ID C8WJU4_EGGLE Unreviewed; 588 AA.
AC C8WJU4;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ACV54176.1};
DE Flags: Precursor;
GN OrderedLocusNames=Elen_0182 {ECO:0000313|EMBL:ACV54176.1};
OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=479437 {ECO:0000313|EMBL:ACV54176.1, ECO:0000313|Proteomes:UP000001377};
RN [1] {ECO:0000313|EMBL:ACV54176.1, ECO:0000313|Proteomes:UP000001377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 /
RC NCTC 11813 / VPI 0255 / 1899 B {ECO:0000313|Proteomes:UP000001377};
RX PubMed=21304654; DOI=10.4056/sigs.33592;
RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT 0255).";
RL Stand. Genomic Sci. 1:174-182(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP001726; ACV54176.1; -; Genomic_DNA.
DR RefSeq; WP_009608969.1; NC_013204.1.
DR AlphaFoldDB; C8WJU4; -.
DR STRING; 479437.Elen_0182; -.
DR PaxDb; 479437-Elen_0182; -.
DR KEGG; ele:Elen_0182; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_3_11; -.
DR OrthoDB; 9813348at2; -.
DR BioCyc; ELEN479437:G1GFY-191-MONOMER; -.
DR Proteomes; UP000001377; Chromosome.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0008202; P:steroid metabolic process; 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; 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:UP000001377};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..588
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039097088"
FT DOMAIN 86..555
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 588 AA; 62634 MW; CAB00EB18225E8BD CRC64;
MREQKLTRRT FLGLGATAAV AGAAGLAGCA PGAKSDAGAD AGAAEGGAAG AGGAAAGGNP
TEFVPSFMNP PAPVDESKVT ETVDVDVCVV GLGLAGVCAL REAAESGAKT FGFDKGSDVG
YRSGEFGTFG SEIHKQLGIE QPETQEVVNE LMKVMGNRPN AQLLNYWIAN SGPDLDWYIG
TAEHELLTSD HDVPTDPEKP YVFPERFPVN ENYNWREENY PCFPGMVHLL PDHGWAMHGT
LEAAQKAGAE ARFNLKGEQL IKEGDKVVGV YASDEDGNIV RINAKKGVVL SCGDMSSDTE
MLTYYAPQAT KYGCFFSTMD KSGKPVNTGD GHKMAMWAGA VMEDGPYAPM THSLGTNSVG
IDPFLMVNQD GKRFANEDVG AQELQNAIKR QKGGVSYQIF DSKWKEQLSA MPQCFGGVTH
YIPPEQEAEY EHAINHFAAG YASDTYFQGE IEQGSIIPAD SIEELAKAVN IPADALVETV
ERYNELAHAG KDADFSKVST RLFPVENPPY YAVPFGDSGM LVLIGGIDCD VDCRALDAEK
NPVPGLFVAG NTMGGRFLVD YPVTVAGASH SMAMSFGRLA GRKAAEGK
//
