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 16-JUN-2009, entry version 67. 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. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=95173124; PubMed=7868621; 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 MEDLINE=97124189; PubMed=8969502; 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 RT of 113 genes."; RL Microbiology 142:3047-3056(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 REGULATION 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 REGULATION. 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 RT arfM (ywiD)."; RL J. Bacteriol. 183:6815-6821(2001). CC -!- FUNCTION: Required for nitrite assimilation. Required for activity CC of the reductase (By similarity). CC -!- CATALYTIC ACTIVITY: Ammonium hydroxide + 3 NAD(P)(+) + H(2)O = CC nitrite + 3 NAD(P)H. CC -!- COFACTOR: Binds 1 2Fe-2S cluster. CC -!- SUBUNIT: Associates with nasD (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- INDUCTION: Positively regulated by tnrA under conditions of CC nitrogen limitation. Induced by arfM. CC -!- SIMILARITY: Contains 1 Rieske domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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; -. DR GeneID; 938331; -. DR GenomeReviews; AL009126_GR; BSU03290. DR KEGG; bsu:BSU03290; -. DR NMPDR; fig|224308.1.peg.330; -. DR SubtiList; BG11097; nasE. DR HOGENOM; P42436; -. DR OMA; P42436; ENEVFAI. DR BioCyc; BSUB224308:BSU0330-MON; -. DR BRENDA; 1.7.1.4; 150. 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:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:EC. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR012748; Nitri_red_NirD. DR InterPro; IPR017941; Rieske_2Fe-2S. DR Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1. DR Pfam; PF00355; Rieske; 1. DR TIGRFAMs; TIGR02378; nirD_assim_sml; 1. DR PROSITE; PS51296; RIESKE; 1. PE 2: Evidence at transcript level; KW 2Fe-2S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; NAD; Nitrate assimilation; Oxidoreductase. FT CHAIN 1 106 Assimilatory nitrite reductase [NAD(P)H] FT small subunit. FT /FTId=PRO_0000096737. FT DOMAIN 8 104 Rieske. FT METAL 49 49 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 51 51 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). FT METAL 68 68 Iron-sulfur (2Fe-2S) (By similarity). FT METAL 71 71 Iron-sulfur (2Fe-2S); via pros nitrogen FT (By similarity). SQ SEQUENCE 106 AA; 11895 MW; 26195A275119523D CRC64; MVNKDVTKVC IGKIEELPEQ LGKTVYIEDK ELAVFKLSDG SIRAIENRCP HKGGVLAEGI VSGQYVFCPM HDWKISLEDG IVQEPDHGCV KTYETLIEGE HVYLVY //