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Respiratory nitrate reductase 1 gamma chain (EC 1.7.99.4) (Cytochrome B-NR) (Nitrate reductase A subunit gamma) (Quinol-nitrate oxidoreductase subunit gamma)

 NARI_ECOLI              Reviewed;         225 AA.
P11350;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
25-OCT-2017, entry version 162.
RecName: Full=Respiratory nitrate reductase 1 gamma chain;
EC=1.7.99.4;
AltName: Full=Cytochrome B-NR;
AltName: Full=Nitrate reductase A subunit gamma;
AltName: Full=Quinol-nitrate oxidoreductase subunit gamma;
Name=narI; Synonyms=chlI; OrderedLocusNames=b1227, JW1218;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2832376; DOI=10.1128/jb.170.4.1721-1729.1988;
Sodergren E.J., Demoss J.A.;
"narI region of the Escherichia coli nitrate reductase (nar) operon
contains two genes.";
J. Bacteriol. 170:1721-1729(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 1-9, AND FORMYLATION AT MET-1.
PubMed=3053688;
Sodergren E.J., Hsu P.Y., Demoss J.A.;
"Roles of the narJ and narI gene products in the expression of nitrate
reductase in Escherichia coli.";
J. Biol. Chem. 263:16156-16162(1988).
[6]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH HEME, METAL
BINDING AT HIS-56; HIS-66; HIS-187 AND HIS-205, COFACTOR, AND SUBUNIT.
PubMed=12910261; DOI=10.1038/nsb969;
Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F.,
Weiner J.H., Strynadka N.C.J.;
"Insights into the respiratory electron transfer pathway from the
structure of nitrate reductase A.";
Nat. Struct. Biol. 10:681-687(2003).
-!- FUNCTION: The nitrate reductase enzyme complex allows E.coli to
use nitrate as an electron acceptor during anaerobic growth. The
gamma chain is a membrane-embedded heme-iron unit resembling
cytochrome b, which transfers electrons from quinones to the beta
subunit.
-!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
acceptor.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:12910261};
Note=Binds 2 heme groups per subunit. Heme 1, called the proximal
or heme Bp in PubMed:12910261, is located at the cytoplasmic
interface, heme 2, called the distal or heme Bd, is located at the
periplasmic interface. Electrons are transferred from the
periplasmic to the cytoplasmic heme.
{ECO:0000269|PubMed:12910261};
-!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta
and a gamma chain. Alpha and beta are catalytic chains; gamma
chains are involved in binding the enzyme complex to the
cytoplasmic membrane. {ECO:0000269|PubMed:12910261}.
-!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
protein.
-!- INDUCTION: By nitrate.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/NAR/";
-----------------------------------------------------------------------
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EMBL; M20147; AAA24197.1; -; Genomic_DNA.
EMBL; U00096; AAC74311.1; -; Genomic_DNA.
EMBL; AP009048; BAA36097.1; -; Genomic_DNA.
PIR; C27737; RDECNG.
RefSeq; NP_415745.1; NC_000913.3.
RefSeq; WP_001160108.1; NZ_LN832404.1.
PDB; 1Q16; X-ray; 1.90 A; C=1-225.
PDB; 1SIW; X-ray; 2.20 A; C=1-225.
PDB; 1Y4Z; X-ray; 2.00 A; C=1-225.
PDB; 1Y5I; X-ray; 1.90 A; C=1-225.
PDB; 1Y5L; X-ray; 2.50 A; C=1-225.
PDB; 1Y5N; X-ray; 2.50 A; C=1-225.
PDB; 3EGW; X-ray; 1.90 A; C=1-225.
PDB; 3IR5; X-ray; 2.30 A; C=1-225.
PDB; 3IR6; X-ray; 2.80 A; C=1-225.
PDB; 3IR7; X-ray; 2.50 A; C=1-225.
PDBsum; 1Q16; -.
PDBsum; 1SIW; -.
PDBsum; 1Y4Z; -.
PDBsum; 1Y5I; -.
PDBsum; 1Y5L; -.
PDBsum; 1Y5N; -.
PDBsum; 3EGW; -.
PDBsum; 3IR5; -.
PDBsum; 3IR6; -.
PDBsum; 3IR7; -.
ProteinModelPortal; P11350; -.
SMR; P11350; -.
BioGrid; 4262233; 10.
DIP; DIP-10313N; -.
IntAct; P11350; 2.
MINT; MINT-1262739; -.
STRING; 316385.ECDH10B_1286; -.
