ID   CYSI_BUCAP              Reviewed;         566 AA.
AC   P0C0B2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Putative sulfite reductase [NADPH] hemoprotein beta-component;
DE            Short=SIR-HP;
DE            Short=SIRHP;
DE            EC=1.8.1.2;
GN   Name=cysI; OrderedLocusNames=BUsg_412;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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   -!- CAUTION: Could be the product of a pseudogene.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE013218; Type=Frameshift; Positions=170;
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DR   EMBL; AE013218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   GenomeReviews; AE013218_GR; BUsg_412.
DR   KEGG; bas:BUsg412; -.
DR   HOGENOM; P0C0B2; -.
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   5: Uncertain;
KW   4Fe-4S; Amino-acid biosynthesis; Complete proteome;
KW   Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    566       Putative sulfite reductase [NADPH]
FT                                hemoprotein beta-component.
FT                                /FTId=PRO_0000199894.
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;  65353 MW;  E6F10AF8BC27F19C CRC64;
     MKKDYKKVFL KNTKEERIKE NSNYLRGTII DDLKDEITNG FTGDNFSLIR FHGMYQDDRD
     LRLERNEQKL EPRYAMMLRC RLPRGIIKAK KWLKIDHFAS KNTLYGTIRL NNLQTFQFHG
     ILKKTLKDAH KMLNKIGLDS LGTANDVNRN VLCTSNPMES LIHQQCYEWV SKISNFLLPQ
     TKAYAEIWLN QKKIATTDQE PILGKTYLPR KFKTTVVVPP YNDVDLYAND MNFIAITKNN
     KIVGFNVLIG GGLSINHGNK NTWPFLAVEL GYITLEKTLS VAESIVTTQR DWGNRTDRKN
     AKTRYTIAKV GLSVFKKEVE KRANMTFETI KPYYFISRGD RFGWTKNINN DWSLTVFIQN
     GRIYDNDKQL VKSGLLKIAN LHTGNFRLTA NQNIVISEIL DKNKKKIEEI AISHGLIKKV
     SSLRENSMAC VSFPTCPLAI AESERILSFF ITKVENIMLK YGIEKEIIIL RISGCPNGCG
     RSLLAEIGLI GKSLGRYNLY IGGNRIGSRI PKIYKENITE QEILIHLDFL IKIWSIERQK
     KEHFGDFVIR RNVVKKVVNP IYDFWN
//