALLKKEELVGKKVGIILSGGNVDMKR 312
Cdd:TIGR01124 250 VTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGlkKYVALHGIRGQTLVAILSGANMNFHR 310
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 16-305 2.31e-73

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: 228.35  E-value: 2.31e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     16 IKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVP 95
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     96 ATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAE-HGFALIPPYDHPDVIAGQGTSAKELLEEVGQ-LDA 173
Cdd:pfam00291  81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLGGdPDA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    174 LFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQ-HLGEYTFAIIRENVDD 252
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVGE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6322631    253 ILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELV--GKKVGIILSG 305
Cdd:pfam00291 241 VVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELkgGDRVVVVLTG 295
eutB PRK07476
threonine dehydratase; Provisional
 8-323 1.83e-69

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 219.07  E-value: 1.83e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     8 DVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIAL 87
Cdd:PRK07476   5 DIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    88 SAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEE 167
Cdd:PRK07476  85 AARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   168 VGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGaqtqhLG-------E 240
Cdd:PRK07476 165 LPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLADS-----LGggigldnR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   241 YTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISGK 320
Cdd:PRK07476 240 YTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMELHRRIINGE 319


                 ...
gi 6322631   321 EDG 323
Cdd:PRK07476 320 VAD 322
PRK12483 PRK12483
threonine dehydratase; Reviewed
 13-312 2.08e-66

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 216.97  E-value: 2.08e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    13 SNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLL 92
Cdd:PRK12483  28 AARVYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    93 NVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELL-EEVGQL 171
Cdd:PRK12483 108 GVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILrQHPGPL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   172 DALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVD 251
Cdd:PRK12483 188 DAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCRHYVD 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322631   252 DILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGA--LLKKEELVGKKVGIILSGGNVDMKR 312
Cdd:PRK12483 268 EVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIkkYAEREGIEGQTLVAIDSGANVNFDR 330
PRK08639 PRK08639
threonine dehydratase; Validated
 8-314 5.87e-66

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 213.13  E-value: 5.87e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     8 DVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIAL 87
Cdd:PRK08639  11 DIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCASAGNHAQGVAY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    88 SAKLLNVPATIVMPEDAPALKVAATAGYGA---HIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:PRK08639  91 ACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEI 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   165 LEEVGQL---DALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEY 241
Cdd:PRK08639 171 LEQLEKEgspDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDL 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322631   242 TFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYA 314
Cdd:PRK08639 251 TFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKTVVCVISGGNNDIERMP 323
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
22-312 1.85e-65

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 214.23  E-value: 1.85e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    22 KTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PRK09224  20 ETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVMP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQ-LDALFVPLGG 180
Cdd:PRK09224 100 VTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHpLDAVFVPVGG 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   181 GGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQE 260
Cdd:PRK09224 180 GGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQEYVDDVITVDTDE 259

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322631   261 LVKCMHFLAERMKVVVEPTACLGFAGalLKK----EELVGKKVGIILSGGNVDMKR 312
Cdd:PRK09224 260 ICAAIKDVFEDTRSIAEPAGALALAG--LKKyvaqHGIEGETLVAILSGANMNFDR 313
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 23-306 4.05e-59

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: 190.03  E-value: 4.05e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDE-KRSKGVIAF-SSGNHAQAIALSAKLLNVPATIVM 100
Cdd:cd00640   1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEgKLPKGVIIEsTGGNTGIALAAAAARLGLKCTIVM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  101 PEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAE-HGFALIPPYDHPDVIAGQGTSAKELLEEVGQ--LDALFVP 177
Cdd:cd00640  81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEdPGAYYVNQFDNPANIAGQGTIGLEILEQLGGqkPDAVVVP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  178 LGGGGLLSGSALAARSLSPGCKIFGVEPEagndgqqsfrsgsivhintpktiadgaqtqhlgeytfaiirenvddILTVS 257
Cdd:cd00640 161 VGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------------------VVTVS 194

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6322631  258 DQELVKCMHFLAERMKVVVEPTACLGFAGAL-LKKEELVGKKVGIILSGG 306
Cdd:cd00640 195 DEEALEAIRLLAREEGILVEPSSAAALAAALkLAKKLGKGKTVVVILTGG 244
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 5-319 5.87e-57

