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Database: UniProt
Entry: A0A2R7YZS6_9ACTN
LinkDB: A0A2R7YZS6_9ACTN
Original site: A0A2R7YZS6_9ACTN 
ID   A0A2R7YZS6_9ACTN        Unreviewed;       672 AA.
AC   A0A2R7YZS6;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:PUA81852.1};
GN   ORFNames=C7S10_07280 {ECO:0000313|EMBL:PUA81852.1};
OS   Nocardioides currus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=2133958 {ECO:0000313|EMBL:PUA81852.1, ECO:0000313|Proteomes:UP000244867};
RN   [1] {ECO:0000313|EMBL:PUA81852.1, ECO:0000313|Proteomes:UP000244867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IB-3 {ECO:0000313|EMBL:PUA81852.1,
RC   ECO:0000313|Proteomes:UP000244867};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PUA81852.1}.
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DR   EMBL; PYXZ01000002; PUA81852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R7YZS6; -.
DR   OrthoDB; 9805351at2; -.
DR   Proteomes; UP000244867; Unassembled WGS sequence.
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; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal 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   Reference proteome {ECO:0000313|Proteomes:UP000244867}.
FT   DOMAIN          65..476
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          537..671
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        361
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   672 AA;  74218 MW;  C4EFED8519C09C70 CRC64;
     MPDTVTAAEA SQDTPAEMTD DAAGYYTPGE PLVDAKAPTG PIADRWSDRK FEARLVNPSN
     RRKLDVIIVG TGLAGASAAA TLGEAGYNVK SFCYQDSPRR AHSIAAQGGI NAAKNYKEDG
     DSVHRLFYDT VKGGDYRSRE SNVYRLAEVS TNIIDQCVAQ GVPFAREYGG LLDNRSFGGV
     QVSRTFYARG QTGQQLLIGA YQALERQVAA GTVQTFTRHE MLELIVVDGK ARGIVSRDMV
     TGAIDTHLAD VVVLASGGYG NVFYLSTNAM GCNVTAAWRA HRKGAYMANP CYTQIHPTCI
     PVSGSHQSKL TLMSESLRND GRIWVPKNEA DCDKDPRDIP EADRDYYLER IYPSFGNLVP
     RDIASRAAKN VCDEGRGVGP KVDGVRRGVY LDFAAAIERL GRDGITEKYD NLLDMYERIT
     GEDPYEVPMR IYPAVHYVMG GVWVDYDLQS TIPGLFVTGE ANFSDHGANR LGASALMQGL
     ADGYFVLPHT IRDYLADGPF EKITEDHPAV VEAHTSVKER IDHFLSVNGT RSVDSYHREL
     GNIMWEYCGM ERTEDGLKKA IDLIRTLKDD FWRNVKVLGT NESLNQSLEK AGRVADFIEL
     GELMCIDALN RRESCGGHFR GESQTEDGEA LRHDDLFAYV AAWEFAGDGE PPVLHKEDLV
     YTAIEMKQRS YK
//
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