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
//