MULTISPECIES: CoA-acylating methylmalonate-semialdehyde

LOCUS       WP_003101230             497 aa            linear   BCT 01-JAN-2025
            dehydrogenase [Pseudomonas].
ACCESSION   WP_003101230
VERSION     WP_003101230.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 497)
  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..497
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..497
                     /product="CoA-acylating methylmalonate-semialdehyde
                     dehydrogenase"
                     /EC_number="1.2.1.-"
                     /calculated_mol_wt=53192
     Region          4..481
                     /region_name="ALDH_F6_MMSDH"
                     /note="Methylmalonate semialdehyde dehydrogenase and ALDH
                     family members 6A1 and 6B2; cd07085"
                     /db_xref="CDD:143404"
     Site            order(60,62,66,69,73,106,109..110,119..126,131,134,137,
                     230,234,237,240,242,417,419..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(146..149,157,172,175,205,222..225,228,246..248,280,
                     382,384,410)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143404"
     Site            order(149,246,277,280)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143404"
ORIGIN      
        1 mgtlhhling emvadngrsa dvfnpstgea ihkvpladgk tlqkaidaar aafpawrntp
       61 pakraqvlyr fkqlleqnea riskliseeh gktledaage lkrgienvey acaapeilkg
      121 eysrnvgpni dawsdfqpig vvagitpfnf pamvplwmyp laiacgntfi lkpserdpss
      181 tlliaelfhe aglpkgvlnv vhgdkeavdg llqapevkai sfvgstpiae yiyaegtkrg
      241 krvqalggak nhavlmpdad ldnavsalmg aaygscgerc maisvavcvg dqvadaliak
      301 lvpqikalki gagtscgldm gplvtaaaqa kvtgyidsgv aqgaelvvdg rgyqvaghen
      361 gfflggslfd rvtpemtiyk eeifgpvlcv vrvnsleeam qlindheygn gtciftrdge
      421 aarlfcdeie vgmvgvnvpl pvpvayhsfg gwkrslfgdl haygpdgvrf ytrrkaitqr
      481 wpqrasheas qfafpsl