ID A0A0Q8CMN3_9MICO Unreviewed; 538 AA.
AC A0A0Q8CMN3;
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=ASD61_05380 {ECO:0000313|EMBL:KRA11509.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA11509.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA11509.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11509.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA11509.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA11509.1,
RC ECO:0000313|Proteomes:UP000051073};
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:KRA11509.1}.
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DR EMBL; LMGR01000001; KRA11509.1; -; Genomic_DNA.
DR RefSeq; WP_055819225.1; NZ_LMGR01000001.1.
DR AlphaFoldDB; A0A0Q8CMN3; -.
DR STRING; 1736567.ASD61_05380; -.
DR Proteomes; UP000051073; 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:UP000051073}.
FT DOMAIN 1..317
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 477..525
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 538 AA; 55612 MW; 2B4F314262A76602 CRC64;
MRVVLVGYGP VGSRFVDEML PAVRDGSVAL TVVGAEETDA YNRVLVAELA VGRTDQESII
VADRAAAEAA GVRIITGTIA SAIDRAATEV ILDSGERVGY DRLVLATGAR ANIPTLDGVA
RGRRDLAHLE KYGPALVGRD DELPLGITVL RDVADAERIS RTVRAGGRIV VLGAGVLGLE
LALAASQAGA EACVVHHGDI PMPRNLDKGG GRVLQAALRR AGVSVVEHSR AEAVSFSEHE
NGDRSFDGLI TADGKQIRGE LLVLSCGVGA RTELATLAGL RTAAGIVVDT DLRSWSDPAI
TAIGDCAHVV PRNAATAEVS VLPGAPTGLI GPGWRQADWL AAQLRAEASG SPLTIAAPAE
RDALVMLKAE GIDVVAIGDV SADPWDPQYA DDVLDPRGPQ RVAQWADPEN GSYVKLVTRG
GVLTAFVCVG MPRTAAELTL LYERGSELPA DRSVLLRFDG PDFTPASDSD VFAPGATVCW
CNGVTVAHIA DSAACGNTTV TCISKDTRAG TGCGGCTGRI AELLRHLEST GGAAAAAV
//
