N-acetylglucosamine-6-phosphate isomerase [Listeria monocytogenes

LOCUS       NP_465881                243 aa            linear   CON 28-AUG-2016
            EGD-e].
ACCESSION   NP_465881
VERSION     NP_465881.1
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 243)
  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 243)
  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 243)
  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 243)
  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 243)
  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 CAD00436.
            RefSeq Category: Reference Genome
                        FGS: First Genome sequenced
                        MOD: Model Organism
                        UPR: UniProt Genome
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Listeria monocytogenes EGD-e"
                     /strain="EGD-e"
                     /db_xref="taxon:169963"
     Protein         1..243
                     /product="N-acetylglucosamine-6-phosphate isomerase"
                     /calculated_mol_wt=26845
     Region          10..240
                     /region_name="GlcN6P_deaminase"
                     /note="Glucosamine-6-phosphate (GlcN6P) deaminase
                     subfamily; GlcN6P deaminase catalyzes the reversible
                     conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and
                     ammonium. The reaction is an aldo-keto isomerization
                     coupled with an amination or deamination. It...; cd01399"
                     /db_xref="CDD:238693"
     Site            order(36..39,66..67,130..131,136,138,165,201)
                     /site_type="active"
                     /db_xref="CDD:238693"
     Site            order(143,145..146,154,209..215,223..225)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238693"
     Site            order(144..145,151..154)
                     /site_type="active"
                     /note="allosteric site [active]"
                     /db_xref="CDD:238693"
     Site            order(156,159..168,170,173..175)
                     /site_type="active"
                     /note="active site lid [active]"
                     /db_xref="CDD:238693"
     Site            order(161,199,203,234,237..240)
                     /site_type="other"
                     /note="hexamer (dimer of trimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:238693"
     CDS             1..243
                     /locus_tag="lmo2358"
                     /coded_by="complement(NC_003210.1:2426270..2427001)"
                     /experiment="EXISTENCE:[PMID:19448609]"
                     /transl_table=11
                     /db_xref="GeneID:984434"
CONTIG      join(WP_009925505.1:1..243)
ORIGIN      
        1 mklirtktyk emsqealevv eqvinendnp vintttgasf dgmfeglvkg inageipiek
       61 vflmnldeyv akrdasftvy tymhqkfydl inkmpkrvel ldgsladftd eiarykkila
      121 enerdlqilg lgvnghlgan epgtpfdarl fladsdesti kstimynnlk edeapsqmlt
      181 lgladmmdak qilvtasger kaeavkglle gpidencpas ilrnhpnvvf iideaagsll
      241 tnh