ID   CYSI_ECO24              Reviewed;         570 AA.
AC   A7ZQK6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-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=EcE24377A_3065;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV20906.1; -; Genomic_DNA.
DR   RefSeq; YP_001464085.1; -.
DR   GeneID; 5589173; -.
DR   GenomeReviews; CP000800_GR; EcE24377A_3065.
DR   KEGG; ecw:EcE24377A_3065; -.
DR   OMA; A7ZQK6; 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_1000068758.
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;  63960 MW;  5AF5E78DFF0A433F CRC64;
     MSEKHPGPLV VEGKLTDAER MKLESNYLRG TIAEDLNDGL TGGFKGDNFL LIRFHGMYQQ
     DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID KFAGENTIYG SIRLTNRQTF
     QFHGILKKNV KPVHQMLHSV GLDALATAND MNRNVLCTSN PYESQLHAEA YEWAKKISEH
     LLPRTRAYAE IWLDQEKVAT TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI
     AENGKLVGFN LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT
     DRKNAKTKYT LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK GIDDNWHLTL
     FIENGRILDY PGRPLKTGLL EIAKIHKGDF RITANQNLII AGVPESEKAK IEKIAKESGL
     MNAVTPQREN SMACVSFPTC PLAMAEAERF LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP
     NGCGRAMLAE VGLVGKAPGR YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK
     EREAGEGFGD FTVRAGIIRP VLDPARDLWD
//