ID   CYSI_VIBHB              Reviewed;         578 AA.
AC   A7MSZ7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 13.
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=VIBHAR_00004;
OS   Vibrio harveyi (strain ATCC BAA-1116 / BB120).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=338187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N.,
RA   Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C.,
RA   Irgon J., Wilson R.K.;
RL   Submitted (AUG-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; CP000789; ABU69064.1; -; Genomic_DNA.
DR   RefSeq; YP_001443291.1; -.
DR   GeneID; 5553777; -.
DR   GenomeReviews; CP000789_GR; VIBHAR_00004.
DR   KEGG; vha:VIBHAR_00004; -.
DR   NMPDR; fig|338187.4.peg.47; -.
DR   OMA; A7MSZ7; 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    578       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_1000068779.
FT   METAL       441    441       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       447    447       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       487    487       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       491    491       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       491    491       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   578 AA;  64673 MW;  7CFB712145E9A2BD CRC64;
     MSANQQSNSQ EVLGEVLGPL SDNERLKRES NLLRGTIEQD LQDRITGGFT ADNFQLIRFH
     GMYQQDDRDI RNERAKQKLE PLHNVMLRAR MPGGIITPKQ WLAIDKFATE HSLYGSIRLT
     TRQTFQFHGV LKPNIKLMHQ TLNSIGIDSI ATAGDVNRNV LCTTNPVESE LHQEAYEWAK
     KISEHLLPKT RAYAEIWLDG EKVESTEEDE PILGKNYLPR KFKTTVVIPP QNDVDVHAND
     LNFVAIADNG KLVGFNVLVG GGLAMTHCDT STYPRRADDF GFIPLEKTLD VAAAVVTTQR
     DWGNRSNRKN AKTKYTLDRV GSDVFKAEVE KRAGVKFEQS RPYEFTERGD RIGWVEGIDG
     KHHLALFIEN GRLLDFPGKP LKTGVAEIAK IHKGDFRMTA NQNLIVAGVP KSQKAKIEKI
     AREHGLMDDG VSEQRKNSMA CVAFPTCPLA MAEAERFLPQ FVTDVEGILE KHGIPEEDNI
     ILRVTGCPNG CGRAMLAEIG LVGKAPGRYN LHLGGNRGGT RVPKMCKENI TDKQILEEID
     QLVARWAAER EEGEAFGDFT IRAGIIQEVF VSKRDFHA
//