GenomeNet

Database: UniProt
Entry: D2PEK3_SULID
LinkDB: D2PEK3_SULID
Original site: D2PEK3_SULID 
ID   D2PEK3_SULID            Unreviewed;       566 AA.
AC   D2PEK3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN   OrderedLocusNames=LD85_0159 {ECO:0000313|EMBL:ADB85959.1};
OS   Sulfolobus islandicus (strain L.D.8.5 / Lassen #2).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=425944 {ECO:0000313|EMBL:ADB85959.1, ECO:0000313|Proteomes:UP000001404};
RN   [1] {ECO:0000313|Proteomes:UP000001404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.D.8.5 / Lassen #2 {ECO:0000313|Proteomes:UP000001404};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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}.
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; CP001731; ADB85959.1; -; Genomic_DNA.
DR   RefSeq; WP_012952231.1; NC_013769.1.
DR   AlphaFoldDB; D2PEK3; -.
DR   GeneID; 8759999; -.
DR   KEGG; sii:LD85_0159; -.
DR   HOGENOM; CLU_014312_6_2_2; -.
DR   Proteomes; UP000001404; 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   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          7..385
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          442..566
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        278
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   566 AA;  62561 MW;  DB49C71AA00A3D95 CRC64;
     MEKIEYDAVV IGGGLAGLMS AHEIASAGFK VAVISKVFPT RSHSAAAEGG IAAYIPGNSD
     PNDNPDYMTY DTVKGGDYLV DQDAAELLSN KSGEIVMLLE RWGALFNRQP DGRVAVRYFG
     GQTYPRTRFV GDKTGMALLH TLFERTSGLN VDFYNEWFSL DLVTDNKKVV GIVAMQMKTL
     TPFFFKTKAV VLATGGMGML YRHTTNSYIN TGDGFGIALR AGAALKDPEF VQFHPTALYP
     SDVLISEAAR GEGGILKNVK GERFMTKYAP KKLDLAPRDI VSRAIITEIR EGRGFPGGYV
     GLDLTHLGEE YIKERLALAV EAAKSFASVD AFTEPIPVRP AQHYYMGGID VDIDGRNPDI
     AGLFSAGEAA CVSVHGANRL GSNSLLDTLV FGQVTGRTVV QFLKSNPGNP TSNYEKEAEK
     VVDDAYKFVK SESGVHFGQI LEKLRDTMWD YVGIYRDEGG LLNAMSEINK LRGMISNMYV
     TDKSKVYNTE FFNALELRNM LDLALTITKS ALERKESRGA HYRTDYPDRD DNNWLKHTIA
     YLRGNTVEVT FKPVKITRWK PEPRVY
//
DBGET integrated database retrieval system