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Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp)

 SDHA_CHICK              Reviewed;         665 AA.
Q9YHT1;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
28-MAR-2018, entry version 108.
RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
EC=1.3.5.1 {ECO:0000305|PubMed:16371358};
AltName: Full=Flavoprotein subunit of complex II;
Short=Fp;
Flags: Precursor;
Name=SDHA;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-324.
PubMed=15373743; DOI=10.1111/j.1365-2052.2004.01184.x;
Fitzsimmons C.J., Savolainen P., Amini B., Hjaelm G., Lundeberg J.,
Andersson L.;
"Detection of sequence polymorphisms in red junglefowl and white
leghorn ESTs.";
Anim. Genet. 35:391-396(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 167-665.
TISSUE=Heart;
Weinreich D.M.;
"OXPHOS genes in mammals and the molecular clock.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[3]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 45-665 IN COMPLEX WITH FAD,
SUBUNIT, SUBCELLULAR LOCATION, AND COFACTOR.
PubMed=15805592; DOI=10.1107/S0907444905000181;
Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A.;
"Crystallization of mitochondrial respiratory complex II from chicken
heart: a membrane-protein complex diffracting to 2.0 A.";
Acta Crystallogr. D 61:380-387(2005).
[4]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 45-665 IN COMPLEXES WITH FAD
AND MALONATE, SUBUNIT, SUBCELLULAR LOCATION, AND COFACTOR.
PubMed=16935256; DOI=10.1016/j.bbabio.2006.06.015;
Huang L.-S., Shen J.T., Wang A.C., Berry E.A.;
"Crystallographic studies of the binding of ligands to the
dicarboxylate site of complex II, and the identity of the ligand in
the 'oxaloacetate-inhibited' state.";
Biochim. Biophys. Acta 1757:1073-1083(2006).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 45-665 IN COMPLEXES WITH FAD;
OXALOACETATE AND 3-NITROPROPIONIC ACID, COFACTOR, FUNCTION, CATALYTIC
ACTIVITY, PATHWAY, ACTIVE SITE, SUBUNIT, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16371358; DOI=10.1074/jbc.M511270200;
Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y.,
Anderson V.E., Berry E.A.;
"3-nitropropionic acid is a suicide inhibitor of mitochondrial
respiration that, upon oxidation by complex II, forms a covalent
adduct with a catalytic base arginine in the active site of the
enzyme.";
J. Biol. Chem. 281:5965-5972(2006).
-!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase
(SDH) that is involved in complex II of the mitochondrial electron
transport chain and is responsible for transferring electrons from
succinate to ubiquinone (coenzyme Q).
{ECO:0000305|PubMed:16371358}.
-!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
{ECO:0000305|PubMed:16371358}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:15805592,
ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
fumarate from succinate (eukaryal route): step 1/1.
{ECO:0000305|PubMed:16371358}.
-!- SUBUNIT: Component of complex II composed of four subunits: the
flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a
cytochrome b560 composed of SDHC and SDHD.
{ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}; Peripheral membrane protein
{ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}; Matrix side
{ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
-!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
FRD/SDH subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CO635738; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF095939; AAC72374.1; -; mRNA.
RefSeq; NP_001264327.1; NM_001277398.1.
UniGene; Gga.993; -.
PDB; 1YQ3; X-ray; 2.20 A; A=45-665.
PDB; 1YQ4; X-ray; 2.33 A; A=45-665.
PDB; 2FBW; X-ray; 2.10 A; A/N=45-665.
PDB; 2H88; X-ray; 1.74 A; A/N=45-665.
PDB; 2H89; X-ray; 2.40 A; A=45-665.
PDB; 2WQY; X-ray; 2.10 A; A/N=45-665.
PDBsum; 1YQ3; -.
PDBsum; 1YQ4; -.
PDBsum; 2FBW; -.
PDBsum; 2H88; -.
PDBsum; 2H89; -.
PDBsum; 2WQY; -.
ProteinModelPortal; Q9YHT1; -.
SMR; Q9YHT1; -.
STRING; 9031.ENSGALP00000021475; -.
PaxDb; Q9YHT1; -.
PRIDE; Q9YHT1; -.
GeneID; 395758; -.
KEGG; gga:395758; -.
CTD; 6389; -.
eggNOG; KOG2403; Eukaryota.
eggNOG; COG1053; LUCA.
HOGENOM; HOG000160475; -.
HOVERGEN; HBG001461; -.
InParanoid; Q9YHT1; -.
KO; K00234; -.
PhylomeDB; Q9YHT1; -.
Reactome; R-GGA-372987; The tricarboxylic acid cycle.
UniPathway; UPA00223; UER01006.
EvolutionaryTrace; Q9YHT1; -.
PRO; PR:Q9YHT1; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:UniProtKB.
GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
Gene3D; 3.50.50.60; -; 2.
Gene3D; 3.90.700.10; -; 1.
InterPro; IPR003953; FAD-binding_2.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR003952; FRD_SDH_FAD_BS.
InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
InterPro; IPR011281; Succ_DH_flav_su_fwd.
InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
Pfam; PF00890; FAD_binding_2; 1.
Pfam; PF02910; Succ_DH_flav_C; 1.
SUPFAM; SSF46977; SSF46977; 1.
SUPFAM; SSF51905; SSF51905; 2.
SUPFAM; SSF56425; SSF56425; 1.
