NARH_SHIFL
ID NARH_SHIFL Reviewed; 512 AA.
AC Q83RN5;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Respiratory nitrate reductase 1 beta chain;
DE EC=1.7.5.1;
GN Name=narH; OrderedLocusNames=SF1228, S1312;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: The nitrate reductase enzyme complex allows S.flexneri to use
CC nitrate as an electron acceptor during anaerobic growth. The beta chain
CC is an electron transfer unit containing four cysteine clusters involved
CC in the formation of iron-sulfur centers. Electrons are transferred from
CC the gamma chain to the molybdenum cofactor of the alpha subunit.
CC {ECO:0000250}.
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;
CC Evidence={ECO:0000250|UniProtKB:P11349};
CC Note=Binds 3 [4Fe-4S] clusters per subunit.
CC {ECO:0000250|UniProtKB:P11349};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000250|UniProtKB:P11349};
CC Note=Binds 1 [3Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P11349};
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 (By
CC similarity). {ECO:0000250|UniProtKB:P11349}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
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DR EMBL; AE005674; AAN42841.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16727.1; -; Genomic_DNA.
DR RefSeq; NP_707134.1; NC_004337.2.
DR AlphaFoldDB; Q83RN5; -.
DR SMR; Q83RN5; -.
DR STRING; 198214.SF1228; -.
DR PRIDE; Q83RN5; -.
DR EnsemblBacteria; AAN42841; AAN42841; SF1228.
DR EnsemblBacteria; AAP16727; AAP16727; S1312.
DR GeneID; 1024183; -.
DR KEGG; sfl:SF1228; -.
DR KEGG; sfx:S1312; -.
DR PATRIC; fig|198214.7.peg.1447; -.
DR HOGENOM; CLU_043374_5_2_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
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 3: Inferred from homology;
KW 3Fe-4S; 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..512
FT /note="Respiratory nitrate reductase 1 beta chain"
FT /id="PRO_0000096721"
FT DOMAIN 7..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 175..206
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 208..237
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|UniProtKB:P11349"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 196
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 217
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 223
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 227
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 244
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 247
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 259
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT CONFLICT 402
FT /note="I -> V (in Ref. 2; AAP16727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 58080 MW; F8AC747E1C0973DB CRC64;
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ GFPTDWENQE
KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY YEPFDFDYQN LHTAPEGSKS
QPIARPRSLI TGERMAKIEK GPNWEDDLGG EFDKLAKDKN FDNIQKAMYS QFENTFMMYL
PRLCEHCLNP ACVATCPSGA IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK
SEKCIFCYPR IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL PMVWYVPPLS
PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK PILRALKRML AMRHYKRAET
VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA NYEDRFVVPS SHRELAREAF PEKNGCGFTF
GDGCHGSDTK FNLFNSRRID AIDVTSKTEP HP
