ID A0A1H2YJZ9_9FLAO Unreviewed; 1177 AA.
AC A0A1H2YJZ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Ferredoxin-nitrate reductase {ECO:0000313|EMBL:SDX05582.1};
GN ORFNames=SAMN04487892_3085 {ECO:0000313|EMBL:SDX05582.1};
OS Allomuricauda zhangzhouensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=1073328 {ECO:0000313|EMBL:SDX05582.1, ECO:0000313|Proteomes:UP000199592};
RN [1] {ECO:0000313|Proteomes:UP000199592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25030 {ECO:0000313|Proteomes:UP000199592};
RA Varghese N., Submissions S.;
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; FNMY01000006; SDX05582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2YJZ9; -.
DR STRING; 1073328.SAMN05216294_3180; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000199592; 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}.
FT DOMAIN 4..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1177 AA; 130950 MW; 6EB27812F439CF5F CRC64;
MQKKDTFDSI CSYCGVGCGI TVKKDAKGVL SVTGNELYPV NKGMLCTKGK TLNYVAQDTS
DRILYPEMRW SRNHPMQRVT WDIAFKRAAA VFKSIIEKHG PNSVGFYVSG QCLTEEYYLA
NKLTKGFLGT NNIDTNSRLC MSSAVVGYKK TVGNDAVPIS YADIELADCF LIAGANPAWC
HPILFRRIEK HKEENPNVKI IVVDPRKTQS CALADLHLQI LPGTDVILFN AMARWLIEKK
KIDKSFIQKH TSNFEAVKQT AFELTIRQAA EKCGISADEI RLAAKMISDA KGFISMWTMG
LNQSVIGVDK NVSLLNLSLL TGQIGKPGSG PFSLTGQPNA MGGREVGGMA SLLAAHRDLG
NPKHRKEVQE FWGSTEIHGE PGYTATEMFD ALESGKMKAV WIVCTNPIVS MPNAKQIEKA
LEKANFVIVQ DISHNSETTK YADLLLPAAG WLEKEGTMTN SERRISYLPK VIDAPGEALP
DVEILWRFAQ EMGFHGFDYT NASQVYDEYC LMTKGTTIDI SGLSYERLKT EGSFQWPVPS
PDHKGTPRLF QDQNYFTSDG KAHFNAPRNL YNKSETTSPE FPLILNTGRV RDQWHTRTKT
GKVKRLTTHI PAPFLEMNKI DAYIRGFKEG DVVTVKSRRG SVRVKLKINY DIREGVVFLP
MHWGKILNND FSRANNLTNN IVDPISKEPD FKYCAVQVEK YRKPFEKIVV VGAGAAAYRF
VQSYREKNWG DTIKVFSKEE HPFYNRVLLP EYVNNDLGWE ALQKLKEGEL EKLKVELFAN
NGIQKIDKEA KQVIDDNGVS HDYDLLILAT GSRAFVPPDV RMDLPGRFTM RERGDADRLK
EYLTKTNLPV NEQHVVIIGG GLLGLELAAA LKKIDINISI IQRSPRLMER QLDPISSRLL
AEDVLERGIQ LYFDNEVSTV FEDKDSPHNL LVNLKTGRTL NCNAIVYAIG TRPNINLAID
AGLKTKRGVL VDPYLKTSDA SIFALGEIAE FDNSLFGITS AAEQQADIAA NYILGDLGST
YSGSVLMNIL KFENLDLCSI GMVNAPQNDS TYEEIILMDV SQRFYKKCIV KDDTLKGAIL
MGDKNEFAEF KRLIEEGVEL SEKRNELLRG ASNREPLKGK MVCTCSQVGD GNLKDAIAGG
CSDFKNLCTQ TGAGLGCGSC KPEVKGILDA QLKTAAV
//
