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 03-AUG-2022, entry version 139.
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:190135;
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}.
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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 AlphaFoldDB; P42436; -.
DR SMR; P42436; -.
DR STRING; 224308.BSU03290; -.
DR PaxDb; P42436; -.
DR PRIDE; P42436; -.
DR DNASU; 938331; -.
DR EnsemblBacteria; CAB12123; CAB12123; BSU_03290.
DR GeneID; 938331; -.
DR KEGG; bsu:BSU03290; -.
DR PATRIC; fig|224308.179.peg.343; -.
DR eggNOG; COG2146; Bacteria.
DR InParanoid; P42436; -.
DR OMA; KCPHKGG; -.
DR PhylomeDB; P42436; -.
DR BioCyc; BSUB:BSU03290-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106316; F:nitrite reductase NADH activity; IEA:RHEA.
DR GO; GO:0106314; F:nitrite reductase NADPH activity; IEA:RHEA.
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;
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 BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 68
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
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
