ID A0A1I1BQ20_9BACT Unreviewed; 1174 AA.
AC A0A1I1BQ20;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Ferredoxin-nitrate reductase {ECO:0000313|EMBL:SFB51756.1};
GN ORFNames=SAMN04489723_115102 {ECO:0000313|EMBL:SFB51756.1};
OS Algoriphagus aquimarinus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=237018 {ECO:0000313|EMBL:SFB51756.1, ECO:0000313|Proteomes:UP000198790};
RN [1] {ECO:0000313|EMBL:SFB51756.1, ECO:0000313|Proteomes:UP000198790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23399 {ECO:0000313|EMBL:SFB51756.1,
RC ECO:0000313|Proteomes:UP000198790};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOKK01000015; SFB51756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1BQ20; -.
DR STRING; 237018.SAMN04489723_115102; -.
DR Proteomes; UP000198790; 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:UP000198790}.
FT DOMAIN 4..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1174 AA; 131110 MW; FF09768B7FBFE440 CRC64;
MIPDKKVKTT CSYCGVGCGI VAEVDSQNKV HVEGDQDHPV NQGMLCSKGR NLHYVVNDTS
DRILYPEMRW SRSHPRERVS WDDGLDRAAG VFKSLIQKYG PNSVGFYISG QCLTEEYYIA
NKLTKGFLGT NNIDTNSRLC MSSAVVAYKK TFGEDSVPIS YEDIELADAF LIAGANPAWC
HPILFRRLEK HKEKNPNVKI IVVDPRKTDS ATFADIHLQI IPGTDIILYN AIGRRIIDIG
LADKEFIANH TENYLSYRKQ VMATSLKEAS SLCGISIDDI KKVAEIIGES KGFISMWAMG
LNQSAIGTDK NFSLLNLSLV TGRIGKPGNG PFSLTGQPNA MGGREVGGMA SLLAVHKDLN
NPVHRQEVAN FWGVNEISPE PGLSATEMFD ALESGEMKAV WIICTNPMVS LPNSKKIEKA
MKNAKFVVVQ DISHKADTVA YADLVLPAAG WLEKEGTMTN SERRISYLNK GINPPGEARP
DVEILCDFAR RMGFRGFNFN NTEEIYEEYC AMTKGTNIDI SYLNYDRLKN EGTFQWPVPE
YRHTGTPRLF ADNKFYTPTQ KAVFNIPAQI TNTSEKTSKE YPLILTTGRV RDQWHTMTKT
GKVSRLRTHY PSPVLEINPI DAYLDKVKDG DVVEVKSKNG VVRVKAKLSK NIREGVVFLP
MHWGKQLQSD LNRANNLTNT VVDPQSKEPD FKFTTVSVSK YKKATEKIVV VGAGAAAFRF
IQNYREHNES DQIHVFSKEP HPFYNRVLLP EYVTEELTWE QLQKIKEHEL KKLKISLHTG
LSIEHIDPEK QVVVDNDGQE YPFDKLILAT GSRPFIPKDA QLDLPGRFTM RNKIDADRFK
DYLDSTNLRP ENQHVVIIGG GLLGLELAAA LQHNRVKVTI VQRASRLMER QLDEVSSKLL
SLDVQERGIH VYFDNEVSTV FDDEEHKSLS ITLKSGKIIY ANAVVYAIGT QPNIKIARDN
GILCGRGIKV NQHLQTNYPN IFAIGEIAEF QNQLFGITSA AEEQAMVLAN YIAGDVSSIY
SGSVLMNILK FKDLELCSIG DILIPENDDS YEEIIFTDIS RRYYKKCIVK DDLLIGAVLM
GDKNEFAEFK SLIENKIELS EKRKSLLMGS SETRPVIGKL VCSCSRVGEG NIKEAIAGGC
SDFTALCQQT GAGLGCGSCK TEVREILHQS KVLA
//
