MULTISPECIES: 2,3-dehydroadipyl-CoA hydratase PaaF [Klebsiella].

LOCUS       WP_002902774             255 aa            linear   BCT 04-JUL-2023
ACCESSION   WP_002902774
VERSION     WP_002902774.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Teufel,R., Mascaraque,V., Ismail,W., Voss,M., Perera,J.,
            Eisenreich,W., Haehnel,W. and Fuchs,G.
  TITLE     Bacterial phenylalanine and phenylacetate catabolic pathway
            revealed
  JOURNAL   Proc Natl Acad Sci U S A 107 (32), 14390-14395 (2010)
   PUBMED   20660314
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Ferrandez,A., Minambres,B., Garcia,B., Olivera,E.R., Luengo,J.M.,
            Garcia,J.L. and Diaz,E.
  TITLE     Catabolism of phenylacetic acid in Escherichia coli.
            Characterization of a new aerobic hybrid pathway
  JOURNAL   J Biol Chem 273 (40), 25974-25986 (1998)
   PUBMED   9748275
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 :: NF007239.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09674
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..255
                     /gene="paaF"
     Protein         1..255
                     /product="2,3-dehydroadipyl-CoA hydratase PaaF"
                     /EC_number="4.2.1.17"
                     /calculated_mol_wt=27210
     Region          1..255
                     /region_name="PRK09674"
                     /note="enoyl-CoA hydratase-isomerase; Provisional"
                     /db_xref="CDD:182026"
     Site            order(23,25,57,61..65,102,104..106,128..129,132)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:119339"
     Site            order(63,106)
                     /site_type="active"
                     /note="oxyanion hole (OAH) forming residues [active]"
                     /db_xref="CDD:119339"
     Site            order(86,94,115..118,130..133,139,141..143,145..146,
                     151..152,154..155,157..158,161,172,175,190,193..194)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:119339"
ORIGIN      
        1 msdllihrhg rvlqltlnrp qarnalnnal ltqiaealea aavddsvgvc visgnarffa
       61 agadlnemae kdlpatlddi rprlwgrida ftkpliasvn gyalgagcel allcdlivag
      121 dnarfglpei tlgimpgagg tqrlirsvgk alasrmvlsg esidarqaqq aglvsdihpa
      181 altdeyalkl attiarhspl alraakqslr lsqevslqag lqqerqlfsl lsatedrreg
      241 idaflqkrtp efkgr