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: 186.98  E-value: 5.87e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631      5 TYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQA 84
Cdd:TIGR02991   2 TLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     85 IALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKEL 164
Cdd:TIGR02991  82 LAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    165 LEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIAD--GAQTQHLGEYT 242
Cdd:TIGR02991 162 VEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGLDNRVT 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631    243 FAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVgIILSGGNVDMKRYATLISG 319
Cdd:TIGR02991 242 FAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPGPCA-VIVSGRNIDMDLHKRIIDG 317
PRK06110 PRK06110
threonine dehydratase;
23-319 8.32e-56

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 184.04  E-value: 8.32e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEK-RSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PRK06110  22 TPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   102 EDAPALKVAATAGYGAHIIRYNR-YTEDREQIGRqLAAEHGFALIPPYdHPDVIAGQGTSAKELLEEVGQLDALFVPLGG 180
Cdd:PRK06110 102 HGNSVEKNAAMRALGAELIEHGEdFQAAREEAAR-LAAERGLHMVPSF-HPDLVRGVATYALELFRAVPDLDVVYVPIGM 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   181 GGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQE 260
Cdd:PRK06110 180 GSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDE 259

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322631   261 LVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISG 319
Cdd:PRK06110 260 VAAAMRAYFTDTHNVAEGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVFARVLAG 318
PLN02550 PLN02550
threonine dehydratase
 22-312 6.79e-53

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 182.81  E-value: 6.79e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    22 KTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PLN02550 109 ESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMP 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEV-GQLDALFVPLGG 180
Cdd:PLN02550 189 VTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHqGPLHAIFVPVGG 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   181 GGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQE 260
Cdd:PLN02550 269 GGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELVDGVVLVSRDA 348

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6322631   261 LVKCMHFLAERMKVVVEPTACLGFAG--ALLKKEELVGKKVGIILSGGNVDMKR 312
Cdd:PLN02550 349 ICASIKDMFEEKRSILEPAGALALAGaeAYCKYYGLKDENVVAITSGANMNFDR 402
PRK08246 PRK08246
serine/threonine dehydratase;
1-309 2.27e-49

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 167.05  E-value: 2.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     1 MIVPTYGDVLDASNRIKEYVNKTPVLTSRMlNDRLGAQIYFKGENFQRVGAFKFRGAMNAVskLSDEKRSKGVIAFSSGN 80
Cdd:PRK08246   2 HAMITRSDVRAAAQRIAPHIRRTPVLEADG-AGFGPAPVWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    81 HAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRY-NRYTeDREQIGRQLAAEHGFALIPPYDHPDVIAGQGT 159
Cdd:PRK08246  79 AGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVgAEYA-DALEAAQAFAAETGALLCHAYDQPEVLAGAGT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   160 SAKELLEEVGQLDALFVPLGGGGLLSGSALAarsLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLG 239
Cdd:PRK08246 158 LGLEIEEQAPGVDTVLVAVGGGGLIAGIAAW---FEGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVG 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322631   240 EYTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAgALL--KKEELVGKKVGIILSGGNVD 309
Cdd:PRK08246 235 EIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALA-ALLsgAYVPAPGERVAVVLCGANTD 305
PRK08813 PRK08813
threonine dehydratase; Provisional
 8-318 9.68e-45

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 155.94  E-value: 9.68e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     8 DVLDASNRIKEYVNKTPVLTSrmlnDRLGaqIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIAL 87
Cdd:PRK08813  25 DVLAAQARLRRYLSPTPLHYA----ERFG--VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAW 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    88 SAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEE 167
Cdd:PRK08813  99 SAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAAH 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   168 VGqlDALFVPLGGGGLLSGSALAARslSPGCKIFGVEPEAGNDGQQSFRsGSIVHINTPKTIADGAQTQHLGEYTFAIIR 247
Cdd:PRK08813 179 AP--DVVIVPIGGGGLASGVALALK--SQGVRVVGAQVEGVDSMARAIR-GDLREIAPVATLADGVKVKIPGFLTRRLCS 253

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322631   248 ENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGAllkkEELVGKKVGIILSGGNVDMKRYATLIS 318
Cdd:PRK08813 254 SLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAAG----RRVSGKRKCAVVSGGNIDATVLATLLS 320
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 23-308 4.62e-24

