AC MF_02023; DC Protein; auto TR HAMAP; MF_02023; -; 1; level=0 XX Names: Sulfite_red XX ID MCCA DE RecName: Full=Dissimilatory sulfite reductase; DE EC=1.8.99.-; DE Flags: Precursor; XX CC -!- FUNCTION: Respiratory sulfite reductase that catalyzes the reduction of CC sulfite to sulfide in a single step, consuming six electrons in the CC process. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide = CC [protein]-dithiol + 2 AH2 + H(+) + sulfite; Xref=Rhea:RHEA:51676, CC Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:50058; CC -!- COFACTOR: CC Name=Cu(+); Xref=ChEBI:CHEBI:49552; CC Note=Exposure to oxygen reduces copper binding and leads to the CC formation of a disulfide bond between the two Cys residues that bind CC the copper ion.; CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Note=Binds 8 heme c groups covalently per monomer.; CC -!- PATHWAY: Sulfur metabolism; sulfite reduction. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the multiheme cytochrome c family. XX DR PROSITE; PS51008; MULTIHEME_CYTC; 2; trigger=no DR Pfam; PF14522; Cytochrome_C7; 1; trigger=no DR Pfam; PF09699; Paired_CXXCH_1; 1; trigger=no DR General; Signal; -; 1; trigger=yes XX KW Copper KW Electron transport KW Heme KW Iron KW Metal-binding KW Oxidoreductase KW Periplasm KW Signal KW Sulfate respiration KW Transport XX GO GO:0005507; F:copper ion binding GO GO:0020037; F:heme binding GO GO:0005506; F:iron ion binding GO GO:0016002; F:sulfite reductase activity GO GO:0070814; P:hydrogen sulfide biosynthetic process GO GO:0042597; C:periplasmic space XX FT From: MCCA_WOLSU (Q7MSJ8) FT BINDING 159 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 171 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 318 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 355 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 360 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 376 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 411 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT Condition: C FT BINDING 423 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="6" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 434 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 437 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 478 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="6" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 491 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="8" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 500 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="7" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 507 FT /ligand="Cu(+)" FT /ligand_id="ChEBI:CHEBI:49552" FT Condition: C FT BINDING 528 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 591 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="8" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 675 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="7" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 155 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT Condition: C FT BINDING 158 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT Condition: C FT BINDING 220 FT /ligand="substrate" FT Condition: K FT BINDING 297 FT /ligand="substrate" FT Condition: Y FT BINDING 314 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT Condition: C FT BINDING 317 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT Condition: C FT BINDING 351 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /note="covalent" FT Condition: C FT BINDING 354 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /note="covalent" FT Condition: C FT BINDING 372 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /note="covalent" FT Condition: C FT BINDING 375 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /note="covalent" FT Condition: C FT BINDING 378 FT /ligand="substrate" FT Condition: R FT BINDING 430 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /note="covalent" FT Condition: C FT BINDING 433 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /note="covalent" FT Condition: C FT BINDING 474 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="6" FT /note="covalent" FT Condition: C FT BINDING 477 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="6" FT /note="covalent" FT Condition: C FT BINDING 496 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="7" FT /note="covalent" FT Condition: C FT BINDING 499 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="7" FT /note="covalent" FT Condition: C FT BINDING 574 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="8" FT /note="covalent" FT Condition: C FT BINDING 590 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="8" FT /note="covalent" FT Condition: C XX Size: 640-710; Related: None; Template: Q7MSJ8; Q8EJI6; Scope: Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.10 2023/01/26 //