ID C8WKP7_EGGLE Unreviewed; 567 AA.
AC C8WKP7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ACV54354.1};
DE Flags: Precursor;
GN OrderedLocusNames=Elen_0363 {ECO:0000313|EMBL:ACV54354.1};
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:ACV54354.1, ECO:0000313|Proteomes:UP000001377};
RN [1] {ECO:0000313|EMBL:ACV54354.1, 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).
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DR EMBL; CP001726; ACV54354.1; -; Genomic_DNA.
DR RefSeq; WP_015759938.1; NC_013204.1.
DR AlphaFoldDB; C8WKP7; -.
DR SMR; C8WKP7; -.
DR STRING; 479437.Elen_0363; -.
DR PaxDb; 479437-Elen_0363; -.
DR KEGG; ele:Elen_0363; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_011398_4_3_11; -.
DR OrthoDB; 9813348at2; -.
DR BioCyc; ELEN479437:G1GFY-371-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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43400:SF12; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING 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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..567
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038944117"
FT DOMAIN 107..543
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 567 AA; 60646 MW; 2A65DA1247A48823 CRC64;
MNQPDKSTLS RRSFLTGAAA TAGLAAFAGL SGCAPQSTTG DAANAATASG ASASGSASAG
AMQTTDPAQA VWPVVEEVEV GAAGEGKIAF VAEPIAASDI VATHDVDVVV CGLGPAGDAA
ALACAEQGLK TVAVEKQTTG NYNSATIGGT NSKLHEHWGM TYDTDAWISD AMIDCAFQGD
MELYRHWLEK NGEAVDWYIS HFDNQNLDDY PLTFAAGDFP DFRDEWDKTS LSRSWNTSLN
LPYPPGELAG ILAGILEQAG VEIRYSCPAC QLVTDDSGKV TGVIVQSDQG FEQYNCAKGV
VLATGGYEFN QQMLKERCRP RGVPGSWLTG AFGNTGDGHQ MGLAVGAAED EFPHAIMLDP
EQLMPYLRVN KLGERFTPEY EPYGHLALAI QAQPGTYDFY VVDSAIGEKI DKIWTPSSSC
YGPKEVWTAA AMSEKALKAD TLEELAKLME VPEAQFVATI ERWNEMAAAG KDEDFNFPGE
MMMTIDTPPY YATKEFADGL CTAGGLLVDT ECRVLDKDRQ PIDGLFAIGL TSGGMFFNTY
PHNLNCLSHT RNCLMGYTVG QVLGDKA
//
