CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001839
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Threonine synthase 
Protein Synonyms/Alias
 TS 
Gene Name
 thrC 
Gene Synonyms/Alias
 b0004; JW0003 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
2******MKLYNLKDHacetylation[1]
7*MKLYNLKDHNEQVSacetylation[1]
57DFVTRSAKILSAFIGacetylation[1]
125LTHIAGDKPVTILTAacetylation[1]
267KSLGLPVKRFIAATNacetylation[1]
291HDGQWSPKATQATLSacetylation[1]
324RRKIWQLKELGYAAVacetylation[1]
344QQTMRELKELGYTSEacetylation[1]
381LGTAHPAKFKESVEAacetylation[1]
383TAHPAKFKESVEAILacetylation[1]
398GETLDLPKELAERADacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L- serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction. 
Sequence Annotation
 MOD_RES 107 107 N6-(pyridoxal phosphate)lysine (By  
Keyword
 3D-structure; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome; Threonine biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 428 AA 
Protein Sequence
MKLYNLKDHN EQVSFAQAVT QGLGKNQGLF FPHDLPEFSL TEIDEMLKLD FVTRSAKILS 60
AFIGDEIPQE ILEERVRAAF AFPAPVANVE SDVGCLELFH GPTLAFKDFG GRFMAQMLTH 120
IAGDKPVTIL TATSGDTGAA VAHAFYGLPN VKVVILYPRG KISPLQEKLF CTLGGNIETV 180
AIDGDFDACQ ALVKQAFDDE ELKVALGLNS ANSINISRLL AQICYYFEAV AQLPQETRNQ 240
LVVSVPSGNF GDLTAGLLAK SLGLPVKRFI AATNVNDTVP RFLHDGQWSP KATQATLSNA 300
MDVSQPNNWP RVEELFRRKI WQLKELGYAA VDDETTQQTM RELKELGYTS EPHAAVAYRA 360
LRDQLNPGEY GLFLGTAHPA KFKESVEAIL GETLDLPKEL AERADLPLLS HNLPADFAAL 420
RKLMMNHQ 428 
Gene Ontology
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0004795; F:threonine synthase activity; IDA:EcoCyc.
 GO:0009088; P:threonine biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
 IPR004450; Thr_synthase_like.
 IPR001926; Trp_syn_b_sub_like_PLP_eny_SF. 
Pfam
 PF00291; PALP 
SMART
  
PROSITE
 PS00165; DEHYDRATASE_SER_THR 
PRINTS