NARI_ECOLI
ID NARI_ECOLI Reviewed; 225 AA.
AC P11350;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Respiratory nitrate reductase 1 gamma chain;
DE EC=1.7.5.1;
DE AltName: Full=Cytochrome B-NR;
DE AltName: Full=Nitrate reductase A subunit gamma;
DE AltName: Full=Quinol-nitrate oxidoreductase subunit gamma;
GN Name=narI; Synonyms=chlI; OrderedLocusNames=b1227, JW1218;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2832376; DOI=10.1128/jb.170.4.1721-1729.1988;
RA Sodergren E.J., Demoss J.A.;
RT "narI region of the Escherichia coli nitrate reductase (nar) operon
RT contains two genes.";
RL J. Bacteriol. 170:1721-1729(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 1-9, AND FORMYLATION AT MET-1.
RX PubMed=3053688; DOI=10.1016/s0021-9258(18)37572-0;
RA Sodergren E.J., Hsu P.Y., Demoss J.A.;
RT "Roles of the narJ and narI gene products in the expression of nitrate
RT reductase in Escherichia coli.";
RL J. Biol. Chem. 263:16156-16162(1988).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP HEME ACQUSITION.
RX PubMed=29282292; DOI=10.1074/jbc.ra117.000229;
RA Haskamp V., Karrie S., Mingers T., Barthels S., Alberge F., Magalon A.,
RA Mueller K., Bill E., Lubitz W., Kleeberg K., Schweyen P., Broering M.,
RA Jahn M., Jahn D.;
RT "The radical SAM protein HemW is a heme chaperone.";
RL J. Biol. Chem. 293:2558-2572(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH HEME, METAL BINDING
RP AT HIS-56; HIS-66; HIS-187 AND HIS-205, COFACTOR, AND SUBUNIT.
RX PubMed=12910261; DOI=10.1038/nsb969;
RA Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F.,
RA Weiner J.H., Strynadka N.C.J.;
RT "Insights into the respiratory electron transfer pathway from the structure
RT of nitrate reductase A.";
RL Nat. Struct. Biol. 10:681-687(2003).
CC -!- FUNCTION: The nitrate reductase enzyme complex allows E.coli to use
CC nitrate as an electron acceptor during anaerobic growth. The gamma
CC chain is a membrane-embedded heme-iron unit resembling cytochrome b,
CC which transfers electrons from quinones to the beta subunit.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:12910261};
CC Note=Binds 2 heme groups per subunit. Heme 1, called the proximal or
CC heme Bp in PubMed:12910261, is located at the cytoplasmic interface,
CC heme 2, called the distal or heme Bd, is located at the periplasmic
CC interface. Electrons are transferred from the periplasmic to the
CC cytoplasmic heme (PubMed:12910261). Heme may be transferred to this
CC protein by HemW (Probable). {ECO:0000269|PubMed:12910261,
CC ECO:0000305|PubMed:29282292};
CC -!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta and a
CC gamma chain. Alpha and beta are catalytic chains; gamma chains are
CC involved in binding the enzyme complex to the cytoplasmic membrane.
CC {ECO:0000269|PubMed:12910261}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15919996}.
CC -!- INDUCTION: By nitrate.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/NAR/";
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DR EMBL; M20147; AAA24197.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74311.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36097.1; -; Genomic_DNA.
DR PIR; C27737; RDECNG.
DR RefSeq; NP_415745.1; NC_000913.3.
DR RefSeq; WP_001160108.1; NZ_LN832404.1.
DR PDB; 1Q16; X-ray; 1.90 A; C=1-225.
DR PDB; 1SIW; X-ray; 2.20 A; C=1-225.
DR PDB; 1Y4Z; X-ray; 2.00 A; C=1-225.
DR PDB; 1Y5I; X-ray; 1.90 A; C=1-225.
DR PDB; 1Y5L; X-ray; 2.50 A; C=1-225.
DR PDB; 1Y5N; X-ray; 2.50 A; C=1-225.
DR PDB; 3EGW; X-ray; 1.90 A; C=1-225.
DR PDB; 3IR5; X-ray; 2.30 A; C=1-225.
DR PDB; 3IR6; X-ray; 2.80 A; C=1-225.
DR PDB; 3IR7; X-ray; 2.50 A; C=1-225.
