ID F7UWV4_EEGSY Unreviewed; 585 AA.
AC F7UWV4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=FAD-dependent oxidoreductase 2 FAD binding domain-containing protein {ECO:0000259|Pfam:PF00890};
GN OrderedLocusNames=EGYY_26720 {ECO:0000313|EMBL:BAK45671.1};
OS Eggerthella sp. (strain YY7918).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=502558 {ECO:0000313|EMBL:BAK45671.1, ECO:0000313|Proteomes:UP000008929};
RN [1] {ECO:0000313|EMBL:BAK45671.1, ECO:0000313|Proteomes:UP000008929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YY7918 {ECO:0000313|EMBL:BAK45671.1,
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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AP012211; BAK45671.1; -; Genomic_DNA.
DR RefSeq; WP_013980913.1; NC_015738.1.
DR AlphaFoldDB; F7UWV4; -.
DR STRING; 502558.EGYY_26720; -.
DR KEGG; eyy:EGYY_26720; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_3_11; -.
DR OrthoDB; 9813348at2; -.
DR Proteomes; UP000008929; Chromosome.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008929};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..585
FT /note="FAD-dependent oxidoreductase 2 FAD binding domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038550013"
FT DOMAIN 74..544
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT REGION 31..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 63453 MW; 8ECB4107037DEB97 CRC64;
MGNIELSRRA FFGLSATAAV AAGAGLAGCS PAATDQNKSE SQGASASNQS DTSTPSFMTP
PEPPTDIKEE KDCDVLVIGL GISGLAALKA AAEQGAKVIG IDKQAELCVI ADAGDFGIVN
SKIQKEIGIE WAPKSEVVNQ LMKDMCYRPN PDLLGYWYDH SGEDFDWYIE GADFEILPNT
WANKQTDKVN YIRPKCFPPL EGYDYKKEYY PYFHGSITTN PNANWASKAA YDSAVKAGAE
TMFSTWAEQL IVDDSGKIVG AYVHDIDDVY TKINAKAVCL CTGDIGGSQE MRDYYVPWAD
EFACVYYDND AKGVVANTGD GHKMGMWAGA HMELGPLAPM THHMGGAMGI NSYLQLNMEG
KRFMNEDIPG QNIADQMSRQ PGKQSWQIFD SKWPEQISLM PDGHGYANHY LTDEEAAELT
TVAESGWSLK LLGIATPSSI DEGSDVKADS IEELAKGMNL PVDVVKAEID RYNELCHKGI
DEDYGKIPTR LFPVETPPFY AIHFDAAGML VVMGGLECNT KLQPLDDESN PIEGLFVAGN
CMGGRFLVEY PVTVAGISLA TALSFGRMAG INAVGKEVID AKDRA
//
