ID   CYSJ_THIRO              Reviewed;         522 AA.
AC   P52674;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component;
DE            Short=SIR-FP;
DE            EC=1.8.1.2;
GN   Name=cysJ;
OS   Thiocapsa roseopersicina.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocapsa.
OX   NCBI_TaxID=1058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 219 / 6311;
RX   PubMed=8695637; DOI=10.1016/0167-4838(96)00066-0;
RA   Bruehl A., Haverkamp T., Gisselmann G., Schwenn J.D.;
RT   "A cDNA clone from Arabidopsis thaliana encoding plastidic
RT   ferredoxin:sulfite reductase.";
RL   Biochim. Biophys. Acta 1295:119-124(1996).
CC   -!- FUNCTION: Catalyzes the 6-electron reduction of sulfite to sulfide.
CC       This is one of several activities required for the biosynthesis of L-
CC       cysteine from sulfate. The flavo-protein component catalyzes the
CC       electron flow from NADPH -> FAD -> FMN to the hemoprotein component (By
CC       similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 1 FMN per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC       beta component is a hemoprotein (By similarity). {ECO:0000250}.
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DR   EMBL; Z23169; CAA80687.1; -; Genomic_DNA.
DR   PIR; S34190; S34190.
DR   AlphaFoldDB; P52674; -.
DR   SMR; P52674; -.
DR   PRIDE; P52674; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; -; 1.
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   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF63380; SSF63380; 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; Transport.
FT   CHAIN           1..522
FT                   /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT                   component"
FT                   /id="PRO_0000199938"
FT   DOMAIN          60..198
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT   DOMAIN          241..399
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          217..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  57784 MW;  C15C8ADAACEFF7A0 CRC64;
     MVLSQLNGLT SPLDERHVHA LQIALKGMTP TQLAWVSGYL AGIGGGPLRM PTEPKAVERI
     TILFGSQTGN AKAVAEQLGA RASEQGMDAR VISMGDFNPR KLSKEQWVLI VVSTHGEGEP
     PENAYALHAF IQDQGAGRLE QLPFAVLGLG DSSYEHFCRT AVDFDRRLAE LGAQRILPLQ
     CCALDYRSDT ERWSSDALNR LSALAPRKAS NVVAMPTLRS HQDLRSHQEQ SRNRARPYDK
     DNPYTATLLE NRRITTLDAV SDVRHLALAI EPDAMHYRPG DALGVWVEND PSLADTILAG
     VGIDGAARIE LGDEELDLRH ALIERLELTQ LHPTTVRGWS RASGRTGAED AGERLEREEQ
     TRIYLAGNDA FRLPDAGDTP LIMIGAGTGV APYRAFLQQR AANGHPGRNW LIFGNRHFHR
     DFLYQLDWQA HRKAGRLDRV SLAFSRDGAE KPYVQQRLRE EGKEILRWLD AGAHLYVCGA
     TAMGQAVDHA LVEIFTIEAG LDPDCASLRR YPARECYATD DL