ID C8WJ63_EGGLE Unreviewed; 512 AA.
AC C8WJ63;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ACV54065.1};
DE Flags: Precursor;
GN OrderedLocusNames=Elen_0071 {ECO:0000313|EMBL:ACV54065.1};
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:ACV54065.1, ECO:0000313|Proteomes:UP000001377};
RN [1] {ECO:0000313|EMBL:ACV54065.1, 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; ACV54065.1; -; Genomic_DNA.
DR RefSeq; WP_015759798.1; NC_013204.1.
DR AlphaFoldDB; C8WJ63; -.
DR STRING; 479437.Elen_0071; -.
DR PaxDb; 479437-Elen_0071; -.
DR KEGG; ele:Elen_0071; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_5_11; -.
DR OrthoDB; 9813348at2; -.
DR BioCyc; ELEN479437:G1GFY-76-MONOMER; -.
DR Proteomes; UP000001377; 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; 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}.
FT DOMAIN 48..482
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 512 AA; 53531 MW; 763DDA3238CDBEB1 CRC64;
MGSTFTRRQF VMGAMVLGGS LALTGCSPKP ESKKQDGASG ATEPVQADII VIGSGLAGSA
CSISAAQNGA SVLLVDKAPF LTSTFLTSKG NVSIAQVPEN KDEWRFESET PDTMDQFVSR
YRNLTEIGKV DAPYPDYSRM QRMMEESCAT IAWVEQLGIT FEKSFTKEMV GTDTVKPDVS
ADPATEAGVQ VANAFAAEFE RLGVRTMLSA EAKELIMDGD AVVGVKVEGP DGVQELRAKA
VVLATGGFGG SAEYCDQLVP AINEMGFQYL GNAMNTGDGM TMASAIGAAL YEDPWVIPNV
IMPTRTLTKA DAGFKKLCDT GMEGAATSSK MLVDSTGARF VNEAAPVTAL ATSMTDNQAG
PYYVLFDSSN AEVVAVIEKG LSTGDVLKGV SIEELADAAG APQLAATFEA YQQAAAAGAD
EAFGKKADML AAYGDGPFYL VKFVPSYVAT MGGVKTDASC QALGENGSVI PGLFAVGEAT
HRFMYNRSFV RHCSNSSALT MGRLTGAALA TA
//
