ID D4CYL8_9FUSO Unreviewed; 267 AA.
AC D4CYL8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Sulfite reductase, subunit B {ECO:0000313|EMBL:EFE85555.1};
DE EC=1.8.-.- {ECO:0000313|EMBL:EFE85555.1};
GN Name=asrB {ECO:0000313|EMBL:EFE85555.1};
GN ORFNames=FUSPEROL_02533 {ECO:0000313|EMBL:EFE85555.1};
OS Fusobacterium periodonticum ATCC 33693.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=546275 {ECO:0000313|EMBL:EFE85555.1, ECO:0000313|Proteomes:UP000003748};
RN [1] {ECO:0000313|EMBL:EFE85555.1, ECO:0000313|Proteomes:UP000003748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33693 {ECO:0000313|EMBL:EFE85555.1,
RC ECO:0000313|Proteomes:UP000003748};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE85555.1}.
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DR EMBL; ACJY01000111; EFE85555.1; -; Genomic_DNA.
DR RefSeq; WP_005975760.1; NZ_GG665898.1.
DR AlphaFoldDB; D4CYL8; -.
DR STRING; 546275.FUSPEROL_02533; -.
DR GeneID; 78420677; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_1_0; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000003748; 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:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:EFE85555.1}.
FT DOMAIN 8..100
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 235
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 240
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 243
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 251
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 267 AA; 29810 MW; 869B2062FF61E7EE CRC64;
MCNCDNPYIP CPAEIIEIIE HTDIEWTFRV KADTSKTKPG QFYEISLPKF GESPISVSGI
GPDFIDFTIR AVGRVTNEIF EYKIGDKLFI RGPYGNGFNL DEYVGKDLVI VVGGSALAPV
RGIIQFVYNN PEKVKSFKLI AGFKSPKDVL FAKDLEEWSK KLDVVLTVDG AEEGYKGNIG
LVTKYIPELK FNDLSNVSAV VVGPPMMMKF SVAEFLKLNV AEKNIWVSYE RNMHCGIGKC
GHCKMDATYI CLDGPVFDYE FAKNLVD
//