ID F2LPT2_BURGS Unreviewed; 851 AA.
AC F2LPT2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Nitrite reductase, large subunit {ECO:0000313|EMBL:AEA64121.1};
GN OrderedLocusNames=bgla_2g16790 {ECO:0000313|EMBL:AEA64121.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA64121.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA64121.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA64121.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR037149};
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; CP002600; AEA64121.1; -; Genomic_DNA.
DR AlphaFoldDB; F2LPT2; -.
DR STRING; 999541.bgla_2g16790; -.
DR KEGG; bgd:bgla_2g16790; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_003291_0_0_4; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000008316; Chromosome 2.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd19943; NirB_Fer2_BFD-like_1; 1.
DR CDD; cd19944; NirB_Fer2_BFD-like_2; 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; 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; 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 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; PF18267; Rubredoxin_C; 1.
DR PIRSF; PIRSF037149; NirB; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR037149}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW 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 ECO:0000256|PIRNR:PIRNR037149};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 9..289
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 322..391
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 426..473
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 561..624
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 634..755
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 832..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 91578 MW; EC0C9F9EE04A8EF5 CRC64;
MEKRTMNPIV VIGHGMVGHK LLESLAAMPG QARRVIVLCE EPRPAYDRVH LSEFFAGKSA
EDLSLVAPGF FEAHPQFELR LGTAAAAIDR AARTVTLADG ETIAYHKLVF ATGSSPFVPP
VPGRDREDCF VYRTIEDLVA MQACGARASS GVVVGGGLLG LECAKALRDM GLDTHVVEFA
PRLMAVQVDE GGGSMLRGRI EALGVQVHTG RNTLEIVDGE AGTHRMRFAD GSHLDTDMIV
FSAGIRPRDQ LARDCGLEIG PRGGIAIDSA CRTSDADIYA IGECAAWNGQ TFGLVAPGYD
MARVVAQQLA GGDAVFAGAD LSTKLKLMGV DVASIGDAHA KTAGCRVVQY ADGRREVYKK
LVTSADGKQL LGAVLVGDAA EYGTLLQMML NRIELPAEPE ALILPQSDGA ARPGLGVDAL
PDTAQICSCN NVSKGRLCEA VVNGATSIGA LKSCTGAGTS CGGCVPLVTQ VMKAEMKKQG
LAVNNHLCEH FAYSRQELYH LVRVEGIRGF GELLAKYGKG LGCDICKPTV ASILASCWNE
FVLKREHASL QDSNDYYLAN IQRDGSYSVV PRMPGGEVTP EGLIAVGQVA RKYGLYTKIT
GGQRVDLFGA RVEQLPLIWE ELIAAGFESG HAYGKSLRTV KSCVGSTWCR YGVGDSVGLA
IDLENRYKGL RAPHKIKFGV SGCTRECAEA QGKDVGVIAT EKGWNLYVCG NGGMKPRHAE
LLASDLDRET LIRYVDRFLM FYIRTADRLQ RTSTWRDNLE GGLDYLIDVV VNDRLGLAEE
LEAQMAHVVE TYECEWKKAV SDPATRRRFR HFVNSEAADT TIAFVEERGQ IRPATPEERA
EAPAATEAVT A
//
