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Database: UniProt/SWISS-PROT
Entry: SDHA_XENTR
LinkDB: SDHA_XENTR
Original site: SDHA_XENTR 
ID   SDHA_XENTR              Reviewed;         665 AA.
AC   Q28ED0; A4QNI5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   16-JAN-2019, entry version 88.
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; ORFNames=TNeu107a09.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) 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; CR848322; CAJ83256.1; -; mRNA.
DR   EMBL; BC135730; AAI35731.1; -; mRNA.
DR   RefSeq; NP_001015989.1; NM_001015989.2.
DR   UniGene; Str.9006; -.
DR   ProteinModelPortal; Q28ED0; -.
DR   SMR; Q28ED0; -.
DR   PRIDE; Q28ED0; -.
DR   GeneID; 548743; -.
DR   KEGG; xtr:548743; -.
DR   CTD; 6389; -.
DR   Xenbase; XB-GENE-956942; sdha.
DR   HOVERGEN; HBG001461; -.
DR   InParanoid; Q28ED0; -.
DR   KO; K00234; -.
DR   OrthoDB; 606981at2759; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IBA:GO_Central.
DR   GO; GO:0045282; C:plasma membrane succinate dehydrogenase complex; IBA:GO_Central.
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; ISS:UniProtKB.
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; IBA:GO_Central.
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   Complete proteome; Electron transport; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     45       Mitochondrion.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   CHAIN        46    665       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000272307.
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;  72706 MW;  6C0A8263F91E0649 CRC64;
     MAFLNVASSR LLSKTLQLGG RVQNCTATCT AATRNFHFSV YGRKDTSAKL SDSISTQYPV
     VDHDFDAVVV GAGGAGLRAA FGLSEAGFNT ACITKLFPTR SHTVAAQGGI NAALGNMEDD
     DWRWHFYDTV KGSDWLGDQD AIHYMTEQAP ASVIELENYG MPFSRTEQGK IYQRAFGGQS
     LKFGKGGQAH RCCCVADRTG HSLLHTLYGR SLRYDTSYFV EYFALDLLME NGECRGVIAL
     CMEDGSIHRF RAKNTVIATG GYGRTFFSCT SAHTCTGDGT AMVTRAGLPC QDLEFVQFHP
     TGIYGAGCLI TEGCRGEGGI LINSEGERFM ERYAPVAKDL ASRDVVSRSM TIEIREGRGC
     GKDKDHVYLQ LHHLPPSQLA SRLPGISETA MIFAGVDVTK EPIPVLPTVH YNMGGIPTNY
     KGQVITHVNG EDRVVPGLYA CGEAASASVH GANRLGANSL LDLVVFGRAC ALSIAESCKP
     GEPVPSIKEN AGEESVANLD KLRFTNGSTR TSELRINMQK TMQNHAAVFR TGSVLKEGCE
     KLSAINSTMD DIKTFDRGIV WNTDLVETLE LQNLMLCALQ TIYGAEARKE SRGAHAREDY
     KVRIDEYDYS KPIQGQQKKS FSEHWRKHTL SYVDGKGKVS LEYRPVIDTT LNEDCVSVPP
     AIRSY
//
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