DrugBank; DB04464; N-Formylmethionine.
TCDB; 5.A.3.1.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
PaxDb; P11350; -.
PRIDE; P11350; -.
EnsemblBacteria; AAC74311; AAC74311; b1227.
EnsemblBacteria; BAA36097; BAA36097; BAA36097.
GeneID; 945808; -.
KEGG; ecj:JW1218; -.
KEGG; eco:b1227; -.
PATRIC; fig|1411691.4.peg.1054; -.
EchoBASE; EB0634; -.
EcoGene; EG10640; narI.
eggNOG; ENOG41076YT; Bacteria.
eggNOG; COG2181; LUCA.
HOGENOM; HOG000237376; -.
InParanoid; P11350; -.
KO; K00374; -.
PhylomeDB; P11350; -.
BioCyc; EcoCyc:NARI-MONOMER; -.
BioCyc; MetaCyc:NARI-MONOMER; -.
BRENDA; 1.7.5.1; 2026.
EvolutionaryTrace; P11350; -.
PRO; PR:P11350; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0044799; C:NarGHI complex; IDA:EcoCyc.
GO; GO:0009325; C:nitrate reductase complex; IDA:CACAO.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0009055; F:electron carrier activity; IDA:EcoCyc.
GO; GO:0020037; F:heme binding; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008940; F:nitrate reductase activity; IDA:EcoCyc.
GO; GO:0019645; P:anaerobic electron transport chain; IBA:GO_Central.
GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
InterPro; IPR023234; NarG-like_domain.
InterPro; IPR036197; NarG-like_sf.
InterPro; IPR003816; Nitrate_red_gam.
Pfam; PF02665; Nitrate_red_gam; 1.
SUPFAM; SSF103501; SSF103501; 1.
TIGRFAMs; TIGR00351; narI; 1.
1: Evidence at protein level;
3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
Direct protein sequencing; Electron transport; Formylation; Heme;
Iron; Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 225 Respiratory nitrate reductase 1 gamma
chain.
/FTId=PRO_0000096723.
TOPO_DOM 1 3 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 4 29 Helical; Name=1.
TOPO_DOM 30 47 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 48 70 Helical; Name=2.
TOPO_DOM 71 82 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 83 112 Helical; Name=3.
TOPO_DOM 113 124 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 125 148 Helical; Name=4.
TOPO_DOM 149 182 Periplasmic.
{ECO:0000269|PubMed:15919996}.
TRANSMEM 183 198 Helical; Name=5.
TOPO_DOM 199 225 Cytoplasmic.
{ECO:0000269|PubMed:15919996}.
METAL 56 56 Iron (heme B 1 axial ligand).
{ECO:0000269|PubMed:12910261}.
METAL 66 66 Iron (heme B 2 axial ligand).
{ECO:0000269|PubMed:12910261}.
METAL 187 187 Iron (heme B 2 axial ligand).
{ECO:0000269|PubMed:12910261}.
METAL 205 205 Iron (heme B 1 axial ligand).
{ECO:0000269|PubMed:12910261}.
MOD_RES 1 1 N-formylmethionine.
{ECO:0000269|PubMed:3053688}.
HELIX 2 10 {ECO:0000244|PDB:1Q16}.
HELIX 12 30 {ECO:0000244|PDB:1Q16}.
HELIX 32 34 {ECO:0000244|PDB:1Q16}.
TURN 41 43 {ECO:0000244|PDB:1Q16}.
HELIX 48 71 {ECO:0000244|PDB:1Q16}.
TURN 74 80 {ECO:0000244|PDB:3EGW}.
HELIX 83 114 {ECO:0000244|PDB:1Q16}.
HELIX 116 121 {ECO:0000244|PDB:1Q16}.
HELIX 124 147 {ECO:0000244|PDB:1Q16}.
HELIX 148 150 {ECO:0000244|PDB:1Q16}.
TURN 151 153 {ECO:0000244|PDB:1SIW}.
HELIX 154 167 {ECO:0000244|PDB:1Q16}.
HELIX 173 177 {ECO:0000244|PDB:1Q16}.
HELIX 182 197 {ECO:0000244|PDB:1Q16}.
HELIX 198 200 {ECO:0000244|PDB:1Q16}.
HELIX 202 208 {ECO:0000244|PDB:1Q16}.
HELIX 211 215 {ECO:0000244|PDB:1Q16}.
STRAND 218 222 {ECO:0000244|PDB:1Q16}.
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


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