CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-025989
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Threonine synthase 
Protein Synonyms/Alias
  
Gene Name
 GK2963 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Geobacillus kaustophilus (strain HTA426) 
NCBI Taxa ID
 235909 
Lysine Modification
Position
Peptide
Type
References
72VMAVAKAKEEGSHTIacetylation[1]
Reference
 [1] Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus.
 Lee DW, Kim D, Lee YJ, Kim JA, Choi JY, Kang S, Pan JG.
 Proteomics. 2013 Aug;13(15):2278-82. [PMID: 23696451
Functional Description
 Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine (By similarity). 
Sequence Annotation
 REGION 186 190 Pyridoxal phosphate binding (By
 BINDING 86 86 Pyridoxal phosphate (By similarity).
 BINDING 315 315 Pyridoxal phosphate (By similarity).
 MOD_RES 60 60 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Amino-acid biosynthesis; Complete proteome; Lyase; Pyridoxal phosphate; Threonine biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 353 AA 
Protein Sequence
MAWKGLLDAY GDFLPLSAAT PRLSLCEGNT PLIPLPRLSE ELGIALYVKV EGANPTGSFK 60
DRGMVMAVAK AKEEGSHTII CASTGNTSAS AAAYAARAGM RCLVVVPNGK IALGKLAQAA 120
MYGAEIFAID GNFDEALKMV RRLSETAPIT LVNSVNPYRI EGQKTAAFEV CDQLGRAPDV 180
LAIPVGNAGN ITAYWKGFKE YHEAKGTGLP QMRGFEAEGA AAIVRNRVIE QPETVATAIR 240
IGNPASWDKA VEAASESRGK IDEVSDAEIL AAYKRLARTE GIFAEPASCA AIAGVIKQRE 300
RNEIERGSLV VAVLTGNGLK DPAIALETAA IEPIVLPNDE QVVLEHLQGV VRA 353 
Gene Ontology
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0004795; F:threonine synthase activity; IEA:EC.
 GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW. 
Interpro
 IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
 IPR026260; Thr_Synthase_Gram_pos_bac.
 IPR004450; Thr_synthase_like.
 IPR001926; Trp_syn_b_sub_like_PLP_eny_SF. 
Pfam
 PF00291; PALP 
SMART
  
PROSITE
 PS00165; DEHYDRATASE_SER_THR 
PRINTS