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Database: UniProt
Entry: D8GKJ8_CLOLD
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Original site: D8GKJ8_CLOLD 
ID   D8GKJ8_CLOLD            Unreviewed;       598 AA.
AC   D8GKJ8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Succinate dehydrogenase flavoprotein subunit {ECO:0000313|EMBL:ADK15338.1};
DE            EC=1.3.99.1 {ECO:0000313|EMBL:ADK15338.1};
GN   OrderedLocusNames=CLJU_c22800 {ECO:0000313|EMBL:ADK15338.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK15338.1, ECO:0000313|Proteomes:UP000001656};
RN   [1] {ECO:0000313|EMBL:ADK15338.1, ECO:0000313|Proteomes:UP000001656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC
RC   {ECO:0000313|Proteomes:UP000001656};
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform based
RT   on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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DR   EMBL; CP001666; ADK15338.1; -; Genomic_DNA.
DR   RefSeq; WP_013238928.1; NZ_LITS01000004.1.
DR   AlphaFoldDB; D8GKJ8; -.
DR   STRING; 748727.CLJU_c22800; -.
DR   KEGG; clj:CLJU_c22800; -.
DR   PATRIC; fig|748727.19.peg.2795; -.
DR   eggNOG; COG1053; Bacteria.
DR   HOGENOM; CLU_014312_8_2_9; -.
DR   OMA; HYSPELY; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000001656; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 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.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ADK15338.1}.
FT   DOMAIN          10..400
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          459..581
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   598 AA;  66104 MW;  0D094DF7C694EA6A CRC64;
     MQIDKIIDTD ILVVGGSGAG SMAAVTAARK GAKVLLAVKG KLGKSGNAIM AGAGFSMDGE
     TAYYKYGLKE ADPKNTKGKL FEQIVKQSFY LSDQNMVEQF VSDCDECCWE LKQWIEKAGH
     KVVFFGEEGY ISSGKAVGVG CRYGVSKAGG IDVIEDFIAV DILMEDKKAV GAVGIEVYTG
     KIIEIRSKSV ILATGGYQPY SFKCTVSDMT GDGMAMAYRA GAKLADMEFL LYIPAVALSP
     SVYKGSIYPF LHSSMLMPIV KNGKGESILD NIPENLLKMA KESEMGKLIF TYYYGDQIAR
     GKGTPNGGVY FDYSNVPFDI YEKALKKAEP LMNIWYRKGF YQGNNLDTFV ENIRKGIPWE
     VGIGSEYSMG GIEVDENMYT GVPGLYAAGE TTSGVFGAMR VADGLIEMLV QGYRAALSAC
     KYIQNVNEPS MKNTNIDSII KDIFSPLERK EGVSPIKIHR NIEKTADVGF NFRRNEEGLT
     KALDEILKIH KYDISAMSTK SKNRVYNYEW IESVQARNLL TCTEAGVRAA LMRKESRGTH
     IRDDYEFVDN DNWLLRIMSS KGEDETMKLS TRKPKVTTME LPGGKNKNIP DYMLSMLK
//
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