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
//