ID   CYSI_PSEA6              Reviewed;         569 AA.
AC   Q15NK1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=Patl_4038;
OS   Pseudoalteromonas atlantica (strain T6c / BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-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.
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DR   EMBL; CP000388; ABG42537.1; -; Genomic_DNA.
DR   RefSeq; YP_663591.1; -.
DR   GeneID; 4175827; -.
DR   GenomeReviews; CP000388_GR; Patl_4038.
DR   KEGG; pat:Patl_4038; -.
DR   NMPDR; fig|342610.3.peg.2295; -.
DR   HOGENOM; Q15NK1; -.
DR   OMA; Q15NK1; TRQAFQM.
DR   BioCyc; PATL342610:PATL_4038-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    569       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000292961.
FT   METAL       433    433       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       439    439       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       478    478       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       482    482       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       482    482       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   569 AA;  63144 MW;  46A2EFB0690E54C4 CRC64;
     MTTDNKFVVE GKLADNERLK GESNFLRGTI AEDLKDDLTG AFVGDNFQLI RFHGMYQQDD
     RDLRAERAKQ KLEPLQNVML RARLPGGIIK PQQWLAIDKF AEEKSLYGSI RLTTRQTFQF
     HGVLKPNIKL MHQTLNQVGI DSIATAGDVN RNVLCTSNPI ESAVHQEAYE WATKISEHLL
     PKTRAYAEIW LDGEKKETTD HEPILGANYL PRKFKTTVAI PPLNDVDVHA NDLNFIAISK
     DGKLVGFNVL VGGGLAMTHG DHATFPRKAS DFGFIKVEDT LAIAEAVVST QRDWGNRVNR
     KNAKTKYTLE RVGVENFKAE VEKRSGVTFG ESQAYEFTER GDRIGWVEGI DGKHHLTLFI
     ENGRILDYPG KPLKTGCAEI AKIHDGDFRL TANQNLIVAG VSEQNKAKVE EIARAHGLIE
     DDLSAQRKDS MACVALPTCP LAMAEAERYL PEAVTQLEGI LAKHAIAQKS IIYRVTGCPN
     GCGRSMLAEI GLVGKGPGKY NLHLGGNRQG TRIPKMYKEN IGEQQIMDEL DVLIGQWAKE
     AQSDESFGDF VIRTGVIAEV VNSAEDFYA
//