ID CYSI_SALTY Reviewed; 570 AA. AC P17845; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 161. 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=STM2947; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX PubMed=2670946; DOI=10.1016/s0021-9258(19)84893-7; RA Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M., RA Kredich N.M.; RT "Characterization of the cysJIH regions of Salmonella typhimurium and RT Escherichia coli B. DNA sequences of cysI and cysH and a model for the RT siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on RT amino acid homology with spinach nitrite reductase."; RL J. Biol. Chem. 264:15726-15737(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: Component of the sulfite reductase complex that catalyzes the CC 6-electron reduction of sulfite to sulfide. This is one of several CC activities required for the biosynthesis of L-cysteine from sulfate. CC -!- CATALYTIC ACTIVITY: CC Reaction=hydrogen sulfide + 3 NADP(+) + 3 H2O = sulfite + 3 NADPH + 4 CC H(+); Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.8.1.2; CC -!- COFACTOR: CC Name=siroheme; Xref=ChEBI:CHEBI:60052; CC Note=Binds 1 siroheme per subunit.; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster per subunit.; CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen CC sulfide from sulfite (NADPH route): step 1/1. CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the CC beta component is a hemoprotein. CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M23007; AAA27047.1; -; Genomic_DNA. DR EMBL; AE006468; AAL21827.1; -; Genomic_DNA. DR PIR; A34354; A34354. DR RefSeq; NP_461868.1; NC_003197.2. DR RefSeq; WP_001290660.1; NC_003197.2. DR AlphaFoldDB; P17845; -. DR SMR; P17845; -. DR STRING; 99287.STM2947; -. DR PaxDb; 99287-STM2947; -. DR GeneID; 1254470; -. DR KEGG; stm:STM2947; -. DR PATRIC; fig|99287.12.peg.3108; -. DR HOGENOM; CLU_001975_3_2_6; -. DR OMA; IKISGCM; -. DR PhylomeDB; P17845; -. DR BioCyc; SENT99287:STM2947-MONOMER; -. DR UniPathway; UPA00140; UER00207. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule. DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central. DR FunFam; 3.30.413.10:FF:000003; Sulfite reductase [NADPH] hemoprotein beta-component; 1. DR FunFam; 3.30.413.10:FF:000004; Sulfite reductase [NADPH] hemoprotein beta-component; 1. DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2. DR HAMAP; MF_01540; CysI; 1. DR InterPro; IPR011786; CysI. DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer. DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf. DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom. DR InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot. DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf. DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS. DR NCBIfam; TIGR02041; CysI; 1. DR NCBIfam; NF010029; PRK13504.1; 1. DR PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1. DR PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1. DR Pfam; PF01077; NIR_SIR; 1. DR Pfam; PF03460; NIR_SIR_ferr; 2. DR PRINTS; PR00397; SIROHAEM. DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2. DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2. DR PROSITE; PS00365; NIR_SIR; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis; Heme; Iron; KW Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..570 FT /note="Sulfite reductase [NADPH] hemoprotein beta- FT component" FT /id="PRO_0000199908" FT BINDING 434 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 440 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 479 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 483 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 483 FT /ligand="siroheme" FT /ligand_id="ChEBI:CHEBI:60052" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" SQ SEQUENCE 570 AA; 64023 MW; 62A9B26F077443C7 CRC64; MSEKHPGPLV VEGKLSDAER MKLESNYLRG TIAEDLNDGL TGGFKGDNFL LIRFHGMYQQ DDRDIRAERA AQKLEPRHAM LLRCRLPGGV ITTTQWQAID KFAADNTIYG SIRLTNRQTF QFHGILKKNV KPVHQMLHSV GLDALATAND MNRNVLCTSN PYESQLHAEA YEWAKKISEH LLPRTRAYAE IWLDQEKVAT TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI AENGKLVGFN LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT DRKNAKTKYT LERVGLETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK GIDDKWHLTL FIENGRILDY PGRPLKTGLL EIAKIHQGEF RITANQNLII ASVPESQKAK IETLARDHGL MNAVKPQREN SMACVSFPTC PLAMAEAERF LPSFTDKVEA ILEKHGIPDE HIVMRVTGCP NGCGRAMLAE IGLVGKAPGR YNLHLGGNRI GSRIPRMYKE NIAEPDILAS LDELIGRWAK EREAGEGFGD FTVRAGIIRP VLDPARDFWE //