ID   CYSJ_CITK8              Reviewed;         601 AA.
AC   A8ANX1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-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=CKO_04119;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-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; CP000822; ABV15185.1; -; Genomic_DNA.
DR   RefSeq; YP_001455620.1; -.
DR   GeneID; 5584181; -.
DR   GenomeReviews; CP000822_GR; CKO_04119.
DR   KEGG; cko:CKO_04119; -.
DR   OMA; A8ANX1; 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    601       Sulfite reductase [NADPH] flavoprotein
FT                                alpha-component.
FT                                /FTId=PRO_1000087631.
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;  66119 MW;  93406AEFEFF5701A CRC64;
     MTTQAPPSAL LPLNPEQLAR LQAATTDLSP TQLAWVSGYF WGMLNQQPGT LAATPAPVAE
     MPGITLISAS QTGNARRVAE ALRDDLLAAK LSVTLVNAGD YKFKQIANEK LLVVVASTQG
     EGEPPEEAVA LRKFLFSKKA PKLDNTAFAV FGLGDTSYEF FCQAGKDFDS KLAELGGERL
     LDRVDADVEY QAAAQEWRAR VVDVLKARAP SASAAQVAVA ATGAVNDVHS SPYTKEAPLS
     ASLAVNQKIT GRDSEKDVRH IEIDLGDSGL RYQPGDALGV WYQNDPELVK EIVELVWLKG
     TEPVTVNGKV LPLAEALQWH FELTVNTANI VENYATLTRS ESLLPLVGDK AQLQHYAATT
     PIVDMLRFSP AQLDADALVG LLRPLTPRLY SIASSQAEVE SEVHITVGAV RYEIEGRARA
     GGASSFLADR VEEEGEVRVF IEHNDNFRLP ANPETPVIMI GPGTGIAPFR AFMQQRAADE
     APGKNWLFFG NPHFTEDFLY QVEWQRYVKE GVLSRIDLAW SRDQKEKIYV QDKLREQGAE
     LWRWINDGAH IYVCGDANCM AKDVEQALLE VIAEFGGMDA EAADEFLSEL RVERRYQRDV
     Y
//