ID Q8XKG1_CLOPE Unreviewed; 263 AA.
AC Q8XKG1;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Anaerobic sulfite reductase subunit B {ECO:0000313|EMBL:BAB81145.1};
GN Name=asrB {ECO:0000313|EMBL:BAB81145.1};
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81145.1, ECO:0000313|Proteomes:UP000000818};
RN [1] {ECO:0000313|EMBL:BAB81145.1, ECO:0000313|Proteomes:UP000000818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81145.1; -; Genomic_DNA.
DR RefSeq; WP_003457280.1; NC_003366.1.
DR AlphaFoldDB; Q8XKG1; -.
DR STRING; 195102.gene:10490703; -.
DR GeneID; 69449346; -.
DR KEGG; cpe:CPE1439; -.
DR HOGENOM; CLU_003827_1_1_9; -.
DR Proteomes; UP000000818; Chromosome.
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; PR00410; PHEHYDRXLASE.
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:UP000000818}.
FT DOMAIN 5..96
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 231
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 236
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 239
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 247
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 263 AA; 29755 MW; 89F6E57880EAAC58 CRC64;
MHNEYTPFIS KILNVKKHTD IEYTFRMEFK GDVKPGQFFE VSLPKFGEAP ISVSGIGEDY
VELTIRRVGV VTNEIFEKYE GDKLFLRGPY GNGFDVNNYK GKEVIVVAGG TGLSPVKGIV
DYFSQNPKDA ESFTLISGFK GPKDILFKDD MKEWEKNMNM IITVDSAEEG YEGNTGLVTK
YIPELEIKDM DNVQVIVVGP PMMMKFTVLE FLKRGIKEEN IWISQERKMC CGLGKCGHCK
IDDTYICLDG PVFNYTKGKL LID
//
