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Database: UniProt
Entry: K4R3G4_STRDJ
LinkDB: K4R3G4_STRDJ
Original site: K4R3G4_STRDJ 
ID   K4R3G4_STRDJ            Unreviewed;       642 AA.
AC   K4R3G4;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:CCK27682.1};
GN   ORFNames=BN159_3303 {ECO:0000313|EMBL:CCK27682.1};
OS   Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK27682.1, ECO:0000313|Proteomes:UP000008043};
RN   [1] {ECO:0000313|EMBL:CCK27682.1, ECO:0000313|Proteomes:UP000008043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC   {ECO:0000313|Proteomes:UP000008043};
RX   PubMed=23043000; DOI=10.1128/JB.01592-12;
RA   Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA   Pelzer S., Kalinowski J., Mack M.;
RT   "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT   heterologous production of the unique antibiotic roseoflavin.";
RL   J. Bacteriol. 194:6818-6827(2012).
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DR   EMBL; HE971709; CCK27682.1; -; Genomic_DNA.
DR   RefSeq; WP_015658059.1; NC_020504.1.
DR   AlphaFoldDB; K4R3G4; -.
DR   STRING; 1214101.BN159_3303; -.
DR   KEGG; sdv:BN159_3303; -.
DR   PATRIC; fig|1214101.3.peg.3351; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_8_1_11; -.
DR   OrthoDB; 9805351at2; -.
DR   Proteomes; UP000008043; 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; 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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 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:UP000008043}.
FT   DOMAIN          10..430
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          491..578
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   642 AA;  71150 MW;  D2EF5D82F03B10EE CRC64;
     MSVVDRQEWD VVVIGAGGAG LRAAIEARER GARTAVICKS LFGKAHTVMA EGGIAAAMAN
     VNEHDSWQVH FRDTMRGGKF LNQWRMAELH AQEAPDRVWE LETWGALFDR TKDGKISQRN
     FGGHEYPRLA HVGDRTGLEL IRTLQQKIVS LQQQDFKETG DYESRLKVFQ ECTVTRVLKD
     GPRVSGVFAY DRETGRFFVL EAPAVVIATG GIGKSFKVTS NSWEYTGDGH ALALLAGAPL
     LNMEFVQFHP TGMVWPPSVK GILVTESVRG DGGVLRNSEG KRFMFDYVPD VFKEKYAESE
     EEGDRWYDDP DNNRRPPELL PRDEVARAIN SEVKAGRGSP HGGVFLDVST RMPAEVIKRR
     LPSMYHQFKE LADVDITAEA MEVGPTCHYV MGGIAVDSDT AAARGVPGLF AAGEVAGGMH
     GSNRLGGNSL SDLLVFGRRA GWHAAEYTAA LAFERPEVDD VQIDTAAAEA LRPFSAESPD
     EAAPENPYSL HQELQQTMND LVGIIRREGE MAHALEKLGE LRVRARRAGV EGHRQFNPGW
     HLALDLRNML LVSECVARAA LERSESRGGH TREDHPTMER VWRNINLLCR LADPTGGLAA
     TDPERGQIDL TRETTDPIRP DLLALFDKEE LVKYLAEEEL YE
//
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