dihydroorotate dehydrogenase electron transfer subunit [Listeria

LOCUS       NP_465359                254 aa            linear   CON 28-AUG-2016
            monocytogenes EGD-e].
ACCESSION   NP_465359
VERSION     NP_465359.1
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 254)
  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 254)
  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 254)
  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 254)
  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 254)
  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 CAC99912.
            RefSeq Category: Reference Genome
                        FGS: First Genome sequenced
                        MOD: Model Organism
                        UPR: UniProt Genome
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Listeria monocytogenes EGD-e"
                     /strain="EGD-e"
                     /db_xref="taxon:169963"
     Protein         1..254
                     /product="dihydroorotate dehydrogenase electron transfer
                     subunit"
                     /calculated_mol_wt=27489
     Region          8..248
                     /region_name="DHOD_e_trans"
                     /note="FAD/NAD binding domain in the electron transfer
                     subunit of dihydroorotate dehydrogenase. Dihydroorotate
                     dehydrogenases (DHODs) catalyze the only redox reaction in
                     pyrimidine de novo biosynthesis. They catalyze the
                     oxidation of (S)-dihydroorotate to...; cd06218"
                     /db_xref="CDD:99814"
     Site            order(48,50..53,67..69,75..77,115,214..215)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(50,52..53)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(74,77,80,84,92,94)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99814"
     Site            order(110,114..117,119)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99814"
     Site            order(115..116,139..141,191..192)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(218,223,226,241)
                     /site_type="other"
                     /note="Iron coordination center [ion binding]"
                     /db_xref="CDD:99814"
     CDS             1..254
                     /gene="pyrDII"
                     /locus_tag="lmo1834"
                     /coded_by="complement(NC_003210.1:1908827..1909591)"
                     /experiment="EXISTENCE:[PMID:19448609]"
                     /transl_table=11
                     /db_xref="GeneID:985877"
CONTIG      join(WP_010989827.1:1..254)
ORIGIN      
        1 mlqtemkviq qteiadkvye liltgecvag mspgqflmlk psrsdllmrr pisicsydkt
       61 aktcillyrv egdgtrdfsk lsegdtidvl gplgkgfdid ttpapktall igggigvppm
      121 yqlgkelaek gvqvmfvngf qsakdsfyaq emaeygtvhi atvdgslgtq gfvtditknf
      181 peepdviysc gpkamlqavk asfpetktyl sleermacgi gacyacvcpk addtnkqfkv
      241 cedgpvfrad evkl