para-aminobenzoate synthase subunit I [Listeria monocytogenes

LOCUS       NP_466272                568 aa            linear   CON 28-AUG-2016
            EGD-e].
ACCESSION   NP_466272
VERSION     NP_466272.1
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 568)
  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 568)
  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 568)
  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 568)
  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 568)
  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 CAD00963.
            RefSeq Category: Reference Genome
                        FGS: First Genome sequenced
                        MOD: Model Organism
                        UPR: UniProt Genome
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Listeria monocytogenes EGD-e"
                     /strain="EGD-e"
                     /db_xref="taxon:169963"
     Protein         1..568
                     /product="para-aminobenzoate synthase subunit I"
                     /calculated_mol_wt=63623
     Region          47..363
                     /region_name="Chorismate_bind"
                     /note="chorismate binding enzyme; cl29920"
                     /db_xref="CDD:453081"
     Region          369..565
                     /region_name="PLPDE_IV"
                     /note="PyridoxaL 5'-Phosphate Dependent Enzymes class IV
                     (PLPDE_IV). This D-amino acid superfamily, one of five
                     classes of PLPDE, consists of branched-chain amino acid
                     aminotransferases (BCAT), D-amino acid transferases
                     (DAAT), and 4-amino-4-deoxychorismate...; cl00224"
                     /db_xref="CDD:444764"
     Site            order(372,391,469,498,525..526,557)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:238254"
     Site            order(391,469,498)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:238254"
     Site            469
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238254"
     CDS             1..568
                     /locus_tag="lmo2750"
                     /coded_by="NC_003210.1:2824648..2826354"
                     /experiment="EXISTENCE:[PMID:19448609]"
                     /transl_table=11
                     /db_xref="GeneID:986907"
CONTIG      join(WP_003722110.1:1..568)
ORIGIN      
        1 msllrfdfeg dtkifenply elvaydlaev lpimkaaena qksgkyvagf vsyeaapafr
       61 snlktkkpse smplvwfgvy dnftdtatet pdssplsfkm dtsfpeytek ieqikaeiaa
      121 gntyqinytv rlqsdvpnnf ssqatyetlq qigkanytal lstsdfeiis aspelffkwk
      181 enllttrpmk gtirrgiteq adleahdwlk ndpknraenv mivdllrndl gmiavpgsvk
      241 vpqlmtlepy ptvwqmtsti taetppetdl tavfkalfpc gsitgapkar tmeiiseled
      301 sprgvycgti gflepngnai fnvpirtiai tdnkatygvg ggivwdseaa sefseihaks
      361 ailekatkfs lieclrieng elfrteyhlk rlqtsadffg ipfnreetek lwtktaqknt
      421 tgtykmrfll hpegahdlal tkidtknkri taqladkpvl sndlflyhkt thrkiyedlk
      481 ntqtdetllw neqgeltefi ngnivlging cfftppvtsg llsgtmrael laknkisekt
      541 lakkdllead yvwlinsvrg fveveikq