ID   CYSI_ACTSZ              Reviewed;         588 AA.
AC   A6VPZ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   16-JUN-2009, entry version 14.
DE   RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component;
DE            Short=SIR-HP;
DE            Short=SIRHP;
DE            EC=1.8.1.2;
GN   Name=cysI; OrderedLocusNames=Asuc_1686;
OS   Actinobacillus succinogenes (strain ATCC 55618 / 130Z).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671;
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., Lowry S., Clum A., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C.,
RA   Richardson P.;
RT   "Complete sequence of Actinobacillus succinogenes 130Z.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme catalyzes the 6-electron reduction of
CC       sulfite to sulfide. This is one of several activities required for
CC       the biosynthesis of L-cysteine from sulfate (By similarity).
CC   -!- CATALYTIC ACTIVITY: H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3
CC       NADPH.
CC   -!- COFACTOR: Binds 1 siroheme per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity).
CC   -!- SUBUNIT: Alpha(8)-beta(4). The alpha component is a flavoprotein,
CC       the beta component is a hemoprotein (By similarity).
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family.
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DR   EMBL; CP000746; ABR75038.1; -; Genomic_DNA.
DR   RefSeq; YP_001344973.1; -.
DR   GeneID; 5349238; -.
DR   GenomeReviews; CP000746_GR; Asuc_1686.
DR   KEGG; asu:Asuc_1686; -.
DR   OMA; A6VPZ1; ITTTQWQ.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH 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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:HAMAP.
DR   HAMAP; MF_01540; -; 1.
DR   InterPro; IPR011786; CysI.
DR   InterPro; IPR006066; Nir_Si_BS.
DR   InterPro; IPR006067; Nir_Sir_4Fe4S.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   TIGRFAMs; TIGR02041; CysI; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Amino-acid biosynthesis; Complete proteome;
KW   Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    588       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000318561.
FT   METAL       443    443       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       449    449       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       488    488       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       492    492       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       492    492       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   588 AA;  66565 MW;  CA199CDA15D40BF1 CRC64;
     MTDSTKQKGL EWQKQGLSDN ERLKAESNFL RGTILDDLED GLTGGFKGDN FQMIRFHGMY
     EQDDRDIRAE RADEKLEARK FMLLRCRLPG GIIKPAQWIE IDKFARDNNY YQSIRLTNRQ
     TFQYHGVPKT KLQEMHRLLH KLGLDSIATA SDMNRNVLCS SNPVESELHQ EAYEWAKKIS
     EHLLPRTNGY LDVWIAGKKV QSSDSFLGQE DEPILGKTYL PRKYKTAVVL PPLNDVDMYG
     NDMNFVGIQD EAGKLVGFNV LVGGGLSFEH GNTKTYPNVA LELGYIPVEQ TLKAAECIVT
     TQRDFGNRAD RKNARLRYTL QNMTLDGFRE EVERRMGFKF ESIRPFEFTE RGDRIGWVKG
     IDDKWHLTCF IESGRITDKP GKPLMTGMLE LAKVHTGDFR ITANQNIIIA NVAEEDKQRI
     EDIAREYGLI GNISKLRENS MSCVSFPTCP LAMAESERAL PEFIDELDNI MAKHDVADDY
     IVTRITGCPN GCGRAMLAEI GLVGKAIGRY NLHLGGDRPG TRIPRMYKEN ITLPEILAEL
     DGLIGRWAKE RNSNEGFGDF VIRAGIIKPV VNAVVDFWDA NLIPTVTA
//