ID A0A1H1KV56_9FLAO Unreviewed; 1173 AA.
AC A0A1H1KV56;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Ferredoxin-nitrate reductase {ECO:0000313|EMBL:SDR65872.1};
GN ORFNames=SAMN05216503_0098 {ECO:0000313|EMBL:SDR65872.1};
OS Polaribacter sp. KT25b.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1855336 {ECO:0000313|EMBL:SDR65872.1, ECO:0000313|Proteomes:UP000199117};
RN [1] {ECO:0000313|Proteomes:UP000199117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT25b {ECO:0000313|Proteomes:UP000199117};
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; LT629752; SDR65872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1KV56; -.
DR STRING; 1855336.SAMN05216503_0098; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000199117; Chromosome i.
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:UP000199117}.
FT DOMAIN 3..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1173 AA; 130904 MW; 1B9FD53069180A37 CRC64;
MIKNEVKTTC SYCGVGCGII VKKDINNKVF VEGDKDHPVN KGMLCSKGMN LHYVANDVSD
RILYPEMRWS RSHPRERVSW DTALDRAANV FKSIIKKHGP DSVAFYVSGQ SLTEEYYIAN
KLTKGFLGTN NIDTNSRLCM SSAVVGYKKT FGEDSVPVSY EDIELADCFL ITGANPAWCH
PILFRRIEKR KEENPNVKII VIDPRRTDSA NFADLHLQLT PGTDVVLYNA IARRLYKRGL
IDEDFIKKHT QGFEDYRKII LDTNLKKASK ICGVSEDDIE KAAEIIGLSK GFISMWAMGL
NQSVIGTDKN TSLLNLSLIT GQVGKPGSGP FSLTGQPNAM GGREVGGMAN LLAVHKDLGN
EEHRREVAQF WGVEKISPKP GLTATEMFDA LERGKLKAVW IACTNPLVSM PNSHQIEKAM
ANSKFVVVQE ISHKSDTVKY ADLVLPAAAW LEKEGTMTNS ERRISYLPKE IDAPGEARPD
VEIFCDFAQR MGFRGFNYNS TAEIYDEYAS MTKGTNIDVS FLNYDRLKNE GTFQWPVNEY
RHSGTPRLFE DKKFYTSSQK AIFNVPSTIE NTSVKTNQDY PLILTTGRIR DQWHTMTKTG
KVSRLKTHYP KPVLEINPVD AYLNGIKDGD VTEIKSANGV VRVRAKITDA IKEGVVFLPM
HWGKVLKSNL NRANNLTNTH IDPVSKEPDF KFTSVSVSKY KKAKEKIIVA GAGAAAFRFL
QNYRDYNQVD EIHVFSKESN LFYNRVLLPE YITEELTWQQ LLKIKNAELS NLDIHIHPET
LIDKIDKETK IVTDSNGETH TFDKLILATG SRAFIPKDVQ IDLPGRFTMR NKSDADEFKK
YLENTGLPPE EQHVVIVGGG LLGLELAAAM KHKNVKITIV QRASRLMERQ LDKISSKLLS
LDVQERGIQI YFDNEVSTVF DDDETGELTI NLKSGKYITA NAIVYAIGTR PNIEIAKNNG
IVCGRGVKVN QHLQSSHPDI FAIGEIAEFN NQLFGITSAA EEQAGILANF IAGDISESYK
GSVLMNILKF NDLNLCSIGE IKVPENDNSY EEIIFTDMSK RYYKKCIVKD DLLIGAVLMG
DKNEFAEFKT MIESKIEMSD KRDTLLRGSS NDVPMLGELV CSCSQVGAGN IEEAIAGGCT
NFTELCNKTG AGLGCGSCKT EVREILNNAK VKV
//
