ID   A0A1D7YFV2_9ACTN        Unreviewed;       697 AA.
AC   A0A1D7YFV2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Nitrite reductase {ECO:0000313|EMBL:AOR34495.1};
GN   ORFNames=BFF78_28665 {ECO:0000313|EMBL:AOR34495.1};
OS   Streptomyces fodineus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR34495.1, ECO:0000313|Proteomes:UP000094960};
RN   [1] {ECO:0000313|Proteomes:UP000094960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA   Kim M.-K., Kim S.B.;
RT   "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CP017248; AOR34495.1; -; Genomic_DNA.
DR   RefSeq; WP_069781044.1; NZ_CP017248.1.
DR   AlphaFoldDB; A0A1D7YFV2; -.
DR   KEGG; spun:BFF78_28665; -.
DR   Proteomes; UP000094960; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:InterPro.
DR   CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE   4: Predicted;
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}.
FT   DOMAIN          4..60
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   697 AA;  74672 MW;  42585AAC527AB525 CRC64;
     MEPIASTPTH CPYCALQCGM NIMPLPQGGV EVTERTDFPV NRGALCGKGR TAAEVLSPAV
     RLTSPLVRSG GRLVEAGWDE ALDRIAERLG SIRREYGADA LGVFGGGGLT NEKAYALGKF
     ARVVLGTSQI DYNGRFCMSS AAAAGTKAFG LDRGLPFPLE DIPKTGCVIL VGSNPAETMP
     PSLRYFTELR ENGGTLIVVD PRRTRTAEQA DLHLAPRPGT DLALALGLLH LVVAEGRTDE
     EYIRERTTGW EEARAAAMAY WPEYVERITG VSVPRLREAV RLFCAPESAM VLTARGPEQQ
     SKGTDTVGAW INLCLATGRA GRPLSGYGCL TGQGNGQGGR EHGQKADQLP GYRKLDDPAA
     RAHVAGVWGV DPDALPGPGR SAYELLDALG TDIRALLLMG SNPVVSAPRA AHIEERIKSL
     DFLAVCDVVL SETAELADVV LPVTQWAEES GTTTSLEGRV LLRRRAIAPP PGVHSDLHVL
     HELSARLGVE KGFPADPEEV FTELRRASAG GPADYSGITY RRLAEETGVF WPCPENPGEA
     NHPGTPRLFL DRFAHADGRA RFVAVTHRPT AEEPDAEYPL LLTTGRVVAQ YQSGAQTRRV
     TELNAAAPGP FVELHPRLAA RIGAAEGDPV TVTSRRGRAT APARITSAIR PDTVFMPFHW
     PGEGRANTLT NPALDPTSRM PEFKSCAVRV EVVGSRA
//