GenomeNet

Database: UniProt
Entry: D4CYL8_9FUSO
LinkDB: D4CYL8_9FUSO
Original site: D4CYL8_9FUSO 
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}.
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; 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
//
DBGET integrated database retrieval system