ID   CYSJ_BAUCH              Reviewed;         595 AA.
AC   Q1LTP1;
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] flavoprotein alpha-component;
DE            Short=SIR-FP;
DE            EC=1.8.1.2;
GN   Name=cysJ; OrderedLocusNames=BCI_0218;
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: 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; CP000238; ABF14003.1; -; Genomic_DNA.
DR   RefSeq; YP_588673.1; -.
DR   GeneID; 4056751; -.
DR   GenomeReviews; CP000238_GR; BCI_0218.
DR   KEGG; bci:BCI_0218; -.
DR   HOGENOM; Q1LTP1; -.
DR   OMA; Q1LTP1; 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    595       Sulfite reductase [NADPH] flavoprotein
FT                                alpha-component.
FT                                /FTId=PRO_0000292965.
FT   DOMAIN       59    197       Flavodoxin-like.
FT   DOMAIN      230    444       FAD-binding FR-type.
FT   NP_BIND      65     69       FMN (By similarity).
FT   NP_BIND     145    176       FMN (By similarity).
FT   NP_BIND     232    284       FAD (By similarity).
FT   NP_BIND     468    595       NADP (By similarity).
SQ   SEQUENCE   595 AA;  67733 MW;  F6F314B06CE8CAAC CRC64;
     MTQQNAPKDL PPLSAEQLDR LQAISSDLSN LQLAWASGYL WNKASHSIPI DYTASQQVIT
     VLSASQTGNA RRLAVQLYED LLAAQLSVVI INAGDYKFKQ IAQEKWLLIV TSTQGDGDPP
     EEAIALYKYL FSKKAPVLNN IQFAIFGLGD SSYTYFAKIG KDFDSRLAEL GAQRLYDRVD
     ADVDYQEKAD IWRREIVKIL QTKLVTVNAK QQLSVINNRI EVKNNLYTKE EPFTAHLVVK
     QKITSRSSKK DIRHLEIDIA GSGLNYQPGD ALGVWYENDP VLISEILELL GLTGNELVQV
     KEKNIPLNEA LQKHYELTNN TAEIVKSYAY ITRNSSLLAL VDDQQQLKQF AFSTPFIDMI
     QRIPVELHPK QLLTLLRPLM PRLYSIASSQ AEVGDEVHLT VSVVRYEIDG KIRTGGASSY
     LAYRLQESEP IRVFIEHNDN FRLPNNPNTA IIMIGSGTGI APFRGFMQQR EATTAKGKNW
     LFFGNQHLTD DFLYQVEWQR YIKNGLLNKI DVAWSQDQNK KIYVQDRLLE KGIELWNWIQ
     DGAHIYVCGN ANLMARDVEK ALVKLIAIHG RMDYEQADEF LSELRIARRF QRDTY
//