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 03-AUG-2022, entry version 166.
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}.
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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 AlphaFoldDB; P42435; -.
DR SMR; P42435; -.
DR STRING; 224308.BSU03300; -.
DR jPOST; P42435; -.
DR PaxDb; P42435; -.
DR PRIDE; P42435; -.
DR EnsemblBacteria; CAB12124; CAB12124; BSU_03300.
DR GeneID; 938329; -.
DR KEGG; bsu:BSU03300; -.
DR PATRIC; fig|224308.179.peg.344; -.
DR eggNOG; COG1251; Bacteria.
DR InParanoid; P42435; -.
DR OMA; FAQVDPW; -.
DR PhylomeDB; P42435; -.
DR BioCyc; BSUB:BSU03300-MON; -.
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:0106316; F:nitrite reductase NADH activity; IEA:RHEA.
DR GO; GO:0106314; F:nitrite reductase NADPH activity; IEA:RHEA.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.10.1100; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.30.413.10; -; 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; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
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 SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR02374; nitri_red_nirB; 1.
PE 2: Evidence at transcript level;
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 BINDING 43..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 193..223
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 635
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 641
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 675
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 679
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 679
FT /ligand="siroheme"
FT /ligand_id="ChEBI:CHEBI:60052"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
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
