Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

MULTISPECIES: NADH:flavin oxidoreductase/NADH oxidase


LOCUS       WP_003113836             368 aa            linear   BCT 11-FEB-2021
            [Pseudomonas].
ACCESSION   WP_003113836
VERSION     WP_003113836.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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 10121205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..368
                     /product="NADH:flavin oxidoreductase/NADH oxidase"
                     /calculated_mol_wt=40188
     Region          4..339
                     /region_name="OYE_YqiM_FMN"
                     /note="Old yellow enzyme (OYE) YqjM-like FMN binding
                     domain. YqjM is involved in the oxidative stress response
                     of Bacillus subtilis. Like the other OYE members, each
                     monomer of YqjM contains FMN as a non-covalently bound
                     cofactor and uses NADPH as a reducing...; cd02932"
                     /db_xref="CDD:239242"
     Site            order(22..23,25,27,57,99,177,180,182,230,264,281,300..301,
                     321,323..325,328)
                     /site_type="active"
                     /db_xref="CDD:239242"
     Site            order(22..23,25,57,99,177,180,230,264,281,300..301,321,
                     323..325,328)
                     /site_type="other"
                     /note="FMN binding site [chemical binding]"
                     /db_xref="CDD:239242"
     Site            order(25,27,177,180,182)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239242"
     Site            order(26,36..37,39..40,43,47,280,282,301,307,330..331)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:239242"
     Site            182
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239242"
ORIGIN      
        1 msllfeplsl rqitlpnria vspmcqysaq eglandwhlv hlgsravgga glviveatav
       61 lpegritadd lgiwsdahve plhritrfie sqgavagvql ahagrkastw rpwlgkhgsv
      121 pigdggwipv apsaipfdpq httpealsea qiealvqafv raaerslaag fkvaevhaah
      181 gyllhqflsp lsnqrrdqyg gcfenrirll lqvtaavrka wpqelplfvr lsatdwvedg
      241 wnpdetvela rhlkdlgvdl idvssggtaa naeipvgpgy qtefaervkk eagiasgtvg
      301 mitepvqaeh ilrtgqadli llarellrdp ywplhaadel rneqmpwppq ylraahrstp
      361 prkslemq