NARH_BRASZ
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-AUG-2022, entry version 48.
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; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified 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}.
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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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR Pfam; PF13247; Fer4_11; 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
