hydroxymethylglutaryl-CoA reductase, degradative [Listeria

LOCUS       WP_003721392             426 aa            linear   BCT 17-JUN-2024
            monocytogenes].
ACCESSION   WP_003721392
VERSION     WP_003721392.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Beach,M.J. and Rodwell,V.W.
  TITLE     Cloning, sequencing, and overexpression of mvaA, which encodes
            Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A
            reductase
  JOURNAL   J Bacteriol 171 (6), 2994-3001 (1989)
   PUBMED   2656635
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 :: TIGR00532.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..426
                     /product="hydroxymethylglutaryl-CoA reductase,
                     degradative"
                     /EC_number="1.1.1.88"
                     /GO_function="GO:0004420 - hydroxymethylglutaryl-CoA
                     reductase (NADPH) activity [Evidence IEA]"
                     /GO_function="GO:0016616 - oxidoreductase activity, acting
                     on the CH-OH group of donors, NAD or NADP as acceptor
                     [Evidence IEA]"
                     /GO_process="GO:0015936 - coenzyme A metabolic process
                     [Evidence IEA]"
                     /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"
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