precorrin-2 dehydrogenase/sirohydrochlorin ferrochelatase family

LOCUS       WP_009912223             159 aa            linear   BCT 17-FEB-2025
            protein [Listeria monocytogenes].
ACCESSION   WP_009912223
VERSION     WP_009912223.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Medvedev,K.E., Kinch,L.N., Schaeffer,R.D. and Grishin,N.V.
  TITLE     Functional analysis of Rossmann-like domains reveals convergent
            evolution of topology and reaction pathways
  JOURNAL   PLoS Comput Biol 15 (12), e1007569 (2019)
   PUBMED   31869345
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Shin,W.H. and Kihara,D.
  TITLE     55 Years of the Rossmann Fold
  JOURNAL   Methods Mol Biol 1958, 1-13 (2019)
   PUBMED   30945211
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Hanukoglu,I.
  TITLE     Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide
            binding sites
  JOURNAL   Biochem Mol Biol Educ 43 (3), 206-209 (2015)
   PUBMED   25704928
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Bhattacharyya,M., Upadhyay,R. and Vishveshwara,S.
  TITLE     Interaction signatures stabilizing the NAD(P)-binding Rossmann
            fold: a structure network approach
  JOURNAL   PLoS One 7 (12), e51676 (2012)
   PUBMED   23284738
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Storbeck,S., Rolfes,S., Raux-Deery,E., Warren,M.J., Jahn,D. and
            Layer,G.
  TITLE     A novel pathway for the biosynthesis of heme in Archaea:
            genome-based bioinformatic predictions and experimental evidence
  JOURNAL   Archaea 2010, 175050 (2010)
   PUBMED   21197080
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Schubert,H.L., Raux,E., Brindley,A.A., Leech,H.K., Wilson,K.S.,
            Hill,C.P. and Warren,M.J.
  TITLE     The structure of Saccharomyces cerevisiae Met8p, a bifunctional
            dehydrogenase and ferrochelatase
  JOURNAL   EMBO J 21 (9), 2068-2075 (2002)
   PUBMED   11980703
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Murphy,M.J. and Siegel,L.M.
  TITLE     Siroheme and sirohydrochlorin. The basis for a new type of
            porphyrin-related prosthetic group common to both assimilatory and
            dissimilatory sulfite reductases
  JOURNAL   J Biol Chem 248 (19), 6911-6919 (1973)
   PUBMED   4583265
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 11447222
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..159
                     /product="precorrin-2 dehydrogenase/sirohydrochlorin
                     ferrochelatase family protein"
                     /EC_number="1.3.1.76"
                     /GO_function="GO:0004325 - ferrochelatase activity
                     [Evidence IEA]"
                     /GO_function="GO:0043115 - precorrin-2 dehydrogenase
                     activity [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0019354 - siroheme biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17313
     Region          1..>140
                     /region_name="CysG2"
                     /note="Siroheme synthase (precorrin-2
                     oxidase/ferrochelatase domain) [Coenzyme transport and
                     metabolism]; COG1648"
                     /db_xref="CDD:441254"
ORIGIN      
        1 mkypimldit gkkvviiggg kvalrkitgl ldagadilvv glkilpeika ldvrvveeay
       61 rpehlhaafm ifictdnlev nqcvlrdrea gqlvndttdq ansdffnmat vtknelmvgi
      121 stgggnpgya kkvkrevsql vanleteeig rrnkkdktc