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Database: UniProt/SWISS-PROT
Entry: SDHA_CHICK
LinkDB: SDHA_CHICK
Original site: SDHA_CHICK 
ID   SDHA_CHICK              Reviewed;         665 AA.
AC   Q9YHT1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   07-NOV-2018, entry version 109.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000305|PubMed:16371358};
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=Fp;
DE   Flags: Precursor;
GN   Name=SDHA;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-324.
RX   PubMed=15373743; DOI=10.1111/j.1365-2052.2004.01184.x;
RA   Fitzsimmons C.J., Savolainen P., Amini B., Hjaelm G., Lundeberg J.,
RA   Andersson L.;
RT   "Detection of sequence polymorphisms in red junglefowl and white
RT   leghorn ESTs.";
RL   Anim. Genet. 35:391-396(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 167-665.
RC   TISSUE=Heart;
RA   Weinreich D.M.;
RT   "OXPHOS genes in mammals and the molecular clock.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 45-665 IN COMPLEX WITH FAD,
RP   SUBUNIT, SUBCELLULAR LOCATION, AND COFACTOR.
RX   PubMed=15805592; DOI=10.1107/S0907444905000181;
RA   Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A.;
RT   "Crystallization of mitochondrial respiratory complex II from chicken
RT   heart: a membrane-protein complex diffracting to 2.0 A.";
RL   Acta Crystallogr. D 61:380-387(2005).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 45-665 IN COMPLEXES WITH FAD
RP   AND MALONATE, SUBUNIT, SUBCELLULAR LOCATION, AND COFACTOR.
RX   PubMed=16935256; DOI=10.1016/j.bbabio.2006.06.015;
RA   Huang L.-S., Shen J.T., Wang A.C., Berry E.A.;
RT   "Crystallographic studies of the binding of ligands to the
RT   dicarboxylate site of complex II, and the identity of the ligand in
RT   the 'oxaloacetate-inhibited' state.";
RL   Biochim. Biophys. Acta 1757:1073-1083(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 45-665 IN COMPLEXES WITH FAD;
RP   OXALOACETATE AND 3-NITROPROPIONIC ACID, COFACTOR, FUNCTION, CATALYTIC
RP   ACTIVITY, PATHWAY, ACTIVE SITE, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16371358; DOI=10.1074/jbc.M511270200;
RA   Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y.,
RA   Anderson V.E., Berry E.A.;
RT   "3-nitropropionic acid is a suicide inhibitor of mitochondrial
RT   respiration that, upon oxidation by complex II, forms a covalent
RT   adduct with a catalytic base arginine in the active site of the
RT   enzyme.";
RL   J. Biol. Chem. 281:5965-5972(2006).
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:0000305|PubMed:16371358}.
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC       {ECO:0000305|PubMed:16371358}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:15805592,
CC         ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1.
CC       {ECO:0000305|PubMed:16371358}.
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.
CC       {ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC       ECO:0000269|PubMed:16935256}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC       ECO:0000269|PubMed:16935256}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC       ECO:0000269|PubMed:16935256}; Matrix side
CC       {ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC       ECO:0000269|PubMed:16935256}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
DR   EMBL; CO635738; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF095939; AAC72374.1; -; mRNA.
DR   RefSeq; NP_001264327.1; NM_001277398.1.
DR   UniGene; Gga.993; -.
DR   PDB; 1YQ3; X-ray; 2.20 A; A=45-665.
DR   PDB; 1YQ4; X-ray; 2.33 A; A=45-665.
DR   PDB; 2FBW; X-ray; 2.10 A; A/N=45-665.
DR   PDB; 2H88; X-ray; 1.74 A; A/N=45-665.
DR   PDB; 2H89; X-ray; 2.40 A; A=45-665.
DR   PDB; 2WQY; X-ray; 2.10 A; A/N=45-665.
DR   PDBsum; 1YQ3; -.
DR   PDBsum; 1YQ4; -.
DR   PDBsum; 2FBW; -.
DR   PDBsum; 2H88; -.
DR   PDBsum; 2H89; -.
DR   PDBsum; 2WQY; -.
DR   ProteinModelPortal; Q9YHT1; -.
