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Database: UniProt
Entry: D7C3D4_STRBB
LinkDB: D7C3D4_STRBB
Original site: D7C3D4_STRBB 
ID   D7C3D4_STRBB            Unreviewed;       648 AA.
AC   D7C3D4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:ADI10159.1};
DE            EC=1.3.5.1 {ECO:0000313|EMBL:ADI10159.1};
GN   Name=sdhA {ECO:0000313|EMBL:ADI10159.1};
GN   OrderedLocusNames=SBI_07039 {ECO:0000313|EMBL:ADI10159.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI10159.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI10159.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI10159.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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DR   EMBL; CP002047; ADI10159.1; -; Genomic_DNA.
DR   RefSeq; WP_014179609.1; NC_016582.1.
DR   AlphaFoldDB; D7C3D4; -.
DR   STRING; 749414.SBI_07039; -.
DR   KEGG; sbh:SBI_07039; -.
DR   PATRIC; fig|749414.3.peg.7241; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_7_0_11; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:ADI10159.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT   DOMAIN          47..452
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          513..647
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   648 AA;  71615 MW;  E0B5A80CBB3B1BFC CRC64;
     MSTYAEYTTG EPISDAKAPD GPIEERWNRR RFEAKLVNPA NRRKHTVIVV GTGLAGGAAG
     ATLAEQGYHV VQFCYQDSPR RAHSIAAQGG INAAKNYRND GDSIRRLFYD TVKGGDFRAR
     ESNVHRLAEV SVEIIDQCVA QGVPFAREYG GLLDTRSFGG VQVSRTFYAR GQTGQQLLLG
     AYQALTRQIA AGNVEMHPRT EMLDLIVIDG RARGIVARDL ISGEVSTYFA DAVVLASGGY
     GNVFYLSTNA KNSNATAIWR AHRRGAYFAN PCFTQIHPTC IPRSGDHQSK LTLMSESLRN
     DGRIWVPKAK GDTRPPAEIP EDERDYYLER IYPSFGNLVP RDIASRAAKN VCDEGRGVGP
     GGQGVYLDFA DAIARMGRKA VSEKYGNLFE MYERITAEDP YQVPMRIYPA IHYTMGGLWV
     DYDLQTTVPG LFAIGEANFS DHGANRLGAS ALMQGLADGY FVLPSTINDY LARHPHGEVD
     PGHPAVTEAV SEVTDRLARL LANDGDRTPD SFHRELGELL WDECGMARTD TGLRKALDRI
     PALREEFWRR IKVPGTGEEL NQSLEKANRV VDYLELAELM CLDALHRAES CGGHFREESQ
     TPDGEAARDD ESFSYAGAWE FSGTGSAPVL HREDLVFEYV HPTQRSYA
//
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