ID   SDHA_CAEEL              Reviewed;         646 AA.
AC   Q09508; Q17616; Q34089;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 3.
DT   27-MAR-2024, entry version 180.
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-1; ORFNames=C03G5.1/D2021.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7739664; DOI=10.1016/0166-6851(94)90163-5;
RA   Kuramochi T., Hirawake H., Kojima S., Takamiya S., Furushima R., Aoki T.,
RA   Komuniecki R., Kita K.;
RT   "Sequence comparison between the flavoprotein subunit of the fumarate
RT   reductase (complex II) of the anaerobic parasitic nematode, Ascaris suum
RT   and the succinate dehydrogenase of the aerobic, free-living nematode,
RT   Caenorhabditis elegans.";
RL   Mol. Biochem. Parasitol. 68:177-187(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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; D30651; BAA21637.1; -; mRNA.
DR   EMBL; FO080313; CCD62793.1; -; Genomic_DNA.
DR   PIR; T15398; T15398.
DR   PIR; T41753; T41753.
DR   RefSeq; NP_509446.1; NM_077045.5.
DR   AlphaFoldDB; Q09508; -.
DR   SMR; Q09508; -.
DR   BioGRID; 46027; 13.
DR   STRING; 6239.C03G5.1.1; -.
DR   DrugCentral; Q09508; -.
DR   EPD; Q09508; -.
DR   PaxDb; 6239-C03G5-1; -.
DR   PeptideAtlas; Q09508; -.
DR   EnsemblMetazoa; C03G5.1.1; C03G5.1.1; WBGene00015391.
DR   GeneID; 181108; -.
DR   KEGG; cel:CELE_C03G5.1; -.
DR   UCSC; C03G5.1.2; c. elegans.
DR   AGR; WB:WBGene00015391; -.
DR   WormBase; C03G5.1; CE03917; WBGene00015391; sdha-1.
DR   eggNOG; KOG2403; Eukaryota.
DR   GeneTree; ENSGT00910000144277; -.
DR   HOGENOM; CLU_014312_6_1_1; -.
DR   InParanoid; Q09508; -.
DR   OMA; FHPTGIW; -.
DR   OrthoDB; 551958at2759; -.
DR   PhylomeDB; Q09508; -.
DR   Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:Q09508; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00015391; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:WormBase.
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; IBA:GO_Central.
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.
DR   World-2DPAGE; 0020:Q09508; -.
PE   2: Evidence at transcript level;
KW   Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW   Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..646
FT                   /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000010339"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         49..54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         72..87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         256
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         422
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         433
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   BINDING         438..439
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   MOD_RES         80
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT   CONFLICT        64
FT                   /note="G -> E (in Ref. 1; BAA21637)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="N -> S (in Ref. 1; BAA21637)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="A -> S (in Ref. 1; BAA21637)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315
FT                   /note="A -> S (in Ref. 1; BAA21637)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        463
FT                   /note="V -> G (in Ref. 1; BAA21637)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483..486
FT                   /note="HNKG -> TTRE (in Ref. 1; BAA21637)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        640
FT                   /note="P -> A (in Ref. 1; BAA21637)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   646 AA;  70398 MW;  CD7CF55A6D26E6D1 CRC64;
     MLRAASNGLR NTVAARSVSL SAANHSDAKR SDIAQYKVVD HAYDAVVVGA GGAGLRAAMG
     LAEGGLKTAV ITKLFPTRSH TVAAQGGINA ALGNMNPDNW RWHFYDTVKG SDWLGDQDAI
     HYMTREAERA VIELENYGMP FSRTTDGKIY QRAFGGQSND FGRGGQAHRT CCVADRTGHS
     LLHTLYGASL QYNCNYFVEY FALDLIMENG VCVGVIAMDL EDGTIHRFRS KNTVLATGGY
     GRAFFSCTSA HTCTGDGTAL TARAGINNSD MEFVQFHPTG IYGAGCLITE GSRGEGGYLV
     NSAGERFMER YAPNAKDLAS RDVVSRSMTV EIMEGRGVGP DKDHIYLQLH HLPAEQLQQR
     LPGISETAMI FAGVDVTKEP IPVIPTVHYN MGGVPTNYKG QVLNYTPKKG DEVVPGLYAA
     GECGAHSVHG ANRLGANSLL DLVIFGRACA IDILKNTSAG VGVPELPKNA GEASVANIDK
     LRHNKGDIST AELRLTMQKS MQNHAAVFRR GDILKEGVKV LSKLYKDQAH LNVADKGLVW
     NSDLIETLEL QNLLINATQT IVAAENREES RGAHARDDFP DRLDELDYSK PLEGQTKKEL
     KDHWRKHSII RSNIETGEVS LDYRPVIDTT LDKSETDWVP PKVRSY
//