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Conserved domains on  [gi|515925163|ref|WP_017355746|]
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MULTISPECIES: pyridoxal-phosphate dependent enzyme [Stenotrophomonas]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 24-314 5.67e-110

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


The actual alignment was detected with superfamily member PLN02970:

Pssm-ID: 444852 [Multi-domain]  Cd Length: 328  Bit Score: 322.40  E-value: 5.67e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:PLN02970  26 HRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYIVV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGG 183
Cdd:PLN02970 106 PKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIVPISG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 184 GGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLRGTLGQPNFALLQPAAS-VLTVRDADT 262
Cdd:PLN02970 186 GGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRASLGDLTWPVVRDLVDdVITVDDKEI 265

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515925163 263 VAAMRLIWQVLKQVVEPS-----SAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:PLN02970 266 IEAMKLCYERLKVVVEPSgaiglAAALSDSFRSNPAWKGCKNVGIVLSGGNVDLGVL 322
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
 24-314 5.67e-110

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 322.40  E-value: 5.67e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:PLN02970  26 HRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYIVV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGG 183
Cdd:PLN02970 106 PKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIVPISG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 184 GGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLRGTLGQPNFALLQPAAS-VLTVRDADT 262
Cdd:PLN02970 186 GGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRASLGDLTWPVVRDLVDdVITVDDKEI 265

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515925163 263 VAAMRLIWQVLKQVVEPS-----SAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:PLN02970 266 IEAMKLCYERLKVVVEPSgaiglAAALSDSFRSNPAWKGCKNVGIVLSGGNVDLGVL 322
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 24-316 1.44e-101

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: 301.19  E-value: 1.44e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:COG1171   23 RRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQGVAYAARLLGIPATIVM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGG 183
Cdd:COG1171  103 PETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQLPDLDAVFVPVGG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 184 GGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLR-GTLGQPNFALLQPAAS-VLTVRDAD 261
Cdd:COG1171  183 GGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAvGRPGELTFEILRDLVDdIVTVSEDE 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515925163 262 TVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDALPW 316
Cdd:COG1171  263 IAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAE 317
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-310 1.58e-99

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: 295.17  E-value: 1.58e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   9 VDDVLAAAARIAPHARVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAAL 88
Cdd:cd01562    1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  89 ALAARTRGIACHVVVPEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELL 168
Cdd:cd01562   81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 169 HGHGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLRG-TLGQPNFAL 247
Cdd:cd01562  161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVkRPGELTFEI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515925163 248 LQPAAS-VLTVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVD 310
Cdd:cd01562  241 IRKLVDdVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 24-306 2.29e-58

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 189.44  E-value: 2.29e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:pfam00291   6 GPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAE-TGGTLVHPYTHSHVIAGQGTAALELLHGHGP-FDTLVVPV 181
Cdd:pfam00291  86 PEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLGGdPDAVVVPV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  182 GGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLR--GTLGQPNFALLQ-PAASVLTVR 258
Cdd:pfam00291 166 GGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGvgDEPGALALDLLDeYVGEVVTVS 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 515925163  259 DADTVAAMRLIWQVLKQVVEPSSAIA-LAAILGAPERF-AGQRVGVVLSG 306
Cdd:pfam00291 246 DEEALEAMRLLARREGIVVEPSSAAAlAALKLALAGELkGGDRVVVVLTG 295
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 26-314 1.69e-48

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: 166.46  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVVPE 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  106 GAVAAKL-------ANIVRHGATLwrCEASIAAREamcaqVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLV 178
Cdd:TIGR01127  81 SAPPSKVkatksygAEVILHGDDY--DEAYAFATS-----LAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  179 VPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGE-RRVDITPdTVCDGLR-GTLGQPNFALLQPAA-SVL 255
Cdd:TIGR01127 154 VPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKiKAVESVR-TIADGIAvKKPGDLTFNIIKEYVdDVV 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 515925163  256 TVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:TIGR01127 233 TVDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLL 291
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
 24-314 5.67e-110

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 322.40  E-value: 5.67e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:PLN02970  26 HRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAAALALAAKLRGIPAYIVV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGG 183
Cdd:PLN02970 106 PKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQVPELDVIIVPISG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 184 GGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLRGTLGQPNFALLQPAAS-VLTVRDADT 262
Cdd:PLN02970 186 GGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRASLGDLTWPVVRDLVDdVITVDDKEI 265

