radical SAM family heme chaperone HemW [Escherichia coli].

LOCUS       WP_000239959             378 aa            linear   BCT 04-JUN-2024
ACCESSION   WP_000239959
VERSION     WP_000239959.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Haskamp,V., Karrie,S., Mingers,T., Barthels,S., Alberge,F.,
            Magalon,A., Muller,K., Bill,E., Lubitz,W., Kleeberg,K.,
            Schweyen,P., Broring,M., Jahn,M. and Jahn,D.
  TITLE     The radical SAM protein HemW is a heme chaperone
  JOURNAL   J Biol Chem 293 (7), 2558-2572 (2018)
   PUBMED   29282292
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Abicht,H.K., Martinez,J., Layer,G., Jahn,D. and Solioz,M.
  TITLE     Lactococcus lactis HemW (HemN) is a haem-binding protein with a
            putative role in haem trafficking
  JOURNAL   Biochem J 442 (2), 335-343 (2012)
   PUBMED   22142238
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Homuth,G., Heinemann,M., Zuber,U. and Schumann,W.
  TITLE     The genes of lepA and hemN form a bicistronic operon in Bacillus
            subtilis
  JOURNAL   Microbiology (Reading) 142 (Pt 7), 1641-1649 (1996)
   PUBMED   8757728
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 :: TIGR00539.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..378
                     /gene="hemW"
     Protein         1..378
                     /product="radical SAM family heme chaperone HemW"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_function="GO:0051989 - coproporphyrinogen
                     dehydrogenase activity [Evidence IEA]"
                     /GO_process="GO:0006779 - porphyrin-containing compound
                     biosynthetic process [Evidence IEA]"
                     /calculated_mol_wt=42413
     Region          1..378
                     /region_name="HemN"
                     /note="Coproporphyrinogen-III oxidase HemN
                     (oxygen-independent) or related Fe-S oxidoreductase
                     [Coenzyme transport and metabolism]; COG0635"
                     /db_xref="CDD:440400"
ORIGIN      
        1 mvklpplsly ihipwcvqkc pycdfnshal kgevphddyv qhllndldnd vayaqgrevk
       61 tifigggtps llsgsamqtl ldgvrarlpl aadaeitmea npgtveadrf vdyqragvnr
      121 isigvqsfse eklkrlgrih gpqeakraak lasglglrsf nldlmhglpd qsleealgdl
      181 rqaielnpph lswyqltiep ntlfgsrppv lpdddalwdi feqghqllta agyqqyetsa
      241 yakpgyqcqh nlnywrfgdy igigcgahgk vtfpdgrilr ttktrhprgf mqgrylesqr
      301 dveaadkpfe ffmnrfrlle paprvefsay tglcedvirp qldeaiaqgy ltecadywqi
      361 tehgklflns llelflae