NARY_ECOLI
ID NARY_ECOLI Reviewed; 514 AA.
AC P19318; P78267;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Respiratory nitrate reductase 2 beta chain;
DE EC=1.7.5.1;
GN Name=narY; OrderedLocusNames=b1467, JW1462;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-18.
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).
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 beta chain is an
CC electron transfer unit containing four cysteine clusters involved in
CC the formation of iron-sulfur centers. Electrons are transferred from
CC the gamma chain to the molybdenum cofactor of the alpha 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 3 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster per subunit. {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 -!- INTERACTION:
CC P19318; P42593: fadH; NbExp=3; IntAct=EBI-555059, EBI-561933;
CC P19318; P09152: narG; NbExp=5; IntAct=EBI-555059, EBI-547248;
CC P19318; P11349: narH; NbExp=3; IntAct=EBI-555059, EBI-555067;
CC P19318; P19317: narW; NbExp=4; IntAct=EBI-555059, EBI-555088;
CC P19318; P04825: pepN; NbExp=3; IntAct=EBI-555059, EBI-545385;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
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DR EMBL; X17110; CAA34965.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74549.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15104.1; -; Genomic_DNA.
DR PIR; F64899; F64899.
DR RefSeq; NP_415984.1; NC_000913.3.
DR RefSeq; WP_000702535.1; NZ_SSZK01000038.1.
DR AlphaFoldDB; P19318; -.
DR SMR; P19318; -.
DR BioGRID; 4262894; 13.
DR BioGRID; 850395; 5.
DR ComplexPortal; CPX-5581; Nitrate reductase Z complex.
DR DIP; DIP-10323N; -.
DR IntAct; P19318; 14.
DR STRING; 511145.b1467; -.
DR TCDB; 5.A.3.1.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P19318; -.
DR PaxDb; P19318; -.
DR PRIDE; P19318; -.
DR EnsemblBacteria; AAC74549; AAC74549; b1467.
DR EnsemblBacteria; BAA15104; BAA15104; BAA15104.
DR GeneID; 946034; -.
DR KEGG; ecj:JW1462; -.
DR KEGG; eco:b1467; -.
DR PATRIC; fig|1411691.4.peg.801; -.
DR EchoBASE; EB0641; -.
DR eggNOG; COG1140; Bacteria.
DR HOGENOM; CLU_043374_5_2_6; -.
DR InParanoid; P19318; -.
DR OMA; CNACAHS; -.
DR PhylomeDB; P19318; -.
DR BioCyc; EcoCyc:NARY-MON; -.
DR BioCyc; MetaCyc:NARY-MON; -.
DR PRO; PR:P19318; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0009325; C:nitrate reductase complex; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; ISM:EcoCyc.
DR GO; GO:0051536; F:iron-sulfur cluster 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:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0042126; P:nitrate metabolic process; IC:ComplexPortal.
DR CDD; cd10557; NarH_beta-like; 1.
DR Gene3D; 1.10.3650.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR029263; Nitr_red_bet_C.
DR InterPro; IPR038262; Nitr_red_bet_C_sf.
DR InterPro; IPR006547; NO3_Rdtase_bsu.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF14711; Nitr_red_bet_C; 1.
DR TIGRFAMs; TIGR01660; narH; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 3Fe-4S; 4Fe-4S; Cell membrane; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Nitrate assimilation; Oxidoreductase; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..514
FT /note="Respiratory nitrate reductase 2 beta chain"
FT /id="PRO_0000096734"
FT DOMAIN 7..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 174..205
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 207..236
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 325..326
FT /note="QR -> HG (in Ref. 1; CAA34965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 58558 MW; 82D997DB093CD818 CRC64;
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TGREGMEYAW FNNVETKPGI GYPKNWEDQE
EWQGGWVRDV NGKIRPRLGN KMGVITKIFA NPVVPQIDDY YEPFTFDYEH LHSAPEGKHI
PTARPRSLID GKRMDKVIWG PNWEELLGGE FEKRARDRNF EAMQKEMYGQ FENTFMMYLP
RLCEHCLNPS CVATCPSGAI YKREEDGIVL IDQDKCRGWR LCISGCPYKK IYFNWKSGKS
EKCIFCYPRI ESGQPTVCSE TCVGRIRYLG VLLYDADRIE EAASTEREVD LYERQCEVFL
DPHDPSVIEE ALKQGIPQNV IDAAQRSPVY KMAMDWKLAL PLHPEYRTLP MVWYVPPLSP
IQSYADAGGL PKSEGVLPAI ESLRIPVQYL ANMLSAGDTG PVLRALKRMM AMRHYMRSQT
VEGVTDTRAI DEVGLSVAQV EEMYRYLAIA NYEDRFVIPT SHREMAGDAF AERNGCGFTF
GDGCHGSDSK FNLFNSSRID AINITEVRDK AEGE