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515925163 263 VAAMRLIWQVLKQVVEPS-----SAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:PLN02970 266 IEAMKLCYERLKVVVEPSgaiglAAALSDSFRSNPAWKGCKNVGIVLSGGNVDLGVL 322
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 24-316 1.44e-101

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: 301.19  E-value: 1.44e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:COG1171   23 RRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNHAQGVAYAARLLGIPATIVM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGG 183
Cdd:COG1171  103 PETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEILEQLPDLDAVFVPVGG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 184 GGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLR-GTLGQPNFALLQPAAS-VLTVRDAD 261
Cdd:COG1171  183 GGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIADGLAvGRPGELTFEILRDLVDdIVTVSEDE 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515925163 262 TVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDALPW 316
Cdd:COG1171  263 IAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSGGNIDPDRLAE 317
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 9-310 1.58e-99

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: 295.17  E-value: 1.58e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   9 VDDVLAAAARIAPHARVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAAL 88
Cdd:cd01562    1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  89 ALAARTRGIACHVVVPEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELL 168
Cdd:cd01562   81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 169 HGHGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLRG-TLGQPNFAL 247
Cdd:cd01562  161 EQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVkRPGELTFEI 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515925163 248 LQPAAS-VLTVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVD 310
Cdd:cd01562  241 IRKLVDdVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
2-314 7.73e-89

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 268.43  E-value: 7.73e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   2 SDSPLPCVDDVLAAAARIAPHARVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSS 81
Cdd:PRK07048   1 SDLLLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  82 GNHGAALALAARTRGIACHVVVPEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQG 161
Cdd:PRK07048  81 GNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 162 TAALELLHGHGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGE-RRVDiTPDTVCDGLRGT- 239
Cdd:PRK07048 161 TAAKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEiVHID-TPRTIADGAQTQh 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515925163 240 LGQPNFAL-LQPAASVLTVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:PRK07048 240 LGNYTFPIiRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLARF 315
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 24-306 2.29e-58

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 189.44  E-value: 2.29e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:pfam00291   6 GPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAE-TGGTLVHPYTHSHVIAGQGTAALELLHGHGP-FDTLVVPV 181
Cdd:pfam00291  86 PEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLGGdPDAVVVPV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  182 GGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLR--GTLGQPNFALLQ-PAASVLTVR 258
Cdd:pfam00291 166 GGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGvgDEPGALALDLLDeYVGEVVTVS 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 515925163  259 DADTVAAMRLIWQVLKQVVEPSSAIA-LAAILGAPERF-AGQRVGVVLSG 306
Cdd:pfam00291 246 DEEALEAMRLLARREGIVVEPSSAAAlAALKLALAGELkGGDRVVVVLTG 295
PRK06815 PRK06815
threonine/serine dehydratase;
24-314 3.82e-55

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 181.81  E-value: 3.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:PRK06815  19 RVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGVALAAKLAGIPVTVYA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGG 183
Cdd:PRK06815  99 PEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQPDLDAVFVAVGG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 184 GGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGE-RRVDITPdTVCDGLRGTL--GQPNFALLQPAAS-VLTVRD 259
Cdd:PRK06815 179 GGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEiVEVAEQP-TLSDGTAGGVepGAITFPLCQQLIDqKVLVSE 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515925163 260 ADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:PRK06815 258 EEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKY 312
PRK06608 PRK06608
serine/threonine dehydratase;
4-310 7.94e-52

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 173.80  E-value: 7.94e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   4 SPLPCVDDVLAAAARIAPHARVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAV-WAMDDAQAARGVVTHSSG 82
Cdd:PRK06608   2 LLLQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLlELKEQGKLPDKIVAYSTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  83 NHGAALALAARTRGIACHVVVPEGAVAAKLANIVRHGA----TLWRCEASIAAREAMcaqvqaETGGTLVHPYTHSHVIA 158
Cdd:PRK06608  82 NHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGevilTNTRQEAEEKAKEDE------EQGFYYIHPSDSDSTIA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 159 GQGTAALELLH--GHGPfDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGE-RRVDITPDTVCDG 235
Cdd:PRK06608 156 GAGTLCYEALQqlGFSP-DAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKiYRLNYSPNTIADG 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515925163 236 LRG-TLGQPNFALLQPAASVLTVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILG-APERFAGQRVGVVLSGGNVD 310
Cdd:PRK06608 235 LKTlSVSARTFEYLKKLDDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNwLKTQSKPQKLLVILSGGNID 311
PRK07334 PRK07334
threonine dehydratase; Provisional
 26-310 1.29e-51

