ID SDHX_YEAST Reviewed; 634 AA.
AC P47052; D6VWD9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE AltName: Full=Flavoprotein subunit of complex II;
DE Short=FP;
DE AltName: Full=SDH1b;
DE Flags: Precursor;
GN OrderedLocusNames=YJL045W; ORFNames=J1194;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=9730279;
RX DOI=10.1002/(sici)1097-0061(199808)14:11<1001::aid-yea304>3.0.co;2-k;
RA Colby G., Ishii Y., Tzagoloff A.;
RT "Suppression of sdh1 mutations by the SDH1b gene of Saccharomyces
RT cerevisiae.";
RL Yeast 14:1001-1006(1998).
CC -!- FUNCTION: Probable minor catalytic subunit of succinate dehydrogenase
CC (SDH) that is involved in complex II of the mitochondrial electron
CC transport chain and is responsible for transferring electrons from
CC succinate to ubiquinone (coenzyme Q). Probably forms a catalytic dimer
CC with SDH2. Electrons flow from succinate to the FAD bound to the
CC catalytic subunit, and sequentially through the iron-sulfur clusters
CC bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
CC {ECO:0000269|PubMed:9730279}.
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:Q00711}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q00711}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q00711}; Matrix side
CC {ECO:0000250|UniProtKB:Q00711}.
CC -!- MISCELLANEOUS: In vitro, can complement a SDH1 disruption and leads to
CC less than 15% of wild-type SDH reductase activity probably due to its
CC lower expression level (compared to SDH1).
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; Z49320; CAA89336.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08755.1; -; Genomic_DNA.
DR PIR; S56817; S56817.
DR RefSeq; NP_012490.1; NM_001181478.1.
DR AlphaFoldDB; P47052; -.
DR SMR; P47052; -.
DR BioGRID; 33713; 268.
DR DIP; DIP-4262N; -.
DR IntAct; P47052; 3.
DR MINT; P47052; -.
DR STRING; 4932.YJL045W; -.
DR iPTMnet; P47052; -.
DR MaxQB; P47052; -.
DR PaxDb; 4932-YJL045W; -.
DR PeptideAtlas; P47052; -.
DR EnsemblFungi; YJL045W_mRNA; YJL045W; YJL045W.
DR GeneID; 853405; -.
DR KEGG; sce:YJL045W; -.
DR AGR; SGD:S000003581; -.
DR SGD; S000003581; YJL045W.
DR VEuPathDB; FungiDB:YJL045W; -.
DR eggNOG; KOG2403; Eukaryota.
DR GeneTree; ENSGT00910000144277; -.
DR HOGENOM; CLU_014312_6_1_1; -.
DR InParanoid; P47052; -.
DR OMA; AMTIEII; -.
DR OrthoDB; 551958at2759; -.
DR BioCyc; YEAST:YJL045W-MONOMER; -.
DR UniPathway; UPA00223; UER01006.
DR BioGRID-ORCS; 853405; 0 hits in 10 CRISPR screens.
DR PRO; PR:P47052; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47052; Protein.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
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:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IMP:SGD.
DR GO; GO:0045333; P:cellular respiration; IMP:SGD.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
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 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..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..634
FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT subunit 2, mitochondrial"
FT /id="PRO_0000010343"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 53..58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 76..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 260
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 427
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 443..444
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT MOD_RES 84
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
SQ SEQUENCE 634 AA; 69382 MW; F00CD157AB9BF9C5 CRC64;
MLSLKKGITK SYILQRTFTS SSVVRQIGEV KSESKPPAKY HIIDHEYDCV VVGAGGAGLR
AAFGLAEAGY KTACLSKLFP TRSHTVAAQG GINAALGNMH PDDWKSHMYD TVKGSDWLGD
QDAIHYMTRE APKSVIELEH YGMPFSRTED GRIYQRAFGG QSKDFGKGGQ AYRTCAVADR
TGHAMLHTLY GQALKNNTHF FIEYFAMDLL THNGEVVGVI AYNQEDGTIH RFRAHKTVIA
TGGYGRAYFS CTSAHTCTGD GNAMVSRAGF PLEDLEFVQF HPSGIYGSGC LITEGARGEG
GFLLNSEGER FMERYAPTAK DLASRDVVSR AITMEIRAGR GVGKNKDHIL LQLSHLPPEV
LKERLPGISE TAAVFAGVDV TQEPIPVLPT VHYNMGGIPT KWTGEALTID EETGEDKVIP
GLMACGEAAC VSVHGANRLG ANSLLDLVVF GRAVANTIAD TLQPGLPHKP LASNIGHESI
ANLDKVRNAR GSLKTSQIRL NMQRTMQKDV SVFRTQDTLD EGVRNITEVD KTFEDVHVSD
KSMIWNSDLV ETLELQNLLT CATQTAVSAS KRKESRGAHA REDYAKRDDV NWRKHTLSWQ
KGTSTPVKIK YRNVIAHTLD ENECAPVPPA VRSY
//
