ID   CYSI_AERHH              Reviewed;         570 AA.
AC   A0KNL0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, 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=AHA_3372;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(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.
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DR   EMBL; CP000462; ABK39442.1; -; Genomic_DNA.
DR   RefSeq; YP_857861.1; -.
DR   GeneID; 4490553; -.
DR   GenomeReviews; CP000462_GR; AHA_3372.
DR   KEGG; aha:AHA_3372; -.
DR   TIGR; AHA_3372; -.
DR   OMA; A0KNL0; 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    570       Sulfite reductase [NADPH] hemoprotein
FT                                beta-component.
FT                                /FTId=PRO_0000292957.
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   570 AA;  62961 MW;  3F7378CE7FDFC436 CRC64;
     MSKQLIPGPV EGPLADNERL KRESDHLRGT IAQDLTDPLT GGFNGDNFQL IRFHGMYQQD
     DRDIRPERTA QKLEPLHNVM LRARLPGGII TPAQWQVIDK FAEDHSLYGS IRLTTRQTFQ
     FHGVLKRDIK MMHQTLNSTG IDSIATAGDV NRNVLCTSNP VESELHQEAY EWAKKISEHL
     LPKTRAYVEI WLDGEKLGGD EEPILGSNYL PRKFKTTVVI PPHNDVDIHA NDLNFVAISD
     HGKLVGFNVL VGGGLAMTHG DTSTYPRKAS DFGFVPLSHV LEVAAAVVST QRDWGNRVNR
     KNAKTKYTLE RVGVEAFKAE VESRAGIQFG PVRPYEFTSR GDRFGWVEGI DGKHHLTLFI
     ENGRLLDFPG KPLKTGMLEI AKVHQGDFRL TANQNLIIAG VPAGEKARIE ALARQYGLLD
     DGVSEQRKQS MACVALPTCP LAMAEAERML PAFVTDIEGL LAKHELANDA IIFRVTGCPN
     GCGRAMLAEV GLVGKAPGRY NLHLGGNLEG TRIPRLHLEN ITEPQILAEL DALIGRWAKD
     RNAGECFGDF VIRAGIIAPV IDSARDFYAA
//