GenomeNet

Database: UniProt
Entry: P19318
LinkDB: P19318
Original site: P19318 
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   10-APR-2019, entry version 160.
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;
RA   Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.;
RT   "Nitrate reductases of Escherichia coli: sequence of the second
RT   nitrate reductase and comparison with that encoded by the narGHJI
RT   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.,
RA   Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
RA   Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
RA   Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
RA   Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 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
CC       an electron acceptor during anaerobic growth. The beta chain is an
CC       electron transfer unit containing four cysteine clusters involved
CC       in the formation of iron-sulfur centers. Electrons are transferred
CC       from the gamma chain to the molybdenum cofactor of the alpha
CC       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;
CC         EC=1.7.5.1;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         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;
CC         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
CC       and a gamma chain. Alpha and beta are catalytic chains; gamma
CC       chains are involved in binding the enzyme complex to the
CC       cytoplasmic membrane.
CC   -!- INTERACTION:
CC       P42593:fadH; NbExp=3; IntAct=EBI-555059, EBI-561933;
CC       P09152:narG; NbExp=5; IntAct=EBI-555059, EBI-547248;
CC       P11349:narH; NbExp=3; IntAct=EBI-555059, EBI-555067;
CC       P19317:narW; NbExp=4; IntAct=EBI-555059, EBI-555088;
CC       P04825:pepN; NbExp=3; IntAct=EBI-555059, EBI-545385;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
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_LN832404.1.
DR   ProteinModelPortal; P19318; -.
DR   SMR; P19318; -.
DR   BioGrid; 4262894; 13.
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   EcoGene; EG10647; narY.
DR   eggNOG; ENOG4108IUE; Bacteria.
DR   eggNOG; COG1140; LUCA.
DR   HOGENOM; HOG000237353; -.
DR   InParanoid; P19318; -.
DR   KO; K00371; -.
DR   PhylomeDB; P19318; -.
DR   BioCyc; EcoCyc:NARY-MONOMER; -.
DR   BioCyc; ECOL316407:JW1462-MONOMER; -.
DR   BioCyc; MetaCyc:NARY-MONOMER; -.
DR   PRO; PR:P19318; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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   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; Complete proteome;
KW   Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN         1    514       Respiratory nitrate reductase 2 beta
FT                                chain.
FT                                /FTId=PRO_0000096734.
FT   DOMAIN        7     35       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      174    205       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      207    236       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        16     16       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        19     19       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        22     22       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        26     26       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       183    183       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       186    186       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       191    191       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       195    195       Iron-sulfur 4 (3Fe-4S). {ECO:0000250}.
FT   METAL       216    216       Iron-sulfur 4 (3Fe-4S). {ECO:0000250}.
FT   METAL       222    222       Iron-sulfur 4 (3Fe-4S). {ECO:0000250}.
FT   METAL       226    226       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       243    243       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       246    246       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       258    258       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       262    262       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   CONFLICT    325    326       QR -> HG (in Ref. 1; CAA34965).
FT                                {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
//
DBGET integrated database retrieval system