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Database: UniProt
Entry: Q9U3X4
LinkDB: Q9U3X4
Original site: Q9U3X4 
ID   SDHA_DICDI              Reviewed;         626 AA.
AC   Q9U3X4; Q54V62;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   26-NOV-2014, entry version 88.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1;
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=FP;
DE   Flags: Precursor;
GN   Name=sdhA; ORFNames=DDB_G0280535;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AX2;
RA   Lay S.P., Fisher P.R.;
RT   "The flavoprotein subunit 1 of Dictyostelium succinate
RT   dehydrogenase.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Matrix side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; AF211482; AAF21045.1; -; Genomic_DNA.
DR   EMBL; AAFI02000037; EAL67069.1; -; Genomic_DNA.
DR   RefSeq; XP_641069.1; XM_635977.1.
DR   ProteinModelPortal; Q9U3X4; -.
DR   SMR; Q9U3X4; 33-626.
DR   STRING; 44689.DDB_0214886; -.
DR   PRIDE; Q9U3X4; -.
DR   EnsemblProtists; DDB0214886; DDB0214886; DDB_G0280535.
DR   GeneID; 8622627; -.
DR   KEGG; ddi:DDB_G0280535; -.
DR   dictyBase; DDB_G0280535; sdhA.
DR   eggNOG; COG1053; -.
DR   InParanoid; Q9U3X4; -.
DR   KO; K00234; -.
DR   OMA; NVFRTEE; -.
DR   PhylomeDB; Q9U3X4; -.
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:Q9U3X4; -.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II; ISS:dictyBase.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:dictyBase.
DR   GO; GO:0046956; P:positive phototaxis; IMP:dictyBase.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:dictyBase.
DR   Gene3D; 1.20.58.100; -; 1.
DR   Gene3D; 3.90.700.10; -; 1.
DR   InterPro; IPR003953; FAD_bind_dom.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat.
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; 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   3: Inferred from homology;
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     24       Mitochondrion. {ECO:0000255}.
FT   CHAIN        25    626       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000327828.
FT   NP_BIND      46     51       FAD. {ECO:0000250}.
FT   NP_BIND      69     84       FAD. {ECO:0000250}.
FT   NP_BIND     434    435       FAD. {ECO:0000250}.
FT   ACT_SITE    318    318       Proton acceptor. {ECO:0000250}.
FT   BINDING     253    253       FAD. {ECO:0000250}.
FT   BINDING     274    274       Substrate. {ECO:0000250}.
FT   BINDING     286    286       Substrate. {ECO:0000250}.
FT   BINDING     385    385       Substrate. {ECO:0000250}.
FT   BINDING     418    418       FAD. {ECO:0000250}.
FT   BINDING     429    429       Substrate. {ECO:0000250}.
FT   MOD_RES      77     77       Tele-8alpha-FAD histidine. {ECO:0000250}.
SQ   SEQUENCE   626 AA;  68516 MW;  C8F27868BD063D67 CRC64;
     MLSSALKLTK KVCSTKSNGL IRSFSTQTQS RDYAVVDHTY DAIVVGAGGA GLRAALGLTE
     KGYKTACITK LFPTRSHTVA AQGGINAALG NADQDDWRWH AYDTVKGSDF LGDQDAIHYM
     CKEAVPTVLE LEQYGVPFSR MDDGRIYQRA FGGQSKNFGK GGQATRCCAA ADRTGHALLH
     TLYGQAVKHN TKFFIEYFVT DLIMENGDCR GVVAINLEDG TIHRFRSHAT VIATGGYGRA
     YFSATSAHTC TGDGNAMVIR AGLPCQDLEF VQFHPTGIYG SGCLITEGAR GEGGYLLNSS
     GERFMPRYAP SVADLASRDV VSRSETMEIR EGRGVGPEKD HCLLNLTHLS PEIIDERLPG
     IRETAMIFAG VDVTKEPIPV IPTVHYNMGG IPTNYKGQVI TQVDGKDKLV KGLYAAGESA
     CVSVHGANRL GANSLLDIVV FGRAVANEIE NTLAKDTPHK PLPPNAGEES IANIDAIRFS
     NGTRSTAEIR LEMQKIMQRN AAVFRDGQVL KEGVELIDKC ARSLINDLKT TDRTMIWNTD
     LIESLELQNL MTQAVLTMHS AEARKESRGA HAREDYKERD DANWMKHTLS YLDVNTGKVT
     LNYRPVVSET LDQSEMETIK PFKRVY
//
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