threonine synthase [Listeria monocytogenes EGD-e].

LOCUS       NP_466069                351 aa            linear   CON 28-AUG-2016
ACCESSION   NP_466069
VERSION     NP_466069.1
DBLINK      BioProject: PRJNA61583
            Assembly: GCF_000196035.1
DBSOURCE    REFSEQ: accession NC_003210.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes EGD-e
  ORGANISM  Listeria monocytogenes EGD-e
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Toledo-Arana,A., Dussurget,O., Nikitas,G., Sesto,N.,
            Guet-Revillet,H., Balestrino,D., Loh,E., Gripenland,J., Tiensuu,T.,
            Vaitkevicius,K., Barthelemy,M., Vergassola,M., Nahori,M.A.,
            Soubigou,G., Regnault,B., Coppee,J.Y., Lecuit,M., Johansson,J. and
            Cossart,P.
  TITLE     The Listeria transcriptional landscape from saprophytism to
            virulence
  JOURNAL   Nature 459 (7249), 950-956 (2009)
   PUBMED   19448609
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Chatterjee,S.S., Hossain,H., Otten,S., Kuenne,C., Kuchmina,K.,
            Machata,S., Domann,E., Chakraborty,T. and Hain,T.
  TITLE     Intracellular gene expression profile of Listeria monocytogenes
  JOURNAL   Infect. Immun. 74 (2), 1323-1338 (2006)
   PUBMED   16428782
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Glaser,P., Frangeul,L., Buchrieser,C., Amend,A., Baquero,F.,
            Berche,P., Bloecker,H., Brandt,P., Chakraborty,T., Charbit,A.,
            Chetouani,F., Couve,E., de Daruvar,A., Dehoux,P., Domann,E.,
            Dominguez-Bernal,G., Duchaud,E., Durand,L., Dussurget,O.,
            Entian,K.-D., Fsihi,H., Garcia-Del Portillo,F., Garrido,P.,
            Gautier,L., Goebel,W., Gomez-Lopez,N., Hain,T., Hauf,J.,
            Jackson,D., Jones,L.-M., Karst,U., Kreft,J., Kuhn,M., Kunst,F.,
            Kurapkat,G., Madueno,E., Maitournam,A., Mata Vicente,J., Ng,E.,
            Nordsiek,G., Novella,S., de Pablos,B., Perez-Diaz,J.-C., Remmel,B.,
            Rose,M., Rusniok,C., Schlueter,T., Simoes,N., Tierrez,A.,
            Vazquez-Boland,J.-A., Voss,H., Wehland,J. and Cossart,P.
  TITLE     Comparative genomics of Listeria species
  JOURNAL   Science 294 (5543), 849-852 (2001)
   PUBMED   11679669
REFERENCE   4  (residues 1 to 351)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (08-NOV-2001) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Glaser,P., Frangeul,L. and Rusniok,C.
  TITLE     Direct Submission
  JOURNAL   Submitted (06-JUN-2001) Glaser P., Institut Pasteur, Genomique des
            Microorganismes Pathogenes, 25 rue du Docteur Roux, 75724 Paris
            Cedex 15, FRANCE
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CAD00624.
            RefSeq Category: Reference Genome
                        FGS: First Genome sequenced
                        MOD: Model Organism
                        UPR: UniProt Genome
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Listeria monocytogenes EGD-e"
                     /strain="EGD-e"
                     /db_xref="taxon:169963"
     Protein         1..351
                     /product="threonine synthase"
                     /EC_number="4.2.3.1"
                     /calculated_mol_wt=36832
     Region          6..320
                     /region_name="Thr-synth_1"
                     /note="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; cd01563"
                     /db_xref="CDD:107206"
     Site            order(25,30..31,53,76,92,95..96,102,119..125,127..129,
                     141..142,172,276..278,280..281,316)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:107206"
     Site            order(59,85,185..189,314)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107206"
     Site            59
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107206"
     CDS             1..351
                     /gene="thrC"
                     /locus_tag="lmo2546"
                     /coded_by="complement(NC_003210.1:2622067..2623122)"
                     /experiment="EXISTENCE:[PMID:19448609]"
                     /note="catalyzes the formation of L-threonine from
                     O-phospho-L-homoserine"
                     /transl_table=11
                     /db_xref="GeneID:986503"
CONTIG      join(WP_003729257.1:1..351)
ORIGIN      
        1 mykgllekyk eylpvtdktp mislaegntp liplpnlske lgvtlygkye glnptgsfkd
       61 rgmvmavaka keegaeavic astgntsaaa aayatraglk ayivipegkv algklaqavm
      121 ygadiisiqg nfdealksvr elaeteavtl vnsvnpyrle gqktaafeic eqlgsapdvl
      181 aipvgnagni saywkgfkew neakasglpr mhgfeaegaa aivqgkpidn petiatairi
      241 gnpaswglae aardesggyi hsvtddeivn aykkiaaqdg vfiepgsaas lagviqhvan
      301 gtikkgetvv cvftgnglkd pdtamsvhei pishvddiea mrthlrsgvk a