ID A0A173MGB8_9BACT Unreviewed; 1165 AA.
AC A0A173MGB8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Ferredoxin-nitrate reductase {ECO:0000313|EMBL:SIT27341.1};
GN ORFNames=SAMN05421788_107210 {ECO:0000313|EMBL:SIT27341.1};
OS Filimonas lacunae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Filimonas.
OX NCBI_TaxID=477680 {ECO:0000313|EMBL:SIT27341.1, ECO:0000313|Proteomes:UP000186917};
RN [1] {ECO:0000313|Proteomes:UP000186917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21054 {ECO:0000313|Proteomes:UP000186917};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FTOR01000007; SIT27341.1; -; Genomic_DNA.
DR RefSeq; WP_076380802.1; NZ_FTOR01000007.1.
DR AlphaFoldDB; A0A173MGB8; -.
DR STRING; 477680.SAMN05421788_107210; -.
DR KEGG; fln:FLA_2565; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000186917; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000186917}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1165 AA; 129154 MW; 96ED508C9B50BBFA CRC64;
MPEMYKTTCC YCGVGCGVIV HQQRDGKIWV EGDKEHPVNK GMLCSKGMNL HYTVMDTTDR
LLYPEIRYSK YGPRQRAGWD EALNRVAAVF TAIIQRFGPD AVAFYASGQC LTEEYYVVNK
LIKGFIGSNN IDTNSRLCMS SAVAAYKMSL GEDIVPGCYD DIELTDCIFI AGANPAWCHP
ILWRRIEAAK AANPNLVIIV SDPRVTQTCA LATLHLQVTP GTDIVLHHAI GRLLIEQGCI
DPVFIRDHTE GIEPYRQAVM QRTLAEAALI CGIEEAAITQ AAHYIGNTDK LMTMWTMGLN
QSAIGVHKNL SLINLHLITG TIGKPGCGPF SLTGQPNAMG GREVGGLSNL LPAHRDLLNA
QHREEVQQFW GGTTLSDKPG LTATQMFEAL NSGRLKAIWI MGTNPLVSLP DVRMAEAALN
KATFVVVQEV SNKPETLAYA DVVLPAAAWT EKEGTMTNAE RRISYLPQLT QPPGEALPDA
EIICRFARKM GYAGFDYPCM EDIYKEHARL TAGTHINISS LSYDVIRRHR TIQWPYNGEM
EQPGTRRLFE DHRFYTASGR ARIHAFGDEN QSEPVSPEYP LILTTGRIRD HWHTMSKTGK
VNKLKQHIPS PFLEMHPEDA AERDIEQDAI VEITNRLGNV RVKVKLTESI KKGLVFLPMH
WGKLFNNDSS RANNLTHVLL DPVSKQPDFK FSAVQVTRYY KPVQHIIVVG AGAGAHAFAR
AHRAWNSRDV ITVFSKEDQP FYNRVMLPDY VSGTQQWRQL VKMTDTEEKQ LNIQLHRGVS
IVHVDRAARA VTDSNGKEHS YDVLILATGS SPALLRDTPV MKGIFTMRTR NDADAFKKYV
QPGKGKIVIV GGGLLGIEMA ASLTEMGMEA ILLQRSSKLM DRQLDVLGSR LLQEELADRH
IEVLYNDEIE RFTGTTRLTG IKLKSGRSLD SQAVLLSIGT VPNIELAKAA GLVCKRGVEV
NTYLQTNDEH IYAIGEIAEF KGVLYGITAA AEQQAAVVAA FLNGDISRYY EGSLFMNILK
LHGADICSLG MVEPPDDPAY EEVVFIDKAR RYYKKCVVYN DRLVGAILIG DRTEFLEFKN
LIEQKMELSE KRLQLLRSGK KADPVLGKLI CSCGNVGEGN LCQKIKEGHN DLKALCEATG
AGMGCGSCRS EVQAIITREC ALVTT
//
