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NORV_SHIF8
ID   NORV_SHIF8              Reviewed;         479 AA.
AC   Q0T1D5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Anaerobic nitric oxide reductase flavorubredoxin {ECO:0000255|HAMAP-Rule:MF_01312};
DE            Short=FlRd {ECO:0000255|HAMAP-Rule:MF_01312};
DE            Short=FlavoRb {ECO:0000255|HAMAP-Rule:MF_01312};
GN   Name=norV {ECO:0000255|HAMAP-Rule:MF_01312};
GN   Synonyms=flrD {ECO:0000255|HAMAP-Rule:MF_01312};
GN   OrderedLocusNames=SFV_2795;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_01312}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01312};
CC       Note=Binds 3 Fe cations per monomer. {ECO:0000255|HAMAP-Rule:MF_01312};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01312};
CC       Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_01312};
CC   -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC       {ECO:0000255|HAMAP-Rule:MF_01312}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01312}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01312}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC       hydrolase group 3 family. {ECO:0000255|HAMAP-Rule:MF_01312}.
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DR   EMBL; CP000266; ABF04880.1; -; Genomic_DNA.
DR   RefSeq; WP_000029605.1; NC_008258.1.
DR   AlphaFoldDB; Q0T1D5; -.
DR   SMR; Q0T1D5; -.
DR   EnsemblBacteria; ABF04880; ABF04880; SFV_2795.
DR   KEGG; sfv:SFV_2795; -.
DR   HOGENOM; CLU_017490_0_1_6; -.
DR   OMA; HVKNNIH; -.
DR   BioCyc; SFLE373384:SFV_RS15550-MON; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016966; F:nitric oxide reductase activity; IEA:InterPro.
DR   CDD; cd00730; rubredoxin; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   HAMAP; MF_01312; NorV; 1.
DR   InterPro; IPR023957; Anaer_NO_rdtase_flvorubredoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF00301; Rubredoxin; 1.
DR   PIRSF; PIRSF005243; ROO; 1.
DR   PRINTS; PR00163; RUBREDOXIN.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Electron transport; Flavoprotein; FMN; Iron; Metal-binding;
KW   Oxidoreductase; Transport.
FT   CHAIN           1..479
FT                   /note="Anaerobic nitric oxide reductase flavorubredoxin"
FT                   /id="PRO_0000305599"
FT   DOMAIN          254..393
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   DOMAIN          423..474
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
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                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         81
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         83
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         147
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         227
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         260..264
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         342..369
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         428
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         431
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         461
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         464
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
SQ   SEQUENCE   479 AA;  54253 MW;  FE56A038F75C0E30 CRC64;
     MSIVVKNNIH WVGQRDWEVR DFHGTEYKTL RGSSYNSYLI REEKNVLIDT VDHKFSREFV
     QNLRNEIDLA DIDYIVINHA EEDHAGALTE LMAQIPDTPI YCTANAIDSI NGHHHHPEWN
     FNVVKTGDTL DIGNGKQLIF VETPMLHWPD SMMTYLTGDA VLFSNDAFGQ HYCDEHLFND
     EVDQTELFEQ CQRYYANILT PFSRLVTPKI TEILGFNLPV DMIATSHGVV WRDNPTQIVE
     LYLKWAADYQ EDRITIFYDT MSNNTRMMAD AIAQGIAETD PRVAVKIFNV ARSDKNEILT
     NVFRSKGVLV GTSTMNNVMM PKIAGLVEEM TGLRFRNKRA SAFGSHGWSG GAMDRLSTRL
     QDAGFEMSLS LKAKWRPDQD ALELCREHGR EIARQWALAP LPQSTVNTVV KEETSATTTA
     DLGPRMQCSV CQWIYDPAKG EPMQDVAPGT PWSEVPDNFL CPECSLGKDV FDELASEAK
 
 
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