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 175.08  E-value: 1.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVVPE 105
Cdd:PRK07334  24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQGVAYHAQRLGIPATIVMPR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 106 GAVAAKL-------ANIVRHGATLwrCEASIAAREamcaqVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLV 178
Cdd:PRK07334 104 FTPTVKVertrgfgAEVVLHGETL--DEARAHARE-----LAEEEGLTFVHPYDDPAVIAGQGTVALEMLEDAPDLDTLV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 179 VPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAAdtarSLAAGERRVDITP--DTVCDGLR-GTLGQPNFALLQPAAS-V 254
Cdd:PRK07334 177 VPIGGGGLISGMATAAKALKPDIEIIGVQTELYP----SMYAAIKGVALPCggSTIAEGIAvKQPGQLTLEIVRRLVDdI 252

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515925163 255 LTVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVD 310
Cdd:PRK07334 253 LLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNID 308
PRK08246 PRK08246
serine/threonine dehydratase;
24-314 3.38e-49

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 166.28  E-value: 3.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRtLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAarGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:PRK08246  22 RRTPVLEAD-GAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPVPAA--GVVAASGGNAGLAVAYAAAALGVPATVFV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGG 183
Cdd:PRK08246  99 PETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVAVGG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 184 GGLAAGTVLAMqalAPTARLVLAEPEGAADTARSLAAGErRVDITPDTVCDGLRG--TLGQPNFALLQ--PAASVLtVRD 259
Cdd:PRK08246 179 GGLIAGIAAWF---EGRARVVAVEPEGAPTLHAALAAGE-PVDVPVSGIAADSLGarRVGEIAFALARahVVTSVL-VSD 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515925163 260 ADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFA-GQRVGVVLSGGNVDLDAL 314
Cdd:PRK08246 254 EAIIAARRALWEELRLAVEPGAATALAALLSGAYVPApGERVAVVLCGANTDPATL 309
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 26-314 1.69e-48

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: 166.46  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVVPE 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  106 GAVAAKL-------ANIVRHGATLwrCEASIAAREamcaqVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLV 178
Cdd:TIGR01127  81 SAPPSKVkatksygAEVILHGDDY--DEAYAFATS-----LAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  179 VPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGE-RRVDITPdTVCDGLR-GTLGQPNFALLQPAA-SVL 255
Cdd:TIGR01127 154 VPVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKiKAVESVR-TIADGIAvKKPGDLTFNIIKEYVdDVV 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 515925163  256 TVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:TIGR01127 233 TVDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLL 291
eutB PRK07476
threonine dehydratase; Provisional
 24-313 1.55e-43

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 151.66  E-value: 1.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:PRK07476  18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGRALAYAARALGIRATICM 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGG 183
Cdd:PRK07476  98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEALPDVATVLVPLSG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 184 GGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGeRRVDITP-DTVCDGLRGTLGQPN---FALLQPAA-SVLTVR 258
Cdd:PRK07476 178 GGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAG-RPVQVEEvPTLADSLGGGIGLDNrytFAMCRALLdDVVLLD 256

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515925163 259 DADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDA 313
Cdd:PRK07476 257 EAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANIDMEL 311
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 26-307 3.18e-43

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: 148.82  E-value: 3.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVW-AMDDAQAARGVVTH-SSGNHGAALALAARTRGIACHVVV 103
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILlAEEEGKLPKGVIIEsTGGNTGIALAAAAARLGLKCTIVM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGG-TLVHPYTHSHVIAGQGTAALELLH--GHGPFDTLVVP 180
Cdd:cd00640   81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGTIGLEILEqlGGQKPDAVVVP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 181 VGGGGLAAGTVLAMQALAPTARLVLAEPEgaadtarslaagerrvditpdtvcdglrgtlgqpnfallqpaasVLTVRDA 260
Cdd:cd00640  161 VGGGGNIAGIARALKELLPNVKVIGVEPE--------------------------------------------VVTVSDE 196

