ID C1D491_DEIDV Unreviewed; 509 AA.
AC C1D491;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative FAD binding protein, putative fumarate reductase flavoprotein subunit {ECO:0000313|EMBL:ACO47972.1};
GN OrderedLocusNames=Deide_3p00500 {ECO:0000313|EMBL:ACO47972.1};
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OG Plasmid pDeide3 {ECO:0000313|Proteomes:UP000002208}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO47972.1, ECO:0000313|Proteomes:UP000002208};
RN [1] {ECO:0000313|EMBL:ACO47972.1, ECO:0000313|Proteomes:UP000002208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC {ECO:0000313|Proteomes:UP000002208};
RC PLASMID=pDeide3 {ECO:0000313|Proteomes:UP000002208};
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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DR EMBL; CP001117; ACO47972.1; -; Genomic_DNA.
DR RefSeq; WP_012694845.1; NC_012528.1.
DR AlphaFoldDB; C1D491; -.
DR KEGG; ddr:Deide_3p00500; -.
DR HOGENOM; CLU_011398_4_6_0; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000002208; Plasmid pDeide3.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 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.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plasmid {ECO:0000313|EMBL:ACO47972.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002208}.
FT DOMAIN 15..480
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 509 AA; 55410 MW; 92634B0D011CBE7D CRC64;
MHLNSDSPSD QHTFDTVVVG AGNAALCAAL SARERGMRVL VLERGPHGKR GGNSYFTDGA
IRFAYNDLND IRDVIPRISD EEAEQIVMPS YSEADYLGDL MRVTGNQSDP ELARQIVTQS
PSTIRWMRDH GVKFDLIYDN QSFLKDGKYH FWGGLPVKTD GKGVGLIERL NVRAEELGIE
VWYESRATRL LTDKGRVTGV LVQRGEQEIT LQAGSVVLAC GSFEASRELR AEHIGQEWDA
AIVRGTEFNT GDGISMALAV GAQRYGDWSG CHAIGTDAGA PKVGDFGKPG DIYKKHSYPL
GLLINKSGLR FVDEGADFRN YTYAKYGREI LKQPGHVAYQ IFDSQVRPML RKEYNLEEAT
FYQADTLEEL ASLLDVDQKQ FLETIGTYNA AVQDGDYNPT VKDGKGTVGI TPPKSNWALA
VEQGPFYAFP VTCGITFAFG GVRVSPQGEV LNADQEAIPG LFAAGEMVGG IFYQNYPGGS
GLMSGAVFGK LAGESSAQYV QASSLALTS
//