NORV_ECOLI
ID NORV_ECOLI Reviewed; 479 AA.
AC Q46877; Q2MAB9; Q46708; Q46709;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Anaerobic nitric oxide reductase flavorubredoxin;
DE Short=FlRd;
DE Short=FlavoRb;
GN Name=norV; Synonyms=flrD, ygaI, ygaJ, ygaK;
GN OrderedLocusNames=b2710, JW2680;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Yano K., Ikebukuro K., Takada Y., Tomiyama M., Karube I.;
RT "Sequencing and characterization of the downstream region of hydA in
RT Escherichia coli.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9660187; DOI=10.1046/j.1432-1327.1998.2540325.x;
RA Wasserfallen A., Ragettli S., Jouanneau Y., Leisinger T.;
RT "A family of flavoproteins in the domains Archaea and Bacteria.";
RL Eur. J. Biochem. 254:325-332(1998).
RN [5]
RP PROTEIN SEQUENCE OF N-TERMINUS, CHARACTERIZATION, AND MUTAGENESIS.
RX PubMed=11123953; DOI=10.1021/bi001844y;
RA Gomes C.M., Vicente J.B., Wasserfallen A., Teixeira M.;
RT "Spectroscopic studies and characterization of a novel electron-transfer
RT chain from Escherichia coli involving a flavorubredoxin and its
RT flavoprotein reductase partner.";
RL Biochemistry 39:16230-16237(2000).
RN [6]
RP IDENTIFICATION OF FUNCTION.
RC STRAIN=K12 / AB1157;
RX PubMed=11751865; DOI=10.1074/jbc.m110471200;
RA Gardner A.M., Helmick R.A., Gardner P.R.;
RT "Flavorubredoxin, an inducible catalyst for nitric oxide reduction and
RT detoxification in Escherichia coli.";
RL J. Biol. Chem. 277:8172-8177(2002).
RN [7]
RP IDENTIFICATION OF FUNCTION.
RX PubMed=12101220; DOI=10.1074/jbc.m203886200;
RA Gomes C.M., Giuffre A., Forte E., Vicente J.B., Saraiva L.M., Brunori M.,
RA Teixeira M.;
RT "A novel type of nitric-oxide reductase. Escherichia coli
RT flavorubredoxin.";
RL J. Biol. Chem. 277:25273-25276(2002).
RN [8]
RP REGULATION OF EXPRESSION; NEGATIVE REGULATION BY FNR.
RC STRAIN=K12;
RX PubMed=12586421; DOI=10.1016/s0378-1097(02)01186-2;
RA da Costa P.N., Teixeira M., Saraiva L.M.;
RT "Regulation of the flavorubredoxin nitric oxide reductase gene in
RT Escherichia coli: nitrate repression, nitrite induction, and possible post-
RT transcription control.";
RL FEMS Microbiol. Lett. 218:385-393(2003).
RN [9]
RP REGULATION OF EXPRESSION; ANAEROBIC AND NO INDUCED EXPRESSION, AND
RP REQUIREMENT FOR SIGMA-54.
RC STRAIN=K12 / AB1157;
RX PubMed=12529359; DOI=10.1074/jbc.m212462200;
RA Gardner A.M., Gessner C.R., Gardner P.R.;
RT "Regulation of the nitric oxide reduction operon (norRVW) in Escherichia
RT coli: role of NorR and sigma 54 in the nitric oxide stress response.";
RL J. Biol. Chem. 278:10081-10086(2003).
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.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 3 Fe cations per monomer.;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Note=Binds 1 FMN per monomer.;
CC -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC Q46877; Q46877: norV; NbExp=2; IntAct=EBI-557904, EBI-557904;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Submicromolar concentrations of NO induce NorV-dependent NO
CC consumption; as NO reductase is sensitive to oxygen, no activity is
CC detected in its presence. Repressed by oxygen in the presence of NO.
CC Different effects on anaerobic induction in the absence of NO, and in
CC the presence of N(O)3- or N(O)2- have been reported. Transcription is
CC negatively regulated by FNR and does not require NarL or NarP.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05933.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D28595; BAA05932.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D28595; BAA05933.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U29579; AAA69220.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75752.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76787.1; -; Genomic_DNA.
DR PIR; B65051; B65051.
DR RefSeq; NP_417190.1; NC_000913.3.
DR RefSeq; WP_000029634.1; NZ_STEB01000027.1.
DR PDB; 2MS3; NMR; -; A=423-479.
DR PDB; 4D02; X-ray; 1.76 A; A=1-479.
DR PDB; 5LLD; X-ray; 2.65 A; A=1-479.
DR PDB; 5LMC; X-ray; 1.90 A; A=1-479.
DR PDB; 6ETB; X-ray; 1.91 A; A/B=1-412.
DR PDBsum; 2MS3; -.
DR PDBsum; 4D02; -.
DR PDBsum; 5LLD; -.
DR PDBsum; 5LMC; -.
DR PDBsum; 6ETB; -.
DR AlphaFoldDB; Q46877; -.
DR SASBDB; Q46877; -.
DR SMR; Q46877; -.
DR DIP; DIP-28070N; -.
DR IntAct; Q46877; 10.
DR STRING; 511145.b2710; -.
DR PaxDb; Q46877; -.
DR PRIDE; Q46877; -.
DR EnsemblBacteria; AAC75752; AAC75752; b2710.
DR EnsemblBacteria; BAE76787; BAE76787; BAE76787.
DR GeneID; 948979; -.
DR KEGG; ecj:JW2680; -.
DR KEGG; eco:b2710; -.
DR PATRIC; fig|1411691.4.peg.4032; -.
DR EchoBASE; EB2793; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1773; Bacteria.
DR HOGENOM; CLU_017490_0_1_6; -.
DR InParanoid; Q46877; -.
DR OMA; HVKNNIH; -.
DR PhylomeDB; Q46877; -.
DR BioCyc; EcoCyc:G7413-MON; -.
DR BioCyc; MetaCyc:G7413-MON; -.
DR UniPathway; UPA00638; -.
DR PRO; PR:Q46877; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR GO; GO:0016966; F:nitric oxide reductase activity; IDA:EcoCyc.
DR GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IDA:EcoCyc.
DR GO; GO:0046210; P:nitric oxide catabolic process; IMP:EcoCyc.
DR GO; GO:0071731; P:response to nitric oxide; IEP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Electron transport;
KW Flavoprotein; FMN; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Transport.
FT CHAIN 1..479
FT /note="Anaerobic nitric oxide reductase flavorubredoxin"
FT /id="PRO_0000216785"
FT DOMAIN 254..393
FT /note="Flavodoxin-like"
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 /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"
FT MUTAGEN 413..479
FT /note="Missing: Unable to accept electrons from nitric
FT oxide reductase FlrD-NAD(+) reductase (norW)."
FT /evidence="ECO:0000269|PubMed:11123953"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4D02"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4D02"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:4D02"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4D02"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:4D02"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:5LMC"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 264..279
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 339..349
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 352..362
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:4D02"
FT HELIX 379..396
FT /evidence="ECO:0007829|PDB:4D02"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:2MS3"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:2MS3"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:2MS3"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:2MS3"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:2MS3"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:2MS3"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:2MS3"
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
