ID   NARZ_ECOLI              Reviewed;        1246 AA.
AC   P19319; P78063; P78154; P78155; P78156;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Respiratory nitrate reductase 2 alpha chain;
DE            EC=1.7.5.1;
GN   Name=narZ; OrderedLocusNames=b1468, JW1463;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
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   SEQUENCE REVISION.
RA   Blasco F.;
RL   Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC   STRAIN=K12;
RA   Bonnefoy V., Ratouchniak J., Blasco F., Chippaux M.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- FUNCTION: The alpha chain is the actual site of nitrate reduction.
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 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Tetramer composed of an alpha, a beta and 2 gamma chains.
CC       Alpha and beta are catalytic chains; gamma chain is involved in binding
CC       the enzyme complex to the cytoplasmic membrane.
CC   -!- INTERACTION:
CC       P19319; P11349: narH; NbExp=6; IntAct=EBI-547262, EBI-555067;
CC       P19319; P0AF26: narJ; NbExp=3; IntAct=EBI-547262, EBI-555043;
CC       P19319; P19317: narW; NbExp=3; IntAct=EBI-547262, EBI-555088;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; X17110; CAA34964.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74550.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15105.2; -; Genomic_DNA.
DR   EMBL; X94992; CAA64449.1; -; Genomic_DNA.
DR   PIR; G64899; G64899.
DR   RefSeq; NP_415985.1; NC_000913.3.
DR   RefSeq; WP_000040458.1; NZ_STEB01000053.1.
DR   AlphaFoldDB; P19319; -.
DR   SMR; P19319; -.
DR   BioGRID; 4262897; 42.
DR   BioGRID; 850360; 3.
DR   ComplexPortal; CPX-5581; Nitrate reductase Z complex.
DR   DIP; DIP-10324N; -.
DR   IntAct; P19319; 29.
DR   STRING; 511145.b1468; -.
DR   TCDB; 5.A.3.1.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR   jPOST; P19319; -.
DR   PaxDb; 511145-b1468; -.
DR   EnsemblBacteria; AAC74550; AAC74550; b1468.
DR   GeneID; 945999; -.
DR   KEGG; ecj:JW1463; -.
DR   KEGG; eco:b1468; -.
DR   PATRIC; fig|511145.12.peg.1534; -.
DR   EchoBASE; EB0642; -.
DR   eggNOG; COG5013; Bacteria.
DR   InParanoid; P19319; -.
DR   OMA; PFIHPFN; -.
DR   OrthoDB; 9759518at2; -.
DR   PhylomeDB; P19319; -.
DR   BioCyc; EcoCyc:NARZ-MONOMER; -.
DR   BioCyc; MetaCyc:NARZ-MONOMER; -.
DR   PHI-base; PHI:10516; -.
DR   PRO; PR:P19319; -.
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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; ISM:EcoCyc.
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; NAS:ComplexPortal.
DR   CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR   CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR   Gene3D; 3.40.50.12440; -; 1.
DR   Gene3D; 4.10.1200.10; nitrate reductase tail; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR006468; NarG.
DR   InterPro; IPR028189; Nitr_red_alph_N.
DR   InterPro; IPR044906; Nitr_red_alph_N_sf.
DR   NCBIfam; TIGR01580; narG; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF14710; Nitr_red_alph_N; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cell membrane; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Molybdenum; Nitrate assimilation;
KW   Oxidoreductase; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..1246
FT                   /note="Respiratory nitrate reductase 2 alpha chain"
FT                   /id="PRO_0000063234"
FT   DOMAIN          43..107
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         50
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         58
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         93
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         223
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /ligand_part="Mo"
FT                   /ligand_part_id="ChEBI:CHEBI:28685"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        1103
FT                   /note="E -> D (in Ref. 1; CAA34964)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1246 AA;  140227 MW;  DB37433A9AB0E16E CRC64;
     MSKLLDRFRY FKQKGETFAD GHGQVMHSNR DWEDSYRQRW QFDKIVRSTH GVNCTGSCSW
     KIYVKNGLVT WEIQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPLIRKRLIE
     LWREALKQHS DPVLAWASIM NDPQKCLSYK QVRGRGGFIR SNWQELNQLI AAANVWTIKT
     YGPDRVAGFS PIPAMSMVSY AAGTRYLSLL GGTCLSFYDW YCDLPPASPM TWGEQTDVPE
     SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTIA ITPDYSEVAK LCDQWLAPKQ
     GTDSALAMAM GHVILKEFHL DNPSDYFINY CRRYSDMPML VMLEPRDDGS YVPGRMIRAS
     DLVDGLGESN NPQWKTVAVN TAGELVVPNG SIGFRWGEKG KWNLESIAAG TETELSLTLL
     GQHDAVAGVA FPYFGGIENP HFRSVKHNPV LVRQLPVKNL TLVDGNTCPV VSVYDLVLAN
     YGLDRGLEDE NSAKDYAEIK PYTPAWGEQI TGVPRQYIET IAREFADTAH KTHGRSMIIL
     GAGVNHWYHM DMNYRGMINM LIFCGCVGQS GGGWAHYVGQ EKLRPQTGWL PLAFALDWNR
     PPRQMNSTSF FYNHSSQWRY EKVSAQELLS PLADASKYSG HLIDFNVRAE RMGWLPSAPQ
     LGRNPLGIKA EADKAGLSPT EFTAQALKSG DLRMACEQPD SSSNHPRNLF VWRSNLLGSS
     GKGHEYMQKY LLGTESGIQG EELGASDGIK PEEVEWQTAA IEGKLDLLVT LDFRMSSTCL
     FSDIVLPTAT WYEKDDMNTS DMHPFIHPLS AAVDPAWESR SDWEIYKGIA KAFSQVCVGH
     LGKETDVVLQ PLLHDSPAEL SQPCEVLDWR KGECDLIPGK TAPNIVAVER DYPATYERFT
     SLGPLMDKLG NGGKGISWNT QDEIDFLGKL NYTKRDGPAQ GRPLIDTAID ASEVILALAP
     ETNGHVAVKA WQALGEITGR EHTHLALHKE DEKIRFRDIQ AQPRKIISSP TWSGLESDHV
     SYNAGYTNVH ELIPWRTLSG RQQLYQDHPW MRAFGESLVA YRPPIDTRSV SEMRQIPPNG
     FPEKALNFLT PHQKWGIHST YSENLLMLTL SRGGPIVWIS ETDARELTIV DNDWVEVFNA
     NGALTARAVV SQRVPPGMTM MYHAQERIMN IPGSEVTGMR GGIHNSVTRV CPKPTHMIGG
     YAQLAWGFNY YGTVGSNRDE FIMIRKMKNV NWLDDEGRDQ VQEAKK
//