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 515925163 261 DTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERF-AGQRVGVVLSGG 307
Cdd:cd00640  197 EALEAIRLLAREEGILVEPSSAAALAAALKLAKKLgKGKTVVVILTGG 244
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
6-311 4.47e-42

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 148.35  E-value: 4.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   6 LPC-VDDVLAAAARIAPHARVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNH 84
Cdd:PRK08638   7 LPVaIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNH 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  85 GAALALAARTRGIACHVVVPEGAVAAKL-------ANIVRHGATLwrcEASIaareAMCAQVQAETGGTLVHPYTHSHVI 157
Cdd:PRK08638  87 AQGVALSCALLGIDGKVVMPKGAPKSKVaatcgygAEVVLHGDNF---NDTI----AKVEEIVEEEGRTFIPPYDDPKVI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 158 AGQGTAALELLHGHGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLR 237
Cdd:PRK08638 160 AGQGTIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADGCD 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515925163 238 -GTLGQPNFALLQPAAS-VLTVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAP--ERFAGQRVGVVLSGGNVDL 311
Cdd:PRK08638 240 vSRPGNLTYEIVRELVDdIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKldQYIQNKKVVAIISGGNVDL 317
PRK08639 PRK08639
threonine dehydratase; Validated
 1-315 1.50e-39

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 143.79  E-value: 1.50e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   1 MSDSPLPCVDDVLAAAARIAPHARVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHS 80
Cdd:PRK08639   1 MTVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  81 SGNHGAALALAARTRGIACHVVVPEGAVAAKLANIVRHGATLWRC--------EASIAAREamCAqvqAETGGTLVHPYT 152
Cdd:PRK08639  81 AGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFVEIvlvgdtfdDSAAAAQE--YA---EETGATFIPPFD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 153 HSHVIAGQGTAALELLHGH---GPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERrvdITP 229
Cdd:PRK08639 156 DPDVIAGQGTVAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKP---VTL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 230 DTV---CDGLR-GTLGQPNFALLQPA-ASVLTVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVL 304
Cdd:PRK08639 233 EKIdkfVDGAAvARVGDLTFEILKDVvDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKTVVCVI 312

                        330
                 ....*....|.
gi 515925163 305 SGGNVDLDALP 315
Cdd:PRK08639 313 SGGNNDIERMP 323
PRK12483 PRK12483
threonine dehydratase; Reviewed
 24-314 1.82e-39

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 145.32  E-value: 1.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:PRK12483  36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQGVALAAARLGVKAVIVM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGH-GPFDTLVVPVG 182
Cdd:PRK12483 116 PRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHpGPLDAIFVPVG 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 183 GGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLR-GTLGQPNFALLQP-AASVLTVRDA 260
Cdd:PRK12483 196 GGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAvAQIGEHTFELCRHyVDEVVTVSTD 275

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515925163 261 DTVAAMRLIWQVLKQVVEPSSAIALAAILGAPER--FAGQRVGVVLSGGNVDLDAL 314
Cdd:PRK12483 276 ELCAAIKDIYDDTRSITEPAGALAVAGIKKYAERegIEGQTLVAIDSGANVNFDRL 331
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
24-314 4.33e-35

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 132.95  E-value: 4.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  24 RVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:PRK09224  19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGVALSAARLGIKAVIVM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PE-------GAVAAKLANIVRHGATLwrceaSIAAREAMcaQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGH-GPFD 175
Cdd:PRK09224  99 PVttpdikvDAVRAFGGEVVLHGDSF-----DEAYAHAI--ELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHpHPLD 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 176 TLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERrvdITPDTVcdGL--RGT----LGQPNFALLQ 249
Cdd:PRK09224 172 AVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGER---VDLPQV--GLfaDGVavkrIGEETFRLCQ 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515925163 250 PAAS-VLTVrDADTV-AAMRLIWQVLKQVVEPSSAIALAAILGAPER--FAGQRVGVVLSGGNVDLDAL 314
Cdd:PRK09224 247 EYVDdVITV-DTDEIcAAIKDVFEDTRSIAEPAGALALAGLKKYVAQhgIEGETLVAILSGANMNFDRL 314
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 9-313 9.13e-34

