Reviewed, UniProtKB/Swiss-Prot P42436 (NASE_BACSU)

Names and origin

Protein names

Recommended name:
    Assimilatory nitrite reductase [NAD(P)H] small subunit
    EC=1.7.1.4

Gene names

Name:	nasE
Synonyms:	nasBD, nirD
Ordered Locus Names:	BSU03290

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	106 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Required for nitrite assimilation. Required for activity of the reductase By similarity.
Catalytic activity	Ammonium hydroxide + 3 NAD(P)+ + H2O = nitrite + 3 NAD(P)H.
Cofactor	Binds 1 2Fe-2S cluster.
Subunit structure	Associates with nasD By similarity.
Subcellular location	Cytoplasm By similarity.
Induction	Positively regulated by tnrA under conditions of nitrogen limitation. Induced by arfM.
Sequence similarities	Contains 1 Rieske domain.

Ontologies

Keywords
Biological process	Nitrate assimilation
Cellular component	Cytoplasm
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW nitrite reductase [NAD(P)H] activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 106	106	Assimilatory nitrite reductase [NAD(P)H] small subunit		PRO_0000096737
Regions
	Domain	8 – 104	97	Rieske
Sites
	Metal binding	49	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	51	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	68	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	71	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42436-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 26195A275119523D	FASTA	106	11,895
	10 20 30 40 50 60 MVNKDVTKVC IGKIEELPEQ LGKTVYIEDK ELAVFKLSDG SIRAIENRCP HKGGVLAEGI 70 80 90 100 VSGQYVFCPM HDWKISLEDG IVQEPDHGCV KTYETLIEGE HVYLVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nasB operon and nasA gene are required for nitrate/nitrite assimilation in Bacillus subtilis." Ogawa K., Akagawa E., Yamane K., Sun Z.-W., Lacelle M., Zuber P., Nakano M.M. J. Bacteriol. 177:1409-1413(1995) [PubMed: 7868621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"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." Yamane K., Kumano M., Kurita K. Microbiology 142:3047-3056(1996) [PubMed: 8969502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Purification and in vitro activities of the Bacillus subtilis TnrA transcription factor." Wray L.V. Jr., Zalieckas J.M., Fisher S.H. J. Mol. Biol. 300:29-40(2000) [PubMed: 10864496] [Abstract] Cited for: REGULATION BY TNRA. Strain: 168.
[5]	"Modulation of anaerobic energy metabolism of Bacillus subtilis by arfM (ywiD)." Marino M., Cruz Ramos H., Hoffmann T., Glaser P., Jahn D. J. Bacteriol. 183:6815-6821(2001) [PubMed: 11698370] [Abstract] Cited for: REGULATION. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D30689 Genomic DNA. Translation: BAA06355.1. D50453 Genomic DNA. Translation: BAA08963.1. AL009126 Genomic DNA. Translation: CAB12123.1.
PIR	I40030.
RefSeq	NP_388211.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	938331.
GenomeReviews	Gene locus BSU03290 in contig AL009126_GR.
KEGG	bsu:BSU03290.
NMPDR	fig|224308.1.peg.330.
Organism-specific databases
SubtiList	BG11097. nasE. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P42436.
OMA	P42436. ENEVFAI.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU0330-MON.
BRENDA	1.7.1.4. 150.
Family and domain databases
InterPro	IPR012748. Nitri_red_NirD. IPR017941. Rieske_2Fe-2S. [Graphical view]
Gene3D	G3DSA:2.102.10.10. Rieske_reg. 1 hit.
Pfam	PF00355. Rieske. 1 hit. [Graphical view]
TIGRFAMs	TIGR02378. nirD_assim_sml. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NASE_BACSU

Accession

Primary (citable) accession number: P42436

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)