ID   CYSI_COLP3              Reviewed;         584 AA.
AC   Q47UW8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, 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=CPS_4760;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ25063.1; -; Genomic_DNA.
DR   RefSeq; YP_271404.1; -.
DR   GeneID; 3518522; -.
DR   GenomeReviews; CP000083_GR; CPS_4760.
DR   KEGG; cps:CPS_4760; -.
DR   NMPDR; fig|167879.3.peg.4622; -.
DR   TIGR; CPS_4760; -.
DR   HOGENOM; Q47UW8; -.
DR   OMA; Q47UW8; TRQAFQM.
DR   BioCyc; CPSY167879:CPS_4760-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    584       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000292960.
FT   METAL       447    447       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       453    453       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       492    492       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       496    496       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       496    496       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   584 AA;  64788 MW;  136505C82F1E25E8 CRC64;
     MSNNFTKVEN PVLIVEGKQA DNERLKAESD YLRGTIKDDL QDRMTGGFTS DNFQLIRTHG
     MYQQDDRDIR AERQKQKLEP LHNVMLRARL PGGIINPTQW LAIDKFADDY TSYGSIRLTT
     RQTFQFHGVL KPNIKLMHQT LNSVGLDSIA TAGDVNRNVL CTSNPVESAL HQEAYEWATK
     ISEHLLPKTR AYAEIWLDEE KVETTEADEI EPILGSNYLP RKFKTTVVIP PNNDIDVHAN
     DLNFVAISEG GELIGFNVLV GGGLAMTHGD KATYPRCADD FGFIPKEHTL AIAAAVVTTQ
     RDWGNRVNRK NAKTKYTLDR VGVDTFKAEV ERRAGIKFSE SRSYEFTHRG DSFGWVEGID
     GKNHLTLFIE NGRILDFNGA NSDSKALKTG MREIAKIHKG DFRLTANQNL IVAGVSAEDK
     TIIEQLAREH GLINDGVSNQ RKSSMACVAF PTCPLAMAEA ERYLPGLVDD VEAILEKNGL
     KDDSIILRVT GCPNGCGRAM LAEIGLVGKG PGKYNMYLGS DLAGSRVPKL YKENVDEAGV
     LSEIDALSAR WSAERNDGEA FGDFVIRAGI VEQVIVSFRD FHHA
//