SDHA_DICDI
ID SDHA_DICDI Reviewed; 626 AA.
AC Q9U3X4; Q54V62;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE AltName: Full=Flavoprotein subunit of complex II;
DE Short=FP;
DE Flags: Precursor;
GN Name=sdhA; ORFNames=DDB_G0280535;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AX2;
RA Lay S.P., Fisher P.R.;
RT "The flavoprotein subunit 1 of Dictyostelium succinate dehydrogenase.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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:0000250|UniProtKB:P31040}.
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:0000250|UniProtKB:P31040};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q0QF01};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000250|UniProtKB:P31040}.
CC -!- SUBUNIT: Component of complex II composed of four subunits: a
CC flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC composed of a large and a small subunit.
CC {ECO:0000250|UniProtKB:Q0QF01}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q0QF01}; Matrix side
CC {ECO:0000250|UniProtKB:Q0QF01}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; AF211482; AAF21045.1; -; Genomic_DNA.
DR EMBL; AAFI02000037; EAL67069.1; -; Genomic_DNA.
DR RefSeq; XP_641069.1; XM_635977.1.
DR AlphaFoldDB; Q9U3X4; -.
DR SMR; Q9U3X4; -.
DR STRING; 44689.DDB0214886; -.
DR PaxDb; Q9U3X4; -.
DR PRIDE; Q9U3X4; -.
DR EnsemblProtists; EAL67069; EAL67069; DDB_G0280535.
DR GeneID; 8622627; -.
DR KEGG; ddi:DDB_G0280535; -.
DR dictyBase; DDB_G0280535; sdhA.
DR eggNOG; KOG2403; Eukaryota.
DR HOGENOM; CLU_014312_6_1_1; -.
DR InParanoid; Q9U3X4; -.
DR OMA; DPIPIQP; -.
DR PhylomeDB; Q9U3X4; -.
DR Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER01006.
DR PRO; PR:Q9U3X4; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:dictyBase.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:dictyBase.
DR GO; GO:0046956; P:positive phototaxis; IMP:dictyBase.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 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 PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..626
FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT subunit, mitochondrial"
FT /id="PRO_0000327828"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 46..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 69..84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 253
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 418
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 434..435
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT MOD_RES 77
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
SQ SEQUENCE 626 AA; 68516 MW; C8F27868BD063D67 CRC64;
MLSSALKLTK KVCSTKSNGL IRSFSTQTQS RDYAVVDHTY DAIVVGAGGA GLRAALGLTE
KGYKTACITK LFPTRSHTVA AQGGINAALG NADQDDWRWH AYDTVKGSDF LGDQDAIHYM
CKEAVPTVLE LEQYGVPFSR MDDGRIYQRA FGGQSKNFGK GGQATRCCAA ADRTGHALLH
TLYGQAVKHN TKFFIEYFVT DLIMENGDCR GVVAINLEDG TIHRFRSHAT VIATGGYGRA
YFSATSAHTC TGDGNAMVIR AGLPCQDLEF VQFHPTGIYG SGCLITEGAR GEGGYLLNSS
GERFMPRYAP SVADLASRDV VSRSETMEIR EGRGVGPEKD HCLLNLTHLS PEIIDERLPG
IRETAMIFAG VDVTKEPIPV IPTVHYNMGG IPTNYKGQVI TQVDGKDKLV KGLYAAGESA
CVSVHGANRL GANSLLDIVV FGRAVANEIE NTLAKDTPHK PLPPNAGEES IANIDAIRFS
NGTRSTAEIR LEMQKIMQRN AAVFRDGQVL KEGVELIDKC ARSLINDLKT TDRTMIWNTD
LIESLELQNL MTQAVLTMHS AEARKESRGA HAREDYKERD DANWMKHTLS YLDVNTGKVT
LNYRPVVSET LDQSEMETIK PFKRVY
