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 04-NOV-2026, entry version 154. DE RecName: Full=Anaerobic sulfite reductase subunit B; GN Name=asrB; OrderedLocusNames=STM2549; 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=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; 99287-STM2549; -. DR GeneID; 1254071; -. DR KEGG; stm:STM2549; -. DR PATRIC; fig|99287.12.peg.2689; -. DR HOGENOM; CLU_003827_1_1_6; -. DR OMA; AADNVYM; -. DR PhylomeDB; P26475; -. DR BioCyc; MetaCyc:MONOMER-12545; -. DR BioCyc; SENT99287:STM2549-MONOMER; -. 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:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro. DR CDD; cd06221; sulfite_reductase_like; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR InterPro; IPR014260; AsrB. 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 NCBIfam; TIGR02911; sulfite_red_B; 1. DR PANTHER; PTHR43513:SF1; ANAEROBIC SULFITE REDUCTASE SUBUNIT B; 1. DR PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1. 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; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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 //