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: 126.12  E-value: 9.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163    9 VDDVLAAAARIAPHARVTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAAL 88
Cdd:TIGR02991   3 LQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGRAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   89 ALAARTRGIACHVVVPEGAVAAKLANIVRHGAtlwrcEASIAAREAMCAQVQ-----AETGGTLVHPYTHSHVIAGQGTA 163
Cdd:TIGR02991  83 AYAAAEEGVRATICMSELVPQNKVDEIRRLGA-----EVRIVGRSQDDAQEEverlvADRGLTMLPPFDHPDIVAGQGTL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  164 ALELLHGHGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLRGTLGQP 243
Cdd:TIGR02991 158 GLEVVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLGGGIGLD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515925163  244 N---FALLQPAA-SVLTVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGqRVGVVLSGGNVDLDA 313
Cdd:TIGR02991 238 NrvtFAMCKALLdEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPG-PCAVIVSGRNIDMDL 310
PRK06110 PRK06110
threonine dehydratase;
26-314 3.48e-30

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 116.63  E-value: 3.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAV-WAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVVP 104
Cdd:PRK06110  22 TPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFdRLARRGPRVRGVISATRGNHGQSVAFAARRHGLAATIVVP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 105 EG-------AVAAKLANIVRHGATLWrceasiAAREAmcAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTL 177
Cdd:PRK06110 102 HGnsveknaAMRALGAELIEHGEDFQ------AAREE--AARLAAERGLHMVPSFHPDLVRGVATYALELFRAVPDLDVV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 178 VVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLRGTLGQPN-FALLQP-AASVL 255
Cdd:PRK06110 174 YVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEaLEVIRAgADRIV 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515925163 256 TVRDADTVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:PRK06110 254 RVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERERLAGKRVGLVLSGGNIDRAVF 312
PLN02550 PLN02550
threonine dehydratase
 26-314 5.47e-26

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 108.08  E-value: 5.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVVPE 105
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGCDAVIAMPV 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 106 GAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGH-GPFDTLVVPVGGG 184
Cdd:PLN02550 190 TTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHqGPLHAIFVPVGGG 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 185 GLAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLR-GTLGQPNFALLQPAAS--VLTVRDAd 261
Cdd:PLN02550 270 GLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAvKEVGEETFRLCRELVDgvVLVSRDA- 348

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515925163 262 TVAAMRLIWQVLKQVVEPSSAIALAAILGAPERFA--GQRVGVVLSGGNVDLDAL 314
Cdd:PLN02550 349 ICASIKDMFEEKRSILEPAGALALAGAEAYCKYYGlkDENVVAITSGANMNFDRL 403
PRK08813 PRK08813
threonine dehydratase; Provisional
 44-314 8.87e-26

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 105.09  E-value: 8.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  44 FKGEHLQRGGAFKFRGACNAVWAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVVPEGAVAAKLANIVRHGATLW 123
Cdd:PRK08813  52 LKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 124 RCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLhGHGPfDTLVVPVGGGGLAAGTVLAMQALAptARL 203
Cdd:PRK08813 132 QHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELA-AHAP-DVVIVPIGGGGLASGVALALKSQG--VRV 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 204 VLAEPEGAADTARSLAAGERrvDITP-DTVCDGLRGTLgqPNFALLQPAAS----VLTVRDADTVAAmrLIWQVLKQVVe 278
Cdd:PRK08813 208 VGAQVEGVDSMARAIRGDLR--EIAPvATLADGVKVKI--PGFLTRRLCSSllddVVIVREAELRET--LVRLALEEHV- 280

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 515925163 279 pSSAIALAAILGAPERFAGQRVGVVLSGGNVDLDAL 314
Cdd:PRK08813 281 -IAEGAGALALAAGRRVSGKRKCAVVSGGNIDATVL 315
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 25-281 5.63e-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: 94.88  E-value: 5.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  25 VTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAV-WAMddAQAARGVVTHSSGNHGAALALAARTRGIACHVVV 103
Cdd:COG0498   66 GTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVsLAL--ERGAKTIVCASSGNGSAALAAYAARAGIEVFVFV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 104 PEGAVA-AKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVH---PYThshvIAGQGTAALELLH--GHGPfDTL 177
Cdd:COG0498  144 PEGKVSpGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNsinPAR----LEGQKTYAFEIAEqlGRVP-DWV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 178 VVPVGGGGLAAGTVLAMQAL------APTARLVLAEPEGAADTARSLAAGERRVDIT-PDTVCDGLRgTLGQPNFALLQP 250
Cdd:COG0498  219 VVPTGNGGNILAGYKAFKELkelgliDRLPRLIAVQATGCNPILTAFETGRDEYEPErPETIAPSMD-IGNPSNGERALF 297

