P42434 (NASC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Assimilatory nitrate reductase catalytic subunit
EC=1.7.99.4

Gene names

Name:	nasC
Synonyms:	narB, nasBB
Ordered Locus Names:	BSU03310

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	710 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic activity	Nitrite + acceptor = nitrate + reduced acceptor.
Cofactor	Binds 1 4Fe-4S cluster Potential. Molybdenum (molybdopterin).
Pathway	Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 1/4.
Induction	Positively regulated by TnrA under nitrogen-limited conditions. Ref.5 Ref.6
Sequence similarities	Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Ontologies

Keywords
Biological process	Nitrate assimilation
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular respiration Inferred from Biological aspect of Ancestor. Source: RefGenome denitrification pathway Inferred from electronic annotation. Source: UniProtKB-UniPathway nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro nitrate reductase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on NAD(P)H Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 710	710	Assimilatory nitrate reductase catalytic subunit		PRO_0000063239
Sites
	Metal binding	26	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	29	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	33	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	63	1	Iron-sulfur (4Fe-4S) Potential
Experimental info
	Sequence conflict	391	1	E → D in BAA08965. Ref.1
	Sequence conflict	391	1	E → D in BAA06353. Ref.4
	Sequence conflict	402	1	M → V in BAA08965. Ref.1
	Sequence conflict	402	1	M → V in BAA06353. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P42434 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: E9DDA80014D47A53	FASTA	710	78,622
	10 20 30 40 50 60 MTERLLRYFR DKQQDVQSEK TYDTQCPFCS MQCKMQLVEQ TIVTRKKYTA IGIDNPTTQG 70 80 90 100 110 120 RLCIKGMNAH QHALNSSRIT RPLLKKNGEF MPVSWEEALN HIKDQVTMIQ TEHGHDAMAV 130 140 150 160 170 180 YGSASITNEE AYLLGKFARV GLQTKYIDYN GRLCMSAAAT AANQTFGADR GLTNPLSDIP 190 200 210 220 230 240 HTRVIILAGT NIAECQPTIM PYFEKAKENG AYFIAIDPRE TATTKIADLH LKIKPGTDAA 250 260 270 280 290 300 LANGLVKIII DEQLINEDFI QSRTNGFEEL KQHTDSLDLN DIAEQTSVSL VDIRKAAVKF 310 320 330 340 350 360 AKETSGMLFT ARGIEQQTDG TAAVKGFLNM VLITGKIGKP YSGYGAITGQ GNGQGAREHG 370 380 390 400 410 420 QKADQLPGYR SIENEEHRAH IAKVWGIHQD ELPRKGVSAY EMMEKINDGD IKGLFLMCSN 430 440 450 460 470 480 PAVSSPNANL VKKALRRLTF FVAIDLFISE TAKYADVILP ASSYLEDEGT MTNVEGRVTL 490 500 510 520 530 540 REASRPCPGE AKHDWQIICD LASALGKGRY FSYTSAEDIF NELREASRGG IADYSGISYG 550 560 570 580 590 600 RLRREGGIHW PCPESDHPGT GRLFTESFAH PDQKAALSVI PNEPPVPKEK PTADYPLYLT 610 620 630 640 650 660 TGRVMSHYLT GVQTRKSAAL AARHFESFME IHPQTAATYN IEDRVLVKIE SPRGSITVRS 670 680 690 700 710 KLSEQIRKDT VFVPIHWADA QNVNDLIGEA LDPACKMPGF KVCAVRIIPI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 391 AND 402.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-710. Strain: 168.
[5]	"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] [Europe PMC] [Abstract] Cited for: INDUCTION BY TNRA. Strain: 168.
[6]	"Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box." Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y. Mol. Microbiol. 49:157-165(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY TNRA.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50453 Genomic DNA. Translation: BAA08965.1. AL009126 Genomic DNA. Translation: CAB12125.2. D30689 Genomic DNA. Translation: BAA06353.1.
PIR	E69665.
RefSeq	NP_388213.2. NC_000964.3.
3D structure databases
ProteinModelPortal	P42434.
SMR	P42434. Positions 15-709.
ModBase	Search...
Protein-protein interaction databases
STRING	224308.BSU03310.
Proteomic databases
PaxDb	P42434.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAB12125; CAB12125; BSU03310.
GeneID	938321.
KEGG	bsu:BSU03310.
PATRIC	18972221. VBIBacSub10457_0339.
Organism-specific databases
GenoList	BSU03310. [Micado]
Phylogenomic databases
eggNOG	COG0243.
HOGENOM	HOG000031440.
KO	K00372.
ProtClustDB	CLSK872771.
Enzyme and pathway databases
BioCyc	BSUB:BSU03310-MONOMER.
UniPathway	UPA00652; UER00706.
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR006655. Mopterin_OxRdtase_prok_CS. [Graphical view]
Pfam	PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. [Graphical view]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
PROSITE	PS00551. MOLYBDOPTERIN_PROK_1. 1 hit. PS00490. MOLYBDOPTERIN_PROK_2. 1 hit. PS00932. MOLYBDOPTERIN_PROK_3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NASC_BACSU

Accession

Primary (citable) accession number: P42434

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	June 16, 2009
Last modified:	May 1, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program