ID NARH_BRASZ Reviewed; 266 AA. AC P85098; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 03-MAY-2023, entry version 52. DE RecName: Full=Respiratory nitrate reductase beta chain; DE EC=1.7.5.1; DE AltName: Full=Respiratory membrane-bound nitrate reductase subunit beta; DE Flags: Fragments; GN Name=narH; OS Bradyrhizobium sp. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Bradyrhizobium. OX NCBI_TaxID=376; RN [1] RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR RP LOCATION, AND INDUCTION. RC STRAIN=USDA 3045 {ECO:0000269|Ref.1}; RA Polcyn W.; RT "Identification of membrane-bound respiratory nitrate reductase from RT Bradyrhizobium sp. (Lupinus) USDA 3045 by tandem mass spectrometry."; RL Submitted (FEB-2007) to UniProtKB. CC -!- FUNCTION: The nitrate reductase enzyme complex allows Bradyrhizobium CC sp. USDA 3045 to use nitrate as an electron acceptor during anaerobic CC growth. The beta chain is an electron transfer unit containing four CC cysteine clusters involved in the formation of iron-sulfur centers. CC Electrons are transferred from the gamma chain to the molybdenum CC cofactor of the alpha subunit. {ECO:0000250|UniProtKB:P11349, CC ECO:0000269|Ref.1}. 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 -!- ACTIVITY REGULATION: Inhibited by micromolar concentrations of azide. CC {ECO:0000269|Ref.1}. CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain. CC Alpha and beta are catalytic chains; gamma chains are involved in CC binding the enzyme complex to the cytoplasmic membrane. CC {ECO:0000269|Ref.1}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.1}. Cytoplasm CC {ECO:0000269|Ref.1}. CC -!- INDUCTION: Induced by anaerobiosis, there is no significant expression CC in an aerobic environment. Expression is further induced in the CC presence of nitrate or nitrite. {ECO:0000269|Ref.1}. 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 AlphaFoldDB; P85098; -. DR SMR; P85098; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.20; -; 3. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. 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 SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 1: Evidence at protein level; KW 3Fe-4S; 4Fe-4S; Cell membrane; Cytoplasm; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Nitrate assimilation; Oxidoreductase; Repeat; Transport. FT CHAIN 1..>266 FT /note="Respiratory nitrate reductase beta chain" FT /id="PRO_0000283779" FT DOMAIN 3..32 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 30..61 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 12 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 15 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 18 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="2" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 39 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 42 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 47 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 51 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 73 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 77 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 81 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 84 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 96 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P11349" FT BINDING 100 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P11349" FT NON_CONS 11..12 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 23..24 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 37..38 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 58..59 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 71..72 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 80..81 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 87..88 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 103..104 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 114..115 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 131..132 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 143..144 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 150..151 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 163..164 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 168..169 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 178..179 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 198..199 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 210..211 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 221..222 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 238..239 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 248..249 FT /evidence="ECO:0000303|Ref.1" FT NON_CONS 256..257 FT /evidence="ECO:0000303|Ref.1" FT NON_TER 266 FT /evidence="ECO:0000303|Ref.1" SQ SEQUENCE 266 AA; 29401 MW; 67C8E2EA3B0B8D6E CRC64; SQVGMVLNLD KCIGCHTCSV TCKEGMEYAW FNNVESKLCE HCLNPACVAT CPSGAIYKRE EDGIVLIDQD KLCISGCPYK CIFCYPRIES GQPTVCSETC VGRYLGVLLY DADRIEEAAS TEHETDLLYE RQLDVFLDPN DPKVIEQAIK QGIPQNVIDA AQRSPVYKLA LPLHPEYRAA DAGELGSNGI LPDVESLRML SAGDTGPVIR SQTVEGVTDT RALEEVGLTE AQAQEMYRYL AIANYEDRFV VPSSHRIDAI NITEVR //