ID   CYSI_ENT38              Reviewed;         570 AA.
AC   A4WDW0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
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=Ent638_3226;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Enterobacter sp. 638.";
RL   Submitted (APR-2007) 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; CP000653; ABP61890.1; -; Genomic_DNA.
DR   RefSeq; YP_001177941.1; -.
DR   GeneID; 5112940; -.
DR   GenomeReviews; CP000653_GR; Ent638_3226.
DR   KEGG; ent:Ent638_3226; -.
DR   NMPDR; fig|399742.4.peg.3072; -.
DR   OMA; A4WDW0; ITTTQWQ.
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    570       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_1000068763.
FT   METAL       434    434       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       440    440       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       479    479       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       483    483       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       483    483       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   570 AA;  64091 MW;  8047CCA10EDB493A CRC64;
     MSEKHPGPLV VEGKLTDAER MKVDSNYLRG TIAEDLNDGL TGGFKGDNFL LIRFHGMYQQ
     DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID KFAHDNTIYG SIRLTNRQTF
     QFHGILKKNV KPVHQMLHSV GLDALATAND MNRNVLCTSN PYESELHAEA YEWAKKISEH
     LLPRTRAYAE IWLDQEKVAT TDVEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI
     AENGKLVGFN LLVGGGLSIE HGNKKTYART ASEFGYIPLE HTLAVAEAVV TTQRDWGNRT
     DRKNAKTKYT LERVGVETFK AEVERRAGIT FEPIRAYEFT GRGDRIGWVK GIDNKWHLTL
     FIENGRILDY PGRPLKTGLL EIAKIHKGEF RITANQNLII AGVPESQKAK IEKLAREHTL
     MDGVKPQREN SMACVSFPTC PLAMAEAERF LPSFTDKVEA VLAKHGIPDE HIVMRVTGCP
     NGCGRALLAE LGLVGKAPGR YNVHLGGNRS GTRIPRMYRE NITEPEILDS LDELVGRWAK
     EREAGEGFGD FTVRAGIIRP VLDPARDFWE
//