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Database: UniProt
Entry: M5PDG8_9BACI
LinkDB: M5PDG8_9BACI
Original site: M5PDG8_9BACI 
ID   M5PDG8_9BACI            Unreviewed;       608 AA.
AC   M5PDG8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Sulfite reductase flavoprotein alpha-component CysJ {ECO:0000313|EMBL:EME74705.1};
GN   ORFNames=BSONL12_13006 {ECO:0000313|EMBL:EME74705.1};
OS   Bacillus sonorensis L12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1274524 {ECO:0000313|EMBL:EME74705.1, ECO:0000313|Proteomes:UP000011907};
RN   [1] {ECO:0000313|EMBL:EME74705.1, ECO:0000313|Proteomes:UP000011907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L12 {ECO:0000313|EMBL:EME74705.1,
RC   ECO:0000313|Proteomes:UP000011907};
RX   PubMed=23538904;
RA   Adimpong D.B., Sorensen K.I., Nielsen D.S., Thorsen L., Rasmussen T.B.,
RA   Derkx P.M., Jespersen L.;
RT   "Draft Whole-Genome Sequence of Bacillus sonorensis Strain L12, a Source of
RT   Nonribosomal Lipopeptides.";
RL   Genome Announc. 1:E0009713-E0009713(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000207-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000207-1};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000207-1};
CC       Note=Binds 1 FMN per subunit. {ECO:0000256|PIRSR:PIRSR000207-1};
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:EME74705.1}.
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DR   EMBL; AOFM01000007; EME74705.1; -; Genomic_DNA.
DR   RefSeq; WP_006638581.1; NZ_AOFM01000007.1.
DR   AlphaFoldDB; M5PDG8; -.
DR   STRING; 1274524.BSONL12_13006; -.
DR   GeneID; 79846159; -.
DR   PATRIC; fig|1274524.3.peg.2810; -.
DR   eggNOG; COG0369; Bacteria.
DR   OrthoDB; 9789468at2; -.
DR   Proteomes; UP000011907; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06199; SiR; 1.
DR   Gene3D; 3.40.50.360; -; 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; IPR010199; CysJ.
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; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   NCBIfam; TIGR01931; cysJ; 1.
DR   PANTHER; PTHR19384:SF128; NADPH OXIDOREDUCTASE A; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF000207; SiR-FP_CysJ; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000207-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRSR:PIRSR000207-1};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000207-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          69..207
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          238..457
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         75..80
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         122..125
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         158..167
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         328
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         395..398
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         413..415
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         419
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         428..431
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         528..529
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         534..538
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         570
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT   BINDING         608
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
SQ   SEQUENCE   608 AA;  67923 MW;  6E25F5B7D2082515 CRC64;
     MQLQVMNSPF NQEQAELLNR LLPTLTESQK AWLSGFLAAS QSFEAAAALE TPAAEIPAAE
     PVQPVSKEVT ILYGSQTGNA QGLAENAGKK LEERGFQVTV SSMSDFKANQ LKKIRNLLVV
     VSTHGEGDPP DNAQSFHEFL HGRRAPKLDD LRFSVLALGD SSYEFFCKTG KDFDQRLEEL
     GGKRLHPRVD CDVDFDDSAS AWLEGVLGGL SEAGGQGKSA APNQAAAPQT ADAVYSRKKP
     FQAEVLENLN LNGRGSNKET RHLELSLEGS GLTYEPGDAL GIYPENDPEL VDMLLQEMKW
     DPDEVVTVDK QGERLPLKEA LTSYFEITVL TKKFLRQAAA LTENEKLREL TAPGNEDRLK
     EYIHGRDLLD FAGDFGPFSA SAQEFVSILR KMPPRLYSIA SSIAANPDEV HLTIGAVRYN
     THGRDRKGVC SILCAERLQP GDTLPVFIQP NKNFKLPENP DTPIIMVGPG TGVAPFRSFM
     QEREETGAKG KSWMFFGDQH FVTDFLYQTE WQKWLKDGVL TKMDIAFSRD SEEKVYVQHR
     MLEHSKELFE WLQEGAAFYI CGDKNHMAKD VHNTLLDIVE KEGGMSREEA EAYLAEMKQQ
     KRYQRDVY
//
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