ID B2IF28_BEII9 Unreviewed; 966 AA.
AC B2IF28;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Nitrite reductase (NAD(P)H), large subunit {ECO:0000313|EMBL:ACB95593.1};
GN OrderedLocusNames=Bind_1970 {ECO:0000313|EMBL:ACB95593.1};
OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB
OS 8712).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Beijerinckia.
OX NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB95593.1, ECO:0000313|Proteomes:UP000001695};
RN [1] {ECO:0000313|Proteomes:UP000001695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC {ECO:0000313|Proteomes:UP000001695};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N.,
RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.;
RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC
RT 9039.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB95593.1, ECO:0000313|Proteomes:UP000001695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712
RC {ECO:0000313|Proteomes:UP000001695};
RX PubMed=20601475; DOI=10.1128/JB.00656-10;
RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C.,
RA Dunfield P.F.;
RT "Complete genome sequence of Beijerinckia indica subsp. indica.";
RL J. Bacteriol. 192:4532-4533(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|ARBA:ARBA00001929};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000256|ARBA:ARBA00005096}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
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DR EMBL; CP001016; ACB95593.1; -; Genomic_DNA.
DR RefSeq; WP_012384949.1; NC_010581.1.
DR AlphaFoldDB; B2IF28; -.
DR STRING; 395963.Bind_1970; -.
DR KEGG; bid:Bind_1970; -.
DR eggNOG; COG1251; Bacteria.
DR eggNOG; COG2146; Bacteria.
DR HOGENOM; CLU_003291_0_0_5; -.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000001695; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR CDD; cd03529; Rieske_NirD; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
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; 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; IPR012748; Rieske-like_NirD.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR041575; Rubredoxin_C.
DR NCBIfam; TIGR02378; nirD_assim_sml; 1.
DR NCBIfam; TIGR02374; nitri_red_nirB; 1.
DR PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13806; Rieske_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF50022; ISP domain; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
DR PROSITE; PS51300; NIRD; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001695}.
FT DOMAIN 9..296
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 322..392
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 423..470
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 561..623
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 633..757
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 848..959
FT /note="Rieske-like [2Fe-2S]"
FT /evidence="ECO:0000259|Pfam:PF13806"
SQ SEQUENCE 966 AA; 104613 MW; DB72B44A1ABB5697 CRC64;
MTERNHREKI MVVGNGMVGH HFVEQLVAHD LHERFDIHVF GAELHHAYDR VHLSEYMAGQ
DARALQLHQD DFHAAHGVTL HLGIHVRSID REKRQIVTGE GDFSYTTLVL ATGSFPFVPP
VPGNVGTAGL VYRTLKDLDM IRAAAQGASH GVVIGGGLLG LEAANALKLL GLAVDVVEFA
PRLMPVQLDD EGGRALRHRI EALGIGVRTA HATQEIVPGT SRRHRLVFSD GTCLETDLVV
FSAGIRPQDA LARDCGLTLG TRGGIAIDDH CRTSDPSIMA VGECAAWRDQ TFGLVAPGYT
MARTAAAVLA GEEAAFTGAD MSTKLKLLGV DVGSIGDAHG TAPGSASYRF IGEADGSYRR
LVLSADGKCV TGAILVGDNS YYDTILQYVQ NGIRPPADPA ALILPQGDGA SLLGADALPA
TATICSCHNV TKGMICEAID GGCGDLASLK KSTKASTGCG GCASLLKQVF EGELTARGVV
VDHSLCEHFS YTRQELYSLV RVHEIKTFEE LMARYGNGGL GCDICKPSVA SILASAWNEP
ITDPAYIPLQ DTNDTFMANM QKNGTYSVVP RIAGGEITPE KLIVLGQVAQ KYGLYTKITG
GQRIDLFGAQ LHQLPDIWGE LLAAGFETGH AYGKSTRTVK SCVGSTWCRY GVQDSVARAL
DLENRYKGLR SPHKLKFAVS GCTRECAEAQ SKDVGVIATE VGWNLYVCGN GGMRPRHAEL
FAIDLDFETL VKYIDRFLMF YIRTADRLQR TAAWRENLEG GLDYLRDVII NDSLGICDEL
ERQMQAVVDS YRCEWRDVLT DEDKLKRFRT FVNDSRSDPN VRVVPERDQV KPADNLPDAV
PDYAGPADWT SVCGIGDLVA NSGVVAWQDG AQVALFYLPN GAPGQNGEPM VYAVDNHDPF
SNANVIGRGI VGDLKGHLVI ASPLYKQHFR LVDGVCLEDE GKRLRTWDAR LRDGQVEIRG
RAPVMV
//
