ID CYSI_YERPP Reviewed; 576 AA. AC A4TPY6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, 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=YPDSF_2988; OS Yersinia pestis (strain Pestoides F). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Yersinia. OX NCBI_TaxID=386656; 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., Di Bartolo G., Chain P., Malfatti S., Shin M., Vergez L., RA Schmutz J., Larimer F., Land M., Hauser L., Worsham P., Chu M., RA Bearden S., Garcia E., Richardson P.; RT "Complete sequence of chromosome of Yersinia pestis Pestoides F."; RL Submitted (FEB-2007) 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; CP000668; ABP41348.1; -; Genomic_DNA. DR RefSeq; YP_001164321.1; -. DR GeneID; 5062879; -. DR GenomeReviews; CP000668_GR; YPDSF_2988. DR KEGG; ypp:YPDSF_2988; -. DR OMA; A4TPY6; 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 1 576 Sulfite reductase [NADPH] hemoprotein FT beta-component. FT /FTId=PRO_1000068784. FT METAL 435 435 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 441 441 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 480 480 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 484 484 Iron (siroheme axial ligand) (By FT similarity). FT METAL 484 484 Iron-sulfur (4Fe-4S) (By similarity). SQ SEQUENCE 576 AA; 64076 MW; 28AA6EF7463B6B87 CRC64; MNEKHPGPLV VSGKLSDGER MKSESNFLRG TIAEDLNNGL TGGFSGDNFL LIRFHGMYQQ DDRDIRAERA EQKLEPRHAM MLRCRLPGGI ITPQQWLGID KFAADNTLYG SIRITNRQTF QFHGILKGNV KPAHQLLNEL GLDALATAND VNRNVLCTSN PVESALHQEA YEWAKKISEH LLPRTRAYAE IWLDAEKVAT TDEEPILGAT YLPRKFKTTV VIPPQNDVDL HANDLNFVAV ADKGKLIGFN VLVGGGLSIA HGDKNTYPRK ASEFGYIPLK HTLAIAEAVV TTQRDWGNRT DRKNAKTKYT LERVGVETFK AEVEKRAGVS FSAIKPYQFI GRGDRIGWVK GVDKKWHLTL FVENGRLLDY PGRSLKTGVA EIAKIHQGDF RLTANQNLIV AGVPEKDKAR IEALAREHGL MDDNVTSQRE NSMACVSFPT CPLAMAEAER FLPEFVTRVE GILQQHGLAD EHIVLRVTGC PNGCGRALLA EVGLVGKAVG RYNLHLGGNR EGTRIPRMYR ENITADEILL ITDQLVGRWA KERHVDEGFG DFVIRAGVIA PVIDSARDFY DVQEAM //