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Entry: A0A1N7DMU9_9NOCA
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ID   A0A1N7DMU9_9NOCA        Unreviewed;      1409 AA.
AC   A0A1N7DMU9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Sulfite reductase (NADPH) alpha subunit {ECO:0000313|EMBL:SIR77147.1};
GN   ORFNames=SAMN05445060_0771 {ECO:0000313|EMBL:SIR77147.1};
OS   Williamsia sterculiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Williamsia.
OX   NCBI_TaxID=1344003 {ECO:0000313|EMBL:SIR77147.1, ECO:0000313|Proteomes:UP000186218};
RN   [1] {ECO:0000313|EMBL:SIR77147.1, ECO:0000313|Proteomes:UP000186218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 203464 {ECO:0000313|EMBL:SIR77147.1,
RC   ECO:0000313|Proteomes:UP000186218};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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}.
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DR   EMBL; FTNT01000002; SIR77147.1; -; Genomic_DNA.
DR   STRING; 1344003.SAMN05445060_0771; -.
DR   Proteomes; UP000186218; 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:UP000186218};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          17..78
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   DOMAIN          848..985
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          1045..1258
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          984..1025
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1409 AA;  152229 MW;  1C24C9E84FFB29D0 CRC64;
     MATLVGVVPE AAAPADTRVT RTACSYCGVG CGIEVTTRVE PGRGPVIAKV SGDKLHPTNH
     GRLCTKGATH AELMRADEQR MRSAYLRPAR GRPAQAVAVD TAVGEVATRM RAIIDEHGPN
     AVAVYVSGQM STEAQYLATK LAKGYLRTTH IESNSRLCMA SAGTGYKQSF GSDGPPGSYQ
     DFDKADLFLV IGSNMADCHP ILYLRMVDRL KQGAKLIVVD PRRTTTADRA DLYLPVRPGS
     DLALLNGLLH LLVESGDIDE EFIAAHTEGW EQMPGFLADY PPERVAELTG LSCDDIRTAA
     GMIADAGEWM SCWTMGLNQS THGTWNTNAI NNLHMATGAL CRPGSGPLSL TGQPNAMGGR
     EMGYMGPGLP GQRVVTSEDD RRFCEQRWGL DAGTIRSDVG PGTIEMFSQM ASGDIKACWI
     ICTNPVASVA NRRTVIAGLE AAELVVVQDA YTDTATAEYA DVLLPAALWA ESDQVMINSE
     RNVTLLQQST QPLGEAKPDW QLIAEVATAL GFGEAFAHTS ASEVFDEITE FWNPRTGWDL
     RGVDHDRLRS TPLQWPCPPP GEPGGDDDRH PIRYLNDGVS QTLFTDDDGT VPELAFATPS
     RRAQFLPRPH MDPAELPDDE YPMVLNTGRL QHQWHTMTKT GKVAKLNKLN PSPFVEIHPD
     DAERLGIRDE HEVEIASRRG RAVFPAVITD RVRPGNCFTP FHWNDEHGEY LTVNAVTNDA
     VDPVSLQPEF KACAVSLRPV AARPEPEVTD VDAHPLAAAL GVPQTVPELD EGEKAYVGGF
     LAGVQSRGGQ VSDGTVATVP VLPPSAPVRG VVRMWVDGML AGMYSGAAGA VDDPVVEKGA
     GQGADGSLIV LWASQTGGAE EFAGTVEGAL TAAGYAPRLV EMDGCGLDQL AAASRVVVVT
     STFGDGGPPD DAADFWERLS SATPDLGGVS FAVLGMGDSS YDDFCGFAAK VDDRFAELGA
     RRLTDIVRCE PDETDRADEW LQRLTPLVDG GEGVSSSGDR DRDDAVSPEV APPHPGGGGG
     GSVTVTEPRV QTAGVEAPAS VFTRANPVHA LLVRNTVLTG AGSQKEVRTF GFDLADHDVE
     YEAGDSLGVM PTNSTQHVDA FLVAAGLDGD VAVDGTTSMR EALRTRHDIC RLTPGLLKFV
     AERSGNGQLA TLLRRDNKNE LAKWMWGRHA VDLLRAFPIE ATPTEWTETL GGLQPRQYSI
     SSSPRESPQE VQLTVSVVRY DGDDGTPRGG VCSTFLADRA DDAGVPIFLN RSPHFRPPAD
     PGTPMIMIGP GTGIAPFRGF LHERRALGHR GDNWLFFGDQ HAADNFYYRS ELEDMFRDGF
     LTRLDVAFSR DQRERIYVQD RMVEHGALLW RWLESGAHFY VCGDATRMAR DVDETLLGII
     SHHGRMGEDE AKAYRKELVA TKRYVRDVY
//
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