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 515925163 251 A-----ASVLTVRDADTVAAMRLIWQVLKQVVEPSS 281
Cdd:COG0498  298 AlresgGTAVAVSDEEILEAIRLLARREGIFVEPAT 333
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 25-280 1.60e-21

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: 92.75  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  25 VTPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVW-AMDDAQA-ARGVVTHSSGNHGAALALAARTRGIACHVV 102
Cdd:cd06448    1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQkSAKQGLNeCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 103 VPEG---AVAAKL----ANIVRHGATLWrcEASIAAREAMcaqVQAETGGTLVHPYTHSHVIAGQGTAALEL---LHGHG 172
Cdd:cd06448   81 VPEStkpRVVEKLrdegATVVVHGKVWW--EADNYLREEL---AENDPGPVYVHPFDDPLIWEGHSSMVDEIaqqLQSQE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 173 PFDTLVVPVGGGGLAAGTVLAMQ-ALAPTARLVLAEPEGAADTARSLAAGERRVDITPDTVCDGLrGTLGQPNFAL---L 248
Cdd:cd06448  156 KVDAIVCSVGGGGLLNGIVQGLErNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSL-GAKTVSSQALeyaQ 234

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 515925163 249 QPAASVLTVRDADTVAAmrlIWQVL---KQVVEPS 280
Cdd:cd06448  235 EHNIKSEVVSDRDAVQA---CLRFAddeRILVEPA 266
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 26-281 6.22e-19

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: 85.72  E-value: 6.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGA-ELAFKGEHLQRGGAFKFRGACNAVwAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVVP 104
Cdd:cd01563   23 TPLVRAPRLGERLGGkNLYVKDEGLNPTGSFKDRGMTVAV-SKAKELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 105 EGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHpYTHSHVIAGQGTAALEL---LHGHGPfDTLVVPV 181
Cdd:cd01563  102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLSN-SLNPYRLEGQKTIAFEIaeqLGWEVP-DYVVVPV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 182 GGGGLAAGTVLAMQALA--------PtaRLVLAEPEGAADTARSLAAGERRVDI--TPDTVCDGLRgtLGQP-NFALLQP 250
Cdd:cd01563  180 GNGGNITAIWKGFKELKelglidrlP--RMVGVQAEGAAPIVRAFKEGKDDIEPveNPETIATAIR--IGNPaSGPKALR 255

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 515925163 251 AA-----SVLTVRDADTVAAMRLIWQVLKQVVEPSS 281
Cdd:cd01563  256 AVresggTAVAVSDEEILEAQKLLARTEGIFVEPAS 291
PRK08197 PRK08197
threonine synthase; Validated
 26-237 2.60e-12

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 66.95  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGA-ELAFKGEHLQRGGAFKFRGACNAVwAMDDAQAARGVVTHSSGNHGAALALAARTRGIACHVVVP 104
Cdd:PRK08197  80 TPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGLAVGV-SRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMP 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 105 EGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETG----GTLVHPYThshvIAGQGTAALELLHGHG---PfDTL 177
Cdd:PRK08197 159 ADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGwfdvSTLKEPYR----IEGKKTMGLELAEQLGwrlP-DVI 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515925163 178 VVPVGGGGLAAGTVLAMQALA-------PTARLVLAEPEGAADTARSLAAGERRVDITPD--TVCDGLR 237
Cdd:PRK08197 234 LYPTGGGVGLIGIWKAFDELEalgwiggKRPRLVAVQAEGCAPIVKAWEEGKEESEFWEDahTVAFGIR 302
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 76-268 4.18e-09

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 57.20  E-value: 4.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  76 VVTHSSGNHGAALALAARTRGIACHVVVPEGAVAAKLANIVRHGAtlwrcEASI-------AAREAmcAQVQAETGGTLV 148
Cdd:PRK08206 119 FATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGA-----ECIItdgnyddSVRLA--AQEAQENGWVVV 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 149 HP-----YTH--SHVIAGQGTAALELLH---GHGPFDTLVVPVGG-GGLAAGTVLAMQALAPTARL--VLAEPEGAADTA 215
Cdd:PRK08206 192 QDtawegYEEipTWIMQGYGTMADEAVEqlkEMGVPPTHVFLQAGvGSLAGAVLGYFAEVYGEQRPhfVVVEPDQADCLY 271