DR   SMR; Q9YHT1; -.
DR   STRING; 9031.ENSGALP00000021475; -.
DR   PaxDb; Q9YHT1; -.
DR   PRIDE; Q9YHT1; -.
DR   GeneID; 395758; -.
DR   KEGG; gga:395758; -.
DR   CTD; 6389; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   eggNOG; COG1053; LUCA.
DR   HOGENOM; HOG000160475; -.
DR   HOVERGEN; HBG001461; -.
DR   InParanoid; Q9YHT1; -.
DR   KO; K00234; -.
DR   PhylomeDB; Q9YHT1; -.
DR   Reactome; R-GGA-372987; The tricarboxylic acid cycle.
DR   UniPathway; UPA00223; UER01006.
DR   EvolutionaryTrace; Q9YHT1; -.
DR   PRO; PR:Q9YHT1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:UniProtKB.
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; IEA:InterPro.
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:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
DR   GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Electron transport; FAD;
KW   Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     44       Mitochondrion.
FT                                {ECO:0000269|PubMed:15805592,
FT                                ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   CHAIN        45    665       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000344984.
FT   NP_BIND      69     74       FAD. {ECO:0000269|PubMed:15805592,
FT                                ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   NP_BIND      92    107       FAD. {ECO:0000269|PubMed:15805592,
FT                                ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   NP_BIND     457    458       FAD. {ECO:0000269|PubMed:15805592,
FT                                ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   ACT_SITE    341    341       Proton acceptor.
FT                                {ECO:0000269|PubMed:16371358}.
FT   BINDING     276    276       FAD. {ECO:0000269|PubMed:15805592,
FT                                ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   BINDING     297    297       Substrate. {ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   BINDING     309    309       Substrate. {ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   BINDING     408    408       Substrate. {ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   BINDING     441    441       FAD. {ECO:0000269|PubMed:15805592,
FT                                ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   BINDING     452    452       Substrate. {ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   MOD_RES     100    100       Tele-8alpha-FAD histidine.
FT                                {ECO:0000269|PubMed:16371358,
FT                                ECO:0000269|PubMed:16935256}.
FT   STRAND       58     68       {ECO:0000244|PDB:2H88}.
FT   HELIX        72     83       {ECO:0000244|PDB:2H88}.
FT   STRAND       88     94       {ECO:0000244|PDB:2H88}.
FT   HELIX        96     98       {ECO:0000244|PDB:2H88}.
FT   HELIX       100    103       {ECO:0000244|PDB:2H88}.
FT   STRAND      114    116       {ECO:0000244|PDB:2H88}.
FT   HELIX       120    130       {ECO:0000244|PDB:2H88}.
FT   TURN        131    133       {ECO:0000244|PDB:2H88}.
FT   HELIX       137    156       {ECO:0000244|PDB:2H88}.
FT   STRAND      167    169       {ECO:0000244|PDB:2H88}.
FT   STRAND      171    179       {ECO:0000244|PDB:2FBW}.
FT   TURN        180    183       {ECO:0000244|PDB:2H88}.
FT   STRAND      186    191       {ECO:0000244|PDB:2FBW}.
FT   HELIX       197    209       {ECO:0000244|PDB:2H88}.
FT   STRAND      215    218       {ECO:0000244|PDB:2H88}.
FT   STRAND      220    228       {ECO:0000244|PDB:2H88}.
FT   STRAND      231    239       {ECO:0000244|PDB:2H88}.
FT   TURN        240    242       {ECO:0000244|PDB:2H88}.
FT   STRAND      245    255       {ECO:0000244|PDB:2H88}.
FT   HELIX       261    263       {ECO:0000244|PDB:2H88}.
FT   STRAND      264    269       {ECO:0000244|PDB:2H88}.
FT   HELIX       276    283       {ECO:0000244|PDB:2H88}.
FT   STRAND      294    301       {ECO:0000244|PDB:2H88}.
FT   TURN        302    304       {ECO:0000244|PDB:2H88}.
FT   HELIX       311    314       {ECO:0000244|PDB:2H88}.
FT   STRAND      318    320       {ECO:0000244|PDB:2H88}.
