ID   CYSI_ENTS8              Reviewed;         570 AA.
AC   A7MJ64;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 12.
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=ESA_00535;
OS   Enterobacter sakazakii (strain ATCC BAA-894).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (JUL-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000783; ABU75826.1; -; Genomic_DNA.
DR   RefSeq; YP_001436662.1; -.
DR   GeneID; 5551850; -.
DR   GenomeReviews; CP000783_GR; ESA_00535.
DR   KEGG; esa:ESA_00535; -.
DR   OMA; A7MJ64; 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_1000068764.
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;  63950 MW;  BC6C15E898ADB63C CRC64;
     MSEKYPGPLV VEGKLSDAER MKRESNFLRG TIAEDLHDGL TGGFNGDNFL LIRFHGMYQQ
     DDRDIRAERA AQKLEPRHAM MLRCRLPGGI MTPQQWLAID KFAEENTIYG SIRLTNRQTF
     QYHGLLKKNV KPAHQMLHSV GLDALATAND MNRNVLCTSN PVESQLHAEA YEWAKKLSEH
     LLPRTRAYAE IWLDQEKVAT TDEEPILGAT YLPRKFKTTV VVPPQNDVDL HANDMNFVAI
     AENGKLVGFN LLVGGGLSIE HGNKKTYART ATEFGYIPLE HTLAVAEAVV TTQRDWGNRT
     DRKNAKTKYT LERVGPDVFK AEVERRAGVT FEPVRPYEFT GRGDRIGWVK GIDDKWHLTL
     FIENGRILDF PDKPLKTGLK EIARIHKGDF RLTANQNLIV AGVPEGDKAK IEQIARAHGL
     MAGVTPQREN SMACVSFPTC PLAMAEAERF LPQFIDKVDG IMAKHGLAEE HIVLRVTGCP
     NGCGRAMLAE LGLVGKAPGR YNLHLGGNRI GTRIPRMYRE NITESEILDN IDELVGRWAQ
     EREPGEGFGD FTVRAGIIRP VLDPARDFWE
//