MULTISPECIES: assimilatory sulfite reductase (NADPH) hemoprotein

LOCUS       WP_004405225             572 aa            linear   BCT 09-JUN-2024
            subunit [Vibrio].
ACCESSION   WP_004405225
VERSION     WP_004405225.1
KEYWORDS    RefSeq.
SOURCE      Vibrio
  ORGANISM  Vibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Askenasy,I., Pennington,J.M., Tao,Y., Marshall,A.G., Young,N.L.,
            Shang,W. and Stroupe,M.E.
  TITLE     The N-terminal Domain of Escherichia coli Assimilatory
            NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain
            That Mediates Holoenzyme Assembly
  JOURNAL   J Biol Chem 290 (31), 19319-19333 (2015)
   PUBMED   26088143
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Crane,B.R., Siegel,L.M. and Getzoff,E.D.
  TITLE     Sulfite reductase structure at 1.6 A: evolution and catalysis for
            reduction of inorganic anions
  JOURNAL   Science 270 (5233), 59-67 (1995)
   PUBMED   7569952
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Gisselmann,G., Klausmeier,P. and Schwenn,J.D.
  TITLE     The ferredoxin:sulphite reductase gene from Synechococcus PCC7942
  JOURNAL   Biochim Biophys Acta 1144 (1), 102-106 (1993)
   PUBMED   8347657
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Ostrowski,J., Wu,J.Y., Rueger,D.C., Miller,B.E., Siegel,L.M. and
            Kredich,N.M.
  TITLE     Characterization of the cysJIH regions of Salmonella typhimurium
            and Escherichia coli B. DNA sequences of cysI and cysH and a model
            for the siroheme-Fe4S4 active center of sulfite reductase
            hemoprotein based on amino acid homology with spinach nitrite
            reductase
  JOURNAL   J Biol Chem 264 (26), 15726-15737 (1989)
   PUBMED   2670946
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 :: TIGR02041.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Vibrio"
                     /db_xref="taxon:662"
     gene            1..572
                     /gene="cysI"
     Protein         1..572
                     /product="assimilatory sulfite reductase (NADPH)
                     hemoprotein subunit"
                     /EC_number="1.8.1.2"
                     /GO_component="GO:0009337 - sulfite reductase complex
                     (NADPH) [Evidence IEA]"
                     /GO_function="GO:0004783 - sulfite reductase (NADPH)
                     activity [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster
                     binding [Evidence IEA]"
                     /GO_process="GO:0000103 - sulfate assimilation [Evidence
                     IEA]"
                     /GO_process="GO:0008652 - amino acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=63913
     Region          7..571
                     /region_name="PRK13504"
                     /note="NADPH-dependent assimilatory sulfite reductase
                     hemoprotein subunit"
                     /db_xref="CDD:237402"
ORIGIN      
        1 msdknllgte lgplsdnerl kgesdflrgt itedlsgktt ggftadnfql irfhgmyqqd
       61 drdiraerak qkleplhnvm lrarmpggii kpeqwlaidr fadestmygs vrlttrqtfq
      121 fhgvlkpnik lmhqtlhkyg idsiatagdv nrnvlctsnp veselhqqay dwatkisehl
      181 lpktkayaei wldgekiegh rdeepilgnn ylprkfkttv vippqndvdv handlnfvai
      241 ekdgqlvgfn vlvggglamt hgdtstyarr addfgfvsld ktldvaaavv ttqrdwgnrs
      301 nrknaktkyt ldrvgidvfk aevekragvk feesrpyeft drgdrigwte gvdgkyhlai
      361 fiengrlldy pgkplktgma eiakihkgdf rmtanqnliv agvpksqkak iekiarehgl
      421 mddsvseqrk ssmacvafpt cplamaeaer flpefvtdve dilekhglpe deniilrvtg
      481 cpngcgraml aeiglvgkap grynlhlggn ragtripkmy kenitdaqil eeidqlvgrw
      541 akernegecf gdftiragii eevfvskrdl ha