NARH_BACSU
ID NARH_BACSU Reviewed; 487 AA.
AC P42176;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Nitrate reductase beta chain;
DE EC=1.7.5.1;
GN Name=narH; OrderedLocusNames=BSU37270;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8846791;
RA Cruz Ramos H., Boursier L., Moszer I., Kunst F., Danchin A., Glaser P.;
RT "Anaerobic transcription activation in Bacillus subtilis: identification of
RT distinct FNR-dependent and -independent regulatory mechanisms.";
RL EMBO J. 14:5984-5994(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=7557333; DOI=10.1111/j.1574-6968.1995.tb07780.x;
RA Hoffmann T., Troup B., Szabo A., Hungerer C., Jahn D.;
RT "The anaerobic life of Bacillus subtilis: cloning of the genes encoding the
RT respiratory nitrate reductase system.";
RL FEMS Microbiol. Lett. 131:219-225(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: 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.
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 -!- 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; Z49884; CAA90046.1; -; Genomic_DNA.
DR EMBL; X91819; CAA62927.1; -; Genomic_DNA.
DR EMBL; X85014; CAA59372.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15755.1; -; Genomic_DNA.
DR PIR; S60086; S60573.
DR RefSeq; NP_391608.1; NC_000964.3.
DR RefSeq; WP_003244173.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42176; -.
DR SMR; P42176; -.
DR STRING; 224308.BSU37270; -.
DR jPOST; P42176; -.
DR PaxDb; P42176; -.
DR PRIDE; P42176; -.
DR EnsemblBacteria; CAB15755; CAB15755; BSU_37270.
DR GeneID; 937047; -.
DR KEGG; bsu:BSU37270; -.
DR PATRIC; fig|224308.179.peg.4038; -.
DR eggNOG; COG1140; Bacteria.
DR InParanoid; P42176; -.
DR OMA; VYFNWQT; -.
DR PhylomeDB; P42176; -.
DR BioCyc; BSUB:BSU37270-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
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..487
FT /note="Nitrate reductase beta chain"
FT /id="PRO_0000096719"
FT DOMAIN 7..36
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 172..203
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 205..234
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 181
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
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 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 193
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 214
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 220
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 224
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 241
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
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 256
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P11349"
FT CONFLICT 21
FT /note="T -> A (in Ref. 3; CAA62927/CAA59372)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="M -> I (in Ref. 3; CAA62927/CAA59372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 55472 MW; 7BCE6F32CC4F4283 CRC64;
MKIKAQIGMV MNLDKCIGCH TCSVTCKNTW TNRSGAEYMY FNNVETKPGI GYPKQWEDQD
KYKGGWTLKK GKLELKSGSK TNRLAGLFYN PNQPSIDDYY EPWNYDYETL TNSPQKKHQP
VARPKSSLTG DFMNIEWGPN WEDDLAGGHI TGLEDPNVQK MEESIKTEFD DVFMMYLPRI
CEHCINPACV SSCPSGAMYK REEDGIVLVD QNACRSWRYC VSSCPYKKVY FNWQTNKAEK
CTLCFPRLEA GLPTICSETC VGRIRYLGVM LYDADKVEEA ASVENEKDLY HSQLDVFLDP
NDPEVAKLAK EQGIPAEWIE AAQQSPIYKM IIDWKIALPL HPEYRTLPMV WYIPPLSPIM
NLFEGKGSRQ TAEDIFPAID QMRIPIDYLA QLLTAGDTDH IRSTLKKMSV MRQYMRAVQT
NKSIDPELIS SVGLTEQQIE DMYRLLAIAK YDDRFVIPSS HREEVSDLYA EQGSCGLSFS
GGPGSCF
