ID Q309Z9_TOXGO Unreviewed; 669 AA.
AC Q309Z9; B6KSQ5; S8EZA4;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 24-JAN-2024, entry version 94.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000256|RuleBase:RU362051};
DE EC=1.3.5.1 {ECO:0000256|RuleBase:RU362051};
GN Name=SDH-Fp {ECO:0000313|EMBL:ABB17193.1};
OS Toxoplasma gondii.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=5811 {ECO:0000313|EMBL:ABB17193.1};
RN [1] {ECO:0000313|EMBL:ABB17193.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RH {ECO:0000313|EMBL:ABB17193.1};
RA Saleh A.M., Bohne W.;
RT "Characterization of the respiratory chain components in Toxoplasma
RT gondii.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH)
CC that is involved in complex II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). {ECO:0000256|RuleBase:RU362051}.
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|RuleBase:RU362051};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR630664-51, ECO:0000256|RuleBase:RU362051};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000256|RuleBase:RU362051}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU362051}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU362051}; Matrix side
CC {ECO:0000256|RuleBase:RU362051}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040,
CC ECO:0000256|RuleBase:RU362051}.
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DR EMBL; DQ228958; ABB17193.1; -; mRNA.
DR AlphaFoldDB; Q309Z9; -.
DR VEuPathDB; ToxoDB:TGARI_215590; -.
DR VEuPathDB; ToxoDB:TGCAST_215590; -.
DR VEuPathDB; ToxoDB:TGCOUG_215590; -.
DR VEuPathDB; ToxoDB:TGDOM2_215590A; -.
DR VEuPathDB; ToxoDB:TGDOM2_215590B; -.
DR VEuPathDB; ToxoDB:TGFOU_215590; -.
DR VEuPathDB; ToxoDB:TGGT1_215590; -.
DR VEuPathDB; ToxoDB:TGMAS_215590A; -.
DR VEuPathDB; ToxoDB:TGMAS_215590B; -.
DR VEuPathDB; ToxoDB:TGME49_215590; -.
DR VEuPathDB; ToxoDB:TGP89_215590; -.
DR VEuPathDB; ToxoDB:TGPRC2_215590A; -.
DR VEuPathDB; ToxoDB:TGPRC2_215590B; -.
DR VEuPathDB; ToxoDB:TGRH88_039020; -.
DR VEuPathDB; ToxoDB:TGRUB_215590; -.
DR VEuPathDB; ToxoDB:TGVAND_215590; -.
DR VEuPathDB; ToxoDB:TGVEG_215590; -.
DR UniPathway; UPA00223; UER01006.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; IPR011281; Succ_DH_flav_su_fwd.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR NCBIfam; TIGR01816; sdhA_forward; 1.
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 2: Evidence at transcript level;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU362051};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR611281-4};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR630664-
KW 51};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362051};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362051};
KW Transit peptide {ECO:0000256|RuleBase:RU362051};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362051};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU362051}.
FT DOMAIN 75..477
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 532..669
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 356
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
FT BINDING 80..85
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 103..118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 291
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 460
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT BINDING 476..477
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-51"
FT MOD_RES 111
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611281-4"
SQ SEQUENCE 669 AA; 72751 MW; C56BB44C3B997CE7 CRC64;
MHASASLTQA LRPYARRPLS SALSRSSLSP ALAAGVARGL NAAQPQATGP SFVQQKRFFT
NVKKPAYRVI DHEYDAIVVG AGGAGLRAAF GLASAGIKTA CLSKLFPTRS HTVAAQGGIN
AALGNMTEDD WRWHAYDTVK GSDWLGDQDA IQHMCREAPK VVRELESYGL PFSRTEDGRI
YQRAFGGQSL RFGKGGQAYR CAAAADRTGH AMLHSLYGQS LAHDCKFFVE YFALDLMMSG
ENDERKCHGV VAMCMEDGSI HRFAAKHTVL ATGGYGRAYQ SCTSAHTCTG DGGGMVSRAG
LPLEDLEFVQ FHPTGIFPAG CLITEGCRGE GGILRNGQGE AFMARYAPTA KDLASRDVVS
RSMTIEIREG RGCGPNRDHM HLDLTHLPPA TLHERLPGIT ETAKIFAGVN AEKEPIPVLP
TVHYNMGGIP TNWRAQVLTT SRSKAGGPDK IVQGLYAAGE AACASVHGAN RLGANSLLDL
VVFGREAART IADECKKDAS APSLPPNAGE ETLAMVDRLR HSNGPLTTAQ IRQRMQKTMQ
DHAAVFRTGA VLREGVEMMK DVAKSFADVG VKDRSLSWNT DLIETLELQN LLTQAVQTIV
GAEARKESRG AHAREDFKER DDKNWMKHTL SWQTHREVEK AEFPLTYRQV ISQPLDNEME
HIPPAKRVY
//