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: 99.98  E-value: 4.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   23 TPVLTSRMLNDRLGAQ-IYFKGENFQRVGAFKFRGAMNAVSKLSdEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:cd01563  23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTVAVSKAK-ELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIpPYDHPDVIAGQGTSAKELLEEVGQL--DALFVPLG 179
Cdd:cd01563 102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLS-NSLNPYRLEGQKTIAFEIAEQLGWEvpDYVVVPVG 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  180 GGGLLSGSALAARSLS--------PgcKIFGVEPEAGNDGQQSFRSG--SIVHINTPKTIADGAQ--TQHLGEYTFAIIR 247
Cdd:cd01563 181 NGGNITAIWKGFKELKelglidrlP--RMVGVQAEGAAPIVRAFKEGkdDIEPVENPETIATAIRigNPASGPKALRAVR 258

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322631  248 ENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEElvgkkvGIILSGGNV 308
Cdd:cd01563 259 ESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREE------GIIDKGERV 313
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 23-303 2.11e-22

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: 96.42  E-value: 2.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   23 TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAfSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:COG0498  67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCA-SSGNGSAALAAYAARAGIEVFVFVPE 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  103 D-APALKVAATAGYGAHIIRYN-RYtEDREQIGRQLAAEHGFALIPPYdHPDVIAGQGTSAKELLEEVGQL-DALFVP-- 177
Cdd:COG0498 146 GkVSPGQLAQMLTYGAHVIAVDgNF-DDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLGRVpDWVVVPtg 223

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  178 -------LGGGGLLSGSALAARSLsPgcKIFGVEPEAGNDGQQSFRSG-SIVHINTPKTIADGAQTQH--LGEYTFAIIR 247
Cdd:COG0498 224 nggnilaGYKAFKELKELGLIDRL-P--RLIAVQATGCNPILTAFETGrDEYEPERPETIAPSMDIGNpsNGERALFALR 300

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631  248 ENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGAL-LKKEELVGKKVGIIL 303
Cdd:COG0498 301 ESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRkLREEGEIDPDEPVVV 357
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 22-307 3.08e-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: 94.67  E-value: 3.08e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   22 KTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSK--GVIAFSSGNHAQAIALSAKLLNVPATIV 99
Cdd:cd06448   1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNEcvHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  100 MPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQL--AAEHGFALIPPYDHPDVIAGQGTSAKEL---LEEVGQLDAL 174
Cdd:cd06448  81 VPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREElaENDPGPVYVHPFDDPLIWEGHSSMVDEIaqqLQSQEKVDAI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  175 FvplggggllsgsalaarsLSPG-------------------CKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQT 235
Cdd:cd06448 161 V------------------CSVGgggllngivqglerngwgdIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGA 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  236 QHLGEYTFAIIRENVDDILTVSDQELVK-CMHFLAERmKVVVEPtAC-----LGFAGALLK----KEELVGKKVGIILSG 305
Cdd:cd06448 223 KTVSSQALEYAQEHNIKSEVVSDRDAVQaCLRFADDE-RILVEP-ACgaalaVVYSGKILDlqleVLLTPLDNVVVVVCG 300


                ..
gi 6322631  306 GN 307
Cdd:cd06448 301 GS 302
PRK08197 PRK08197
threonine synthase; Validated
 23-177 1.01e-16

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 80.04  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    23 TPVLTSRMLNDRLGA-QIYFKGENFQRVGAFKFRGAMNAVSKlSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PRK08197  80 TPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGLAVGVSR-AKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMP 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322631   102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVG-QL-DALFVP 177
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLGwRLpDVILYP 236
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 22-303 3.59e-15

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: 74.47  E-value: 3.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   22 KTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLsdEKR---SKG--VIAFSSGNHAQAIALSAKLLNVPA 96
Cdd:cd01561   2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDA--EKRgllKPGttIIEPTSGNTGIGLAMVAAAKGYRF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   97 TIVMPEDAPALKVAATAGYGAHIIR----YNRYTEDREQIGRQLAAEHGFALIP-PYDHPD-VIAGQGTSAKELLEEV-G 169
Cdd:cd01561  80 IIVMPETMSEEKRKLLRALGAEVILtpeaEADGMKGAIAKARELAAETPNAFWLnQFENPAnPEAHYETTAPEIWEQLdG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  170 QLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEagndgqqsfrsGSIVHINTPKTiadGAQTQHLGE-YTFAII-R 247
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPV-----------GSVLFSGGPPG---PHKIEGIGAgFIPENLdR 225

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631  248 ENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELV-GKKVGIIL 303
Cdd:cd01561 226 SLIDEVVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGpGKTIVTIL 282
PRK05638 PRK05638
threonine synthase; Validated
 23-305 4.58e-15