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515925163 216 RSLAAGE-RRVDITPDTVCDGLrgTLGQPN---FALLQPAASV-LTVRDADTVAAMRL 268
Cdd:PRK08206 272 QSAVDGKpVAVTGDMDTIMAGL--ACGEPNplaWEILRNCADAfISCPDEVAALGMRI 327
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 26-212 4.72e-09

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 56.37  E-value: 4.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRgacNAVWAMDDAQAaRGVVTH-------SSGNHGAALALAARTRGIA 98
Cdd:cd01561    3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDR---IALYMIEDAEK-RGLLKPgttiiepTSGNTGIGLAMVAAAKGYR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  99 CHVVVPEGAVAAKLANIVRHGATLWRCEAS----IAAREAMCAQVQAETGG--------TLVHPYTHSHviagqgTAALE 166
Cdd:cd01561   79 FIIVMPETMSEEKRKLLRALGAEVILTPEAeadgMKGAIAKARELAAETPNafwlnqfeNPANPEAHYE------TTAPE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515925163 167 LLHG-HGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAA 212
Cdd:cd01561  153 IWEQlDGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSV 199
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 24-281 1.22e-07

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: 52.38  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   24 RVTPVLRSRTLDAMSGA-ELAFKGEHLQRGGAFKFRGACNAVwamddAQAARG----VVTHSSGNHGAALALAARTRGIA 98
Cdd:TIGR00260  21 GVTPLFRAPALAANVGIkNLYVKELGHNPTLSFKDRGMAVAL-----TKALELgndtVLCASTGNTGAAAAAYAGKAGLK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163   99 CHVVVPEGAVAA-KLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVH-----PYThshvIAGQGTAA---LELLH 169
Cdd:TIGR00260  96 VVVLYPAGKISLgKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNsansiPYR----LEGQKTYAfeaVEQLG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  170 GHGPfDTLVVPVGGGG-----LAAGTVLAMQALAPTARLVLAEPEGAADTARSLAAGERRVDI-TPDTVCDGLRgtLGQP 243
Cdd:TIGR00260 172 WEAP-DKVVVPVPNSGnfgaiWKGFKEKKMLGLDSLPVKRGIQAEGAADIVRAFLEGGQWEPIeTPETLSTAMD--IGNP 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 515925163  244 N------FALLQPAASVLTVRDADTVAAMRLIWQVLKQVVEPSS 281
Cdd:TIGR00260 249 AnwpralEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHS 292
PRK08329 PRK08329
threonine synthase; Validated
 25-189 1.26e-07

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 52.52  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  25 VTPVLRSrtldamsGAELAFKGEHLQRGGAFKFRGACNAVWAMDDaQAARGVVTHSSGNHGAALALAARTRGIACHVVVP 104
Cdd:PRK08329  64 ITPTVKR-------SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKE-EGINEVVIDSSGNAALSLALYSLSEGIKVHVFVS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 105 EGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQGTAALELLHGHGPFDTLVVPVGGG 184
Cdd:PRK08329 136 YNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVPVGSG 215


                 ....*
gi 515925163 185 GLAAG 189
Cdd:PRK08329 216 TLFLG 220
PRK05638 PRK05638
threonine synthase; Validated
 26-184 1.32e-06

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 49.43  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMsGAELAFKGEHLQRGGAFKFRGACNAV-WAMDdaQAARGVVTHSSGNHGAALALAARTRGIACHVVVP 104
Cdd:PRK05638  67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVsYGLP--YAANGFIVASDGNAAASVAAYSARAGKEAFVVVP 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 105 EGAVAAKLANIVRHGATLWRCEASIaaREAMCAQVQAETGGTLVHPYTHSHVIA--GQGTAALELLHGHGPfDTLVVPVG 182
Cdd:PRK05638 144 RKVDKGKLIQMIAFGAKIIRYGESV--DEAIEYAEELARLNGLYNVTPEYNIIGleGQKTIAFELWEEINP-THVIVPTG 220


                 ..
gi 515925163 183 GG 184
Cdd:PRK05638 221 SG 222
PLN02356 PLN02356
phosphateglycerate kinase
 26-211 4.79e-06

