MULTISPECIES: radical SAM family heme chaperone HemW [Klebsiella].

LOCUS       WP_002916617             378 aa            linear   BCT 04-JUN-2024
ACCESSION   WP_002916617
VERSION     WP_002916617.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     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=42319
     Region          1..376
                     /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 manlpplsly ihipwcvqkc pycdfnshal kgevphddyv qhllndlqad aqyaqgreig
       61 tifigggtps llsgpamqtl ldgvraclpl aagaeitmea npgtveadrf vdyqragvnr
      121 isigvqsfse pklqrlgrih gpeeakraar lasglglrsf nldlmhglpd qsleealddl
      181 rqaialnpph lswyqltiep ntlfgsrppv lpdddalwdi feqghqllsa agyqqyetsa
      241 yakpgfqcqh nlnywrfgdy lgigcgahgk itfpdgrilr taktrhprgy megrylerqh
      301 dveeadkpfe ffmnrfrlle aapraefsry tgleeaairp qldaaiaqgy lqedeqnwqi
      361 tehgklflns llelflne