SDHAA_XENLA
ID SDHAA_XENLA Reviewed; 665 AA.
AC Q6PA58;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit A, mitochondrial;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE AltName: Full=Flavoprotein subunit of complex II A;
DE Short=Fp;
DE Flags: Precursor;
GN Name=sdha-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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: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; BC060446; AAH60446.1; -; mRNA.
DR RefSeq; NP_001083473.1; NM_001090004.1.
DR AlphaFoldDB; Q6PA58; -.
DR SMR; Q6PA58; -.
DR DNASU; 398946; -.
DR GeneID; 398946; -.
DR KEGG; xla:398946; -.
DR CTD; 398946; -.
DR Xenbase; XB-GENE-17344569; sdha.L.
DR OrthoDB; 606981at2759; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 398946; Expressed in heart and 20 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
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; -; 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..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT CHAIN 46..665
FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT subunit A, mitochondrial"
FT /id="PRO_0000272305"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 71..76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 94..109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 443
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 459..460
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT MOD_RES 102
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
SQ SEQUENCE 665 AA; 72854 MW; 2C5F88CABBE479D5 CRC64;
MALLKVAPSR LLSRALQLAS RVQNCTPTVT TARRNFHFTV YGRKDTSAKV SDSISTQYPV
VDHEFDAVVV GAGGAGLRAA FGLSEAGFNT ACITKLFPTR SHTVAAQGGI NAALGNMEDD
DWRWHFYDTV KGSDWLGDQD AIHYMTEQAP ASVIELENYG MPFSRTEQGK IYQRAFGGQS
LKYGKGGQAH RCCCVADRTG HSLLHTLYGR SLRYDTSYFV EYFALDLLME NGECRGVIAL
CMEDGSIHRF RAKNTVIATG GYGRTFFSCT SAHTSTGDGT AMVTRAGLPC QDLEFVQFHP
TGIYGAGCLI TEGCRGEGGI LINSEGERFM ERYAPVAKDL ASRDVVSRSM TIEIREGRGC
GKDKDHVYLQ LHHLPPSQLA SRLPGISETA MIFAGVDVTK EPIPVLPTVH YNMGGIPTNY
KGQVITHVNG EDRVVPGLYS CGEAASASVH GANRLGANSL LDLVVFGRAC ALSIAESCKP
GEAVPSIKEN AGEESVANLD KLRYANGSTR TSEIRINMQK TMQNHAAVFR TGSVLKEGCE
KLSVINSSMD DIKTFDRGIV WNTDLVETLE LQNLMLCALQ TINGAEARKE SRGAHAREDY
KVRIDEYDFS KPLQGQQKKS FNEHWRKHTL SYVDKKGKVS LEYRPVIDTT LNEDCASVPP
AIRSY
