MULTISPECIES: type I 3-dehydroquinate dehydratase [Shigella].

LOCUS       WP_000860164             252 aa            linear   BCT 17-NOV-2023
ACCESSION   WP_000860164
VERSION     WP_000860164.1
KEYWORDS    RefSeq.
SOURCE      Shigella
  ORGANISM  Shigella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Light,S.H., Minasov,G., Shuvalova,L., Duban,M.E., Caffrey,M.,
            Anderson,W.F. and Lavie,A.
  TITLE     Insights into the mechanism of type I dehydroquinate dehydratases
            from structures of reaction intermediates
  JOURNAL   J Biol Chem 286 (5), 3531-3539 (2011)
   PUBMED   21087925
  REMARK    Erratum:[J Biol Chem. 2015 Jul 31;290(31):19008. PMID: 26232400]
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01093.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Shigella"
                     /db_xref="taxon:620"
     gene            1..252
                     /gene="aroD"
     Protein         1..252
                     /product="type I 3-dehydroquinate dehydratase"
                     /EC_number="4.2.1.10"
                     /GO_function="GO:0003855 - 3-dehydroquinate dehydratase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009423 - chorismate biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=27387
     Region          1..252
                     /region_name="aroD"
                     /note="type I 3-dehydroquinate dehydratase; PRK02412"
                     /db_xref="CDD:235036"
     Site            order(21,46,48,82,143,170,213,232..233,236)
                     /site_type="active"
                     /db_xref="CDD:188633"
     Site            170
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188633"
     Site            order(182,186,189,214..215,219,241,245,248)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188633"
ORIGIN      
        1 mktvtvkdlv igagapkiiv slmakdiarv ksealayrea dfdilewrvd hfadlsnves
       61 vmaaakilre tmpekpllft frsakeggeq aisteayial nraaidsglv dmidlelftg
      121 ddqvketvay ahahdvkvvm snhdfhktpe aeeiiarlrk mqsfdadipk ialmpqstsd
      181 vltllaatle mqeqyadrpi itmsmaktgv isrlvgevfg saatfgavkk asapgqisvn
      241 dlrtvltilh qa