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Database: UniProt
Entry: M3ADN9_9PROT
LinkDB: M3ADN9_9PROT
Original site: M3ADN9_9PROT 
ID   M3ADN9_9PROT            Unreviewed;       819 AA.
AC   M3ADN9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=NAD(P)H-nitrite reductase {ECO:0000313|EMBL:EME70589.1};
GN   ORFNames=H261_07478 {ECO:0000313|EMBL:EME70589.1};
OS   Paramagnetospirillum caucaseum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=1244869 {ECO:0000313|EMBL:EME70589.1, ECO:0000313|Proteomes:UP000011744};
RN   [1] {ECO:0000313|EMBL:EME70589.1, ECO:0000313|Proteomes:UP000011744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO-1 {ECO:0000313|EMBL:EME70589.1,
RC   ECO:0000313|Proteomes:UP000011744};
RX   PubMed=24723706;
RA   Grouzdev D.S., Dziuba M.V., Sukhacheva M.S., Mardanov A.V., Beletskiy A.V.,
RA   Kuznetsov B.B., Skryabin K.G.;
RT   "Draft Genome Sequence of Magnetospirillum sp. Strain SO-1, a Freshwater
RT   Magnetotactic Bacterium Isolated from the Ol'khovka River, Russia.";
RL   Genome Announc. 2:e00235-14(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EME70589.1}.
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DR   EMBL; AONQ01000015; EME70589.1; -; Genomic_DNA.
DR   RefSeq; WP_008615956.1; NZ_AONQ01000015.1.
DR   AlphaFoldDB; M3ADN9; -.
DR   STRING; 1244869.H261_07478; -.
DR   PATRIC; fig|1244869.3.peg.1512; -.
DR   eggNOG; COG1251; Bacteria.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000011744; Unassembled WGS sequence.
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   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 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; 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; 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          8..288
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          322..390
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          429..477
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          491..540
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          566..629
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          640..777
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   819 AA;  88258 MW;  EA9A77574665DBFB CRC64;
     MNAVPRQKLV VIGNGMAGMR TVEELLAIAP ARYDITVFGA EPHPNYNRIM LSSVLAGEKQ
     VDDIVINPRA WYADNGITLH TGDPVVGIDR AAKTVTSANG VVVPYDKLLL ATGSKPLMPP
     LPGLELPGVV AFRDIADVEK MLDAAEAKQR AVVIGGGLLG LEAAWGLKRR GMPVALVHLM
     PTLMERQLDV EAGGLLQKDL TERGLHFFTS GQTEEIMGVE DGRAQGVKLT DGREIPADLV
     VVAIGIRPNV DLAKASGLDI NRGIAVGDDM ATSDPAIYSV GECVEHRGQI FGLVAPIWEQ
     AKVCASRLAG RDDAHYETPP LSTRLKITGI DVFSAGQLAA QDEADEELVY RDSARGIYKK
     LVLRADKVVG AVMYGDVADG SWYFQLIREK ADVAAIRDRM IFGQAYADAT CKGHAGGVDV
     AAMSDDAQVC GCNGVSKGAI VRAITGKGLT SLDEVKAHTK ASASCGQCAS VVQAILTHVT
     GEVVEAKAAG MCGCTDLSHD EVRKEILHQG LKTQDAVRSA LGWRHADGCA KCRPALNYYL
     LCAWPAEYVD DYQSRFINER VHANIQKDGT YSVVPRMWGG LTTPDELRAI ADVADKYEIP
     TVKVTGGQRI DLLGVKKEDL PGVWADLGKA GLISGHAYSK GLRTVKTCVG SEWCRFGTQD
     STGLGVKLEK LMWGSWTPHK VKLAVSGCPR NCAEATIKDI GVVCVEAGYD ISVGGNGGIE
     LRGTDHLVRV ATEGEVLEYA GAFMQIYREE ARYLERTAPW VERVGMDYVK KRVVEDAEGR
     RAAFARFVFS QEYAQIDPWA ERASGRVDAH EFKTLAEVG
//
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