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Database: UniProt
Entry: A0A0Q7FND6_9FLAO
LinkDB: A0A0Q7FND6_9FLAO
Original site: A0A0Q7FND6_9FLAO 
ID   A0A0Q7FND6_9FLAO        Unreviewed;      1172 AA.
AC   A0A0Q7FND6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=NAD(P)H-nitrite reductase {ECO:0000313|EMBL:KQW98912.1};
GN   ORFNames=ASC72_12330 {ECO:0000313|EMBL:KQW98912.1};
OS   Flavobacterium sp. Root420.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736533 {ECO:0000313|EMBL:KQW98912.1, ECO:0000313|Proteomes:UP000051729};
RN   [1] {ECO:0000313|EMBL:KQW98912.1, ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|EMBL:KQW98912.1,
RC   ECO:0000313|Proteomes:UP000051729};
RX   PubMed=26633631; DOI=.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root420 {ECO:0000313|Proteomes:UP000051729};
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=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008747}.
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:KQW98912.1}.
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DR   EMBL; LMEF01000030; KQW98912.1; -; Genomic_DNA.
DR   RefSeq; WP_056194059.1; NZ_LMEF01000030.1.
DR   AlphaFoldDB; A0A0Q7FND6; -.
DR   STRING; 1736533.ASC72_12330; -.
DR   OrthoDB; 9792592at2; -.
DR   Proteomes; UP000051729; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR   CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR041957; CT_Nitrate-R-NapA-like.
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; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          3..59
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1172 AA;  129856 MW;  08CFC7537FF23FD2 CRC64;
     MQNTKMKTTC SYCGVGCGII VTNDAKNGVM VTGDKDHPVN KGMLCSKGMN LHYVVNDTSD
     RILYPEMRGS KSYPLERVSW DTALDRAAAV FTSIIKKHGP DSVGFYISGQ CLTEEYYLVN
     KLVKGFLKTN NIDTNSRLCM SSAVVGYKKT FGEDSVPIAY DDIELADTFL ITGANPAWCH
     PILFRRIEKH KENNPKIKII VIDPRRTDTA AFADLHLQII PGSDIILYHA IARRIIEKGY
     VDHDFVKNNA ENFKQYKDLV LGTSLEKASK LCGISVNDIK LAADIIGKAK GFISLWAMGL
     NQSAVGVDKN TALLNLSLLT GQIGKPGSGP FSLTGQPNAM GGREVGGMAT LLAAHKDIAN
     PEHRKEVADF WGVDEISDKP GLTATEMFEA LESGKMKAVW IICTNPMVSL PDSRRIEKAL
     QKAKFVVVQD ISHNADTSKY ADLLLPAAGW LEKEGTMTNS ERRISYLPKG INAPGEALPD
     IEILIRFAKK MNFNGFNFNS AEEVYKEHCA LTKNTNIDIS FLNYHRLRTE GTFQWPVPDY
     GHPGTPRLFT DKKFYTPSKK AIFNLPTAIE NTSEQPSPQF PFILTTGRVR DQWHTMTKTG
     KVSRLMTHTP SPVLEINPID AYKNDIKNGD IVIVSSKNGE VRVKAKVTDS IREKVVFLPM
     HWGKQLDNDL NRTNNLTNTV VDPVSKEPDF KYTTVAITKY VKPFQKIAIV GAGAAAFRFI
     QNYREFNSTD EIIVFSNEVN PFYNRVLLPE YMTGEFTWQQ LLKVKDGEAL SKLKITMKAG
     VAIDKINATA KTITDSLGET HTFDSLILAT GSRPFIPENA QLHLPGRFTV RRKEDADRLK
     AYLDNTGLPP EEQHVVIIGG GLLGLELAAA LKHKKVKITI IQRASRLMER QLDLISSKLL
     AEEVQLRDIQ IYFDNEVSTV FETENPNELE IALKSGRIIT ANTIVYTIGT IPNIEIARET
     GLACGRGVKV NQYLQSSNPD IYAIGEIAEF DNKLFGITSA AEEQADILAN YLAGDISSYY
     KGSVLMNILK LEDINLCSIG DIEIPENDDS YEEIVFADLK QRYYKKCIVK NDLLVGAILM
     GDKNEFAEFK TMIESKIELS DKRNSLLRGS SNAKPVLGKL VCSCSQVGAG NIEETIKGGV
     NNFTDLCKNT GAGLGCGSCK TEVKEILAKC KV
//
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