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P42434

- NASC_BACSU

UniProt

P42434 - NASC_BACSU

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Protein

Assimilatory nitrate reductase catalytic subunit

Gene

nasC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.

Catalytic activityi

Nitrite + acceptor = nitrate + reduced acceptor.

Cofactori

Binds 1 4Fe-4S cluster.Curated
Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation
Metal bindingi29 – 291Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation
Metal bindingi33 – 331Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation
Metal bindingi63 – 631Iron-sulfur (4Fe-4S)PROSITE-ProRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. molybdenum ion binding Source: InterPro
  4. nitrate reductase activity Source: UniProtKB-EC
  5. oxidoreductase activity, acting on NAD(P)H Source: RefGenome

GO - Biological processi

  1. cellular respiration Source: RefGenome
  2. denitrification pathway Source: UniProtKB-UniPathway
  3. nitrate assimilation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciBSUB:BSU03310-MONOMER.
UniPathwayiUPA00652; UER00706.

Names & Taxonomyi

Protein namesi
Recommended name:
Assimilatory nitrate reductase catalytic subunit (EC:1.7.99.4)
Gene namesi
Name:nasC
Synonyms:narB, nasBB
Ordered Locus Names:BSU03310
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU03310. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 710710Assimilatory nitrate reductase catalytic subunitPRO_0000063239Add
BLAST

Proteomic databases

PaxDbiP42434.

Expressioni

Inductioni

Positively regulated by TnrA under nitrogen-limited conditions.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU03310.

Structurei

3D structure databases

ProteinModelPortaliP42434.
SMRiP42434. Positions 15-709.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 77594Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0243.
HOGENOMiHOG000031440.
InParanoidiP42434.
KOiK00372.
OrthoDBiEOG6CVV7G.
PhylomeDBiP42434.

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
[Graphical view]
PfamiPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SMARTiSM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
PROSITEiPS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42434-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTERLLRYFR DKQQDVQSEK TYDTQCPFCS MQCKMQLVEQ TIVTRKKYTA
60 70 80 90 100
IGIDNPTTQG RLCIKGMNAH QHALNSSRIT RPLLKKNGEF MPVSWEEALN
110 120 130 140 150
HIKDQVTMIQ TEHGHDAMAV YGSASITNEE AYLLGKFARV GLQTKYIDYN
160 170 180 190 200
GRLCMSAAAT AANQTFGADR GLTNPLSDIP HTRVIILAGT NIAECQPTIM
210 220 230 240 250
PYFEKAKENG AYFIAIDPRE TATTKIADLH LKIKPGTDAA LANGLVKIII
260 270 280 290 300
DEQLINEDFI QSRTNGFEEL KQHTDSLDLN DIAEQTSVSL VDIRKAAVKF
310 320 330 340 350
AKETSGMLFT ARGIEQQTDG TAAVKGFLNM VLITGKIGKP YSGYGAITGQ
360 370 380 390 400
GNGQGAREHG QKADQLPGYR SIENEEHRAH IAKVWGIHQD ELPRKGVSAY
410 420 430 440 450
EMMEKINDGD IKGLFLMCSN PAVSSPNANL VKKALRRLTF FVAIDLFISE
460 470 480 490 500
TAKYADVILP ASSYLEDEGT MTNVEGRVTL REASRPCPGE AKHDWQIICD
510 520 530 540 550
LASALGKGRY FSYTSAEDIF NELREASRGG IADYSGISYG RLRREGGIHW
560 570 580 590 600
PCPESDHPGT GRLFTESFAH PDQKAALSVI PNEPPVPKEK PTADYPLYLT
610 620 630 640 650
TGRVMSHYLT GVQTRKSAAL AARHFESFME IHPQTAATYN IEDRVLVKIE
660 670 680 690 700
SPRGSITVRS KLSEQIRKDT VFVPIHWADA QNVNDLIGEA LDPACKMPGF
710
KVCAVRIIPI
Length:710
Mass (Da):78,622
Last modified:June 16, 2009 - v3
Checksum:iE9DDA80014D47A53
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti391 – 3911E → D in BAA08965. (PubMed:8969502)Curated
Sequence conflicti391 – 3911E → D in BAA06353. (PubMed:7868621)Curated
Sequence conflicti402 – 4021M → V in BAA08965. (PubMed:8969502)Curated
Sequence conflicti402 – 4021M → V in BAA06353. (PubMed:7868621)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50453 Genomic DNA. Translation: BAA08965.1.
AL009126 Genomic DNA. Translation: CAB12125.2.
D30689 Genomic DNA. Translation: BAA06353.1.
PIRiE69665.
RefSeqiNP_388213.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12125; CAB12125; BSU03310.
GeneIDi938321.
KEGGibsu:BSU03310.
PATRICi18972221. VBIBacSub10457_0339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50453 Genomic DNA. Translation: BAA08965.1 .
AL009126 Genomic DNA. Translation: CAB12125.2 .
D30689 Genomic DNA. Translation: BAA06353.1 .
PIRi E69665.
RefSeqi NP_388213.2. NC_000964.3.

3D structure databases

ProteinModelPortali P42434.
SMRi P42434. Positions 15-709.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU03310.

Proteomic databases

PaxDbi P42434.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12125 ; CAB12125 ; BSU03310 .
GeneIDi 938321.
KEGGi bsu:BSU03310.
PATRICi 18972221. VBIBacSub10457_0339.

Organism-specific databases

GenoListi BSU03310. [Micado ]

Phylogenomic databases

eggNOGi COG0243.
HOGENOMi HOG000031440.
InParanoidi P42434.
KOi K00372.
OrthoDBi EOG6CVV7G.
PhylomeDBi P42434.

Enzyme and pathway databases

UniPathwayi UPA00652 ; UER00706 .
BioCyci BSUB:BSU03310-MONOMER.

Family and domain databases

InterProi IPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR006655. Mopterin_OxRdtase_prok_CS.
IPR027467. MopterinOxRdtase_cofactor_BS.
[Graphical view ]
Pfami PF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view ]
SMARTi SM00926. Molybdop_Fe4S4. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
PROSITEi PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00551. MOLYBDOPTERIN_PROK_1. 1 hit.
PS00490. MOLYBDOPTERIN_PROK_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiNASC_BACSU
AccessioniPrimary (citable) accession number: P42434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 16, 2009
Last modified: October 29, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3