SDHA_CAEEL
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 03-AUG-2022, entry version 172.
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; 11.
DR STRING; 6239.C03G5.1; -.
DR DrugCentral; Q09508; -.
DR World-2DPAGE; 0020:Q09508; -.
DR EPD; Q09508; -.
DR PaxDb; Q09508; -.
DR PeptideAtlas; Q09508; -.
DR PRIDE; 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 CTD; 181108; -.
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; DPIPIQP; -.
DR OrthoDB; 606981at2759; -.
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 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: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; IBA:GO_Central.
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 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
