ID   CYSI_SODGM              Reviewed;         566 AA.
AC   Q2NVN3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-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=SG0517;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA   Hattori M., Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights
RT   into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT   host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE73792.1; -; Genomic_DNA.
DR   RefSeq; YP_454197.1; -.
DR   GeneID; 3868218; -.
DR   GenomeReviews; AP008232_GR; SG0517.
DR   KEGG; sgl:SG0517; -.
DR   NMPDR; fig|343509.6.peg.1172; -.
DR   HOGENOM; Q2NVN3; -.
DR   OMA; Q2NVN3; TRQAFQM.
DR   BioCyc; SGLO343509:SG0517-MON; -.
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    566       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000292964.
FT   METAL       430    430       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       436    436       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       475    475       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       479    479       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       479    479       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   566 AA;  63389 MW;  5EA815C37573BFD5 CRC64;
     MSEQQPKAKF SDNERLKGES RFLRGTIAQD LQDGLTGGFN GDNFQLIRFH GMYQQDDRDL
     RAERAEEKLE PLINMMLRCR LPGGVITPQQ WLGIDAFAAE QTLYGSIRLT TRQTFQFHGV
     LKPKLKGMHQ LLHCLGLDSI ATAGDVNRNV LCTSNPVESV LHRQAWEWAK KISEHLLPKT
     RAYAEIWLDG EKTETTDQEP ILGPTYLPRK FKTTVVVPPL NDVDLHANDL NFVAISDNGQ
     LVGFNVLVGG GLAMTHGDKS TYPRKASEFG FIALDDTLKI AEAVVTTQRD WGNRSNRKNA
     KTKYTLESEG VGAFREEVEV RAGVQFAPIR PYAFTERGDR FGWVKGIDNQ WHLTLFIENG
     RILDYPDRTL KTGLAEIARR HKGDFRLTAN QNLIIAGVDK KDKAAIEALA RRHGLINDDA
     TPQRKASMAC VAFPTCPLAM AEAERFLPQF VSNVETIMSG HGLAEDEIIL RVTGCSNGCG
     RAMLAEIGLV GKAIGRYNLY LGGDRIGTRI PRIYRENITE DEILSIIDDT AGRWARERQP
     QESYGDYLVR AGIVRPVVDS ARDFYD
//