MULTISPECIES: CoA-acylating methylmalonate-semialdehyde

LOCUS       WP_004146794             501 aa            linear   BCT 31-DEC-2024
            dehydrogenase [Enterobacteriaceae].
ACCESSION   WP_004146794
VERSION     WP_004146794.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Dubourg,H., Stines-Chaumeil,C., Didierjean,C., Talfournier,F.,
            Rahuel-Clermont,S., Branlant,G. and Aubry,A.
  TITLE     Expression, purification, crystallization and preliminary X-ray
            diffraction data of methylmalonate-semialdehyde dehydrogenase from
            Bacillus subtilis
  JOURNAL   Acta Crystallogr D Biol Crystallogr 60 (Pt 8), 1435-1437 (2004)
   PUBMED   15272169
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10162887
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..501
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53465
     Region          4..485
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(61,63,67,70,74,107,110..111,120..127,132,135,138,
                     231,235,238,241,243,421,423..424,426..427,430,433..434,
                     436,438..441,450,454,456,470,477..482,484..485)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(147..150,158,173,176,206,223..226,229,247..249,281,
                     386,388,414)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(150,247,278,281)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mtitgnfigg ktvisssnet mpvydpatgk avrevtvsta qevseaiqva rdafdswsrt
       61 tplrrarvlf nfkmlleqhv eelagiivse hgkvwsdalg eltrgmevve facgiphlik
      121 geyssdvgtg vdsyslmqpl gvvagitpfn fpamvpmwmf plalacgnsf vlkppalapt
      181 aavrlaellk eaglpdgvfn vvhcsnedae qlytdpriaa vsfvgssgva eyiyktasah
      241 gkrvqafgaa knhaivmpda dldatvnaim ggafgsager cmalpvvvav gdetadklia
      301 rlkplvealk vgpgcmrgqe enemgpvvsd thqkkvlgyi dkgesegakl vvdgrklrvp
      361 gydagyyvgg tlfdhvtpem tiwreeifgp vlgivraady dsalelvnsh efgngsavft
      421 snghtarefv hdvqagmvgv nvpvpvpmaf hsfggwkrsv fgalnvhgpd gvrfytrmkt
      481 atvrwpagqq tvsefsmptl g