NORV_ECOSM
ID NORV_ECOSM Reviewed; 479 AA.
AC B1LQ28;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=EcSMS35_2833;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000970; ACB15538.1; -; Genomic_DNA.
DR RefSeq; WP_000029604.1; NC_010498.1.
DR AlphaFoldDB; B1LQ28; -.
DR BMRB; B1LQ28; -.
DR SMR; B1LQ28; -.
DR EnsemblBacteria; ACB15538; ACB15538; EcSMS35_2833.
DR KEGG; ecm:EcSMS35_2833; -.
DR HOGENOM; CLU_017490_0_1_6; -.
DR OMA; HVKNNIH; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000007011; 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_0000341309"
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; 5A06B0348EB6BBC6 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
NVFRSKGMLV GTSTMNNVMM PKIAGLVEEM TGLRFRNKRA SAFGSHGWSG GAVDRLSTRL
QDAGFEMSLS LKAKWRPDQD ALELCREHGR EIARQWALAP LPQSTVNTVV KEETSATTTA
DLGPRMQCSV CQWIYDPAKG EPMQDVAPGT PWSEVPDNFL CPECSLGKDV FDELASEAK
