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 24-JAN-2024, entry version 130. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE005674; AAN42841.1; -; Genomic_DNA. DR EMBL; AE014073; AAP16727.1; -; Genomic_DNA. DR RefSeq; NP_707134.1; NC_004337.2. DR RefSeq; WP_000702649.1; NZ_CP123365.1. DR AlphaFoldDB; Q83RN5; -. DR SMR; Q83RN5; -. DR STRING; 198214.SF1228; -. DR PaxDb; 198214-SF1228; -. 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; 3.30.70.20; -; 3. DR Gene3D; 1.10.3650.10; nitrate reductase domain like; 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 NCBIfam; TIGR01660; narH; 1. DR PANTHER; PTHR43518; NITRATE REDUCTASE BETA SUBUNIT; 1. DR PANTHER; PTHR43518:SF1; RESPIRATORY NITRATE REDUCTASE 1 BETA CHAIN; 1. DR Pfam; PF13247; Fer4_11; 1. DR Pfam; PF14711; Nitr_red_bet_C; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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 //