ID   CYSJ_SHEON              Reviewed;         607 AA.
AC   Q8EAZ9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000255|HAMAP-Rule:MF_01541};
DE            Short=SiR-FP {ECO:0000255|HAMAP-Rule:MF_01541};
DE            EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01541};
GN   Name=cysJ {ECO:0000255|HAMAP-Rule:MF_01541};
GN   OrderedLocusNames=SO_3738;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- FUNCTION: Component of the sulfite reductase complex that catalyzes the
CC       6-electron reduction of sulfite to sulfide. This is one of several
CC       activities required for the biosynthesis of L-cysteine from sulfate.
CC       The flavoprotein component catalyzes the electron flow from NADPH ->
CC       FAD -> FMN to the hemoprotein component. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH +
CC         sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01541};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01541};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01541};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01541};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01541};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC       sulfide from sulfite (NADPH route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC       beta component is a hemoprotein. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: Belongs to the NADPH-dependent sulphite reductase
CC       flavoprotein subunit CysJ family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family. {ECO:0000255|HAMAP-Rule:MF_01541}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01541}.
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DR   EMBL; AE014299; AAN56721.1; -; Genomic_DNA.
DR   RefSeq; NP_719277.1; NC_004347.2.
DR   RefSeq; WP_011073521.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EAZ9; -.
DR   SMR; Q8EAZ9; -.
DR   STRING; 211586.SO_3738; -.
DR   PaxDb; 211586-SO_3738; -.
DR   KEGG; son:SO_3738; -.
DR   PATRIC; fig|211586.12.peg.3621; -.
DR   eggNOG; COG0369; Bacteria.
DR   HOGENOM; CLU_001570_17_7_6; -.
DR   OrthoDB; 9816402at2; -.
DR   PhylomeDB; Q8EAZ9; -.
DR   BioCyc; SONE211586:G1GMP-3473-MONOMER; -.
DR   UniPathway; UPA00140; UER00207.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01541; CysJ; 1.
DR   InterPro; IPR010199; CysJ.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR029758; CysJ_Proteobact.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Electron transport; FAD;
KW   Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome; Transport.
FT   CHAIN           1..607
FT                   /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT                   component"
FT                   /id="PRO_0000199936"
FT   DOMAIN          66..204
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   DOMAIN          239..456
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         72..77
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         119..122
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         155..164
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         327
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         361
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         395..398
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         413..415
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         428..431
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         527..528
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         533..537
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         569
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
FT   BINDING         607
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01541"
SQ   SEQUENCE   607 AA;  66620 MW;  C6042663547ACD22 CRC64;
     MLLKELSSLA SPLSQSQVDK LKQLTAELNS VQLAWVSGYL AATANTSGSA IQVAASVTEA
     QAAQTVTILY GSQTGNGRGI AKALAEKAKT QGYSVNLASM GEYNVRQLKQ ETLLLLVVST
     HGEGEAPDDA IELHKFLATK RAPQLNNLHY SVLALGDSSY EFFCQTGKDF DARLSALGAK
     ALLPLVECDV DYEAAAGQWH ADVLTAVKPL IQTTANVVAL NEINSTSAQV ASESEFTKQN
     PYRAEVLVSQ KITGRDSDRD VRHVEIDLGE SGLHYEVGDA LGVWFSNSEI LVGEILAGLG
     LAADAKVTVG SESISLKQAL IDKKELTQLY PGLVKAWAEL SASSELLALS EDKEQLRQFI
     LNHQFVDLVT NYKLPAEANL DANKLLELLR PLTPRLYSIA SSQTEVDTEV HLTVALVEDE
     HQGQTRFGGA SHFLASAQEG AEVKVYVEPN KHFRLPENPD TPVIMIGPGT GVAPFRAFMQ
     ERVAQGAKGD SWLFFGNPHF EQDFLYQTEW QQYLKNGDLT RIDVAFSRDQ AHKIYVQHRI
     KEQGQALWQW LQNGAHLYIC GDAERMAKDV HQALLAVAVE FGGLSSEAAE EYFETLRSHK
     RYQKDVY
//