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Database: UniProt
Entry: A0A2T0U4P4_9SPHI
LinkDB: A0A2T0U4P4_9SPHI
Original site: A0A2T0U4P4_9SPHI 
ID   A0A2T0U4P4_9SPHI        Unreviewed;      1170 AA.
AC   A0A2T0U4P4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Ferredoxin-nitrate reductase {ECO:0000313|EMBL:PRY52808.1};
GN   ORFNames=B0I27_105277 {ECO:0000313|EMBL:PRY52808.1};
OS   Arcticibacter pallidicorallinus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=1259464 {ECO:0000313|EMBL:PRY52808.1, ECO:0000313|Proteomes:UP000238034};
RN   [1] {ECO:0000313|EMBL:PRY52808.1, ECO:0000313|Proteomes:UP000238034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9313 {ECO:0000313|EMBL:PRY52808.1,
RC   ECO:0000313|Proteomes:UP000238034};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-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:PRY52808.1}.
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DR   EMBL; PVTH01000005; PRY52808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0U4P4; -.
DR   Proteomes; UP000238034; 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; 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:UP000238034}.
FT   DOMAIN          7..63
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1170 AA;  129837 MW;  A7719524723DFF20 CRC64;
     MMQSERGKSF TSTCCYCGVG CGVKVRVEGN NTVSVEGDKE HPVNKGMLCS KGMNLQYTVN
     DKSDRLLHPQ MRYNKNMPLQ RVSWDAALTR TAAVFSTLIE KYGPDSVAFY ASGQCLTEEY
     YVINKLIKGF IGSNNIDTNS RLCMSSAVTA YKMALGEDSV PICYDDIELS DCLFVTGANP
     AWCHPILWRR IEAHKAANPH IKIIIVDPRA TDSCSIADLH LQINPGTDVT LNYAIGRVLI
     ESDNIDMDFI RQHSEGFDRY RELVFEKTLA ESAAICGVAE SDILLTATYI ASAKGFLTMW
     TMGLNQSAIG VNKNLSLINL NLITGHIGKP GSGPFSLTGQ PNAMGGREVG GLANLLPAHR
     DLNNGGHRAE VQKFWGGTAI SDKAGLTATE MFEALHDGRL KAIWIICTNP LTSLPNARFV
     EQALKKAKYV VVQDISDQTE SLAYADVILP AAAWTEKEGT MTNSERRISH LQKLVDPPGE
     ALPDAEIICR FASKMGFKGF DYACMEDIYK EHTRLTKQTN LNIDGLSYSL IDEHKTIQWP
     FNKKSNTGTA RLFGNKLFYT PSRKAIIHSP PDHLSSEMPD TEYPLILTTG RVRDHWHTMT
     KTGKVSKLKQ HTKDAYLEIH PADALELGIE NGQVSVVRSR RGEVQVKARI STAMKRGVVF
     LPMHWGKILG NDLNRTNNIT STLIDPISKE PDFKYCAVRV EKWSKAPQRI VIIGAGAGAF
     GFVKSHRQIN KNDHITVFSK EDSPFYNRVM LPDYISGEQR WEQLVKMTDE EEPEYNIRLL
     RGVSVEYINR EAKYVTDSRG NKTPYDVLIM ATGSRATLPR HVPSLPGIFS MRNRTDADSF
     KKYLPAKAHV VIVGGGLLGL EMAASLREIG VDITIVQRVS RFLNRQLDPL GSQLLHEEIT
     EQGCDIFYND EVQVYYGRSK LTGIGLKSGR KINCDAMIIA IGTTPNIELA RSCGLNCKRG
     VIVNERLQTS DPDIFAIGEI AEFKGILYGI TAAAEQQAEV VSGYLNGDIG SFYKGSIFMN
     IIKIHGFDLC SIGMPECPDD PQYEEIVFID KAKRYYKKCI VHQDRLVGTI LIGDKSEFQE
     FRELIANQTE LSEKRLTLLR SGKTSERVLG KLICSCNNVG SGNITKQMDA GCIDFGELCS
     LTGAGMGCGS CRPEVKRILE QLRTEETMAS
//
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