ID D7C8H3_STRBB Unreviewed; 1380 AA.
AC D7C8H3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Assimilatory nitrate reductase large subunit {ECO:0000313|EMBL:ADI06362.1};
GN OrderedLocusNames=SBI_03241 {ECO:0000313|EMBL:ADI06362.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI06362.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI06362.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI06362.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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; CP002047; ADI06362.1; -; Genomic_DNA.
DR RefSeq; WP_014175839.1; NC_016582.1.
DR STRING; 749414.SBI_03241; -.
DR KEGG; sbh:SBI_03241; -.
DR PATRIC; fig|749414.3.peg.3359; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_000422_6_2_11; -.
DR Proteomes; UP000000377; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN 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 CDD; cd06199; SiR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.360; -; 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 Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
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; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 11..72
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 845..983
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1009..1229
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 738..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1380 AA; 147911 MW; 6914EC9DBC447549 CRC64;
MVAPDAWAEG TTKVRTVCSY CGVGCGMVLD VGRGPDGRRT VLKAAGDKEH PANFGRLCTK
GATTADMLVA PGRLTTALVR PDRGEEPQPA PVAAAIAETA RRLRAIVDEH GPDAVALYVS
GQMSLEAQYL ANKLAKGFLR TNQIESNSRL CMASAGTGYK LSLGADGPPG SYQDFDKADV
FFVIGANMAD CHPILFLRMM DRVKSAGAKL IVVDPRRTAT AAKADLFLQI RPGTDLALLN
GLLHLLHADG HTDPEFIAAH TEGWEAMPAF LADYPPAAVA EITGIPEDDI REAARLIGEA
GEWTSCWTMG LNQSTHGTWN TNALVNLHLA TGAICRPGSG PFSLTGQPNA MGGREMGYMG
PGLPGQRSVL VDADRAFVEE LWELEPGALR ADGVGKGTVE MFQKMAEGDI KACWIICTNP
VASVANRKTV IEGLEAAEFV VTQDVFAETE TNAYADVVLP GALWTETEGV LINSERNLTL
ARPAADPPGE AMADWRIIAA VARAMGYEKG FAYDSAEEVF EEIKRAWNPA TGWDLRGVSY
ERLRTTPVQW PAATADGPDR NPIRYVGEDG SPTFPTPSGR AVFYARPHLP AVEMPDDDYP
YVLNTGRLQH QWHTLTKTAK VPKLNKLNPG PFVEVHPRDA ARLGIAEGDS VEVASRRGRA
VLPAVVTDRV RPGCCFAPFH WNDLFGEYLS VNAVTSDAVD PLSFQPELKV CAVSLTKVAT
PVTVRAPAPV GVPAPAPAGV PASAPASGSA PSGPAPFGLE PAPPPVLAEH ERRYLTGFLT
GIPSGAPGVP VLPPDAPFSP EHALWVNGVL AGMYSRAEET GSTAYGAGGS PQSSSLAADA
PHRQVVILWA SQTGNAEEFA TAAAQRLSAH GHPASLLPME GADPAALPSD ADLLLITSTF
GDGDAPDNGA GFWAALASSD APRLKGRRYA VLAFGDSSYD DFCGHGRRLD QRMEELDAVR
LAPRTDCEPD YETEAGAWLD QVLTALKSTE QPAPAPAPAA PAAPRPSRPA PVTARLIGNR
LLSLPGAGKE VRRFTFDTRD DDTPLAYEAG DALAVHPVNW PELVTEWLAV TGLDADAAVQ
ITSVGEVSFA EALLRHLDIT RVTPGLLRFA AARARDPREL RKLLRPDNKG ELARWSWGRQ
AVDLAAECGI RAGAQAWADV LGRLQPRLYS ISSSPLTDPH LVSLTVSVVR YENPDGRPRQ
GVCSPFLADA GPGTPVPVRV QRSPHFRPPA DPATPAVMVG PGTGIAPFIG FLEERRARGH
RAPNWLFFGE QHSATDFYYE EELAAFLAES TLTRLDTAFS RDQRAKLYVQ DRMREHGPQL
WSWLLDGAHF YVCGDASRMA KDVDRALREI ATVHGGLDEA EAEAYVKQLA ADKRYVRDVY
//
