ID F7UVC4_EEGSY Unreviewed; 532 AA.
AC F7UVC4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:BAK45147.1};
GN Name=SdhA {ECO:0000313|EMBL:BAK45147.1};
GN OrderedLocusNames=EGYY_20570 {ECO:0000313|EMBL:BAK45147.1};
OS Eggerthella sp. (strain YY7918).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=502558 {ECO:0000313|EMBL:BAK45147.1, ECO:0000313|Proteomes:UP000008929};
RN [1] {ECO:0000313|EMBL:BAK45147.1, ECO:0000313|Proteomes:UP000008929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YY7918 {ECO:0000313|EMBL:BAK45147.1,
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; BAK45147.1; -; Genomic_DNA.
DR RefSeq; WP_013980391.1; NC_015738.1.
DR AlphaFoldDB; F7UVC4; -.
DR STRING; 502558.EGYY_20570; -.
DR KEGG; eyy:EGYY_20570; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_3_11; -.
DR OrthoDB; 3197124at2; -.
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; 2.
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 PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..532
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038695677"
FT DOMAIN 62..505
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 56618 MW; 88ADB27FC735B154 CRC64;
MKTISRRAFL SGSAAAGIGV AALGLAACSP SGDGAEKEPE KGAEESKETA KTYEPSQTVD
CDMVVVGGGN SGMSACLEGI EQGLNVVLLE KEPNLGGTLF GTEGILGLGS QLQLEKGIEL
PDRYQMVKEE LEYTNYRTDP LLWNDVIGAS GEDIDWLHEK GVQFPVMDNY LGQSAYSTFH
WWEGETGAAA VETLAGIIMQ SGATVMTSTP VVDLKVDNGK VVGVYAEAEN GDIVEVNAKA
VVLASGGIAN DLELLGEKMG WDLSEAQSLF PIHNVGDGIR MATGVGAKED VVSLMNVFSV
RNHAPTDPIT IGGTMQPVSL YVNEQGERFL SEDLCLKKFF ALLTNAFNAQ KQGFSIIDQG
VVDRMEGEGC FCGVAAVKAG DKLTGLKDQL EEACKETDPV AFRGETVAEL AQAMGVDPKT
LEATVARYNE LCAAGKDEDF GKDPAYLTPL EKGPFYAVTP VFSIFQTMGG ISIDRNMRVI
NENGEPIEGL YSAGTTSCGL YKETYCYQVS GGMNAYCCYT GRNAARQIAA SI
//
