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Database: UniProt
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   08-NOV-2023, entry version 130.
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; Phasianidae;
OC   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 leghorn
RT   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 AND
RP   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 dicarboxylate
RT   site of complex II, and the identity of the ligand in the 'oxaloacetate-
RT   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 respiration
RT   that, upon oxidation by complex II, forms a covalent adduct with a
RT   catalytic base arginine in the active site of the enzyme.";
RL   J. Biol. Chem. 281:5965-5972(2006).
CC   -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH)
CC       that is involved in complex II of the mitochondrial electron transport
CC       chain and is responsible for transferring electrons from succinate to
CC       ubiquinone (coenzyme Q). {ECO:0000305|PubMed:16371358}.
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:0000305|PubMed:16371358};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC         ECO:0000269|PubMed:16935256};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC       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 cytochrome
CC       b560 composed of SDHC and SDHD. {ECO:0000269|PubMed:15805592,
CC       ECO:0000269|PubMed:16371358, 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 {ECO:0000269|PubMed:15805592,
CC       ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
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DR   EMBL; CO635738; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF095939; AAC72374.1; -; mRNA.
DR   RefSeq; NP_001264327.1; NM_001277398.1.
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   PDB; 6MYO; X-ray; 2.20 A; A=45-665.
DR   PDB; 6MYP; X-ray; 2.10 A; A=45-665.
DR   PDB; 6MYQ; X-ray; 1.97 A; A=45-665.
DR   PDB; 6MYR; X-ray; 2.15 A; A=45-665.
DR   PDB; 6MYS; X-ray; 2.37 A; A=45-665.
DR   PDB; 6MYT; X-ray; 2.27 A; A=45-665.
DR   PDB; 6MYU; X-ray; 1.97 A; A=45-665.
DR   PDBsum; 1YQ3; -.
DR   PDBsum; 1YQ4; -.
DR   PDBsum; 2FBW; -.
DR   PDBsum; 2H88; -.
DR   PDBsum; 2H89; -.
DR   PDBsum; 2WQY; -.
DR   PDBsum; 6MYO; -.
DR   PDBsum; 6MYP; -.
DR   PDBsum; 6MYQ; -.
DR   PDBsum; 6MYR; -.
DR   PDBsum; 6MYS; -.
DR   PDBsum; 6MYT; -.
DR   PDBsum; 6MYU; -.
DR   AlphaFoldDB; Q9YHT1; -.
DR   SMR; Q9YHT1; -.
DR   STRING; 9031.ENSGALP00000021475; -.
DR   PaxDb; 9031-ENSGALP00000021475; -.
DR   GeneID; 395758; -.
DR   KEGG; gga:395758; -.
DR   CTD; 6389; -.
DR   VEuPathDB; HostDB:geneid_395758; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   InParanoid; Q9YHT1; -.
DR   OrthoDB; 551958at2759; -.
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; 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); IDA:UniProtKB.
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:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
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; IC:UniProtKB.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 4.10.80.40; succinate dehydrogenase protein domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 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; IPR030664; SdhA/FrdA/AprA.
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   NCBIfam; TIGR01816; sdhA_forward; 1.
DR   NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Reference proteome; Transit peptide; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:15805592,
FT                   ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256"
FT   CHAIN           45..665
FT                   /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT                   subunit, mitochondrial"
FT                   /id="PRO_0000344984"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:16371358"
FT   BINDING         69..74
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:15805592,
FT                   ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256"
FT   BINDING         92..107
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:15805592,
FT                   ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256"
FT   BINDING         276
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:15805592,
FT                   ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:16371358,
FT                   ECO:0000269|PubMed:16935256"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:16371358,
FT                   ECO:0000269|PubMed:16935256"
FT   BINDING         408
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:16371358,
FT                   ECO:0000269|PubMed:16935256"
FT   BINDING         441
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:15805592,
FT                   ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256"
FT   BINDING         452
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:16371358,
FT                   ECO:0000269|PubMed:16935256"
FT   BINDING         457..458
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:15805592,
FT                   ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256"
FT   MOD_RES         100
FT                   /note="Tele-8alpha-FAD histidine"
FT                   /evidence="ECO:0000269|PubMed:16371358,
FT                   ECO:0000269|PubMed:16935256"
FT   STRAND          58..68
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           72..83
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          88..94
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           100..103
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           120..130
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           137..156
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          171..179
FT                   /evidence="ECO:0007829|PDB:2WQY"
FT   TURN            180..183
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          186..191
FT                   /evidence="ECO:0007829|PDB:2WQY"
FT   HELIX           197..209
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          215..218
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          220..228
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          231..239
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            240..242
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          245..255
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          264..269
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           276..283
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          294..301
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            302..304
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           311..314
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          318..320
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           328..331
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            333..335
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           336..338
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           341..353
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            354..356
FT                   /evidence="ECO:0007829|PDB:6MYQ"
FT   TURN            359..362
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          364..368
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           374..380
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           382..392
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            396..398
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          401..411
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          413..416
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          420..426
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          429..438
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           440..442
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          446..448
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           457..475
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            487..490
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           491..501
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          504..508
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           509..523
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          524..528
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           530..545
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           546..549
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   HELIX           561..585
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          593..595
FT                   /evidence="ECO:0007829|PDB:6MYQ"
FT   HELIX           619..621
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          625..632
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            633..636
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   STRAND          637..644
FT                   /evidence="ECO:0007829|PDB:2H88"
FT   TURN            652..654
FT                   /evidence="ECO:0007829|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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