ID   CYSI_SHESR              Reviewed;         565 AA.
AC   Q0HYB3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=Shewmr7_0893;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000444; ABI41892.1; -; Genomic_DNA.
DR   RefSeq; YP_736949.1; -.
DR   GeneID; 4256545; -.
DR   GenomeReviews; CP000444_GR; Shewmr7_0893.
DR   KEGG; shm:Shewmr7_0893; -.
DR   HOGENOM; Q0HYB3; -.
DR   OMA; Q0HYB3; 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    565       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_1000068773.
FT   METAL       429    429       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       435    435       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       474    474       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       478    478       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       478    478       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   565 AA;  62971 MW;  21367FC10822A517 CRC64;
     MSEQKLALNE YLKTDSDYLR GTIKEGLDSS VTGSFSDGDQ QLIKFHGFYQ QDDRDLRNER
     KEQKLEPLYS FMLRARVPGG VCTPKQWLGV DEIASTLTSS NSIRLTTRQT FQYHGIPKRN
     LKTIIQGLDR EALDSIAACG DVNRNVMCNP NPVESKLHAQ AYEVAKKLSD HLLPHTRAYA
     EIWLDEEKLL TTEDETVEPV YGKTYLPRKF KMAVAVPPDN DVDVYTNDLG FIAVAENGEL
     VGFNLTAGGG MGSTHGEVET FPRLADDFGF IKTEDVMKFA EAVMTVQRDW GNRTNRKRSR
     LKYTIVDHGY EKFKAEVEAR AGVKFEPKRD VVIGDRGDRY GWVEGVDGKW HLTLFIESGR
     IKDVPGKSLQ TGMREIAKIH KGDFRMTSNQ NMIIAGVAPE DKATIEGLAR KHGLLGQVLT
     QTRGHSIACV ALPTCPLAMA EAERYFPEFI DHIDALQAKN GISDQAIVVR MTGCPNGCAR
     PFAAEIGLVG KAPGRYNLYL GANFEGTRLN KMYRENIQEA EILAELDALF ARYAVERNAG
     ETFGNFTVRT GVVKAVIDAA KDFHG
//