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 03-AUG-2022, entry version 124.
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; Q9YHT1; -.
DR PRIDE; Q9YHT1; -.
DR GeneID; 395758; -.
DR KEGG; gga:395758; -.
DR CTD; 6389; -.
DR VEuPathDB; HostDB:geneid_395758; -.
DR eggNOG; KOG2403; Eukaryota.
DR InParanoid; Q9YHT1; -.
DR OrthoDB; 606981at2759; -.
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:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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: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; -; 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; 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 PANTHER; PTHR11632; PTHR11632; 1.
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; 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
