CYSI_SALTY
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 03-AUG-2022, entry version 148.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH +
CC sulfite; 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}.
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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; P17845; -.
DR EnsemblBacteria; AAL21827; AAL21827; STM2947.
DR GeneID; 1254470; -.
DR KEGG; stm:STM2947; -.
DR PATRIC; fig|99287.12.peg.3108; -.
DR HOGENOM; CLU_001975_3_2_6; -.
DR OMA; MGMTHGD; -.
DR PhylomeDB; P17845; -.
DR BioCyc; SENT99287:STM2947-MON; -.
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:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IBA:GO_Central.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR Gene3D; 3.30.413.10; -; 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 PANTHER; PTHR11493; PTHR11493; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF55124; SSF55124; 2.
DR SUPFAM; SSF56014; SSF56014; 2.
DR TIGRFAMs; TIGR02041; CysI; 1.
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