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 75.62  E-value: 4.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    23 TPVLTSRMLnDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKrSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:PRK05638  67 TPLIRARIS-EKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYA-ANGFIVASDGNAAASVAAYSARAGKEAFVVVPR 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   103 DAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQlDALFVPLGGGG 182
Cdd:PRK05638 145 KVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEINP-THVIVPTGSGS 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   183 LLSGSALAARSL-SPGC-----KIFGVEPEAGNDgqqsfrSGSIVHINTPK---TIADGAQTQH--LGEYTFAIIRENVD 251
Cdd:PRK05638 224 YLYSIYKGFKELlEIGVieeipKLIAVQTERCNP------IASEILGNKTKcneTKALGLYVKNpvMKEYVSEAIKESGG 297

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322631   252 DILTVSDQELVKCMHFLAERmKVVVEPTACLGFAGALLKKEELV---GKKVGIILSG 305
Cdd:PRK05638 298 TAVVVNEEEIMAGEKLLAKE-GIFAELSSAVVMPALLKLGEEGYiekGDKVVLVVTG 353
PRK08329 PRK08329
threonine synthase; Validated
 34-307 2.34e-13

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 69.86  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    34 RLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAfSSGNHAQAIALSAKLLNVPATIVMPEDAPALKVAATA 113
Cdd:PRK08329  69 KRSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVID-SSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLS 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   114 GYGA--HIIRYNRYTEDREQIgrQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGGGGLLSGSALAA 191
Cdd:PRK08329 148 RLGAelHFVEGDRMEVHEEAV--KFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSGTLFLGIWKGF 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   192 RSL------SPGCKIFGVEPEagndGQQSFRSGSivhiNTPKTIADGAQTQH--LGEYTFAIIRENVDDILTVSDQELVK 263
Cdd:PRK08329 226 KELhemgeiSKMPKLVAVQAE----GYESLCKRS----KSENKLADGIAIPEppRKEEMLRALEESNGFCISVGEEETRA 297

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 6322631   264 CMHFLaERMKVVVEPTACLGFAG-ALLKKEELV--GKKVGIILSGGN 307
Cdd:PRK08329 298 ALHWL-RRMGFLVEPTSAVALAAyWKLLEEGLIegGSKVLLPLSGSG 343
PRK06381 PRK06381
threonine synthase; Validated
 23-306 3.10e-11

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 63.19  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    23 TPVLTSRMLNDRLG-AQIYFKGENFQRVGAFKFRGAMNAVsKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:PRK06381  16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHV-RRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   102 EDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTS--AKELLEEVGQL-DALFVPL 178
Cdd:PRK06381  95 RSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDIEAYSaiAYEIYEALGDVpDAVAVPV 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   179 GGGGLLSGSALAARSLSPGC------KIFGVEPEAGNDGQQSFRSGS--IVHINtPKTIADGAQTQHL-------GEYTF 243
Cdd:PRK06381 175 GNGTTLAGIYHGFRRLYDRGktsrmpRMIGVSTSGGNQIVESFKRGSseVVDLE-VDEIRETAVNEPLvsyrsfdGDNAL 253

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322631   244 AIIRENVDDILTVSDQELVKCMHFL--AERMKVVVEPTACLGFAGALLKKEELVGKKVgIILSGG 306
Cdd:PRK06381 254 EAIYDSHGYAFGFSDDEMVKYAELLrrMEGLNALPASASALAALVKYLKKNGVNDNVV-AVITGR 317
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 22-269 7.18e-10

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 59.51  E-value: 7.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    22 KTPVLTSRMLNDRLG-AQIYFKGENfQRVG--AFKFRGAMNAVSKL------------------SDEKRSK-GVIAFSS- 78
Cdd:PRK08206  44 PTPLVALPDLAAELGvGSILVKDES-YRFGlnAFKALGGAYAVARLlaeklgldiselsfeeltSGEVREKlGDITFATa 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    79 --GNHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALI-----PPYDHP 151
Cdd:PRK08206 123 tdGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEAQENGWVVVqdtawEGYEEI 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   152 --DVIAGQGTSAKELLEEVGQLDA----LFVPLGGGgllsgsalaarSLSPG-----CKIFG--------VEPEAGNDGQ 212
Cdd:PRK08206 203 ptWIMQGYGTMADEAVEQLKEMGVppthVFLQAGVG-----------SLAGAvlgyfAEVYGeqrphfvvVEPDQADCLY 271

