LOCUS       WP_106005623             723 aa            linear   BCT 24-JUN-2025
DEFINITION  molybdopterin-dependent oxidoreductase [Neomoorella humiferrea].
ACCESSION   WP_106005623
VERSION     WP_106005623.1
KEYWORDS    RefSeq.
SOURCE      Neomoorella humiferrea (Moorella humiferrea)
  ORGANISM  Neomoorella humiferrea
            Bacteria; Bacillati; Bacillota; Clostridia; Neomorellales;
            Neomoorellaceae; Neomoorella.
REFERENCE   1  (residues 1 to 723)
  AUTHORS   Schneider,F., Lowe,J., Huber,R., Schindelin,H., Kisker,C. and
            Knablein,J.
  TITLE     Crystal structure of dimethyl sulfoxide reductase from Rhodobacter
            capsulatus at 1.88 A resolution
  JOURNAL   J Mol Biol 263 (1), 53-69 (1996)
   PUBMED   8890912
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 :: NF012602.7
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00384.28
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..723
                     /organism="Neomoorella humiferrea"
                     /db_xref="taxon:676965"
     Protein         1..723
                     /product="molybdopterin-dependent oxidoreductase"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=77442
     Region          5..30
                     /region_name="TAT_signal"
                     /note="TAT (twin-arginine translocation) pathway signal
                     sequence; pfam10518"
                     /db_xref="CDD:463131"
     Region          45..723
                     /region_name="BisC"
                     /note="Anaerobic selenocysteine-containing dehydrogenase
                     [Energy production and conversion]; COG0243"
                     /db_xref="CDD:440013"
ORIGIN      
        1 mleqkisrrt fikgslvaga vaafggslvp lkgaeaaeap easatkvvpt icemcgvkcg
       61 vlahvkdgrv wrltgnpkdp qsggrlcarg nagtktlydp drlkgplkrv gdgkfepisw
      121 eqafkeigek lielkgrygp qtlvwlahpe lisplekhfm aafgspnytg hgptcyssrn
      181 vafeqmyggv pgvdyrniky yiafgrnltg giknpdiqki vaakaegahl vavdprfndf
      241 ayfadewlpi rpgtdlamil aminviiren lydasfvaer tvgfeelkag vasytpewaa
      301 qitgidaati ariarelaaa kpaaavdpgw havtgsqyyn svqtaravaa lnallgnlga
      361 kgglsfppti kfgdpgplmg pkppaavapr wdgaggekwp lnkahgiiqi fpervkedkp
      421 ypvkavviqh lnpvrsstns aafiealkql elvvaidiqm ndtayyahyv lpeatylery
      481 dplmtagnkv ilrqpavqpl fdtkgaeeii ggiakaaglg eyfnftleqy ndamlaplgl
      541 tqaelartgv aevaaqppdy tklktpsgki elacqafvka gstltpawep plvepkenef
      601 rfiqghvpmh thtttdnnay lhalmpenel winparaakl giktgdvvev tskvgsvkvk
      661 arvtecihpe avflahgfgc gvplrklayn sganggalip iitapvsgaa aqcetlvtvr
      721 kag
//