NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=AX2;
Lay S.P., Fisher P.R.;
"The flavoprotein subunit 1 of Dictyostelium succinate dehydrogenase.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
DOI=10.1038/nature03481; PubMed=15875012 [NCBI, ExPASy, EBI, Israel, Japan]
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).

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) (By similarity).
CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol.
COFACTOR: FAD (By similarity).
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle .
SUBUNIT: Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit (By similarity).
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side (By similarity).
SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF211482; AAF21045.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AAFI02000037; EAL67069.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_641069.1; -.

3D structure databases

HSSP

P10444; 1NEK. [HSSP ENTRY / PDB]

ModBase

Q9U3X4.

Organism-specific databases

dictyBase

DDB_G0280535; sdhA.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0008177;	Molecular function: succinate dehydrogenase (ubiquinone) activity (inferred from electronic annotation from EC).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0046956;	Biological process: positive phototaxis (inferred from mutant phenotype from dictyBase).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003953; FAD_bind2_N.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR003952; FRD_SDH_FAD_BS.
IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR011281; Succ_DHase_flav_su_fwd.
IPR014006; Succ_Dhase_frdA_Gneg.
Graphical view of domain structure.

Pfam

PF00890; FAD_binding_2; 1.
PF02910; Succ_DH_flav_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.

TIGRFAMs

TIGR01816; sdhA_forward; 1.
TIGR01812; sdhA_frdA_Gneg; 1.

PROSITE

PS00504; FRD_SDH_FAD_BINDING; 1.

Genome annotation databases

GeneID

3392159; -.

KEGG

ddi:DDB_0214886; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide; Transport; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 24`	`24`	`Mitochondrion (Potential).`
`CHAIN`	`25 626`	`602`	`Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial.`	`PRO_0000327828`
`NP_BIND`	`69 84`	`16`	`FAD (By similarity).`
`ACT_SITE`	`318 318`		`Proton acceptor (By similarity).`
`BINDING`	`274 274`		`Substrate (By similarity).`
`BINDING`	`286 286`		`Substrate (By similarity).`
`BINDING`	`385 385`		`Substrate (By similarity).`
`BINDING`	`429 429`		`Substrate (By similarity).`
`MOD_RES`	`77 77`		`Tele-8alpha-FAD histidine (By similarity).`

Sequence information

Length: 626 AA [This is the length of the unprocessed precursor]

Molecular weight: 68516 Da [This is the MW of the unprocessed precursor]

CRC64: C8F27868BD063D67 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLSSALKLTK KVCSTKSNGL IRSFSTQTQS RDYAVVDHTY DAIVVGAGGA GLRAALGLTE 

        70         80         90        100        110        120 
KGYKTACITK LFPTRSHTVA AQGGINAALG NADQDDWRWH AYDTVKGSDF LGDQDAIHYM 

       130        140        150        160        170        180 
CKEAVPTVLE LEQYGVPFSR MDDGRIYQRA FGGQSKNFGK GGQATRCCAA ADRTGHALLH 

       190        200        210        220        230        240 
TLYGQAVKHN TKFFIEYFVT DLIMENGDCR GVVAINLEDG TIHRFRSHAT VIATGGYGRA 

       250        260        270        280        290        300 
YFSATSAHTC TGDGNAMVIR AGLPCQDLEF VQFHPTGIYG SGCLITEGAR GEGGYLLNSS 

       310        320        330        340        350        360 
GERFMPRYAP SVADLASRDV VSRSETMEIR EGRGVGPEKD HCLLNLTHLS PEIIDERLPG 

       370        380        390        400        410        420 
IRETAMIFAG VDVTKEPIPV IPTVHYNMGG IPTNYKGQVI TQVDGKDKLV KGLYAAGESA 

       430        440        450        460        470        480 
CVSVHGANRL GANSLLDIVV FGRAVANEIE NTLAKDTPHK PLPPNAGEES IANIDAIRFS 

       490        500        510        520        530        540 
NGTRSTAEIR LEMQKIMQRN AAVFRDGQVL KEGVELIDKC ARSLINDLKT TDRTMIWNTD 

       550        560        570        580        590        600 
LIESLELQNL MTQAVLTMHS AEARKESRGA HAREDYKERD DANWMKHTLS YLDVNTGKVT 

       610        620 
LNYRPVVSET LDQSEMETIK PFKRVY

Q9U3X4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools