NASC_BACSU
ID NASC_BACSU Reviewed; 710 AA.
AC P42434;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Assimilatory nitrate reductase catalytic subunit;
DE EC=1.7.-.-;
GN Name=nasC; Synonyms=narB, nasBB; OrderedLocusNames=BSU03310;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [2]
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 [3]
RP SEQUENCE REVISION TO 391 AND 402.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-710.
RC STRAIN=168;
RX PubMed=7868621; DOI=10.1128/jb.177.5.1409-1413.1995;
RA Ogawa K., Akagawa E., Yamane K., Sun Z.-W., Lacelle M., Zuber P.,
RA Nakano M.M.;
RT "The nasB operon and nasA gene are required for nitrate/nitrite
RT assimilation in Bacillus subtilis.";
RL J. Bacteriol. 177:1409-1413(1995).
RN [5]
RP INDUCTION BY TNRA.
RC STRAIN=168;
RX PubMed=10864496; DOI=10.1006/jmbi.2000.3846;
RA Wray L.V. Jr., Zalieckas J.M., Fisher S.H.;
RT "Purification and in vitro activities of the Bacillus subtilis TnrA
RT transcription factor.";
RL J. Mol. Biol. 300:29-40(2000).
RN [6]
RP INDUCTION BY TNRA.
RX PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT associated with a TnrA box.";
RL Mol. Microbiol. 49:157-165(2003).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
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 -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 1/4.
CC -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC conditions. {ECO:0000269|PubMed:10864496, ECO:0000269|PubMed:12823818}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; D50453; BAA08965.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12125.2; -; Genomic_DNA.
DR EMBL; D30689; BAA06353.1; -; Genomic_DNA.
DR PIR; E69665; E69665.
DR RefSeq; NP_388213.2; NC_000964.3.
DR RefSeq; WP_003246484.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; P42434; -.
DR SMR; P42434; -.
DR STRING; 224308.BSU03310; -.
DR PaxDb; P42434; -.
DR PRIDE; P42434; -.
DR EnsemblBacteria; CAB12125; CAB12125; BSU_03310.
DR GeneID; 938321; -.
DR KEGG; bsu:BSU03310; -.
DR PATRIC; fig|224308.179.peg.345; -.
DR eggNOG; COG0243; Bacteria.
DR InParanoid; P42434; -.
DR OMA; GMNAHQH; -.
DR PhylomeDB; P42434; -.
DR BioCyc; BSUB:BSU03310-MON; -.
DR UniPathway; UPA00652; UER00706.
DR Proteomes; UP000001570; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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 Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..710
FT /note="Assimilatory nitrate reductase catalytic subunit"
FT /id="PRO_0000063239"
FT DOMAIN 19..77
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 33
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT CONFLICT 391
FT /note="E -> D (in Ref. 1; BAA08965 and 4; BAA06353)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="M -> V (in Ref. 1; BAA08965 and 4; BAA06353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 78622 MW; E9DDA80014D47A53 CRC64;
MTERLLRYFR DKQQDVQSEK TYDTQCPFCS MQCKMQLVEQ TIVTRKKYTA IGIDNPTTQG
RLCIKGMNAH QHALNSSRIT RPLLKKNGEF MPVSWEEALN HIKDQVTMIQ TEHGHDAMAV
YGSASITNEE AYLLGKFARV GLQTKYIDYN GRLCMSAAAT AANQTFGADR GLTNPLSDIP
HTRVIILAGT NIAECQPTIM PYFEKAKENG AYFIAIDPRE TATTKIADLH LKIKPGTDAA
LANGLVKIII DEQLINEDFI QSRTNGFEEL KQHTDSLDLN DIAEQTSVSL VDIRKAAVKF
AKETSGMLFT ARGIEQQTDG TAAVKGFLNM VLITGKIGKP YSGYGAITGQ GNGQGAREHG
QKADQLPGYR SIENEEHRAH IAKVWGIHQD ELPRKGVSAY EMMEKINDGD IKGLFLMCSN
PAVSSPNANL VKKALRRLTF FVAIDLFISE TAKYADVILP ASSYLEDEGT MTNVEGRVTL
REASRPCPGE AKHDWQIICD LASALGKGRY FSYTSAEDIF NELREASRGG IADYSGISYG
RLRREGGIHW PCPESDHPGT GRLFTESFAH PDQKAALSVI PNEPPVPKEK PTADYPLYLT
TGRVMSHYLT GVQTRKSAAL AARHFESFME IHPQTAATYN IEDRVLVKIE SPRGSITVRS
KLSEQIRKDT VFVPIHWADA QNVNDLIGEA LDPACKMPGF KVCAVRIIPI