FT   HELIX       328    331       {ECO:0000244|PDB:2H88}.
FT   TURN        333    335       {ECO:0000244|PDB:2H88}.
FT   HELIX       336    338       {ECO:0000244|PDB:2H88}.
FT   HELIX       341    353       {ECO:0000244|PDB:2H88}.
FT   TURN        354    356       {ECO:0000244|PDB:1YQ3}.
FT   TURN        359    362       {ECO:0000244|PDB:2H88}.
FT   STRAND      364    368       {ECO:0000244|PDB:2H88}.
FT   HELIX       374    380       {ECO:0000244|PDB:2H88}.
FT   HELIX       382    392       {ECO:0000244|PDB:2H88}.
FT   TURN        396    398       {ECO:0000244|PDB:2H88}.
FT   STRAND      401    411       {ECO:0000244|PDB:2H88}.
FT   STRAND      413    416       {ECO:0000244|PDB:2H88}.
FT   STRAND      420    426       {ECO:0000244|PDB:2H88}.
FT   STRAND      429    438       {ECO:0000244|PDB:2H88}.
FT   HELIX       440    442       {ECO:0000244|PDB:2H88}.
FT   STRAND      446    448       {ECO:0000244|PDB:2H88}.
FT   HELIX       457    475       {ECO:0000244|PDB:2H88}.
FT   TURN        487    490       {ECO:0000244|PDB:2H88}.
FT   HELIX       491    501       {ECO:0000244|PDB:2H88}.
FT   STRAND      504    508       {ECO:0000244|PDB:2H88}.
FT   HELIX       509    523       {ECO:0000244|PDB:2H88}.
FT   STRAND      524    528       {ECO:0000244|PDB:2H88}.
FT   HELIX       530    545       {ECO:0000244|PDB:2H88}.
FT   HELIX       546    549       {ECO:0000244|PDB:2H88}.
FT   HELIX       561    585       {ECO:0000244|PDB:2H88}.
FT   STRAND      595    598       {ECO:0000244|PDB:2FBW}.
FT   HELIX       619    621       {ECO:0000244|PDB:2H88}.
FT   STRAND      625    632       {ECO:0000244|PDB:2H88}.
FT   TURN        633    636       {ECO:0000244|PDB:2H88}.
FT   STRAND      637    644       {ECO:0000244|PDB:2H88}.
FT   TURN        652    654       {ECO:0000244|PDB:2H88}.
SQ   SEQUENCE   665 AA;  72931 MW;  9476AA19A7A3AE84 CRC64;
     MAAVVAASRS LAKCWLRPAV RAWPAACQTH ARNFHFTVDG KKNASTKVSD SISTQYPVVD
     HEFDAVVVGA GGAGLRAAFG LSEAGFNTAC VTKLFPTRSH TVAAQGGINA ALGNMEDDNW
     RWHFYDTVKG SDWLGDQDAI HYMTEQAPAA VIELENYGMP FSRTEEGKIY QRAFGGQSLQ
     FGKGGQAHRC CCVADRTGHS LLHTLYGRSL RYDTSYFVEY FALDLLMENG ECRGVIALCI
     EDGTIHRFRA KNTVIATGGY GRTYFSCTSA HTSTGDGTAM VTRAGLPCQD LEFVQFHPTG
     IYGAGCLITE GCRGEGGILI NSQGERFMER YAPVAKDLAS RDVVSRSMTI EIREGRGCGP
     EKDHVYLQLH HLPPQQLATR LPGISETAMI FAGVDVTKEP IPVLPTVHYN MGGIPTNYKG
     QVITHVNGED KVVPGLYACG EAASASVHGA NRLGANSLLD LVVFGRACAL TIAETCKPGE
     PVPSIKPNAG EESVANLDKL RFADGTIRTS EARLNMQKTM QSHAAVFRTG SILQEGCEKL
     SQIYCDLAHL KTFDRGIVWN TDLVETLELQ NLMLCALQTI YGAEARKESR GAHAREDYKF
     RIDDFDYSKP LQGQQKRPFE EHWRKHTLSY VDVKSGKVTL KYRPVIDRTL NEEDCSSVPP
     AIRSY
//
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