NARZ_ECOLI
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 03-AUG-2022, entry version 182.
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; Proteobacteria; 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; BAA15105.1; -; 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; P19319; -.
DR PRIDE; P19319; -.
DR EnsemblBacteria; AAC74550; AAC74550; b1468.
DR EnsemblBacteria; BAA15105; BAA15105; BAA15105.
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 PhylomeDB; P19319; -.
DR BioCyc; EcoCyc:NARZ-MON; -.
DR BioCyc; MetaCyc:NARZ-MON; -.
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; IC:ComplexPortal.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR Gene3D; 4.10.1200.10; -; 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 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; SSF50692; 1.
DR TIGRFAMs; TIGR01580; narG; 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
