ID B1W4P5_STRGG Unreviewed; 1419 AA.
AC B1W4P5;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Putative assimilatory nitrate reductase large subunit {ECO:0000313|EMBL:BAG23062.1};
GN OrderedLocusNames=SGR_6233 {ECO:0000313|EMBL:BAG23062.1};
OS Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG23062.1, ECO:0000313|Proteomes:UP000001685};
RN [1] {ECO:0000313|EMBL:BAG23062.1, ECO:0000313|Proteomes:UP000001685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX PubMed=18375553; DOI=10.1128/JB.00204-08;
RA Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA Yamashita A., Hattori M., Horinouchi S.;
RT "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT griseus IFO 13350.";
RL J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG23062.1; -; Genomic_DNA.
DR RefSeq; WP_012381807.1; NC_010572.1.
DR GeneID; 6212033; -.
DR KEGG; sgr:SGR_6233; -.
DR PATRIC; fig|455632.4.peg.6392; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_000422_6_2_11; -.
DR Proteomes; UP000001685; 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 Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 13..74
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 880..1018
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1049..1268
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 736..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1419 AA; 151772 MW; 9B68CE26E061BAE9 CRC64;
MTVPTPPPDA PATDRVRTVC SYCGVGCGIV LDTAAGPDGR RTVVKASGDR AHPSNAGRLC
TKGATGADLL AAPGRLTTAL ARTDRGERPV PLARDAAIAE TARRLRSVLD AHGPDAVALY
VSGQMTLEAQ YLANKLAKGF LRTNTVESNS RLCMASAGSG YKLSLGADGP PGSYDDFAHA
DVFLVTGANM ADCHPILFLR MMERVKAGAK LIVVDPRRNA TAAKADLYLR IRPGTDLALL
NGLLHLLVEN GHTDPAFIAE HTEGWERMPA FLRDYPPAAV AEITGIPEDD IRQAARWIGE
AGEWMSCWTM GLNQSTHGTW NTNAIVNLHL ATGAICRPGS GPFSLTGQPN AMGGREMGYL
GPGLPGQRSV LVDEDRAFTE ELWGVPPGTL RADGSGSGTV DMFRRMAKGE IKACWIICTN
PVASVANRRT VIEGLEAAEF VVTQDVFADT ETNAYADVVL PAALWAESEG VMINSERTLT
LSRRATDPPG EAWPDWRIIA EVARAMGYED AFGYTSAEEV FAEITRAWNP RTGYDLRGVT
YGRLRETPVQ WPSADVEGPA RNPVRYLNDG VSQELTVRPD GSVPRIAFPL PGGRAVFHAR
PHLPPAETPD EDFPFVLNTG RLQHQWHTLT KTARIAKLNR LDPAPFVEIH PDDAAALGIG
EDDGVEVASR RGRAVLPARI TDRVGAGECF APFHWNDLFG EYLGVNAVTN DAVDPVSFQP
EFKVCAVRLT KVAVSAPRHP PADARRPSPA GGPGRGDAPD PAGASGPGET PGPVVLPGFL
GASDRPVDTS GLVGVLGPAD TAPPVLTDPE RRYLAGFLAG LGARPEGTPV LPAGAPFAPD
HALWVNGVLA GTYSRLAGTP DPGAAPAPSA GGPEQPGRPV VVLWASQTGN AEEAAATAAR
TLAAEGYRTT LLGMDDGTPD ALPSPADLLV VTSTFGDGDA PDNGSGFWEA LNAPRTPGLE
GLRYAVLALG DSSYDDFCGH GRRLDERLGE LGAERLLPRT DCEPEYEQPF GQWLKEVRAA
LEGTAAATPS AVTATAAPAG PAPDRPSRAA PVTALLTGNR LLSLPGATKE VRAFTIDTRS
ADTPLTYTAG DALGVQPLNS PELVAEWLAV TGLDPAAEVD VPGHGPLALG EALRRHLDIA
RITPDLLRLV ANRTGDRSLR KLLRPDNKGE RDRWAWGRQA VDVLAEHPVR ATAAAWAEVL
GPLRPRLYSI ASSPLVDPHR MRLTVSVIRY ESRRGRMRKG VASAFLADAP PDSPLPVFVQ
RNERFRPPAD PATPMIMVGP GTGVAPFLGF LEERRALGHP GRNWLFFGEQ HRATDFYHRD
EFDALSRSGT LTRLDTAFSR DQRSKVYIQD RMREHGAQLW SWLRDGAHLY VCGDASRMAK
DVDRALRDIA VAHGGLDPDT AAAQVKQLAS DRRYVRDVY
//
