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};
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; 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
//