ID G4RJK2_THETK Unreviewed; 581 AA.
AC G4RJK2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN Name=frdA {ECO:0000313|EMBL:CCC81747.1};
GN OrderedLocusNames=TTX_1104 {ECO:0000313|EMBL:CCC81747.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC81747.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC81747.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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DR EMBL; FN869859; CCC81747.1; -; Genomic_DNA.
DR RefSeq; WP_014127002.1; NC_016070.1.
DR AlphaFoldDB; G4RJK2; -.
DR STRING; 768679.TTX_1104; -.
DR PaxDb; 768679-TTX_1104; -.
DR GeneID; 11261992; -.
DR KEGG; ttn:TTX_1104; -.
DR PATRIC; fig|768679.9.peg.1113; -.
DR eggNOG; arCOG00571; Archaea.
DR HOGENOM; CLU_014312_6_2_2; -.
DR OrthoDB; 23539at2157; -.
DR Proteomes; UP000002654; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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; 4.10.80.40; succinate dehydrogenase protein 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; IPR003952; FRD_SDH_FAD_BS.
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 InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
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 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.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCC81747.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002654};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..396
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 458..581
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 581 AA; 63908 MW; 65B95B88F6B34856 CRC64;
MDFIYCDVVV VGSGLAGLRA AIAAAESKPD LEVCVVTKVS GPRSHSIAAE GGMAGVLYPE
KTGDSAELHA YDTVKGGDFL VDQDAALMLA QEAPKEIFYL EKLGVPWNRD ADGRIALRLF
GGMSKPRTAF ARDKTGFFVM SALYRAARSL PIKFYEEHLV TKLFIKRGQF AGLIALDLRR
GELRLFRAKA GVIATGGGGR MFKLTTMGFA NTGEMWGIAL REGIALKDME FVQWHPTALV
PSGILISEAA RAEGAYLVNK LGERFMARYA PQRMELAPRD VVARAIATEC MAGRGFIHEE
SKMCYVGLDL RHIDPQRMKE RLPLLMEVVR TYAGLDPTKD LIPVAPAVHY FMGGIHTDLH
GRVLDANGRW IIGLWAAGEA ASVSVHGANR LGSNSLAECA VWGRLTGIQA AEFASSTQQP
PALDLEAKTV YGAEERRIFD KLLHRESGGI SLGQVKSAIQ EALHSGAGIF RHKSTIEEAL
TKVTRTAAKV MQVNVHDVGR TYNMELKELL ELDGAVLAAQ VILMGAYFRQ ESRGSHYRLD
HPSRDDSRWL VHTIAYRYGD GVVLKWEPVR ILKWPPEVRS Y
//
