ID A0A0P6Y4X7_9CHLR Unreviewed; 597 AA.
AC A0A0P6Y4X7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=SE15_04715 {ECO:0000313|EMBL:KPL84416.1};
OS Thermanaerothrix daxensis.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Thermanaerothrix.
OX NCBI_TaxID=869279 {ECO:0000313|EMBL:KPL84416.1, ECO:0000313|Proteomes:UP000050544};
RN [1] {ECO:0000313|EMBL:KPL84416.1, ECO:0000313|Proteomes:UP000050544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GNS-1 {ECO:0000313|EMBL:KPL84416.1,
RC ECO:0000313|Proteomes:UP000050544};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Thermanaerothrix daxensis DSM 23592.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000030};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR630664-51};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPL84416.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGKO01000002; KPL84416.1; -; Genomic_DNA.
DR RefSeq; WP_054520929.1; NZ_LGKO01000002.1.
DR AlphaFoldDB; A0A0P6Y4X7; -.
DR STRING; 869279.SE15_04715; -.
DR PATRIC; fig|869279.4.peg.954; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000050544; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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 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.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR630664-51};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR630664-
KW 51}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050544};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 8..418
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 473..597
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 485..512
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 283
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 35..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 401
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 417..418
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
SQ SEQUENCE 597 AA; 66391 MW; 55326758882CBCF2 CRC64;
MVHTHTFDVV IVGGGGAGLM AALYASKKAR TAVVSKLYPT RSHTGTAQGG IGAALGNLEE
DHWEWHAFDT VKGSDYLGDQ DAIEFMCREA IQAVYDLEHM GLPFSRTPEG RIDQRFFGGH
TNNVTGKPVR RSCYAADRTG HMILQTLYQQ CIKNGIRFFD EFQVMDLLIQ NGAVAGVVAV
ELATGDLHVF HSKAVVFATG GHGRMWEVTS NAYAYTGDGV AVTLRRGIPA EDMEFFQFHP
TGIYKLGILI TEAVRGEGGV LINGKGERFM ERYAPRIKDL ASRDVVSRAI YLEIKEGRGV
NGKNYLYLDV RPETVNYYAE KDGRTRPDGS PYRVTAEEIL AKIPDITDFC RTYLGVDPVK
DLIPIQPTAH YAMGGIPTNK YAEVVIDSQN TVLPGLYAAG ECACVSVHGA NRLGTNSLVD
LVVFGKYAGI KAAEYANGVD FQPLPEDPTD FTRQQIDALR QGDGREKAAQ IGRELRHLMF
DKVGVFRTEE GLREAVEEIK ELRERFRHVR VSDNGRAFNT ELLNTWELGN LLDLALVTAV
SALARKESRG AHAREDYPER DDVNWLKHTL AWLDGEHVRL DYKPVVITQY VPKERVY
//
