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Conserved domains on  [gi|693735233|gb|AIS40991|]
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threonine synthase, partial [Candidatus Tremblaya phenacola]

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) ...
 1-104 5.12e-23

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 cd01560:

Pssm-ID: 444852 [Multi-domain]  Cd Length: 460  Bit Score: 91.53  E-value: 5.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735233   1 SSVCTAFQFCKRSSLFVFSPLKSISEYQAEQMYNHLSKKAFNICFNGKFDCCQDIVKILL----CRNRSNSGTANSINWS 76
Cdd:cd01560  145 SAAIEGFRGKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFadedFNKKLKLSSANSINWA 224

                         90       100
                 ....*....|....*....|....*....
gi 693735233  77 RLLFQTAYYFISYFRVTIE-PKEKATFLI 104
Cdd:cd01560  225 RILAQIVYYFYAYLQLLKRgEGEKVEFSV 253
 
Name Accession Description Interval E-value
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
 1-104 5.12e-23

Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.


Pssm-ID: 107203 [Multi-domain]  Cd Length: 460  Bit Score: 91.53  E-value: 5.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735233   1 SSVCTAFQFCKRSSLFVFSPLKSISEYQAEQMYNHLSKKAFNICFNGKFDCCQDIVKILL----CRNRSNSGTANSINWS 76
Cdd:cd01560  145 SAAIEGFRGKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFadedFNKKLKLSSANSINWA 224

                         90       100
                 ....*....|....*....|....*....
gi 693735233  77 RLLFQTAYYFISYFRVTIE-PKEKATFLI 104
Cdd:cd01560  225 RILAQIVYYFYAYLQLLKRgEGEKVEFSV 253
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 16-96 9.79e-12

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: 59.44  E-value: 9.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735233  16 FVFSPLKSISEYQAEQMYNHlskKAFNICFNGKFDCCQDIVKILLcrNRSNSGTANSINWSRLLFQTAYYFISYFRVTIE 95
Cdd:COG0498  140 FVFVPEGKVSPGQLAQMLTY---GAHVIAVDGNFDDAQRLVKELA--ADEGLYAVNSINPARLEGQKTYAFEIAEQLGRV 214


                 .
gi 693735233  96 P 96
Cdd:COG0498  215 P 215
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 16-86 2.97e-05

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: 40.83  E-value: 2.97e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 693735233   16 FVFSPLKSISEyqaEQMYNHLSKKAFNICFNGKFDCCQDIVKILLCRNRS-NSGTANSInWSRLLFQTAYYF 86
Cdd:TIGR00260  97 VVLYPAGKISL---GKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKPAlGLNSANSI-PYRLEGQKTYAF 164
 
Name Accession Description Interval E-value
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
 1-104 5.12e-23

Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.


Pssm-ID: 107203 [Multi-domain]  Cd Length: 460  Bit Score: 91.53  E-value: 5.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735233   1 SSVCTAFQFCKRSSLFVFSPLKSISEYQAEQMYNHLSKKAFNICFNGKFDCCQDIVKILL----CRNRSNSGTANSINWS 76
Cdd:cd01560  145 SAAIEGFRGKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFadedFNKKLKLSSANSINWA 224

                         90       100
                 ....*....|....*....|....*....
gi 693735233  77 RLLFQTAYYFISYFRVTIE-PKEKATFLI 104
Cdd:cd01560  225 RILAQIVYYFYAYLQLLKRgEGEKVEFSV 253
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 16-96 9.79e-12

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: 59.44  E-value: 9.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735233  16 FVFSPLKSISEYQAEQMYNHlskKAFNICFNGKFDCCQDIVKILLcrNRSNSGTANSINWSRLLFQTAYYFISYFRVTIE 95
Cdd:COG0498  140 FVFVPEGKVSPGQLAQMLTY---GAHVIAVDGNFDDAQRLVKELA--ADEGLYAVNSINPARLEGQKTYAFEIAEQLGRV 214


                 .
gi 693735233  96 P 96
Cdd:COG0498  215 P 215
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 16-86 2.97e-05

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: 40.83  E-value: 2.97e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 693735233   16 FVFSPLKSISEyqaEQMYNHLSKKAFNICFNGKFDCCQDIVKILLCRNRS-NSGTANSInWSRLLFQTAYYF 86
Cdd:TIGR00260  97 VVLYPAGKISL---GKLAQALGYNAEVVAIDGNFDDAQRLVKQLFEDKPAlGLNSANSI-PYRLEGQKTYAF 164
 
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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