ID A0A2S6IM86_9ACTN Unreviewed; 1418 AA.
AC A0A2S6IM86;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=NADPH-dependent sulfite reductase flavoprotein alpha-component {ECO:0000313|EMBL:PPK95357.1};
GN ORFNames=CLV92_106178 {ECO:0000313|EMBL:PPK95357.1};
OS Kineococcus xinjiangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=512762 {ECO:0000313|EMBL:PPK95357.1, ECO:0000313|Proteomes:UP000239485};
RN [1] {ECO:0000313|EMBL:PPK95357.1, ECO:0000313|Proteomes:UP000239485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22857 {ECO:0000313|EMBL:PPK95357.1,
RC ECO:0000313|Proteomes:UP000239485};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-2018) 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=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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PPK95357.1}.
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DR EMBL; PTJD01000006; PPK95357.1; -; Genomic_DNA.
DR Proteomes; UP000239485; Unassembled WGS sequence.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
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; PS00551; MOLYBDOPTERIN_PROK_1; 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:UP000239485};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 6..67
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 865..1002
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1048..1267
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 830..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1040
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 149280 MW; 941B59AE693ABB6E CRC64;
MGGGCTERVR TVCSYCGVGC GIVLDVRVEA DGRRVPLKAT GDRQHPANAG RLCTKGATSA
EVLTAPGRLG TALVRARRGA EAVPTAVGEA IALTARRLRE VLDEHGPDAL ALYVSGQMSL
EAQYLANKLA KGFWRTNQIE SNSRLCMASA GAGYKLSLGA DGPPGSYDDL DAADVFLVIG
SNMADCHPIL FLRMMDRVKA GAKLIVVDPR RTATAEKADL FLQIAPGTDL ALLNGLLHLL
VAGGHVDEEF IAACTQGWEE MAEFLADYSP AEVARTTGLA EADVRAAAEL IGTAGNWVSC
WTMGLNQSTH GTWNTNALVN LHLATGAICR TGSGPFSLTG QPNAMGGREM GYMGPGLPGQ
RSVLVAEDRA FTEELWGLPA GTIRADGSGR GTVEMFQRMA DGEIRACWVI CTNPVASVGN
RDTVVEALRR ADFVVTQDVF AATETNAHAD VVLPAAMWSE ADAVMVNSER NLTLAPRAVD
PPGEALPDWL LIARVAREMG YGEAFSHGSA EEVFEELKQA WNPATGWDLR GVSHERLRGG
SVQWPAADPA GPVRNPVRYV DGGAGGVAGQ PPDGARPRPV FPTPNGRAVF WPRPHIDPAE
MPDDQFPFVL NTGRVQHQWH TRTKTGTVAK LERLNPGPFL EVNPADAQAL GVGDGDAVEV
VSRRGRAVLP AVVSDRVLPG CCFAPFHWGE LFAAGVSVNA VTSDAVDPVS FQPELKVCAV
SLARVAAVST AAPPVAVSAG AVPAPRGAAE PAGALGGLLG LAGPAPVFDE AERRYLAGFL
AGLSGALPGA PEGSGGRGGV PVLPSGAPLR PEVALWVDGL LAGAFSRATA APGLPRPRPA
PDESAPGGAP VAGAAQDAPR VGRPLLVLWA SQTGTAEETA AAVAERLQRE GLAPQLVAMD
DCAPAQLPAA ADLLVLSSTF GDGDAPDNGA AFWESLSAPG APRLAGSRFA VLAFGDSSYG
DFCGHGRRLD ERLADLGAAR LLPRADSEPG DETPQRWLEA VLAALAGEPP APASPSSQQQ
PTPAPTPSAP TPPDAPPTAH PAPRSGRSAT GTAHLVGNRL LSLPGAAKEV RELVLDTGGS
EVPLDYEAGD ALGVLPCNDP GLVAELLEVT GLDPGEVVDV AGAGGVPFGE ALQHHLEVCR
LGPDLLRFVA ERTGSRDLKG LLRPDNRGEL AKWSWGRQVV DVLAEHRPEV SAKELTGILK
PLQPRQYSIS SSPLADPHRV RLTVSVLRYT APTGRPRTGV ASAHLADAPA GSPVRVFVQR
SPHFRPPADP SAPVVMVGPG TGIAPFLGFL QERRARGHLG RNWLFFGEQH RASDFYYRDE
LDELFREGTL TRLDTAFSRD QRAKVYVQDR MREQGRQLWA WLREGAHVYV CGDAARMAKD
VDAALRWVAA VHGGLGEDAG AAFVKRLAKE RRYVRDVY
//
