NORV_ECODH
ID NORV_ECODH Reviewed; 479 AA.
AC B1XCN7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Anaerobic nitric oxide reductase flavorubredoxin;
DE Short=FlRd;
DE Short=FlavoRb;
GN Name=norV; Synonyms=flrD; OrderedLocusNames=ECDH10B_2878;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
RN [2]
RP FUNCTION.
RX PubMed=12142437; DOI=10.1128/jb.184.16.4640-4643.2002;
RA Hutchings M.I., Mandhana N., Spiro S.;
RT "The NorR protein of Escherichia coli activates expression of the
RT flavorubredoxin gene norV in response to reactive nitrogen species.";
RL J. Bacteriol. 184:4640-4643(2002).
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 reductase at rubredoxin and are
CC transferred sequentially to the FMN center and the di-iron center. Also
CC able to function as an aerobic oxygen reductase (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12142437}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 3 Fe cations per monomer. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN per monomer. {ECO:0000250};
CC -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Transcription is negatively regulated by FNR and does not
CC require NarL or NarP (By similarity). Anaerobically activated by
CC nitroprusside in both rich and minimal media. In anaerobic minimal
CC medium, activated by nitrate. In rich medium aerobic cultures activated
CC by nitroprusside. NorR required for activation. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000305}.
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DR EMBL; CP000948; ACB03828.1; -; Genomic_DNA.
DR RefSeq; WP_000029634.1; NC_010473.1.
DR AlphaFoldDB; B1XCN7; -.
DR SMR; B1XCN7; -.
DR KEGG; ecd:ECDH10B_2878; -.
DR HOGENOM; CLU_017490_0_1_6; -.
DR OMA; HVKNNIH; -.
DR BioCyc; ECOL316385:ECDH10B_RS14615-MON; -.
DR UniPathway; UPA00638; -.
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_0000341308"
FT DOMAIN 254..393
FT /note="Flavodoxin-like"
FT DOMAIN 423..479
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 /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 260..264
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 342..369
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 54234 MW; 17AC889A6924AB41 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 GAVDRLSTRL
QDAGFEMSLS LKAKWRPDQD ALKLCREHGR EIARQWALAP LPQSTVNTVV KEETSATTTA
DLGPRMQCSV CQWIYDPAKG EPMQDVAPGT PWSEVPDNFL CPECSLGKDV FEELASEAK
