ASRC_SALTY
ID ASRC_SALTY Reviewed; 337 AA.
AC P0A1Y2; P26476;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Anaerobic sulfite reductase subunit C;
DE EC=1.8.1.-;
GN Name=asrC; OrderedLocusNames=STM2550;
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=EB303;
RX PubMed=1704886; DOI=10.1128/jb.173.4.1544-1553.1991;
RA Huang C.J., Barrett E.L.;
RT "Sequence analysis and expression of the Salmonella typhimurium asr operon
RT encoding production of hydrogen sulfide from sulfite.";
RL J. Bacteriol. 173:1544-1553(1991).
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: This enzyme catalyzes the hydrogen sulfide production from
CC sulfite. It is strictly anaerobic. It is regulated by electron
CC acceptors rather than by cysteine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 3 NAD(+) = 4 H(+) + 3 NADH +
CC sulfite; Xref=Rhea:RHEA:55316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 3 [4Fe-4S] clusters per subunit.;
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Note=Binds 1 siroheme per subunit.;
CC -!- PATHWAY: Sulfur metabolism; sulfite reduction.
CC -!- SUBUNIT: The anaerobic sulfite reductase seems to consist of three
CC subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By sulfite.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000305}.
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DR EMBL; M57706; AAA99277.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21444.1; -; Genomic_DNA.
DR PIR; C38453; C38453.
DR RefSeq; NP_461485.1; NC_003197.2.
DR RefSeq; WP_000020685.1; NC_003197.2.
DR AlphaFoldDB; P0A1Y2; -.
DR SMR; P0A1Y2; -.
DR STRING; 99287.STM2550; -.
DR PaxDb; P0A1Y2; -.
DR PRIDE; P0A1Y2; -.
DR DNASU; 1254072; -.
DR EnsemblBacteria; AAL21444; AAL21444; STM2550.
DR GeneID; 1254072; -.
DR KEGG; stm:STM2550; -.
DR PATRIC; fig|99287.12.peg.2690; -.
DR HOGENOM; CLU_072599_1_0_6; -.
DR OMA; KVRMHDF; -.
DR PhylomeDB; P0A1Y2; -.
DR BioCyc; MetaCyc:MON-12546; -.
DR BioCyc; SENT99287:STM2550-MON; -.
DR UniPathway; UPA00370; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0050311; F:sulfite reductase (ferredoxin) activity; IBA:GO_Central.
DR GO; GO:0016002; F:sulfite reductase activity; IBA:GO_Central.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR Gene3D; 3.30.413.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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 InterPro; IPR014261; Sulphite_reductase_C.
DR PANTHER; PTHR11493; PTHR11493; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF55124; SSF55124; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR02912; sulfite_red_C; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cytoplasm; Electron transport; Heme; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..337
FT /note="Anaerobic sulfite reductase subunit C"
FT /id="PRO_0000199965"
FT DOMAIN 171..200
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 203..232
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
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"
FT BINDING 180
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 247..250
FT /note="TPRV -> SGAL (in Ref. 1; AAA99277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37291 MW; 183FE2F669B34CBF CRC64;
MSIDIDIIKA RAKNEYRLSK VRGEAMISVR IPGGILPAHL LTVARDIAET WGNGQIHLTT
RQKLAMPGIR YEDIDNVNAA LEPFLREIEI ELCDVQVEDT KAGYLAIGGR NIVACQGNRI
CQKANTDTTG LSRRLEKLVY PSPYHLKTVI VGCPNDCAKA SMADLGIIGV AKMRFTADRC
IGCGACVKAC SHHAVGCLAL KNGKAVKEES ACIGCGECVL ACPTLAWQRK PDQLWQVRLG
GRTSKKTPRV GKLFLNWVTE DVIKQVIVNL YEFEKEMLGG KPIYLHMGHL IDKGGYLRFK
ERVLRGVQLN PEAMVAERIY WAEDESVARM HLKPAGH