DR PDBsum; 1Q16; -.
DR PDBsum; 1SIW; -.
DR PDBsum; 1Y4Z; -.
DR PDBsum; 1Y5I; -.
DR PDBsum; 1Y5L; -.
DR PDBsum; 1Y5N; -.
DR PDBsum; 3EGW; -.
DR PDBsum; 3IR5; -.
DR PDBsum; 3IR6; -.
DR PDBsum; 3IR7; -.
DR AlphaFoldDB; P11350; -.
DR SMR; P11350; -.
DR BioGRID; 4262233; 13.
DR ComplexPortal; CPX-1974; Nitrate reductase A complex.
DR DIP; DIP-10313N; -.
DR IntAct; P11350; 2.
DR STRING; 511145.b1227; -.
DR DrugBank; DB07349; (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE.
DR DrugBank; DB04464; N-Formylmethionine.
DR TCDB; 5.A.3.1.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P11350; -.
DR PaxDb; P11350; -.
DR PRIDE; P11350; -.
DR EnsemblBacteria; AAC74311; AAC74311; b1227.
DR EnsemblBacteria; BAA36097; BAA36097; BAA36097.
DR GeneID; 945808; -.
DR KEGG; ecj:JW1218; -.
DR KEGG; eco:b1227; -.
DR PATRIC; fig|1411691.4.peg.1054; -.
DR EchoBASE; EB0634; -.
DR eggNOG; COG2181; Bacteria.
DR HOGENOM; CLU_092378_1_0_6; -.
DR InParanoid; P11350; -.
DR OMA; LFHWGIW; -.
DR PhylomeDB; P11350; -.
DR BioCyc; EcoCyc:NARI-MON; -.
DR BioCyc; MetaCyc:NARI-MON; -.
DR BRENDA; 1.7.5.1; 2026.
DR EvolutionaryTrace; P11350; -.
DR PRO; PR:P11350; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0044799; C:NarGHI complex; IDA:EcoCyc.
DR GO; GO:0009325; C:nitrate reductase complex; IDA:CACAO.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008940; F:nitrate reductase activity; IDA:EcoCyc.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0042126; P:nitrate metabolic process; IDA:ComplexPortal.
DR InterPro; IPR023234; NarG-like_domain.
DR InterPro; IPR036197; NarG-like_sf.
DR InterPro; IPR003816; Nitrate_red_gam.
DR Pfam; PF02665; Nitrate_red_gam; 1.
DR SUPFAM; SSF103501; SSF103501; 1.
DR TIGRFAMs; TIGR00351; narI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Electron transport; Formylation; Heme; Iron;
KW Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..225
FT /note="Respiratory nitrate reductase 1 gamma chain"
FT /id="PRO_0000096723"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 4..29
FT /note="Helical; Name=1"
FT TOPO_DOM 30..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 48..70
FT /note="Helical; Name=2"
FT TOPO_DOM 71..82
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 83..112
FT /note="Helical; Name=3"
FT TOPO_DOM 113..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 125..148
FT /note="Helical; Name=4"
FT TOPO_DOM 149..182
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT TRANSMEM 183..198
FT /note="Helical; Name=5"
FT TOPO_DOM 199..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT BINDING 56
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:12910261"
FT BINDING 66
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:12910261"
FT BINDING 187
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:12910261"
FT BINDING 205
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:12910261"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:3053688"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 12..30
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 48..71
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 74..80
FT /evidence="ECO:0007829|PDB:3EGW"
FT HELIX 83..114
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 124..147
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1SIW"
FT HELIX 154..167
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1Q16"
SQ SEQUENCE 225 AA; 25497 MW; A0D7989D00D05B72 CRC64;
MQFLNMFFFD IYPYIAGAVF LIGSWLRYDY GQYTWRAASS QMLDRKGMNL ASNLFHIGIL
GIFVGHFFGM LTPHWMYEAW LPIEVKQKMA MFAGGASGVL CLIGGVLLLK RRLFSPRVRA
TTTGADILIL SLLVIQCALG LLTIPFSAQH MDGSEMMKLV GWAQSVVTFH GGASQHLDGV
AFIFRLHLVL GMTLFLLFPF SRLIHIWSVP VEYLTRKYQL VRARH
