ID   DHSA_PONAB              Reviewed;         664 AA.
AC   Q5R616;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JUN-2009, entry version 40.
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;
OS   Pongo abelii (Sumatran orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Component of complex II composed of four subunits: the
CC       flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a
CC       cytochrome b560 composed of SDHC and SDHD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- MISCELLANEOUS: The complex, present in mitochondria, can be
CC       degraded to form EC 1.3.99.1, which no longer reacts with
CC       ubiquinone.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily.
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DR   EMBL; CR860684; CAH92800.1; -; mRNA.
DR   RefSeq; NP_001126633.1; -.
DR   UniGene; Pab.18686; -.
DR   SMR; Q5R616; 54-664.
DR   GeneID; 100173631; -.
DR   HOVERGEN; Q5R616; -.
DR   BRENDA; 1.3.5.1; 269192.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR003953; FAD_bind2_N.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR004112; Fum_Rdtase/Succ_DH_flav_C.
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   PRINTS; PR00368; FADPNR.
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; Phosphoprotein;
KW   Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT       1     43       Mitochondrion (By similarity).
FT   CHAIN        44    664       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000272304.
FT   NP_BIND      91    106       FAD (By similarity).
FT   ACT_SITE    340    340       Proton acceptor (By similarity).
FT   BINDING     296    296       Substrate (By similarity).
FT   BINDING     308    308       Substrate (By similarity).
FT   BINDING     407    407       Substrate (By similarity).
FT   BINDING     451    451       Substrate (By similarity).
FT   MOD_RES      99     99       Tele-8alpha-FAD histidine (By
FT                                similarity).
FT   MOD_RES     252    252       Phosphothreonine (By similarity).
SQ   SEQUENCE   664 AA;  72692 MW;  705C3B8852ADFE21 CRC64;
     MSGVRGLSRL LSARRLALAK AWPTVLQTGA RGFHFTVDGN KRASAKVSDS ISAQYPVVDH
     EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
     WHFYDTVKGS DWLGDQDAIH YMTEQAPAAV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
     GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
     DGSIHRIRAK NTVVATGGYG RTYFSCTSAH TSTGDGTAMI TRAGLPCQDL EFVQFHPTGI
     YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
     KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
     VLRHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IEESCRPGDK
     VPPIKPNAGE ESVMNLDKLR FADGSIRTSE LRLSMQKSMQ NHAAVFRVGS VLQEGCGKIS
     KLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
     IDEYDYSKPI QGQQKKPFEE HWRKHTLSYV DVSTGKVTLE YRPVIDKTLN EADCATVPPA
     IRSY
//