ID   CYSJ_ENTS8              Reviewed;         600 AA.
AC   A7MJ63;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 15.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component;
DE            Short=SIR-FP;
DE            EC=1.8.1.2;
GN   Name=cysJ; OrderedLocusNames=ESA_00533;
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: 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; CP000783; ABU75824.1; -; Genomic_DNA.
DR   RefSeq; YP_001436661.1; -.
DR   GeneID; 5551773; -.
DR   GenomeReviews; CP000783_GR; ESA_00533.
DR   KEGG; esa:ESA_00533; -.
DR   OMA; A7MJ63; EQLAWVS.
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    600       Sulfite reductase [NADPH] flavoprotein
FT                                alpha-component.
FT                                /FTId=PRO_1000087636.
FT   DOMAIN       63    201       Flavodoxin-like.
FT   DOMAIN      235    449       FAD-binding FR-type.
FT   NP_BIND      69     73       FMN (By similarity).
FT   NP_BIND     149    180       FMN (By similarity).
FT   NP_BIND     237    289       FAD (By similarity).
FT   NP_BIND     473    600       NADP (By similarity).
SQ   SEQUENCE   600 AA;  66548 MW;  58E4C1E4C63B438B CRC64;
     MTTQAPPNAL LPLSPEQLAR LQTATHDFTP TQLAWLSGYF WGMVNQQPGA AVMQKPAAPA
     SVITLISASQ TGNARRVAEA LRDDLLAAQL NVNLVNAGDY KFKQIAQEKL LIVVASTQGE
     GDPPEEAVAL HKFLLSKKAP KLDGTAFAVF GLGDTSYEHF CQAGKDFDTR LAELGAERLL
     DRVDADVEYQ AAAQAWRQRV VDVLKARVPK EAPSQAAITA SGAVNLVDST PYTKESPLTA
     TLSVNQKITG RHSEKDVRHI EIDLGDAGLR YQPGDALGVW YQNDPALVQE LLELLWLKGD
     EPVTVGEKTL PLSEALQWHF ELTVNTAAIV ENYATLTRSE ALLPLVGDKA KLQDYAARTP
     IVDMVRFAPA QLEADQLLGL LRPLTPRLYS IASSQAEVEN EVHITVGVVR FDIEGRVRAG
     GASSYLADRL EEDSEVRVFI EHNDNFRLPA TPETPVIMIG PGTGIAPFRA FMQQREADGA
     TGKNWLFFGN PHFTEDFLYQ VEWQRYVKEG LLTRIDLAWS RDQDHKIYVQ DKIREQGAEL
     WRWLQEGAHL YVCGDANRMA KDVEQALLEV IAAYGGMDAE AADEYLSELR VERRYQRDVY
//