(data stored in SCRATCH zone)

SWISSPROT: NASE_BACSU

ID   NASE_BACSU              Reviewed;         106 AA.
AC   P42436;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 130.
DE   RecName: Full=Assimilatory nitrite reductase [NAD(P)H] small subunit;
DE            EC=1.7.1.4;
GN   Name=nasE; Synonyms=nasBD, nirD; OrderedLocusNames=BSU03290;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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   [2]
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   [3]
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   [4]
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   [5]
RP   INDUCTION BY ARFM.
RC   STRAIN=168;
RX   PubMed=11698370; DOI=10.1128/jb.183.23.6815-6821.2001;
RA   Marino M., Cruz Ramos H., Hoffmann T., Glaser P., Jahn D.;
RT   "Modulation of anaerobic energy metabolism of Bacillus subtilis by arfM
RT   (ywiD).";
RL   J. Bacteriol. 183:6815-6821(2001).
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: Required for nitrite assimilation. Required for activity of
CC       the reductase (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:7868621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite;
CC         Xref=Rhea:RHEA:24632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.7.1.4;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + 3 NAD(+) + NH4(+) = 5 H(+) + 3 NADH + nitrite;
CC         Xref=Rhea:RHEA:24628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.7.1.4;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC       Note=Binds 1 [2Fe-2S] cluster.;
CC   -!- SUBUNIT: Associates with NasD. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC       conditions. Induced by ArfM. {ECO:0000269|PubMed:10864496,
CC       ECO:0000269|PubMed:11698370, ECO:0000269|PubMed:12823818}.
DR   EMBL; D30689; BAA06355.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08963.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12123.1; -; Genomic_DNA.
DR   PIR; I40030; I40030.
DR   RefSeq; NP_388211.1; NC_000964.3.
DR   RefSeq; WP_003246252.1; NZ_JNCM01000030.1.
DR   STRING; 224308.BSU03290; -.
DR   PaxDb; P42436; -.
DR   PRIDE; P42436; -.
DR   DNASU; 938331; -.
DR   EnsemblBacteria; CAB12123; CAB12123; BSU03290.
DR   GeneID; 938331; -.
DR   KEGG; bsu:BSU03290; -.
DR   PATRIC; fig|224308.179.peg.343; -.
DR   eggNOG; ENOG4105KH3; Bacteria.
DR   eggNOG; COG2146; LUCA.
DR   HOGENOM; HOG000128541; -.
DR   InParanoid; P42436; -.
DR   KO; K00363; -.
DR   OMA; KCPHKGG; -.
DR   PhylomeDB; P42436; -.
DR   BioCyc; BSUB:BSU03290-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR012748; Rieske-like_NirD.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   TIGRFAMs; TIGR02378; nirD_assim_sml; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P42436.
DR   SWISS-2DPAGE; P42436.
KW   2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; NAD;
KW   Nitrate assimilation; Oxidoreductase; Reference proteome.
FT   CHAIN           1..106
FT                   /note="Assimilatory nitrite reductase [NAD(P)H] small
FT                   subunit"
FT                   /id="PRO_0000096737"
FT   DOMAIN          8..104
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   METAL           49
FT                   /note="Iron-sulfur (2Fe-2S)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   METAL           51
FT                   /note="Iron-sulfur (2Fe-2S); via pros nitrogen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   METAL           68
FT                   /note="Iron-sulfur (2Fe-2S)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   METAL           71
FT                   /note="Iron-sulfur (2Fe-2S); via pros nitrogen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   106 AA;  11895 MW;  26195A275119523D CRC64;
     MVNKDVTKVC IGKIEELPEQ LGKTVYIEDK ELAVFKLSDG SIRAIENRCP HKGGVLAEGI
     VSGQYVFCPM HDWKISLEDG IVQEPDHGCV KTYETLIEGE HVYLVY
//

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