ID A0A0Q6PUD7_9MICO Unreviewed; 567 AA.
AC A0A0Q6PUD7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=FAD/NAD(P)-binding oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASC63_10830 {ECO:0000313|EMBL:KQV08510.1};
OS Leifsonia sp. Root112D2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV08510.1, ECO:0000313|Proteomes:UP000051914};
RN [1] {ECO:0000313|EMBL:KQV08510.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08510.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV08510.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08510.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQV08510.1}.
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DR EMBL; LMCU01000001; KQV08510.1; -; Genomic_DNA.
DR RefSeq; WP_055815388.1; NZ_LMCU01000001.1.
DR AlphaFoldDB; A0A0Q6PUD7; -.
DR STRING; 1736426.ASC63_10830; -.
DR OrthoDB; 1145at2; -.
DR Proteomes; UP000051914; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
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 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 PRINTS; PR00368; FADPNR.
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:UP000051914}.
FT DOMAIN 6..333
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 506..554
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT REGION 406..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 58265 MW; 3A7D849D768D36C5 CRC64;
MSRPLRVVLV GYGPVGARFV EELLPSVRGG TVEVTVVGAE DADAYNRVLI AEYAVGHTDR
AALTVTDTPA AIDAGVRMLR GARVTAIDTE AHNVTVVVTG ATAGLPGTER VEYDRLVLAT
GSRANIPTLD GIERTARDRP SLLRAGADAI AHDPSLPAGV TVLRDLADAE RVRAIVEAGQ
RLIVLGAGVL GLELALAAAG QGAQVSVVHH GGYPMPRNLD RGGGTVLSDS LREAGIEVIA
HSRAESVLLG SPEAIGDDSA SNNSGAQRFE ALCCADGKII AGDLLVLSCG VSPRTELATL
AGLPTAGGIL VDTELRSWGD DDVFAIGDCA HVAARPDDGA AEGVHGAPSG LIGPGWRQAE
WLAGRLAGEA VGGTPLPALA AERPAIVMLK AEGIDVVSAG VVDPEPWDRE PQNSELAASG
DAAHPAARRQ VSQWADPEHG RYVKMVTRGG VLEGMVSVGM PRTGAELMLL FERGSELPAD
RSILLRHDGP DEVSTTVTGE LSADETVCWC NAVTVGHIHD AIDDGNTTVA CVGSATRAGT
GCGGCKGRIA ELIDRFSASG DPVAIGV
//