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 47.68  E-value: 4.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVW-AMDDAQ-AARGVVTH-SSGNHGAALALAARTRGIACHVV 102
Cdd:PLN02356  54 TPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEeALESGQlFPGGVVTEgSAGSTAISLATVAPAYGCKCHVV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 103 VPEGAVAAKLANIVRHGATLWRCE----------ASIAAREA---------------MCAQVQAETGGTLV----HPYTH 153
Cdd:PLN02356 134 IPDDVAIEKSQILEALGATVERVRpvsithkdhyVNIARRRAleanelaskrrkgseTDGIHLEKTNGCISeeekENSLF 213

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515925163 154 SHVIAG-----------------QGTAALELLHGHGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGA 211
Cdd:PLN02356 214 SSSCTGgffadqfenlanfrahyEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGS 288
PRK06450 PRK06450
threonine synthase; Validated
 26-190 6.36e-06

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 47.04  E-value: 6.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRsrtldamsGAELAFKGEHLQRGGAFKFRGACNAVWAMDDaQAARGVVTHSSGNHGAALALAARTRGIACHVVVPE 105
Cdd:PRK06450  59 TPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAE-KGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPE 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 106 GAVAAKLANIVRHGATLWRCEASiaaREAMcaQVQAETGGTlvhpYTHSHVIA-----GQGTAALELL--HGHGPFDTLV 178
Cdd:PRK06450 130 TASGGKLKQIESYGAEVVRVRGS---REDV--AKAAENSGY----YYASHVLQpqfrdGIRTLAYEIAkdLDWKIPNYVF 200

                        170
                 ....*....|..
gi 515925163 179 VPVGGGGLAAGT 190
Cdd:PRK06450 201 IPVSAGTLLLGV 212
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 26-267 6.93e-05

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: 43.88  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRgacnAVWAM-DDAQAaRGVVTH-------SSGNHGAALALAARTRGI 97
Cdd:COG0031   14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDR----IALSMiEDAEK-RGLLKPggtiveaTSGNTGIGLAMVAAAKGY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  98 ACHVVVPEGAVAAKLANIVRHGATLWRCEAS--IAAREAMCAQVQAETGGTLV--------HPYTHSHviagqgTAALEL 167
Cdd:COG0031   89 RLILVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAAETPGAFWpnqfenpaNPEAHYE------TTGPEI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163 168 LHG-HGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAAdTARSLAAGERRVditpdtvcdglRGtLGqPNF- 245
Cdd:COG0031  163 WEQtDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSP-LLSGGEPGPHKI-----------EG-IG-AGFv 228

                        250       260
                 ....*....|....*....|....*
gi 515925163 246 -ALLQPAA--SVLTVRDADTVAAMR 267
Cdd:COG0031  229 pKILDPSLidEVITVSDEEAFAMAR 253
PRK10717 PRK10717
cysteine synthase A; Provisional
 26-212 6.21e-04

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 41.00  E-value: 6.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  26 TPVLRSRTLDAMSGAELAFKGEHLQRGGAFKFRGACNAVWamdDAQAaRG-------VVTHSSGNHGAALALAARTRGIA 98
Cdd:PRK10717  14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIW---DAEK-RGllkpggtIVEGTAGNTGIGLALVAAARGYK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  99 CHVVVPEGAVAAKLANIVRHGATLWRCEASIAAREAMCAQVQAETGGTLVHPYTHSHVIAGQ-----------GTAALEL 167
Cdd:PRK10717  90 TVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNNYVKGAGRLAEELVASEPNGAIWANQfdnpanreahyETTGPEI 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515925163 168 LHG-HGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLVLAEPEGAA 212
Cdd:PRK10717 170 WEQtDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSA 215
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 96-204 3.75e-03

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 38.66  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515925163  96 GIACHVVVpEGAVAAKLANIVR---------HGATLWRCEAS---IAAREAMCAQVQAETGGTLVHPYTHSHVIAGQG-- 161
Cdd:PRK03910  89 GLKCVLLL-ENPVPTEAENYLAngnvllddlFGAEIHVVPAGtdmDAQLEELAEELRAQGRRPYVIPVGGSNALGALGyv 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515925163 162 TAALELLH----GHGPFDTLVVPVGGGGLAAGTVLAMQALAPTARLV 204
Cdd:PRK03910 168 ACALEIAQqlaeGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVI 214
 
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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