MULTISPECIES: SDR family oxidoreductase [Pseudomonas].

LOCUS       WP_003090991             292 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_003090991
VERSION     WP_003090991.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Kallberg,Y., Oppermann,U. and Persson,B.
  TITLE     Classification of the short-chain dehydrogenase/reductase
            superfamily using hidden Markov models
  JOURNAL   FEBS J 277 (10), 2375-2386 (2010)
   PUBMED   20423462
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Ladenstein,R., Winberg,J.O. and Benach,J.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : Structure-function relationships in short-chain alcohol
            dehydrogenases
  JOURNAL   Cell Mol Life Sci 65 (24), 3918-3935 (2008)
   PUBMED   19011748
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
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 10143283
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..292
                     /product="SDR family oxidoreductase"
                     /EC_number="1.-.-.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=30620
     Region          12..256
                     /region_name="TER_DECR_SDR_a"
                     /note="Trans-2-enoyl-CoA reductase (TER) and
                     2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR;
                     cd05369"
                     /db_xref="CDD:187627"
     Site            order(21,24..26,45..47,70..73,98..100,121,148..150,166,
                     192..195,197)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            order(46,73,100..103,111,113..114,117,150,152,162,194)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:187627"
     Site            order(75,106..108,110..112,115..116,119,123..124,127..128,
                     131,135,138,142,152,155..158,160,163..164,167..168,
                     171..172,174..181,183,194,218..220,222..224,228,231..232,
                     235,240,242..247,249..256)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
     Site            order(102,152,162,166)
                     /site_type="active"
                     /db_xref="CDD:187627"
     Site            order(106..108,110,115..116,119,124,127..128,155..158,160,
                     163..164,167..168,171..172,175,178..179)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187627"
ORIGIN      
        1 msydsifrpg lfdgqtiivt gggsgigrct ahelaalgah vvlvgrkaek lektageive
       61 dggsvswhac direeeavkt lvanilaerg tihhlvnnag gqypsplasi sqkgfetvlr
      121 tnlvggflva revfnqsmsk tggsivnmla dmwggmpgmg hsgaarsgme nftrtaavew
      181 ghagvrvnav apgwiassgm dtyegafkav iptlrehvpl krigseseva aaivfllspg
      241 aafvsgntir idgaasqgsr afplfkgkpg qsrayngfhr aylpdvlkdq ed