NARG_BACSU
ID NARG_BACSU Reviewed; 1228 AA.
AC P42175;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Nitrate reductase alpha chain;
DE EC=1.7.5.1;
GN Name=narG; OrderedLocusNames=BSU37280;
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).
RN [5]
RP SEQUENCE REVISION TO 47.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- FUNCTION: The alpha chain is the actual site of nitrate reduction.
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; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; Z49884; CAA90045.1; -; Genomic_DNA.
DR EMBL; X91819; CAA62926.1; -; Genomic_DNA.
DR EMBL; X85014; CAA59371.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15756.2; -; Genomic_DNA.
DR PIR; S60085; S60085.
DR RefSeq; NP_391609.2; NC_000964.3.
DR RefSeq; WP_003243085.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P42175; -.
DR SMR; P42175; -.
DR STRING; 224308.BSU37280; -.
DR jPOST; P42175; -.
DR PaxDb; P42175; -.
DR PRIDE; P42175; -.
DR EnsemblBacteria; CAB15756; CAB15756; BSU_37280.
DR GeneID; 938358; -.
DR KEGG; bsu:BSU37280; -.
DR PATRIC; fig|224308.179.peg.4039; -.
DR eggNOG; COG5013; Bacteria.
DR InParanoid; P42175; -.
DR OMA; PFIHPFN; -.
DR PhylomeDB; P42175; -.
DR BioCyc; BSUB:BSU37280-MON; -.
DR PRO; PR:P42175; -.
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: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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR Gene3D; 4.10.1200.10; -; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF14710; Nitr_red_alph_N; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01580; narG; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..1228
FT /note="Nitrate reductase alpha chain"
FT /id="PRO_0000063232"
FT DOMAIN 47..111
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 97
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 227
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT CONFLICT 47
FT /note="D -> T (in Ref. 1; CAA90045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1228 AA; 139099 MW; 60E6B3A83422CBF8 CRC64;
MKKKKRSPLF RRLNYFSPIE HHSNKHSQTT REDRDWENVY RNRWQYDKVV RSTHGVNCTG
SCSWNIYVKN GIVTWEGQNL NYPSTGPDMP DFEPRGCPRG ASFSWYIYSP LRVKYPYVRG
VLINLWREAL QTHQNPLEAW KSIVENPEKA KSYKQARGKG GFVRAEWPEV LKLISASLLY
TVMKYGPDRN VGFSPIPAMS MISHASGSRF MSLIGGPMLS FYDWYADLPP ASPQIWGDQT
DVPESSDWYN SGYIITWGSN VPLTRTPDAH FLAEARYKGA KVISISPDFA ESSKFADDWL
SIRQGTDGAL AMAMGHVILQ EFYVNQETER FIEYAKQYTD FPFLVTLSKE NGVYTAGRFL
HAKDIGRKTK HDQWKPAVWD EQTSSFAIPQ GTMGSRWDGQ QKWNLHMIDE ETGEPIEPRL
SVLGIEDEIG TVRIPYFSND GNKVLERDLP IKKMNLNGEE TYITTVFDLI LANYGVNRGI
GERSAVSYDD PEPFTPAWQE QMTGIKKEAV VKIAREFAQN AIDTDGRSMI IVGAGINHWF
NSDTIYRAVL NLVLLVGAQG VNGGGWAHYV GQEKLRPAEG WQTIATAKDW EGVPKLQNGT
SFFYFATDQW RYEDQPISDL ASPIAASSRY KHHADYNVLA ARLGWLPSYP TFNQNGIDLY
KEAEKAGAAT PEDVGAYVAS QLQEKKLKFA IEDPDNEVNF PRNLFVWRAN LISSSGKGHE
YFLKHLLGTT NGLMNDDSDS IRPEEIKWRE QAPEGKLDLL INLDFRMAGT ALYSDIVLPA
ATWYEKHDLS STDMHPFIHP FAPAISAPWE SKSDWDIFKA LSKAVSDLAE EVDMEPVKEV
VATPLLHDTM QELAQPFGKI NDWSKGECEA IPGKTMPNIQ VVERDYKHIF HKMTALGPNV
ALKPSGTKGM SWSIADEYES LKQRLGEITS DSVAKGCPNI SEAKQAAEAI LTLSSTSNGK
VAVKAWESLE NITNLKLKDL AEEREEECFT FEQITAQPKT VITSPAFTGS EKGGRRYSPF
TTNVEKLIPW RTLTGRQSYY VDHELMMEFG ETMATFKPIL QHRPFLSKRP DQEGKEIVLN
YLTPHNKWSV HSMYFDSLPM LTLFRGGPTV WMNKDDAEDT DIKDNDWIEC FNRNGVVVAR
AVLSHRIPKG MAFMHHAQDR HINVPGTKLT NNRGGTHNSP TRIHVKPTQM IGGYAQLSYG
FNYYGPTGNQ RDLNVVIRKL KEVDWLED