TIGRFAMs; TIGR01816; sdhA_forward; 1.
TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Electron transport; FAD;
Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
Oxidoreductase; Reference proteome; Transit peptide; Transport;
Tricarboxylic acid cycle.
TRANSIT 1 44 Mitochondrion.
{ECO:0000269|PubMed:15805592,
ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
CHAIN 45 665 Succinate dehydrogenase [ubiquinone]
flavoprotein subunit, mitochondrial.
/FTId=PRO_0000344984.
NP_BIND 69 74 FAD. {ECO:0000269|PubMed:15805592,
ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
NP_BIND 92 107 FAD. {ECO:0000269|PubMed:15805592,
ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
NP_BIND 457 458 FAD. {ECO:0000269|PubMed:15805592,
ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
ACT_SITE 341 341 Proton acceptor.
{ECO:0000269|PubMed:16371358}.
BINDING 276 276 FAD. {ECO:0000269|PubMed:15805592,
ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
BINDING 297 297 Substrate. {ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
BINDING 309 309 Substrate. {ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
BINDING 408 408 Substrate. {ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
BINDING 441 441 FAD. {ECO:0000269|PubMed:15805592,
ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
BINDING 452 452 Substrate. {ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
MOD_RES 100 100 Tele-8alpha-FAD histidine.
{ECO:0000269|PubMed:16371358,
ECO:0000269|PubMed:16935256}.
STRAND 58 68 {ECO:0000244|PDB:2H88}.
HELIX 72 83 {ECO:0000244|PDB:2H88}.
STRAND 88 94 {ECO:0000244|PDB:2H88}.
HELIX 96 98 {ECO:0000244|PDB:2H88}.
HELIX 100 103 {ECO:0000244|PDB:2H88}.
STRAND 114 116 {ECO:0000244|PDB:2H88}.
HELIX 120 130 {ECO:0000244|PDB:2H88}.
TURN 131 133 {ECO:0000244|PDB:2H88}.
HELIX 137 156 {ECO:0000244|PDB:2H88}.
STRAND 167 169 {ECO:0000244|PDB:2H88}.
STRAND 171 179 {ECO:0000244|PDB:2FBW}.
TURN 180 183 {ECO:0000244|PDB:2H88}.
STRAND 186 191 {ECO:0000244|PDB:2FBW}.
HELIX 197 209 {ECO:0000244|PDB:2H88}.
STRAND 215 218 {ECO:0000244|PDB:2H88}.
STRAND 220 228 {ECO:0000244|PDB:2H88}.
STRAND 231 239 {ECO:0000244|PDB:2H88}.
TURN 240 242 {ECO:0000244|PDB:2H88}.
STRAND 245 255 {ECO:0000244|PDB:2H88}.
HELIX 261 263 {ECO:0000244|PDB:2H88}.
STRAND 264 269 {ECO:0000244|PDB:2H88}.
HELIX 276 283 {ECO:0000244|PDB:2H88}.
STRAND 294 301 {ECO:0000244|PDB:2H88}.
TURN 302 304 {ECO:0000244|PDB:2H88}.
HELIX 311 314 {ECO:0000244|PDB:2H88}.
STRAND 318 320 {ECO:0000244|PDB:2H88}.
HELIX 328 331 {ECO:0000244|PDB:2H88}.
TURN 333 335 {ECO:0000244|PDB:2H88}.
HELIX 336 338 {ECO:0000244|PDB:2H88}.
HELIX 341 353 {ECO:0000244|PDB:2H88}.
TURN 354 356 {ECO:0000244|PDB:1YQ3}.
TURN 359 362 {ECO:0000244|PDB:2H88}.
STRAND 364 368 {ECO:0000244|PDB:2H88}.
HELIX 374 380 {ECO:0000244|PDB:2H88}.
HELIX 382 392 {ECO:0000244|PDB:2H88}.
TURN 396 398 {ECO:0000244|PDB:2H88}.
STRAND 401 411 {ECO:0000244|PDB:2H88}.
STRAND 413 416 {ECO:0000244|PDB:2H88}.
STRAND 420 426 {ECO:0000244|PDB:2H88}.
STRAND 429 438 {ECO:0000244|PDB:2H88}.
HELIX 440 442 {ECO:0000244|PDB:2H88}.
STRAND 446 448 {ECO:0000244|PDB:2H88}.
HELIX 457 475 {ECO:0000244|PDB:2H88}.
TURN 487 490 {ECO:0000244|PDB:2H88}.
HELIX 491 501 {ECO:0000244|PDB:2H88}.
STRAND 504 508 {ECO:0000244|PDB:2H88}.
HELIX 509 523 {ECO:0000244|PDB:2H88}.
STRAND 524 528 {ECO:0000244|PDB:2H88}.
HELIX 530 545 {ECO:0000244|PDB:2H88}.
HELIX 546 549 {ECO:0000244|PDB:2H88}.
HELIX 561 585 {ECO:0000244|PDB:2H88}.
STRAND 595 598 {ECO:0000244|PDB:2FBW}.
HELIX 619 621 {ECO:0000244|PDB:2H88}.
STRAND 625 632 {ECO:0000244|PDB:2H88}.
TURN 633 636 {ECO:0000244|PDB:2H88}.
STRAND 637 644 {ECO:0000244|PDB:2H88}.
TURN 652 654 {ECO:0000244|PDB:2H88}.
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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