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
//