NARV_ECOLI
ID NARV_ECOLI Reviewed; 226 AA.
AC P0AF32; P19316;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Respiratory nitrate reductase 2 gamma chain;
DE EC=1.7.5.1;
GN Name=narV; OrderedLocusNames=b1465, JW1460;
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=2233673; DOI=10.1007/bf00283030;
RA Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.;
RT "Nitrate reductases of Escherichia coli: sequence of the second nitrate
RT reductase and comparison with that encoded by the narGHJI operon.";
RL Mol. Gen. Genet. 222:104-111(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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 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).
CC -!- FUNCTION: This is a second nitrate reductase enzyme which can
CC substitute for the NRA enzyme and allows E.coli to use nitrate as an
CC electron acceptor during anaerobic growth. The gamma chain is a
CC membrane-embedded heme-iron unit resembling cytochrome b, which
CC 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; Evidence={ECO:0000250};
CC Note=Binds 2 heme groups per subunit. Heme 1 is located at the
CC cytoplasmic interface, heme 2 is located at the periplasmic interface.
CC Electrons are transferred from the periplasmic to the cytoplasmic heme.
CC {ECO:0000250};
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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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DR EMBL; X17110; CAA34967.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74547.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15102.1; -; Genomic_DNA.
DR PIR; S11430; S11430.
DR RefSeq; NP_415982.1; NC_000913.3.
DR RefSeq; WP_000617115.1; NZ_STEB01000053.1.
DR AlphaFoldDB; P0AF32; -.
DR SMR; P0AF32; -.
DR BioGRID; 4263337; 14.
DR ComplexPortal; CPX-5581; Nitrate reductase Z complex.
DR STRING; 511145.b1465; -.
DR TCDB; 5.A.3.1.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P0AF32; -.
DR PaxDb; P0AF32; -.
DR PRIDE; P0AF32; -.
DR EnsemblBacteria; AAC74547; AAC74547; b1465.
DR EnsemblBacteria; BAA15102; BAA15102; BAA15102.
DR GeneID; 66674682; -.
DR GeneID; 946029; -.
DR KEGG; ecj:JW1460; -.
DR KEGG; eco:b1465; -.
DR PATRIC; fig|1411691.4.peg.803; -.
DR EchoBASE; EB0638; -.
DR eggNOG; COG2181; Bacteria.
DR HOGENOM; CLU_092378_1_0_6; -.
DR InParanoid; P0AF32; -.
DR OMA; FLPMSQK; -.
DR PhylomeDB; P0AF32; -.
DR BioCyc; EcoCyc:NARV-MON; -.
DR BioCyc; MetaCyc:NARV-MON; -.
DR PRO; PR:P0AF32; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0009325; C:nitrate reductase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; ISM: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:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IDA:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0042126; P:nitrate metabolic process; IC: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 Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..226
FT /note="Respiratory nitrate reductase 2 gamma chain"
FT /id="PRO_0000096731"
FT TOPO_DOM 1..4
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 5..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 31..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..71
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 72..83
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 84..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 114..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 126..149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 150..183
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 184..199
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 200..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT BINDING 57
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:0000250"
FT BINDING 67
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:0000250"
FT BINDING 188
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:0000250"
FT BINDING 206
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:0000250"
SQ SEQUENCE 226 AA; 26018 MW; 1D5FAC307F3D5B84 CRC64;
MIQYLNVFFY DIYPYICATV FFLGSWLRYD YGQYTWRASS SQMLDKRGMV IWSNLFHIGI
LGIFFGHLFG MLTPHWMYAW FLPVAAKQLM AMVLGGICGV LTLIGGAGLL WRRLTNQRVR
ATSTTPDIII MSILLIQCLL GLSTIPFSAQ YPDGSEMMKL VGWAQSIVTF RGGSSEMLNG
VAFVFRLHLV LGMTIFLLFP FTRLVHVWSA PFEYFTRRYQ IVRSRR
