MULTISPECIES: glutaredoxin-dependent arsenate reductase

LOCUS       WP_002916278             140 aa            linear   BCT 06-MAR-2020
            [Klebsiella].
ACCESSION   WP_002916278
VERSION     WP_002916278.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Liu,J., Gladysheva,T.B., Lee,L. and Rosen,B.P.
  TITLE     Identification of an essential cysteinyl residue in the ArsC
            arsenate reductase of plasmid R773
  JOURNAL   Biochemistry 34 (41), 13472-13476 (1995)
   PUBMED   7577935
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 :: NF007456.1
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10026
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..140
                     /gene="arsC"
     Protein         1..140
                     /product="glutaredoxin-dependent arsenate reductase"
                     /EC_number="1.20.4.1"
                     /GO_function="GO:0008794 - arsenate reductase
                     (glutaredoxin) activity [Evidence IEA]"
                     /calculated_mol_wt=15322
     Region          2..140
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Site            order(11,59,93,106)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239332"
ORIGIN      
        1 msitiyhnpd cgtsrntlal irnsgaeptv iyyletppsg delrqllaam gipvrallrk
       61 nvepydalgl aedrftddqi idfmlqhpil inrpivttpq gtrlcrpsev vleiltapqk
      121 gafvkedgep vidaagqrvk