ID A0A0Q8DQN9_9ACTN Unreviewed; 521 AA.
AC A0A0Q8DQN9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Nitrite reductase {ECO:0000313|EMBL:KRA29784.1};
GN ORFNames=ASD81_18880 {ECO:0000313|EMBL:KRA29784.1};
OS Nocardioides sp. Root614.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA29784.1, ECO:0000313|Proteomes:UP000051699};
RN [1] {ECO:0000313|EMBL:KRA29784.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA29784.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA29784.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA29784.1,
RC ECO:0000313|Proteomes:UP000051699};
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:KRA29784.1}.
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DR EMBL; LMGV01000008; KRA29784.1; -; Genomic_DNA.
DR RefSeq; WP_056715183.1; NZ_LMGV01000008.1.
DR AlphaFoldDB; A0A0Q8DQN9; -.
DR OrthoDB; 9768666at2; -.
DR Proteomes; UP000051699; 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 PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
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:UP000051699}.
FT DOMAIN 13..344
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 467..508
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 521 AA; 54776 MW; 77DC85E08C219344 CRC64;
MPESHRPDQP RKRLVVVGSG MATTRLIEEL VARNATATPD GWDITVLGDE PVAPYNRILL
SAVLEGTHRP EALTLRSPGW YADNGVDLRL GARVLGVDRD HRDVMLVDGT LIEYDALVLA
TGSIPTLPPI RGLVRMDGSL HPSVHAFRSL SDCEGLVEAI EAIDDQGPIN KRAVVVGGGL
LGLQVARALG ARGLDTEIVE GGEHLLHQQI NTSAGKILAR DLKKLGVSVY TGARAVRLQS
PDEPATPGLS GIGSVRVLDP LPRNPGKVAL RLDNGFNLDT DLLVLTAGGR PSTALARGCG
LEVRRGIVVD DQLASVTDPA IHALGDCVEH DGRTTGFVPP AWEQAGILAG ILCNEAVKYD
GSRIVARLRA TDLDVAVLGD AEREITAGGE VVEVSNPISG SHRRLVVRDG RIVAATLVGD
LSRVGLITQH FDRQTVLGAH EPGNLLMPER SGEEGSAALT LPDDAEVCAC AGVSAGRIRA
CSSFEQARDT TRATTGCGGC APTVRQLLGS RPALATSQKG S
//
