ID   CYSI_THIRO              Reviewed;         559 AA.
AC   P52673;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 48.
DE   RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component;
DE            Short=SIR-HP;
DE            Short=SIRHP;
DE            EC=1.8.1.2;
GN   Name=cysI;
OS   Thiocapsa roseopersicina.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Thiocapsa.
OX   NCBI_TaxID=1058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 219 / 6311;
RX   MEDLINE=96305328; PubMed=8695637;
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: This enzyme catalyzes the 6-electron reduction of
CC       sulfite to sulfide. This is one of several activities required for
CC       the biosynthesis of L-cysteine from sulfate (By similarity).
CC   -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC       NADPH.
CC   -!- COFACTOR: Binds 1 siroheme per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein,
CC       the beta component is a hemoprotein (By similarity).
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family.
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DR   EMBL; Z23169; CAA80688.1; -; Genomic_DNA.
DR   PIR; S34191; S34191.
DR   HSSP; P17846; 7GEP.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011786; CysI.
DR   InterPro; IPR006066; Nir_Si_BS.
DR   InterPro; IPR006067; Nir_Sir_4Fe4S.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   TIGRFAMs; TIGR02041; CysI; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis; Heme; Iron;
KW   Iron-sulfur; Metal-binding; NADP; Oxidoreductase.
FT   CHAIN         1    559       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000199911.
FT   METAL       423    423       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       429    429       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       468    468       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       472    472       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       472    472       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   559 AA;  62272 MW;  6337D0DE9C941C70 CRC64;
     MSAPIHENER IKARSNCLRG TLRESLADTL TGAISPEDTQ ISKFHGFYQQ DHRDRRQARP
     EQYLEPYFGF MLRAPLPGGV CTPAQWLAID GMGRELGGGS LRLTTRQSFQ YHGILKRDIA
     SVIRGINAVM IDSIGGCGDV NRNVLCNPNP VESALHREVY DWAKRISEHL LPRTRAYHEI
     WLDGEQVGGG EDVEPIYGRT YLPRKFKTAV GVPPHNDVDV YANDLGFAAV ADGSRLIGFN
     VSAGGTGRNT GIPATFPRLA DVLGFVEPER TLAVAEAVVT TQRHFGDRLD RTQARLKYTI
     ERMGLDAFRD EVERRAGIRF APARPIGFTD QGDRTAWVRG QDGRWHLTLY IESGRLIDGP
     GQSSMQGLRE IARIHQGDFR ITPNQNLIVA RVPEPGKSEI EALARKYGLL DKGIALRLNG
     MSCVALPTCP LAMAEAERYY PDFLAQVERL TRKHGLAEQE IVTRMTGCPN GCARPYLAEL
     ALVGKGPGRY NLMLGGNGRR YRLNRLYREN LDEAAILAEI DTLLGRYAAC RQPGERFGDY
     LIRDGIVRPV VNPAEDFHE
//