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Database: UniProt/SWISS-PROT
Entry: SDHAA_XENLA
LinkDB: SDHAA_XENLA
Original site: 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   16-JAN-2019, entry version 100.
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
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).
CC       {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;
CC       fumarate 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}.
DR   EMBL; BC060446; AAH60446.1; -; mRNA.
DR   RefSeq; NP_001083473.1; NM_001090004.1.
DR   UniGene; Xl.83156; -.
DR   ProteinModelPortal; Q6PA58; -.
DR   SMR; Q6PA58; -.
DR   PRIDE; Q6PA58; -.
DR   GeneID; 398946; -.
DR   KEGG; xla:398946; -.
DR   CTD; 398946; -.
DR   Xenbase; XB-GENE-17344569; sdha.
DR   HOVERGEN; HBG001461; -.
DR   KO; K00234; -.
DR   OrthoDB; 606981at2759; -.
DR   UniPathway; UPA00223; UER01006.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
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; Transit peptide;
KW   Transport; Tricarboxylic acid cycle.
FT   TRANSIT       1     45       Mitochondrion.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   CHAIN        46    665       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit A, mitochondrial.
FT                                /FTId=PRO_0000272305.
FT   NP_BIND      71     76       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   NP_BIND      94    109       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   NP_BIND     459    460       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   ACT_SITE    343    343       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     278    278       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     299    299       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     311    311       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     410    410       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     443    443       FAD. {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     454    454       Substrate.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   MOD_RES     102    102       Tele-8alpha-FAD histidine.
FT                                {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
//
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