ID   CYSI_VIBC3              Reviewed;         577 AA.
AC   A5F3I5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
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=VC0395_A2796;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Heidelberg J.;
RL   Submitted (MAR-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; CP000627; ABQ21061.1; -; Genomic_DNA.
DR   RefSeq; YP_001218654.1; -.
DR   RefSeq; YP_002818687.1; -.
DR   GeneID; 5135522; -.
DR   GeneID; 7776748; -.
DR   GenomeReviews; CP000627_GR; VC0395_A2796.
DR   KEGG; vco:VC0395_A2796; -.
DR   OMA; A5F3I5; TRQAFQM.
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    577       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_1000073552.
FT   METAL       440    440       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       446    446       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       486    486       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       490    490       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       490    490       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   577 AA;  64371 MW;  807070BF8B98E6DA CRC64;
     MSANQNPSVQ EVLGEVLGPW SDNERLKRES HFLRGTIEQD LQDRITGGFT ADNFQLIRFH
     GMYQQDDRDI RAERSKQKLE PLHNVMLRAR MPGGIITPHQ WLAIDKFATE HTLYGSIRLT
     TRQTFQFHGV LKPNIKLMHQ TLNSIGIDSI ATAGDVNRNV LCTSNPVESQ LHLQAYEWAK
     KISEHLLPKT RAYAEIWLDG EKIEGPDEEP ILGSNYLPRK FKTTVVIPPH NDVDVHANDL
     NFVAIGENGQ LIGFNVLVGG GLAMTHGDTS TYPRRADDFG FIPLEKTLEV AAAVVSTQRD
     WGNRSNRKNA KTKYTLDRVG VEVFKAEVEK RAGITFAPSR AYEFTSRGDR IGWVEGIDGK
     HHLTLFIENG RILDFPGKPL KTGVAEIAKV HQGDFRMTAN QNLIVAGVPA DQKQQIEQLA
     RSHGLIDDGV SEQRINSMAC VAFPTCPLAM AEAERFLPSF VTEVEGILAK HALPKEENII
     LRVTGCPNGC GRAMLAEIGL VGKAPGRYNL HLGGNRNGTR IPKMYKENIT DTQILQEIDE
     LVGRWASERL DGEGFGDFTI RAGIIEEVII SKRDFYA
//