MULTISPECIES: tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE

LOCUS       WP_003122839             207 aa            linear   BCT 01-JAN-2025
            [Pseudomonas].
ACCESSION   WP_003122839
VERSION     WP_003122839.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Subedi,B.P., Corder,A.L., Zhang,S., Foss,F.W. Jr. and Pierce,B.S.
  TITLE     Steady-state kinetics and spectroscopic characterization of
            enzyme-tRNA interactions for the non-heme diiron
            tRNA-monooxygenase, MiaE
  JOURNAL   Biochemistry 54 (2), 363-376 (2015)
   PUBMED   25453905
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Kaminska,K.H., Baraniak,U., Boniecki,M., Nowaczyk,K., Czerwoniec,A.
            and Bujnicki,J.M.
  TITLE     Structural bioinformatics analysis of enzymes involved in the
            biosynthesis pathway of the hypermodified nucleoside ms(2)io(6)A37
            in tRNA
  JOURNAL   Proteins 70 (1), 1-18 (2008)
   PUBMED   17910062
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Harrison,P.M., Hempstead,P.D., Artymiuk,P.J. and Andrews,S.C.
  TITLE     Structure-function relationships in the ferritins
  JOURNAL   Met Ions Biol Syst 35, 435-477 (1998)
   PUBMED   9444766
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Nordlund,P. and Eklund,H.
  TITLE     Di-iron-carboxylate proteins
  JOURNAL   Curr Opin Struct Biol 5 (6), 758-766 (1995)
   PUBMED   8749363
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Theil,E.C.
  TITLE     Ferritin: structure, gene regulation, and cellular function in
            animals, plants, and microorganisms
  JOURNAL   Annu Rev Biochem 56, 289-315 (1987)
   PUBMED   3304136
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 10533077
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..207
                     /product="tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase
                     MiaE"
                     /EC_number="1.14.99.69"
                     /GO_function="GO:0045301 -
                     tRNA-(2-methylthio-N-6-(cis-hydroxy)isopentenyl
                     adenosine)-hydroxylase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006400 - tRNA modification [Evidence
                     IEA]"
                     /calculated_mol_wt=23213
     Region          4..199
                     /region_name="MiaE"
                     /note="tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE); pfam06175"
                     /db_xref="CDD:114868"
     Site            order(40,71,74,102,116,119,124,153,156,160)
                     /site_type="active"
                     /db_xref="CDD:153119"
     Site            order(40,71,74,124,153,156)
                     /site_type="other"
                     /note="dinuclear metal binding site [ion binding]"
                     /db_xref="CDD:153119"
     Site            order(41,48,51,62,65..66,69,72,75..76)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:153119"
ORIGIN      
        1 mtctmlpeid qflacstpaa wveaalerqd vmlldhkace mkaaatamql igkysgrldl
       61 vnkmsrlare elrhfeqvla ilkkrgirvv nvsasryasa lrdlvrkqep qrltdtlvvg
      121 afiearscer faalvphlda elakfyggll ksesrhfqdy lklayqygde advertievv
      181 rakeaeliss pdnefrfhsg lpvdlva