ID   CYSI_BAUCH              Reviewed;         566 AA.
AC   Q1LTP2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=BCI_0217;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF13903.1; -; Genomic_DNA.
DR   RefSeq; YP_588672.1; -.
DR   GeneID; 4056488; -.
DR   GenomeReviews; CP000238_GR; BCI_0217.
DR   KEGG; bci:BCI_0217; -.
DR   HOGENOM; Q1LTP2; -.
DR   OMA; Q1LTP2; TRQAFQM.
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    566       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000292958.
FT   METAL       430    430       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       436    436       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       475    475       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       479    479       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       479    479       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   566 AA;  63931 MW;  241F9CAD6D6E7ED4 CRC64;
     MNKKIPKAIL SDNERLKVAS NFLRGTIAQD LQDNITGGFK GDNIQLIRFH GMYQQDDRDL
     RVERTCQKLE PLINMMLRCR LPGGIITPQQ WLGIDSFATK HTLYGSIRLT TRQTFQFHGV
     LKPNLKNMHK LLHSLGLDSI ATAGDMNRNV LCTSNPVESV LHQQVCNYAK MISEHFLPKT
     RAYAEIWLDG EKTETTEQEP ILGANYLPRK FKISIVVPPL NDVDLHANDL NFIAISNLGQ
     LVGFNVLVGG GLAMTHNDKS TYPRTASELG YISVVDTIKI AEAVITTQRD LGDRSNRKHA
     KTKYTIERVG VEFFKKEVEV RAGIKFKHIR PYSFTERGDR FGWVQGIDNQ WHLTLFIENG
     RIIDDSHRKL KTGMLEIARI HQGDFRITAN QNIIIAGVEK KHKATIELLA RQYGLINNNI
     TLQRKASMAC VAFPTCPLAM AEAERFLPQF VTKVENIMSR HGLGQEKIIL RVTGCPNGCG
     RAMLAEIGLV GKTIGRYNLY LGGDSIGTRI PRIYRENLTE EEILSIINDT TGRWARERQP
     DESYGDYVVR AGIIRPVINS ALDFHN
//