AC MF_01182; DC Protein; auto TR HAMAP; MF_01182; -; 1; level=0 XX Names: Cytochrom_C552 XX ID NRFA DE RecName: Full=Cytochrome c-552; DE EC=1.7.2.2; DE AltName: Full=Ammonia-forming cytochrome c nitrite reductase; DE Short=Cytochrome c nitrite reductase; DE Flags: Precursor; GN Name=nrfA; XX CC -!- FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six CC electrons in the process. CC -!- CATALYTIC ACTIVITY: CC Reaction=6 Fe(III)-[cytochrome c] + 2 H2O + NH4(+) = 6 Fe(II)- CC [cytochrome c] + 8 H(+) + nitrite; Xref=Rhea:RHEA:13089, Rhea:RHEA- CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.2; case CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per monomer.; end case case or or or or CC -!- COFACTOR: CC Name=heme c; Xref=ChEBI:CHEBI:61717; CC Note=Binds 5 heme c groups covalently per monomer.; end case CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the cytochrome c-552 family. XX DR PROSITE; PS51008; MULTIHEME_CYTC; 1; trigger=no DR Pfam; PF02335; Cytochrom_C552; 1; trigger=no DR General; Signal; -; 1; trigger=yes XX case KW Calcium end case KW Electron transport case or or or or KW Heme end case case KW Iron KW Metal-binding end case KW Oxidoreductase KW Periplasm KW Signal KW Transport XX case GO GO:0005509; F:calcium ion binding end case case GO GO:0005506; F:iron ion binding end case GO GO:0042279; F:nitrite reductase (cytochrome, ammonia-forming) activity GO GO:0006807; P:nitrogen compound metabolic process GO GO:0042597; C:periplasmic space XX FT From: NRFA_ECOLI (P0ABK9) FT BINDING 94 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 Group: 1; Condition: H FT BINDING 126 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 Group: 1; Condition: K FT BINDING 164 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 Group: 1; Condition: H FT BINDING 213 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 Group: 1; Condition: H FT BINDING 215 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: E FT BINDING 216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: Y FT BINDING 261 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: K FT BINDING 263 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: Q FT BINDING 275 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 Group: 1; Condition: H FT BINDING 286 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 Group: 1; Condition: H FT BINDING 301 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 Group: 1; Condition: H FT BINDING 318 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 Group: 1; Condition: H FT BINDING 393 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 Group: 1; Condition: H FT BINDING 122 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT Group: 3; Condition: C FT BINDING 125 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="1" FT /note="covalent" FT Group: 3; Condition: C FT BINDING 160 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT Group: 4; Condition: C FT BINDING 163 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="2" FT /note="covalent" FT Group: 4; Condition: C FT BINDING 209 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /note="covalent" FT Group: 5; Condition: C FT BINDING 212 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="3" FT /note="covalent" FT Group: 5; Condition: C FT BINDING 216 FT /ligand="substrate" FT Condition: Y FT BINDING 264 FT /ligand="substrate" FT Condition: H FT BINDING 282 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /note="covalent" FT Group: 6; Condition: C FT BINDING 285 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="4" FT /note="covalent" FT Group: 6; Condition: C FT BINDING 314 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /note="covalent" FT Group: 7; Condition: C FT BINDING 317 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="5" FT /note="covalent" FT Group: 7; Condition: C XX Size: 463-538; Related: None; Template: P0ABK9; Scope: Bacteria; Bacteroidota Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.32 2023/01/26 //