(data stored in ACNUC7421 zone)

SWISSPROT: NASD_BACSU

ID   NASD_BACSU              Reviewed;         805 AA.
AC   P42435;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 158.
DE   RecName: Full=Nitrite reductase [NAD(P)H];
DE            EC=1.7.1.4;
GN   Name=nasD; Synonyms=nasBC, nirB; OrderedLocusNames=BSU03300;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=168;
RX   PubMed=7868621; DOI=10.1128/jb.177.5.1409-1413.1995;
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   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
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 of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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   INDUCTION 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   INDUCTION BY ARFM.
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 arfM
RT   (ywiD).";
RL   J. Bacteriol. 183:6815-6821(2001).
RN   [6]
RP   INDUCTION BY TNRA.
RX   PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA   Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT   "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT   associated with a TnrA box.";
RL   Mol. Microbiol. 49:157-165(2003).
CC   -!- FUNCTION: Required for nitrite assimilation.
CC       {ECO:0000269|PubMed:7868621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite;
CC         Xref=Rhea:RHEA:24632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.7.1.4;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O + 3 NAD(+) + NH4(+) = 5 H(+) + 3 NADH + nitrite;
CC         Xref=Rhea:RHEA:24628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.7.1.4;
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC       Note=Binds 1 siroheme per subunit.;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC       conditions. Induced by ArfM. {ECO:0000269|PubMed:10864496,
CC       ECO:0000269|PubMed:11698370, ECO:0000269|PubMed:12823818}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000305}.
DR   EMBL; D30689; BAA06354.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08964.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12124.1; -; Genomic_DNA.
DR   PIR; I40029; I40029.
DR   RefSeq; NP_388212.1; NC_000964.3.
DR   RefSeq; WP_003234637.1; NZ_JNCM01000030.1.
DR   SMR; P42435; -.
DR   STRING; 224308.BSU03300; -.
DR   jPOST; P42435; -.
DR   PaxDb; P42435; -.
DR   PRIDE; P42435; -.
DR   EnsemblBacteria; CAB12124; CAB12124; BSU03300.
DR   GeneID; 938329; -.
DR   KEGG; bsu:BSU03300; -.
DR   PATRIC; fig|224308.179.peg.344; -.
DR   eggNOG; ENOG4108IFG; Bacteria.
DR   eggNOG; COG1251; LUCA.
DR   HOGENOM; HOG000196165; -.
DR   InParanoid; P42435; -.
DR   KO; K00362; -.
DR   OMA; FAQVDPW; -.
DR   PhylomeDB; P42435; -.
DR   BioCyc; BSUB:BSU03300-MONOMER; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-EC.
DR   GO; GO:0042128; P:nitrate assimilation; IBA:GO_Central.
DR   Gene3D; 1.10.10.1100; -; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR017121; Nitrite_Rdtase_lsu.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   Pfam; PF04324; Fer2_BFD; 2.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PIRSF; PIRSF037149; NirB; 1.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   SUPFAM; SSF55124; SSF55124; 1.
DR   TIGRFAMs; TIGR02374; nitri_red_nirB; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P42435.
DR   SWISS-2DPAGE; P42435.
KW   4Fe-4S; FAD; Flavoprotein; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Nitrate assimilation; Oxidoreductase; Reference proteome.
FT   CHAIN           1..805
FT                   /note="Nitrite reductase [NAD(P)H]"
FT                   /id="PRO_0000199961"
FT   NP_BIND         43..79
FT                   /note="FAD"
FT                   /evidence="ECO:0000255"
FT   NP_BIND         193..223
FT                   /note="NAD or NADP"
FT                   /evidence="ECO:0000255"
FT   METAL           635
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           641
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           675
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000250"
FT   METAL           679
FT                   /note="Iron (siroheme axial ligand)"
FT                   /evidence="ECO:0000250"
FT   METAL           679
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   805 AA;  88432 MW;  5ED3295AF3E0CA29 CRC64;
     MGKKQLVLVG NGMAGVRAIE EILSVAKDEF QITIFGAEPH PNYNRILLSK VLQGDTDIKD
     ITLNDWDWYE ENNIQLYTNE TVIKVDTENK TVITDADRIQ PYDELILATG SVPFILPIPG
     ADKKGVTAFR DIKDTDTMLA ASKQYKKAAV IGGGLLGLEA ARGLLNLGMD VSVIHLAPFL
     MERQLDATAG RLLQNELEKQ GMTFLLEKQT EEIVGDDRVE GLRFKDGTSI EADLVVMAVG
     IRPNTTLGAE SGIPVNRGII VNDYMQTEIP HIYAVGECAE HRGIAYGLVA PLYEQAKVLA
     KHMCGIETKP YEGSVLSTQL KVSGVEVFSA GDFNESEEKK AIKVFDEQDG IYKKIVLRGN
     QIVGAVLFGD SSEGNRLFSM IQKEADISET SKISILQPLS QEAGTSITAA MSDDEIICGC
     NGVSKGAIIQ AIQEKGCSST DEIKACTGAS RSCGGCKPLV EEILQHTLGS DFDASAQKEA
     ICGCTTLSRD EVVEEIKAKG LSHTREVMNV LGWKTPEGCS KCRPALNYYL GMINPTKYED
     DRTSRFVNER MHANIQKDGT YSVVPRMYGG VTNSTDLRKI ADVVDKYEIP LVKMTGGQRI
     DLIGVKKEDL PKVWEDLDMP SGYAYGKTLR TVKTCVGEQF CRFGTQDSMA LGIALEKKFE
     GLNTPHKVKM AVSACPRNCA ESGIKDLGVV GIDGGWELYV GGNGGTHLRA GDLLMKVKTN
     EEVLEYAGAY LQYYRETANY LERTSAWLER VGLSHVQSVL NDPEKRQELN GRMNETLSVH
     KDPWKDFLED KQTSKELFEN VVTTS
//

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