MULTISPECIES: histidinol dehydrogenase [Shigella].

LOCUS       WP_000009597             434 aa            linear   BCT 17-JUN-2024
ACCESSION   WP_000009597
VERSION     WP_000009597.1
KEYWORDS    RefSeq.
SOURCE      Shigella
  ORGANISM  Shigella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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 :: TIGR00069.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Shigella"
                     /db_xref="taxon:620"
     gene            1..434
                     /gene="hisD"
     Protein         1..434
                     /product="histidinol dehydrogenase"
                     /EC_number="1.1.1.23"
                     /GO_function="GO:0004399 - histidinol dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0000105 - histidine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=46184
     Region          5..427
                     /region_name="hisD"
                     /note="bifunctional histidinal dehydrogenase/ histidinol
                     dehydrogenase; Reviewed; PRK00877"
                     /db_xref="CDD:234853"
     Site            order(58,130,132..133,141,162,185..186,188,209..211,
                     213..214,262)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:119329"
     Site            order(83..84,87..88,90,93..94,97..98,101..102,109,111,
                     115..119,122,124,136..140,204,219,223,250..251,254..255,
                     257..259,261..262,331,336,339..340,342..350,352,354..355,
                     357..361,363,365,375..376,378..382,384..385,388..395,
                     410..411,413..419)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:119329"
     Site            order(138,140,237,262,326..327,356,360..361,367,414,416,
                     419)
                     /site_type="active"
                     /note="product binding site [active]"
                     /db_xref="CDD:119329"
     Site            order(140,237,259,262,326..327,356,360..361,367,414,416,
                     419)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:119329"
     Site            order(259,262,360,419)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:119329"
     Site            326..327
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:119329"
ORIGIN      
        1 msfntiidwn sctaeqqrql lmrpaisase sitrtvndil dnvktrgdea lreysakfdk
       61 ttvtalkvsa deiaaaserl sdelkqamav avksietfht aqklppvdve tqlgvrcqqv
      121 trpvasvgly ipggsaplfs tvlmlatpar iagckkvvlc spppiadeil yaaqlcdvqd
      181 vfnvggaqai aalafgtesv pkvdkifgpg nafvteakrq vsqrldgaai dmpagpsevl
      241 viadsgatpd fvasdllsqa ehgpdsqvil ltpdadmarr vaeaverqla elpraettrq
      301 alnasrlivt kdlaqcveis nqygpehlii qtrnarelvd gitsagsvfl gdwspesagd
      361 yasgtnhvlp tygytatcss lgladfqkrm tvqelskegf salastietl aaaerltahk
      421 navtlrvnvl keqa