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Database: UniProt
Entry: F7V0T4_EEGSY
LinkDB: F7V0T4_EEGSY
Original site: F7V0T4_EEGSY 
ID   F7V0T4_EEGSY            Unreviewed;       303 AA.
AC   F7V0T4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   03-MAY-2023, entry version 60.
DE   SubName: Full=2-polyprenylphenol hydroxylase {ECO:0000313|EMBL:BAK44377.1};
GN   Name=UbiB {ECO:0000313|EMBL:BAK44377.1};
GN   OrderedLocusNames=EGYY_12120 {ECO:0000313|EMBL:BAK44377.1};
OS   Eggerthella sp. (strain YY7918).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=502558 {ECO:0000313|EMBL:BAK44377.1, ECO:0000313|Proteomes:UP000008929};
RN   [1] {ECO:0000313|EMBL:BAK44377.1, ECO:0000313|Proteomes:UP000008929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YY7918 {ECO:0000313|EMBL:BAK44377.1,
RC   ECO:0000313|Proteomes:UP000008929};
RX   PubMed=21914883;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete Genomic Sequence of the Equol-Producing Bacterium Eggerthella sp.
RT   Strain YY7918, Isolated from Adult Human Intestine.";
RL   J. Bacteriol. 193:5570-5571(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YY7918 {ECO:0000313|Proteomes:UP000008929};
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genome sequence of the equol-producing bacterium Eggerthella sp.
RT   strain YY7918 isolated from adult human intestine.";
RL   Submitted (JUN-2011) 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; AP012211; BAK44377.1; -; Genomic_DNA.
DR   RefSeq; WP_013979627.1; NC_015738.1.
DR   AlphaFoldDB; F7V0T4; -.
DR   STRING; 502558.EGYY_12120; -.
DR   KEGG; eyy:EGYY_12120; -.
DR   eggNOG; COG0543; Bacteria.
DR   HOGENOM; CLU_003827_1_1_11; -.
DR   OMA; NTARYGK; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000008929; 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; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR   InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   PRINTS; PR00371; FPNCR.
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:UP000008929}.
FT   DOMAIN          33..133
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         269
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         274
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         277
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         285
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   303 AA;  34109 MW;  86D55A874899C3F0 CRC64;
     MPNSCAVSTV QVAPFVDTPS PLSGTELMAA NPYRPWPARI TSIVELTATE KLFEFRLIDE
     RIREAFRHEP GQFVEVSIFG VGEAPISISS SPSKHGFIEL CVRRTGAFTE VLHTMQCGDI
     VGLRGPFGRG FPFEEMKGHD ILLVAGGLGI APLRSLINNI HDERSEFGNV TIIYGSKNPS
     EVMFRQQFEM WRHRKDFDLY LTVDHPDATW DGEVGLVTKP FEHLDIDATN TFGAVCGPPV
     MYRFVIDEMR KKNISYDHIY VSFERHMKCG MGKCGHCQIG HQYVCIDGPV FNYWEAKNIQ
     GSM
//
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