CoA-acylating methylmalonate-semialdehyde dehydrogenase

LOCUS       WP_003114170             502 aa            linear   BCT 31-DEC-2024
            [Pseudomonas aeruginosa].
ACCESSION   WP_003114170
VERSION     WP_003114170.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 502)
  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..502
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..502
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=54433
     Region          5..481
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(62,64,68,71,75,108,111..112,121..128,133,136,139,
                     232,236,239,242,244,417,419..420,422..423,426,429..430,
                     432,434..437,446,450,452,466,473..478,480..481)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143404"
     Site            order(148..151,159,174,177,207,224..227,230,248..250,282,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(151,248,279,282)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 makaipqlid gewrgsrsre lvevtdpatq dvlalapkat adeieqaias aqrafetwre
       61 vpaperarlm lryqhllkeh hdelgellar etgknladak gdvwrgievv ehaanvaslm
      121 mgetvenvar eidtaswiqp lgvcagitpf nfpamiplwm fplaiacgnt fvlkpseqdp
      181 ltpnrlaelf leagapkgvl qvihggreqv dallthpdir aisfvgsvav gqhvyrtgta
      241 hlkrvqafag aknhmvilpd ankaqvlgnl vgascgaagq rcmaisaavf vgaarewipe
      301 laermavlrp ghwqdpdaay gplispqarq rvlrliaegk aegaeclldg sqcqvegypn
      361 gnwlgptlfr avtpkmglyr eeifgpvlac levesleeai alvnanpygn gtslftrsgg
      421 aarryqhavq vgqvginvpi pvplpffsft gwkgsfygdl haygkqavrf ytetktvtsr
      481 wfddepttde ssagpnmtih lk