Reviewed, UniProtKB/Swiss-Prot Q9YHT1 (DHSA_CHICK)

Names and origin

Protein names

Recommended name:
    Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
    EC=1.3.5.1
Alternative name(s):
    Flavoprotein subunit of complex II
      Short name=Fp

Gene names

Name:

SDHA

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	665 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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).
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	FAD.
Enzyme regulation	Inhibited by oxaloacetate.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Subunit structure	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. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment By similarity. Ref.3 Ref.4 Ref.5
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.3 Ref.4 Ref.5.
Miscellaneous	The complex, present in mitochondria, can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone By similarity.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	respiratory electron transport chain Inferred from sequence or structural similarity. Source: UniProtKB succinate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 44

44

Mitochondrion

Chain

45 – 665

621

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

PRO_0000344984

Regions

Nucleotide binding

92 – 107

16

FAD

Sites

Active site

341

1

Proton acceptor Ref.5

Binding site

297

1

Substrate

Binding site

309

1

Substrate

Binding site

408

1

Substrate

Binding site

452

1

Substrate

Amino acid modifications

Modified residue

100

1

Tele-8alpha-FAD histidine

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

665

Helix Strand Turn

Details...

Beta strand

1 – 3

3

Beta strand

5 – 13

9

Turn

14 – 17

4

Beta strand

20 – 25

6

Helix

31 – 43

13

Beta strand

49 – 52

4

Beta strand

54 – 62

9

Beta strand

65 – 73

9

Turn

74 – 76

3

Beta strand

79 – 89

11

Helix

95 – 97

3

Beta strand

98 – 103

6

Helix

110 – 117

8

Beta strand

128 – 135

8

Turn

136 – 138

3

Helix

145 – 148

4

Beta strand

152 – 154

3

Helix

162 – 165

4

Turn

167 – 169

3

Helix

170 – 172

3

Helix

175 – 187

13

Turn

193 – 196

4

Beta strand

198 – 202

5

Helix

208 – 214

7

Helix

216 – 226

11

Turn

230 – 232

3

Beta strand

235 – 245

11

Beta strand

247 – 250

4

Beta strand

254 – 260

7

Beta strand

263 – 272

10

Helix

274 – 276

3

Beta strand

280 – 282

3

Helix

291 – 307

17

Turn

321 – 324

4

Helix

325 – 335

11

Beta strand

340 – 342

3

Helix

343 – 357

15

Beta strand

358 – 362

5

Helix

364 – 380

17

Helix

381 – 383

3

Helix

395 – 419

25

Beta strand

429 – 432

4

Helix

453 – 455

3

Beta strand

459 – 466

8

Turn

467 – 470

4

Beta strand

471 – 478

8

Turn

486 – 488

3

Sequences

	Sequence		Length	Mass (Da)
	Q9YHT1-1 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: 9476AA19A7A3AE84	FASTA	665	72,931
	10 20 30 40 50 60 MAAVVAASRS LAKCWLRPAV RAWPAACQTH ARNFHFTVDG KKNASTKVSD SISTQYPVVD 70 80 90 100 110 120 HEFDAVVVGA GGAGLRAAFG LSEAGFNTAC VTKLFPTRSH TVAAQGGINA ALGNMEDDNW 130 140 150 160 170 180 RWHFYDTVKG SDWLGDQDAI HYMTEQAPAA VIELENYGMP FSRTEEGKIY QRAFGGQSLQ 190 200 210 220 230 240 FGKGGQAHRC CCVADRTGHS LLHTLYGRSL RYDTSYFVEY FALDLLMENG ECRGVIALCI 250 260 270 280 290 300 EDGTIHRFRA KNTVIATGGY GRTYFSCTSA HTSTGDGTAM VTRAGLPCQD LEFVQFHPTG 310 320 330 340 350 360 IYGAGCLITE GCRGEGGILI NSQGERFMER YAPVAKDLAS RDVVSRSMTI EIREGRGCGP 370 380 390 400 410 420 EKDHVYLQLH HLPPQQLATR LPGISETAMI FAGVDVTKEP IPVLPTVHYN MGGIPTNYKG 430 440 450 460 470 480 QVITHVNGED KVVPGLYACG EAASASVHGA NRLGANSLLD LVVFGRACAL TIAETCKPGE 490 500 510 520 530 540 PVPSIKPNAG EESVANLDKL RFADGTIRTS EARLNMQKTM QSHAAVFRTG SILQEGCEKL 550 560 570 580 590 600 SQIYCDLAHL KTFDRGIVWN TDLVETLELQ NLMLCALQTI YGAEARKESR GAHAREDYKF 610 620 630 640 650 660 RIDDFDYSKP LQGQQKRPFE EHWRKHTLSY VDVKSGKVTL KYRPVIDRTL NEEDCSSVPP AIRSY

References

[1]	"Detection of sequence polymorphisms in red junglefowl and white leghorn ESTs." Fitzsimmons C.J., Savolainen P., Amini B., Hjaelm G., Lundeberg J., Andersson L. Anim. Genet. 35:391-396(2004) [PubMed: 15373743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-324.
[2]	"OXPHOS genes in mammals and the molecular clock." Weinreich D.M. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 167-665. Tissue: Heart.
[3]	"Crystallization of mitochondrial respiratory complex II from chicken heart: a membrane-protein complex diffracting to 2.0 A." Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A. Acta Crystallogr. D 61:380-387(2005) [PubMed: 15805592] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 45-665 IN COMPLEX WITH FAD, SUBUNIT, SUBCELLULAR LOCATION.
[4]	"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." Huang L.-S., Shen J.T., Wang A.C., Berry E.A. Biochim. Biophys. Acta 1757:1073-1083(2006) [PubMed: 16935256] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 45-665 IN COMPLEXES WITH FAD AND MALONATE, SUBUNIT, SUBCELLULAR LOCATION.
[5]	"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." Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y., Anderson V.E., Berry E.A. J. Biol. Chem. 281:5965-5972(2006) [PubMed: 16371358] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 45-665 IN COMPLEXES WITH FAD; OXALOACETATE AND 3-NITROPROPIONIC ACID, ACTIVE SITE, SUBUNIT, MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CO635738 mRNA. No translation available.
AF095939 mRNA. Translation: AAC72374.1.

IPI

IPI00682371.

UniGene

Gga.993

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YQ3	X-ray	2.20	A	45-665	[»]
1YQ4	X-ray	2.33	A	45-665	[»]
2FBW	X-ray	2.10	A/N	45-665	[»]
2H88	X-ray	1.74	A/N	45-665	[»]
2H89	X-ray	2.40	A	45-665	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9YHT1.

Proteomic databases

PRIDE

Q9YHT1.

Genome annotation databases

Ensembl

ENSGALT00000021508; ENSGALP00000021475; ENSGALG00000013167; Gallus gallus. [Genome view]

Phylogenomic databases

eggNOG

veNOG05302.

HOGENOM

HBG293998.

HOVERGEN

Q9YHT1.

InParanoid

Q9YHT1.

Family and domain databases

InterPro

IPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_frdA_Gneg.
[Graphical view]

Pfam

PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

TIGRFAMs

TIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.

PROSITE

PS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DHSA_CHICK

Accession

Primary (citable) accession number: Q9YHT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	July 22, 2008
Last modified:	February 9, 2010
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)