FAD-dependent oxidoreductase [Klebsiella pneumoniae].

LOCUS       WP_014343039             593 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_014343039
VERSION     WP_014343039.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Todone,F., Vanoni,M.A., Mozzarelli,A., Bolognesi,M., Coda,A.,
            Curti,B. and Mattevi,A.
  TITLE     Active site plasticity in D-amino acid oxidase: a crystallographic
            analysis
  JOURNAL   Biochemistry 36 (19), 5853-5860 (1997)
   PUBMED   9153426
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 :: NF013434.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF01266.30
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         1..593
                     /product="FAD-dependent oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=63698
     Region          7..360
                     /region_name="OYE_like_4_FMN"
                     /note="Old yellow enzyme (OYE)-related FMN binding domain,
                     group 4. Each monomer of OYE contains FMN as a
                     non-covalently bound cofactor, uses NADPH as a reducing
                     agent with oxygens, quinones, and alpha,beta-unsaturated
                     aldehydes and ketones, and can act as...; cd04735"
                     /db_xref="CDD:240086"
     Site            order(27,29,61,103,175,231,322..323)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:240086"
     Site            order(27,29,61,103,231,322..323)
                     /site_type="other"
                     /note="putative FMN binding site [chemical binding]"
                     /db_xref="CDD:240086"
     Site            order(173,175)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:240086"
     Site            175
                     /site_type="active"
                     /note="putative catalytic residue [active]"
                     /db_xref="CDD:240086"
     Region          373..466
                     /region_name="COG3976"
                     /note="Uncharacterized conserved protein, contains
                     FMN-binding domain [General function prediction only]"
                     /db_xref="CDD:443175"
     Region          442..>556
                     /region_name="PRK06481"
                     /note="flavocytochrome c"
                     /db_xref="CDD:180584"
ORIGIN      
        1 mtsnerilqp ftlpngtelk nrllmapmtt ctgyfdgtvt selveyyrar agsigtiive
       61 ccfiddygla fpgaigidnd ekiaglakia eaikaegska ilqiyhggrm vdpqliggrq
      121 pvapsaiaap regaampral sgeevegmia kfgdgvrrai lagfdgveih gantyliqqf
      181 yspnsnqrdd ewggsrdnra rfplavldit hkmarqyadd afiigyrfsp eemevpgirf
      241 ddtmyllekl aargvdylhf svgatlrpsi vdtsdptpli ekycamrsdt laqvpvmgvg
      301 gvvnaadaeq gldhgydlia vgraciaypd wasriaagee lelfidstqr ealhipeplw
      361 rfslveamir dmsmgdakfk pgmfvetvhd danelvinvs lendhiadie laaspvqtve
      421 fttsfeeire riltantphv daisgatsqs eavkkavaka mlksskalaa eeggndaapk
      481 sydvvvvgsg gaglaaaiqa hdegasvliv ekmptiggnt ikasagmnaa etrfqrvkgi
      541 edskelfyqe tlkgghnktt rsccavslkt rrkplsgwrt galcsttlpp pvg