ASRB_SALTY
ID ASRB_SALTY Reviewed; 272 AA.
AC P26475;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Anaerobic sulfite reductase subunit B;
GN Name=asrB; OrderedLocusNames=STM2549;
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
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. Repressed by oxygen.
CC -!- SIMILARITY: Belongs to the PyrK 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; M57706; AAA99276.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21443.1; -; Genomic_DNA.
DR PIR; B38453; B38453.
DR RefSeq; NP_461484.1; NC_003197.2.
DR RefSeq; WP_000017587.1; NC_003197.2.
DR AlphaFoldDB; P26475; -.
DR SMR; P26475; -.
DR STRING; 99287.STM2549; -.
DR PaxDb; P26475; -.
DR EnsemblBacteria; AAL21443; AAL21443; STM2549.
DR GeneID; 1254071; -.
DR KEGG; stm:STM2549; -.
DR PATRIC; fig|99287.12.peg.2689; -.
DR HOGENOM; CLU_003827_1_1_6; -.
DR OMA; NTARYGK; -.
DR PhylomeDB; P26475; -.
DR BioCyc; MetaCyc:MON-12545; -.
DR BioCyc; SENT99287:STM2549-MON; -.
DR UniPathway; UPA00370; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR014260; Sulphite_reductase_B.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR TIGRFAMs; TIGR02911; sulfite_red_B; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Cytoplasm; Electron transport; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; NAD; Reference proteome; Transport.
FT CHAIN 1..272
FT /note="Anaerobic sulfite reductase subunit B"
FT /id="PRO_0000148385"
FT DOMAIN 14..105
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 113..129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 168..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 245
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 248
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 256
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT CONFLICT 16
FT /note="P -> A (in Ref. 1; AAA99276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 30609 MW; 5C73ACCC200AE302 CRC64;
MSHCSCHDKP QHSLLPAAYR ILSITRHTPL EWNFRVAVDF PAHWGQFVEV SLPRVGEAPI
SVSDYGDGWI DLLIRNVGKV TSALFTLKEG DNVWLRGCYG NGYPVDTLRH KPLLVVAGGT
GVAPVKGLMR YFVENPQEIG QLDMILGYKN RDCVLYKEEM ATWRGKHNLV LTLDEGEADD
RYQIGRVTDR LADMTLSDID TMQAIVVGPP IMITFTVKML LQKGLKPEQI WVDYERRMAC
SVGKCGHCRM GEVYVCTDGP IFNYAVAQRF AD
