ID   CYSI_SHEDO              Reviewed;         562 AA.
AC   Q12QQ5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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; OrderedLocusNames=Sden_0933;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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(4). 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; CP000302; ABE54221.1; -; Genomic_DNA.
DR   RefSeq; YP_561944.1; -.
DR   GeneID; 4016878; -.
DR   GenomeReviews; CP000302_GR; Sden_0933.
DR   KEGG; sdn:Sden_0933; -.
DR   NMPDR; fig|318161.14.peg.914; -.
DR   HOGENOM; Q12QQ5; -.
DR   OMA; Q12QQ5; ITTTQWQ.
DR   BioCyc; SDEN318161:SDEN_0933-MON; -.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:HAMAP.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR   HAMAP; MF_01540; -; 1.
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; Complete proteome;
KW   Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    562       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000292963.
FT   METAL       426    426       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       432    432       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       471    471       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       475    475       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       475    475       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   562 AA;  62333 MW;  85847875212193C6 CRC64;
     MSEQKLAVNE YLKTDSDYLR GTIQEGLDTQ VTGSFSDGDQ QLIKFHGFYQ QDDRDLRNER
     KEQKLEPLYS FMLRARVPGG ICTPAQWLDV DKISSTLTTS NSIRLTTRQT FQYHGIPKRN
     LKTLIQGLDK AALDSIAACG DVNRNVMCNP NPVESKLHAQ AYAVAKELSD HLLPHTRAYA
     EIWLDEEKLV GETVEPVYGN TYLPRKFKMA VSVPPDNDVD VYTNDLGFIA IAEDGQLVGF
     NLVAGGGMGS THGEVETFPR LADDFGFIKT ADVIKFAEAV MTVQRDWGNR VVRKRARLKY
     TIVDHGFDAF KAEVENRAGV KFAPKRDVVI GDRGDRYGWV EGIDSKWHLT LFIESGRIKD
     LPGQTLQTGL REIAKIHKGD FRMTSNQNMI IAGVAAEDKA EIEGLARKHG LMGQVLTGTR
     GHSIACVALP TCPLAMAEAE RYFPEFIDHI DALQAKHGIS DQSIVVRMTG CPNGCARPFA
     AEIGLVGKAP GRYNLYLGAN FEGTRLNKMH KENIQEAEIL AELDTLFGRY ATERDAGETF
     GNFTVRIGVV KAVNDAAKDF HG
//