pimeloyl-ACP methyl ester esterase BioH [Photobacterium profundum].

LOCUS       WP_011216996             254 aa            linear   BCT 01-JUL-2024
ACCESSION   WP_011216996
VERSION     WP_011216996.1
KEYWORDS    RefSeq.
SOURCE      Photobacterium profundum
  ORGANISM  Photobacterium profundum
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Photobacterium.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Sanishvili,R., Yakunin,A.F., Laskowski,R.A., Skarina,T.,
            Evdokimova,E., Doherty-Kirby,A., Lajoie,G.A., Thornton,J.M.,
            Arrowsmith,C.H., Savchenko,A., Joachimiak,A. and Edwards,A.M.
  TITLE     Integrating structure, bioinformatics, and enzymology to discover
            function: BioH, a new carboxylesterase from Escherichia coli
  JOURNAL   J Biol Chem 278 (28), 26039-26045 (2003)
   PUBMED   12732651
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Tomczyk,N.H., Nettleship,J.E., Baxter,R.L., Crichton,H.J.,
            Webster,S.P. and Campopiano,D.J.
  TITLE     Purification and characterisation of the BIOH protein from the
            biotin biosynthetic pathway
  JOURNAL   FEBS Lett 513 (2-3), 299-304 (2002)
   PUBMED   11904168
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 :: TIGR01738.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Photobacterium profundum"
                     /db_xref="taxon:74109"
     gene            1..254
                     /gene="bioH"
     Protein         1..254
                     /product="pimeloyl-ACP methyl ester esterase BioH"
                     /EC_number="3.1.1.85"
                     /GO_function="GO:0052689 - carboxylic ester hydrolase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009102 - biotin biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28011
     Region          11..253
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
ORIGIN      
        1 mttalcwqte gqgsdlvlih gwgmngavwq qllplltpfy rvhwvdmpgy ghshdisads
       61 ieemaqllld kspisatwlg wslgglvatq aallapervt rlvtvasspr faaegtwrgi
      121 qpqvlddfrr qlgddfqltv erflalqamg sptarqdikl lkqavlsrpq pnpealsigl
      181 rlladvdlra qlgditqpwl rlygrldglv pakvakdmdq lapqscrqif aaashapfis
      241 hpeefvqtlk dfik