3-hydroxy-3-methylglutaryl-CoA reductase [Listeria monocytogenes

LOCUS       NP_464352                426 aa            linear   CON 28-AUG-2016
            EGD-e].
ACCESSION   NP_464352
VERSION     NP_464352.1
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 426)
  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 426)
  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 426)
  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 426)
  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 426)
  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 CAC98903.
            RefSeq Category: Reference Genome
                        FGS: First Genome sequenced
                        MOD: Model Organism
                        UPR: UniProt Genome
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Listeria monocytogenes EGD-e"
                     /strain="EGD-e"
                     /db_xref="taxon:169963"
     Protein         1..426
                     /product="3-hydroxy-3-methylglutaryl-CoA reductase"
                     /calculated_mol_wt=45724
     Region          6..423
                     /region_name="HMG-CoA_reductase_classII"
                     /note="Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA)
                     reductase (HMGR); cd00644"
                     /db_xref="CDD:153082"
     Site            order(7,12,15..16,33,41,44..45,47..61,77..85,110,112,114,
                     161,171,173,207..213,243,246..248,250..251,254..255,
                     257..258,260..261,264,267..268,271,275..276,280..283,
                     285..286,289,293,296,298,328,332,334..335,369,372..375,
                     379,381..382,384..385,388..389,413)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:153082"
     Site            order(80,146,149,179..186,188,211,213,261,264,280,283,
                     325..327,378)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:153082"
     Site            order(80,264,280,378)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:153082"
     Site            order(80,258,261..262,264..265,268,365,369,374)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:153082"
     Site            375..390
                     /site_type="other"
                     /note="flexible flap"
                     /db_xref="CDD:153082"
     CDS             1..426
                     /locus_tag="lmo0825"
                     /coded_by="NC_003210.1:851225..852505"
                     /experiment="EXISTENCE:[PMID:19448609]"
                     /transl_table=11
                     /db_xref="GeneID:985372"
CONTIG      join(WP_003721392.1:1..426)
ORIGIN      
        1 mnafdkfykk tveerhaila eyadlneeeq aflastgals fdkanhmien tigiyslplg
       61 lgmnmllndk ryvvpmamee psvvaaqsag akliaqnggi tgsatkrkmi gqielisvsd
      121 iqaakeniia neeqliaian qahpslqkrg ggavkiqvrt aqtandetlf ivhllvdtqe
      181 amganmvntm vetlapelem ltngtanmri lsnlvdeata tavcrinpes latktqsgew
      241 vrdriiaaye fadadiyraa thnkgimngi davimafgnd wraveaasha yaartgsykp
      301 mskwskdadg ylvgeltlpm pvafvggsia ihpiaslskk iarvesakel amlvcavglt
      361 qnlaalkalv tegiqrghms lqakslamta gaeadeieiv atflqeskql nvvaakefia
      421 klrsek