ID   CYSJ_ENT38              Reviewed;         601 AA.
AC   A4WDW1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component;
DE            Short=SIR-FP;
DE            EC=1.8.1.2;
GN   Name=cysJ; OrderedLocusNames=Ent638_3227;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Enterobacter sp. 638.";
RL   Submitted (APR-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; CP000653; ABP61891.1; -; Genomic_DNA.
DR   RefSeq; YP_001177942.1; -.
DR   GeneID; 5112941; -.
DR   GenomeReviews; CP000653_GR; Ent638_3227.
DR   KEGG; ent:Ent638_3227; -.
DR   NMPDR; fig|399742.4.peg.3073; -.
DR   OMA; A4WDW1; FHKDGAL.
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    601       Sulfite reductase [NADPH] flavoprotein
FT                                alpha-component.
FT                                /FTId=PRO_1000087635.
FT   DOMAIN       64    202       Flavodoxin-like.
FT   DOMAIN      236    450       FAD-binding FR-type.
FT   NP_BIND      70     74       FMN (By similarity).
FT   NP_BIND     150    181       FMN (By similarity).
FT   NP_BIND     238    290       FAD (By similarity).
FT   NP_BIND     474    601       NADP (By similarity).
SQ   SEQUENCE   601 AA;  66366 MW;  D4C25C7138BF8496 CRC64;
     MTTQAPPSNL LPLNPEQLAR LQAATTDFSP TQLAWVSGYF WGMLNQQPGA VVNAPATAVE
     IPAITLISAS QTGNARRVAE ALRDDLLAAK LNVNLVNAGD YKFKQIASEK LVVVVASTQG
     EGEPAEEAVA LHKFLFSKKA PKLDGTAFAV FGLGDTSYEF FCQSGKDFDS KLAELGAERL
     LDRVDADVEY QAAAAEWRAR IVDVLKARVP KDTPAQAANS ASGAVNEVST SPYTKEEPLV
     ASLSVNQKIT GRDSEKDVRH IEIDLGDSGL RYQPGDALGV WYQNDPALVK ELVELLWLKG
     TEQVNVEGKT LPLSEALQWH FELTVNTANI VENYATLTRS ETLLPLVGDK AKLQHYAATT
     PIVDMVRFSP AQLDAEALIG LLRPLTPRLY SIASSQAEVE SEVHITVGAV RFDIEGRARA
     GGASSFLADR VEEEGEVRVF IEHNDNFRLP ANPETPVIMI GPGTGIAPFR AFMQQRAAEE
     APGKNWLFFG NPHFTEDFLY QVEWQRYVKE GVLSRIDLAW SRDQKQKIYV QDKLREQGAE
     LWAWINNGAH LYVCGDANRM AKDVEQALLE VIAEFGGMDI ETADEFLSEL RVERRYQRDV
     Y
//