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   213 QSFRSGSIVHI-------------NTPKTIAdgaqtqhlgeytFAIIRENVDDILTVSDQELVKCMHFLA 269
Cdd:PRK08206 272 QSAVDGKPVAVtgdmdtimaglacGEPNPLA------------WEILRNCADAFISCPDEVAALGMRILA 329
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 23-305 8.25e-10

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: 58.93  E-value: 8.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     23 TPVLTSRMLNDRLGAQ-IYFKGENFQRVGAFKFRGAMNAVSKLSDEKRsKGVIAFSSGNHAQAIALSAKLLNVPATIVMP 101
Cdd:TIGR00260  23 TPLFRAPALAANVGIKnLYVKELGHNPTLSFKDRGMAVALTKALELGN-DTVLCASTGNTGAAAAAYAGKAGLKVVVLYP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    102 EDAPAL-KVAATAGYGAHIIRYNRYTEDREQIGRQLAaEHGFAL-------IPPYdhpdvIAGQGTSAKELLEEVGQL-- 171
Cdd:TIGR00260 102 AGKISLgKLAQALGYNAEVVAIDGNFDDAQRLVKQLF-EDKPALglnsansIPYR-----LEGQKTYAFEAVEQLGWEap 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    172 DALFVPLGGGGLLSgsalaarSLSPGCKIF------------GVEPEAGNDGQQSFR-SGSIVHINTPKTIAD----GAQ 234
Cdd:TIGR00260 176 DKVVVPVPNSGNFG-------AIWKGFKEKkmlgldslpvkrGIQAEGAADIVRAFLeGGQWEPIETPETLSTamdiGNP 248

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631    235 TQhlGEYTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELV---GKKVGIILSG 305
Cdd:TIGR00260 249 AN--WPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTadpAERVVCALTG 320
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 14-271 3.06e-08

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: 54.28  E-value: 3.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   14 NRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLsdEKR---SKG--VIAFSSGNHAQAIALS 88
Cdd:COG0031   5 DSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDA--EKRgllKPGgtIVEATSGNTGIGLAMV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   89 AKLLNVPATIVMPEDAPALKVAATAGYGAHIIRynryTEDREQIG------RQLAAEHGFALIP-PYDHPDVIAG--QGT 159
Cdd:COG0031  83 AAAKGYRLILVMPETMSKERRALLRAYGAEVVL----TPGAEGMKgaidkaEELAAETPGAFWPnQFENPANPEAhyETT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631  160 sAKELLEEV-GQLDALFVPlggggllsgsalaaRSLSPGCKIFGVEPEagndgqqsfrsGSIVHintPKTIADGAQTQHL 238
Cdd:COG0031 159 -GPEIWEQTdGKVDAFVAGvgtggtitgvgrylKERNPDIKIVAVEPE-----------GSPLL---SGGEPGPHKIEGI 223

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 6322631  239 GEytfAII-----RENVDDILTVSDQELVKCMHFLAER 271
Cdd:COG0031 224 GA---GFVpkildPSLIDEVITVSDEEAFAMARRLARE 258
PRK06450 PRK06450
threonine synthase; Validated
 16-305 2.03e-07

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 51.66  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    16 IKEYVN----KTPVLTsrmlndrlGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDeKRSKGVIAFSSGNHAQAIALSAKL 91
Cdd:PRK06450  48 IKHFISlgegRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    92 LNVPATIVMPEDAPALKVAATAGYGAHIIRYNrytEDREQIGRQlAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQL 171
Cdd:PRK06450 119 AGIEVKIFVPETASGGKLKQIESYGAEVVRVR---GSREDVAKA-AENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWK 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631   172 --DALFVPLGGGGLLSGSALAARSL------SPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQH--LGEY 241
Cdd:PRK06450 195 ipNYVFIPVSAGTLLLGVYSGFKHLldsgviSEMPKIVAVQTEQVSPLCAKFKGISYTPPDKVTSIADALVSTRpfLLDY 274

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322631   242 TFAIIRENVDDIlTVSDQELVKCMHFLAeRMKVVVEPTACLGFAGalLKKEElVGKKVgIILSG 305
Cdd:PRK06450 275 MVKALSEYGECI-VVSDNEIVEAWKELA-KKGLLVEYSSATVYAA--YKKYS-VNDSV-LVLTG 332
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 16-271 1.48e-05

