ID   A0A1G9ZJU9_9FIRM        Unreviewed;       269 AA.
AC   A0A1G9ZJU9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Anaerobic sulfite reductase subunit B {ECO:0000313|EMBL:SDN20793.1};
GN   ORFNames=SAMN05660299_02325 {ECO:0000313|EMBL:SDN20793.1};
OS   Megasphaera paucivorans.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=349095 {ECO:0000313|EMBL:SDN20793.1, ECO:0000313|Proteomes:UP000199309};
RN   [1] {ECO:0000313|EMBL:SDN20793.1, ECO:0000313|Proteomes:UP000199309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16981 {ECO:0000313|EMBL:SDN20793.1,
RC   ECO:0000313|Proteomes:UP000199309};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR006816-2};
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DR   EMBL; FNHQ01000030; SDN20793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9ZJU9; -.
DR   STRING; 349095.SAMN05660299_02325; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000199309; Unassembled WGS sequence.
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   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; 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   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   PRINTS; PR00406; CYTB5RDTASE.
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   4: Predicted;
KW   2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199309}.
FT   DOMAIN          6..101
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         237
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         242
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         245
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         253
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   269 AA;  30181 MW;  929E0F4CD6E1064E CRC64;
     MAKNEYLPFR STILKVIRHS EKEYTFRMAY DKANEFPVKP GQFFEISIPK YGEAPISVSG
     ITHHSLDFTI RRVGSLTDEI FENYEGGSFF MRGPYGNGFD VTMFKDKDIV LVAGGSGLSP
     VHGVIDYFAD HMEECRSLTV IAGFKSIEDI LFRADIVRWK EDGICIIDTV DAAPEGYTGR
     TGMVTKYISA LQFKNMAHVI AVVVGPPPMI KWSIKGLKDI GVDEEDIWLS ESRKMCCGLG
     KCGHCRIGDI YVCQDGPVFK YTKLRTLID
//