GenomeNet

Database: RefSeq
Entry: WP_010074030
LinkDB: WP_010074030
Original site: WP_010074030 
LOCUS       WP_010074030             120 aa            linear   BCT 29-DEC-2023
DEFINITION  3-hydroxyacyl-CoA dehydrogenase NAD-binding domain-containing
            protein [Clostridium cellulovorans].
ACCESSION   WP_010074030
VERSION     WP_010074030.1
KEYWORDS    RefSeq.
SOURCE      Clostridium cellulovorans
  ORGANISM  Clostridium cellulovorans
            Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
            Clostridium.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Birktoft,J.J., Holden,H.M., Hamlin,R., Xuong,N.H. and Banaszak,L.J.
  TITLE     Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary
            chain tracing at 2.8-A resolution
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8262-8266 (1987)
   PUBMED   3479790
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 :: NF014757.4
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF02737.22
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Clostridium cellulovorans"
                     /db_xref="taxon:1493"
     Protein         1..120
                     /product="3-hydroxyacyl-CoA dehydrogenase NAD-binding
                     domain-containing protein"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /GO_process="GO:0006631 - fatty acid metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=13300
     Region          3..>118
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:450167"
ORIGIN      
        1 mkkigvigag vmgvgvahsl aksgfqvili disgdilens kneiyknirf qtffnkgkdv
       61 esadtiisri vfssdyqlln dvdvvienvt ekwevkkevy eridsicneq kdvsadtsqr
//
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