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: 45.73  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     16 IKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDE---KRSKGVIAFSSGNHAQAIALSAKLL 92
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRgllKPGDTIIEATSGNTGIALAMVAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     93 NVPATIVMPEDAPALKVAATAGYGAHIIrynrYTEDRE------QIGRQLAAE-HGFALIPPYDHPD-VIAGQGTSAKEL 164
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELI----LTPGEEgmkgaiDKAEELAAEtNKYVMLDQFENPAnPEAHYKTTGPEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    165 LEEV-GQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSgsivhintPKTIadgaqtQHLG-EYT 242
Cdd:TIGR01136 157 WRDTdGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPG--------PHKI------QGIGaGFI 222

                         250       260       270
                  ....*....|....*....|....*....|
gi 6322631    243 FAII-RENVDDILTVSDQELVKCMHFLAER 271
Cdd:TIGR01136 223 PKILdLSLIDEVITVSDEDAIETARRLARE 252
cysM PRK11761
cysteine synthase CysM;
16-120 1.56e-05

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 46.02  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    16 IKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLsdEKR---SKG--VIAFSSGNHAQAIALSAK 90
Cdd:PRK11761   6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQA--EKRgeiKPGdtLIEATSGNTGIALAMIAA 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 6322631    91 LLNVPATIVMPEDAPALKVAATAGYGAHII 120
Cdd:PRK11761  84 IKGYRMKLIMPENMSQERRAAMRAYGAELI 113
PLN02569 PLN02569
threonine synthase
 33-169 9.38e-05

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 44.03  E-value: 9.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    33 DRLGAQ------IYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSK----GVIAFSSGNHAQAIALSAKLLNVPATIVMPE 102
Cdd:PLN02569 140 ERLGKEflgmndLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMAkpvvGVGCASTGDTSAALSAYCAAAGIPSIVFLPA 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322631   103 DAPAL-KVAATAGYGAHIIRYNRYTEDREQIGRQLAAEhgfalIPPYD----HPDVIAGQGTSAKELLEEVG 169
Cdd:PLN02569 220 DKISIaQLVQPIANGALVLSIDTDFDGCMRLIREVTAE-----LPIYLanslNSLRLEGQKTAAIEILQQFD 286
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 16-303 1.58e-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: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     16 IKEYVNKTPVLTsrmLN--DRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDE---KRSKGVIAFSSGNHAQAIALSAK 90
Cdd:TIGR01139   1 ISELIGNTPLVR---LNriEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRgllKPGKTIVEPTSGNTGIALAMVAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631     91 LLNVPATIVMPEDAPALKVAATAGYGAHIIrynrYTEDREQIG------RQLAAEHG--FALIPPYDHP-DVIAGQGTSA 161
Cdd:TIGR01139  78 ARGYKLILTMPETMSIERRKLLKAYGAELV----LTPGAEGMKgaiakaEEIAASTPnsYFMLQQFENPaNPEIHRKTTG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    162 KELLEEV-GQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEP---------EAGNDGQQSFRSGSIvhintPKtIAD 231
Cdd:TIGR01139 154 PEIWRDTdGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPaespvlsggKPGPHKIQGIGAGFI-----PK-NLN 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322631    232 gaqtqhlgeytfaiiRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGAL-LKKEELVGKKVGIIL 303
Cdd:TIGR01139 228 ---------------RSVIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALkLAKRPEPDKLIVVIL 285
D-Ser-dehyd cd06447
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 245-298 1.37e-03

D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.


Pssm-ID: 107208  Cd Length: 404  Bit Score: 40.02  E-value: 1.37e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 6322631  245 IIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKK 298
Cdd:cd06447 326 LMEPLLSGIYTVEDDELYRLLAMLKDSENIEVEPSAAAGFTGPAQVLSEAEGKR 379
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 16-120 9.96e-03

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 37.48  E-value: 9.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322631    16 IKEYVNK-TPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMnAVSKLSDEKRSKGVIAFS-SGNHAQAIALSAKLLN 93
Cdd:PRK13803 264 LQNYAGRpTPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNAL-GQALLAKRMGKTRIIAETgAGQHGVATATACALFG 342

                         90       100       110
                 ....*....|....*....|....*....|
gi 6322631    94 VPATIVMPED---APALKVAATAGYGAHII 120
Cdd:PRK13803 343 LKCTIFMGEEdikRQALNVERMKLLGANVI 372
 
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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