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UniProtKB/Swiss-Prot entry P42436


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NASE_BACSU
Primary accession number P42436
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 63)
Name and origin of the protein
Protein name Assimilatory nitrite reductase [NAD(P)H] small subunit
Synonym EC 1.7.1.4
Gene name
Name: nasE
Synonyms: nasBD, nirD
OrderedLocusNames: BSU03290
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=7868621 [NCBI, ExPASy, EBI, Israel, Japan]
Ogawa K., Akagawa E., Yamane K., Sun Z.-W., Lacelle M., Zuber P., Nakano M.M.;
"The nasB operon and nasA gene are required for nitrate/nitrite assimilation in Bacillus subtilis.";
J. Bacteriol. 177:1409-1413(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969502 [NCBI, ExPASy, EBI, Israel, Japan]
Yamane K., Kumano M., Kurita K.;
"The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes.";
Microbiology 142:3047-3056(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
REGULATION BY TNRA.
STRAIN=168;
DOI=10.1006/jmbi.2000.3846; PubMed=10864496 [NCBI, ExPASy, EBI, Israel, Japan]
Wray L.V. Jr., Zalieckas J.M., Fisher S.H.;
"Purification and in vitro activities of the Bacillus subtilis TnrA transcription factor.";
J. Mol. Biol. 300:29-40(2000).
[5]
REGULATION.
STRAIN=168;
DOI=10.1128/JB.183.23.6815-6821.2001; PubMed=11698370 [NCBI, ExPASy, EBI, Israel, Japan]
Marino M., Cruz Ramos H., Hoffmann T., Glaser P., Jahn D.;
"Modulation of anaerobic energy metabolism of Bacillus subtilis by arfM (ywiD).";
J. Bacteriol. 183:6815-6821(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D30689; BAA06355.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D50453; BAA08963.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99105; CAB12123.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I40030; I40030.
RefSeq NP_388211.1; -.
3D structure databases
ModBase P42436.
Enzyme and pathway databases
BioCyc BSUB224308:BSU0330-MON; -.
Organism-specific databases
SubtiList BG11097; nasE. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0051537; Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008942; Molecular function: nitrite reductase [NAD(P)H] activity (inferred from electronic annotation from InterPro).
GO:0042128; Biological process: nitrate assimilation (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR012748; Nitri_red_NirD.
IPR005806; Rieske_reg.
Graphical view of domain structure.
Gene3D G3DSA:2.102.10.10; Rieske_reg; 1.
Pfam PF00355; Rieske; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02378; nirD_assim_sml; 1.
PROSITE PS51296; RIESKE; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P42436.
Genome annotation databases
GeneID 938331; -.
GenomeReviews AL009126_GR; BSU03290.
KEGG bsu:BSU03290; -.
NMPDR fig|224308.1.peg.330; -.
Phylogenomic databases
HOGENOM P42436; -.
Genome annotation databases
CMR P42436; BSU03290.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; NAD; Nitrate assimilation; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1   106  106     Assimilatory nitrite reductase [NAD(P)H] small subunit. PRO_0000096737
DOMAIN   8   104  97     Rieske. 
METAL   49    49        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   51    51        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
METAL   68    68        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   71    71        Iron-sulfur (2Fe-2S); via pros nitrogen (By similarity). 
Sequence information
Length: 106 AA [This is the length of the unprocessed precursor] Molecular weight: 11895 Da [This is the MW of the unprocessed precursor] CRC64: 26195A275119523D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVNKDVTKVC IGKIEELPEQ LGKTVYIEDK ELAVFKLSDG SIRAIENRCP HKGGVLAEGI 

        70         80         90        100 
VSGQYVFCPM HDWKISLEDG IVQEPDHGCV KTYETLIEGE HVYLVY 

P42436 in FASTA format

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View entry in raw text format (no links)
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