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Database: UniProt
Entry: A0A0M8W6D9_9NOCA
LinkDB: A0A0M8W6D9_9NOCA
Original site: A0A0M8W6D9_9NOCA 
ID   A0A0M8W6D9_9NOCA        Unreviewed;       490 AA.
AC   A0A0M8W6D9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Electron transfer flavoprotein {ECO:0000313|EMBL:KOV76933.1};
GN   ORFNames=ADL03_42680 {ECO:0000313|EMBL:KOV76933.1};
OS   Nocardia sp. NRRL S-836.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1519492 {ECO:0000313|EMBL:KOV76933.1, ECO:0000313|Proteomes:UP000037746};
RN   [1] {ECO:0000313|Proteomes:UP000037746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-836 {ECO:0000313|Proteomes:UP000037746};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV76933.1}.
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DR   EMBL; LGDY01000164; KOV76933.1; -; Genomic_DNA.
DR   RefSeq; WP_053739317.1; NZ_LGDY01000164.1.
DR   AlphaFoldDB; A0A0M8W6D9; -.
DR   STRING; 1519492.ADL03_42680; -.
DR   PATRIC; fig|1519492.3.peg.9127; -.
DR   OrthoDB; 9768666at2; -.
DR   Proteomes; UP000037746; 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; PR00469; PNDRDTASEII.
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:UP000037746}.
FT   DOMAIN          3..308
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          331..397
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          432..480
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   490 AA;  50741 MW;  FBEA343582AEFD87 CRC64;
     MRRVVIVGYG MAGARLADEL RRRDPDIAIT VIGAEPHAAY NRVLLSTVVA GSMTPAATRL
     HDDGWAAAHD IDLRLGHEVV AIDRVTRTVE LAATRGASAR SDRAEGPRVT VPYDALVLAT
     GSTPWVPPAE GLVEDGTLAE GVVAFRTLDD CARIEAKARK GMPVAVLGGG LLGIEAARGL
     AGRGCLVTVV HPVGHLMERQ LDPGAGGVLA RTLGKLGIEF RLNALAAKYL PGDGLVLDDG
     THVPAELVVV SAGVRAETSL AVEAGLTVDR GIVVDDVLRT SDPRIHAIGD CAQHPGTVSG
     LVQPAWDQAA VLADRLTGAN PAARYSGTSV VTRLKARDVD LAALGDVHTD VDCPDAEVLC
     FQEPSRGRYA KLVLRDDRVT GAIVLGAPDA AATITQLYDR GIPAPTDRLA LLLGRALPAE
     AASPADLPSS AVICRCNTVS KGQIVSAWRA GAETVPQLAE ATRATTGCGG CKDAVCGLLD
     WLGASQPATA
//
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