ID A0A2S8SW32_9BACT Unreviewed; 479 AA.
AC A0A2S8SW32;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Nitrite reductase [NAD(P)H], large subunit {ECO:0000313|EMBL:PQV65005.1};
GN ORFNames=B1R32_10212 {ECO:0000313|EMBL:PQV65005.1};
OS Abditibacterium utsteinense.
OC Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC Abditibacteriaceae; Abditibacterium.
OX NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV65005.1, ECO:0000313|Proteomes:UP000237684};
RN [1] {ECO:0000313|EMBL:PQV65005.1, ECO:0000313|Proteomes:UP000237684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV65005.1,
RC ECO:0000313|Proteomes:UP000237684};
RX PubMed=29475572;
RA Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL Syst. Appl. Microbiol. 0:0-0(2018).
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}.
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:PQV65005.1}.
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DR EMBL; NIGF01000002; PQV65005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8SW32; -.
DR InParanoid; A0A2S8SW32; -.
DR OrthoDB; 9768666at2; -.
DR Proteomes; UP000237684; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
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 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; IPR041575; Rubredoxin_C.
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; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000237684}.
FT DOMAIN 4..287
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 324..388
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 424..471
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 479 AA; 51615 MW; 3B7ADFDD819B4DF2 CRC64;
MKEHLVVIGN GMAGARTVEE IVRRAPDKFR ISMFGDEPHG NYNRILLSDV LGGAQQPEDI
FLHPLDWYRS RGITLHAGVR ARHINRARRE VVGDGGVVET YDKLIIATGS RPLMPPVEGL
LNPEGERKAG IFVMRTLDDC AAIAGYAVKS ERAVVVGGGL LGLEAARGLM RYGAQVTVVH
RNRILMSQQL DESSGAMLCA QMEKLGVRVL LEKITAEIEG QDHVTGVKFA DGQRLDCDMV
VFACGIVPNI EVGREGGFLS ERGLLVDDQM RSQGEENVFV VGECAQHRGV TYGLVAPLWE
QGKVLAEVIS GKNPHAAYHG SKQVTKLKVM GVELASLGEV QPRPGDEEIV YREARRGIYK
KLVVRDGKLA GAILLGDVIK AAALTQTFDR QSALPDDRAA LLFDIGKGTG KASAMLEMPD
EAPVCNCNGV SKGAIRRAAA QGPCTPEAVM SCTRAGSGCG SCKTLVREIV EWVRDSKAA
//
