ID   CYSJ_BUCAP              Reviewed;         602 AA.
AC   Q8K9D3;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component;
DE            Short=SIR-FP;
DE            EC=1.8.1.2;
GN   Name=cysJ; OrderedLocusNames=BUsg_413;
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: Catalyzes the 6-electron reduction of sulfite to
CC       sulfide. This is one of several activities required for the
CC       biosynthesis of L-cysteine from sulfate. The flavo-protein
CC       component catalyzes the electron flow from NADPH -> FAD -> FMN to
CC       the hemoprotein component (By similarity).
CC   -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC       NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 FMN per subunit (By similarity).
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein,
CC       the beta component is a hemoprotein (By similarity).
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AE013218; AAM67958.1; -; Genomic_DNA.
DR   RefSeq; NP_660747.1; -.
DR   HSSP; P38038; 1DDG.
DR   GeneID; 1005748; -.
DR   GenomeReviews; AE013218_GR; BUsg_413.
DR   KEGG; bas:BUsg413; -.
DR   HOGENOM; Q8K9D3; -.
DR   OMA; Q8K9D3; EQLAWVS.
DR   BioCyc; BAPH198804:BUSG413-MON; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion 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:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01541; -; 1.
DR   InterPro; IPR010199; CysJ.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD_bd.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   TIGRFAMs; TIGR01931; cysJ; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis;
KW   Electron transport; FAD; Flavoprotein; FMN; NADP; Oxidoreductase;
KW   Transport.
FT   CHAIN         1    602       Sulfite reductase [NADPH] flavoprotein
FT                                alpha-component.
FT                                /FTId=PRO_0000199921.
FT   DOMAIN       68    206       Flavodoxin-like.
FT   DOMAIN      237    451       FAD-binding FR-type.
FT   NP_BIND      74     78       FMN (By similarity).
FT   NP_BIND     154    185       FMN (By similarity).
FT   NP_BIND     239    291       FAD (By similarity).
FT   NP_BIND     475    602       NADP (By similarity).
SQ   SEQUENCE   602 AA;  69930 MW;  FA3793147889B7B3 CRC64;
     MKNKNPFNIF FPLSLDKIEN LEKIKKNCSS IQYAWLSGYF WNLANQTPSR LICEKNEFFR
     KDNEEKIITI ISASQTGNAR QLAKRFNKYL KNENKKTNLI DAADYNFKKI KNERFLILII
     STQGEGEPPE EALSFYKFIM SKKAPRLENL HYSVFGLGDV SYNLFCQAGK DFDKRFSELG
     GKSLLHRLDS DIEYESNYIQ WSEELLLAIN KIDVSTCSVF KKNDKKNFID KLNYTKYKPA
     VATVLLNQKI TGRNSTKDVH HIELDITNSN IVYTPGDALG VWYQNSSQLI KQILKLLSIR
     ISDKVKVKDK IITIFEALKK NFELTTNTKH IIQKYTDVTQ NKFLKKIISD NKKLNNYVKK
     TPLLKMIYDH PKKLSSQQLI SILRPLKPRL YSISSSQSEM NDEVHITVGV VKKQISGTIH
     LGGSSSYLSQ FLKIDDSVKI FVEEKSNFRL PENKDVPIIM IGSGTGIAPF RAFIQQRDND
     KATGKNWIFF GNPNFTEDFL YQLEWQKYLK KKLLTKMSLA WSRDQKEKIY VQDKIRENGK
     ELWEWVNQGA QIYVCGNASK MAKDVEKELL DVFSKNGSMD IEESSEFLNN LRITRRYQRD
     VY
//