ID   CYSI_VIBVU              Reviewed;         578 AA.
AC   Q8DCK1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 40.
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=VV1_1403;
OS   Vibrio vulnificus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H.,
RA   Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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; AE016795; AAO09852.1; -; Genomic_DNA.
DR   RefSeq; NP_760325.1; -.
DR   HSSP; P17846; 1AOP.
DR   GeneID; 1178324; -.
DR   GenomeReviews; AE016795_GR; VV1_1403.
DR   KEGG; vvu:VV1_1403; -.
DR   HOGENOM; Q8DCK1; -.
DR   OMA; Q8DCK1; AFQFHGI.
DR   BioCyc; VVUL216895:VV1_1403-MON; -.
DR   BRENDA; 1.8.1.2; 277169.
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_0000199915.
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;  64943 MW;  146CF39788F73AD2 CRC64;
     MTFSIENNKQ VVLGEELGKL SDNERLKTQS NFLRGTIEQD LQDRITGGFT ADNFQLIRFH
     GMYQQDDRDI RNERAKQKLE PLHNVMLRAR MPGGIITPKQ WLAIDKFATE HSLYGSIRLT
     TRQTFQFHGV LKPNIKLMHQ TLNSIGIDSI ATAGDVNRNV LCTTNPVESE LHQEAYEWAK
     KISEHLLPKT KAYAEIWLDG EKVETTEDDE PILGKTYLPR KFKTTVVIPP QNDVDVHAND
     LNFVAIAEKG KLIGFNVLVG GGLAMTHGDT STYPRRADDF GYIPLEKTLD VAAAVVTTQR
     DWGNRSNRKN AKTKYTLDRV GTDVFKAEVE KRAGIKFEVS RPYEFTERGD RIGWVEGIDG
     KHHLTLFIEN GRLLDYPGKP LKTGVAEIAK IHKGDFRMTA NQNLIVAGVS KSNKAKIEKL
     AREHGLMDEG VSEQRKNAMA CVAFPTCPLA MAEAERFLPQ FVTDVEGILD KHGLDKEDNI
     ILRVTGCPNG CGRAMLAEIG LVGKAPGRYN LHLGGNRGGT RVPKMYKENI TDKQILEEID
     QLVGRWANER LPNECFGDFT VRVGIIEEVI ISKRDFYA
//