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Database: UniProt
Entry: A0A2I9DTY7_9FLAO
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Original site: A0A2I9DTY7_9FLAO 
ID   A0A2I9DTY7_9FLAO        Unreviewed;      1177 AA.
AC   A0A2I9DTY7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Nitrate reductase {ECO:0000313|EMBL:GBF19044.1};
GN   Name=narB {ECO:0000313|EMBL:GBF19044.1};
GN   ORFNames=C21_01209 {ECO:0000313|EMBL:GBF19044.1};
OS   Arenibacter sp. NBRC 103722.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Arenibacter.
OX   NCBI_TaxID=1113929 {ECO:0000313|EMBL:GBF19044.1, ECO:0000313|Proteomes:UP000095208};
RN   [1] {ECO:0000313|EMBL:GBF19044.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-21 {ECO:0000313|EMBL:GBF19044.1};
RA   Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H., Amachi S.;
RT   "Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-
RT   Accumulating Bacterium Isolated from Surface Marine Sediment.";
RL   Genome Announc. 4:e01155-16(2016).
RN   [2] {ECO:0000313|EMBL:GBF19044.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C-21 {ECO:0000313|EMBL:GBF19044.1};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) 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:GBF19044.1}.
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DR   EMBL; BDGL02000004; GBF19044.1; -; Genomic_DNA.
DR   RefSeq; WP_031443931.1; NZ_BDGL02000004.1.
DR   AlphaFoldDB; A0A2I9DTY7; -.
DR   Proteomes; UP000095208; 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; cd19942; Fer2_BFD-like; 1.
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; 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095208}.
FT   DOMAIN          4..60
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1177 AA;  131889 MW;  21A0654322A0C244 CRC64;
     MQKKNEHKTI CSYCGVGCGI VVEQDSKGNI SVEGDQDYPV NKGMLCSKGK NLNYVAQDVS
     DRILYPEMRW SRNHPLQRVS WDTAFDRAAA VFKSIIEKHG PDSVGFYVSG QCLTEEYYLV
     NKLTKGFIGT NNIDTNSRLC MSSAVVGYKK MLGEDSVPIS YEDIELSDCF LIAGANPAWC
     HPILFRRIEN HKENNPDVKI IVVDPRKTQT CAAADLHLQI LPGTDVILFN AIARWLIEKK
     KIDRNFIKKH TVNFDAVKDS AFQLSMKKAA ELCGIPVEDI KKAAMYIGNA NAFISMWTMG
     LNQSVIGVSK NVALMNLSLL TGQIGKPGAG PFSLTGQPNA MGGREVGGMA SLLAAHRELG
     NPKHRKEVSD FWGGKEIKSE PGYTATEMFD ALENGKMKAV WIICTNPIVS LPNVHKAEKA
     LKNANFVVVQ DISHNSETTK FADLLLPAAG WLEKEGTMTN SERRISYLPK VIDAPGEALP
     DAEILWKFAQ KMGYHGFDYK NASEVYDEHC LLTKGTEIDI SGLSYDRLKN EGSFQWPVPH
     DKHMGTPRLF TDYQFFTNDR KSHFNAPYSL YNKSELTTPE YPLILNTGRI RDQWHTRTKT
     GKVKRLLTHI PDPYLEMNKV DAYLRKLKDG DIAVIKSRRG TVRVKVKVNF DIREKVVFLP
     MHWGKVLNND FGRANNLTND LVDPVSKEPD FKYCAVEVAK YVKPKQKILI IGAGAAAYRF
     IQTYREKNET DELHVFSKEK DPFYNRVLLP EYVSEELSWE ALEKLKKGEL EKLDITLHSG
     LGVTQIDRKN KTVMDDDGFE HAYDILVMAT GSRAFVPSEV QINMPGRFTM RERGDADKLR
     KYLEDTGLPS EEQHVVIVGG GLLGLELAAA LKNRNVNISI IQRAPRLMER QLDRIASRLL
     AEDVSDRGIK VYFDNEVSTV FEERDDKNSL SITLKTGRTI KCNAIVYAIG TRPNIELAKH
     SDLKTGRGVV VNEYLQTSDP NIFALGEIAE FRNALFGITS AAEQQADTAA KYILGDFSSI
     YNGSILMNIL KFENLDLCSL GMVNAPLDDN SYEEIILMDV SKKYYKKCIV KDDTLKGAIL
     MGDKNEFAEF KRLIEEEIEL SEKRNELLRG QKNSVPLKGK LVCSCSQVGE GNLIETINTG
     CEDFSKLCSE TGAGLGCGSC KPEIQDILRK QLQTVTS
//
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