AC MF_01312; DC Protein; auto TR HAMAP; MF_01312; -; 1; level=0 XX Names: NorV XX ID NORV DE RecName: Full=Anaerobic nitric oxide reductase flavorubredoxin; DE Short=FlRd; DE Short=FlavoRb; GN Name=norV; Synonyms=flrD; XX CC -!- FUNCTION: Anaerobic nitric oxide reductase; uses NADH to detoxify CC nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has CC at least 2 reductase partners, only one of which (NorW, flavorubredoxin CC reductase) has been identified. NO probably binds to the di-iron CC center; electrons enter from the NorW at rubredoxin and are transferred CC sequentially to the FMN center and the di-iron center. Also able to CC function as an aerobic oxygen reductase. case and CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Note=Binds 3 Fe cations per monomer.; end case case CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Note=Binds 1 FMN per monomer.; end case CC -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. case CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo- CC hydrolase group 3 family. end case XX DR Pfam; PF00258; Flavodoxin_1; 1; trigger=no DR Pfam; PF00753; Lactamase_B; 1; trigger=no DR Pfam; PF00301; Rubredoxin; 1; trigger=no DR Pfam; PF00070; Pyr_redox; 1; trigger=no DR PIRSF; PIRSF005243; ROO; 1; trigger=no DR PRINTS; PR00163; RUBREDOXIN; 1; trigger=no DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1; trigger=yes DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1; trigger=no XX KW Cytoplasm KW Transport KW Electron transport KW Oxidoreductase case KW Flavoprotein KW FMN end case case or KW Metal-binding KW Iron end case XX GO GO:0009055; F:electron transfer activity GO GO:0016491; F:oxidoreductase activity GO GO:0005737; C:cytoplasm XX FT From: NORV_ECOLI (Q46877) FT DOMAIN 423..474 FT /note="Rubredoxin-like" FT REGION 30..210 FT /note="Zinc metallo-hydrolase" FT BINDING 79 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 81 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT Group: 1; Condition: E FT BINDING 83 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT Group: 1; Condition: D FT BINDING 147 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 166 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT Group: 1; Condition: D FT BINDING 166 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT Group: 1; Condition: D FT BINDING 227 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT Group: 1; Condition: H FT BINDING 428 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="3" FT Group: 2; Condition: C FT BINDING 431 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="3" FT Group: 2; Condition: C FT BINDING 461 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="3" FT Group: 2; Condition: C FT BINDING 464 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="3" FT Group: 2; Condition: C XX Size: 479-521; Related: None; Template: Q46877; Scope: Bacteria; Aeromonas Bacteria; Aliivibrio Bacteria; Citrobacter Bacteria; Escherichia Bacteria; Enterobacter Bacteria; Klebsiella Bacteria; Pectobacterium Bacteria; Salmonella Bacteria; Serratia Bacteria; Shigella Bacteria; Vibrio Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: ECO57 lacks the flavodoxin-like domain and is not used in alignment. Restricted to lineages where there is norR upstream and norW downstream. XX # Revision 1.38 2022/11/19 //