Reviewed, UniProtKB/Swiss-Prot P47052 (DHSX_YEAST)

Names and origin

Protein names

Recommended name:
    Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial
    EC=1.3.5.1
Alternative name(s):
    Flavoprotein subunit of complex II
      Short name=FP
    SDH1b

Gene names

Ordered Locus Names:	YJL045W
ORF Names:	J1194

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	634 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	Probable minor catalytic 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). Probably forms a catalytic dimer with SDH2. Electrons flow from succinate to the FAD bound to the catalytic subunit, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4.
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	FAD.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	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.
Miscellaneous	In vitro, can complement a SDH1 disruption and leads to less than 15% of wild-type SDH reductase activity probably due to its lower expression level (compared to SDH1).
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	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro succinate dehydrogenase (ubiquinone) activity Ref.2 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 – 25	25	Mitochondrion Potential
	Chain	26 – 634	609	Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial		PRO_0000010343
Regions
	Nucleotide binding	76 – 91	16	FAD By similarity
Sites
	Active site	325	1	Proton acceptor By similarity
	Binding site	281	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	392	1	Substrate By similarity
	Binding site	438	1	Substrate By similarity
Amino acid modifications
	Modified residue	84	1	Tele-8alpha-FAD histidine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47052-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: F00CD157AB9BF9C5	FASTA	634	69,382
	10 20 30 40 50 60 MLSLKKGITK SYILQRTFTS SSVVRQIGEV KSESKPPAKY HIIDHEYDCV VVGAGGAGLR 70 80 90 100 110 120 AAFGLAEAGY KTACLSKLFP TRSHTVAAQG GINAALGNMH PDDWKSHMYD TVKGSDWLGD 130 140 150 160 170 180 QDAIHYMTRE APKSVIELEH YGMPFSRTED GRIYQRAFGG QSKDFGKGGQ AYRTCAVADR 190 200 210 220 230 240 TGHAMLHTLY GQALKNNTHF FIEYFAMDLL THNGEVVGVI AYNQEDGTIH RFRAHKTVIA 250 260 270 280 290 300 TGGYGRAYFS CTSAHTCTGD GNAMVSRAGF PLEDLEFVQF HPSGIYGSGC LITEGARGEG 310 320 330 340 350 360 GFLLNSEGER FMERYAPTAK DLASRDVVSR AITMEIRAGR GVGKNKDHIL LQLSHLPPEV 370 380 390 400 410 420 LKERLPGISE TAAVFAGVDV TQEPIPVLPT VHYNMGGIPT KWTGEALTID EETGEDKVIP 430 440 450 460 470 480 GLMACGEAAC VSVHGANRLG ANSLLDLVVF GRAVANTIAD TLQPGLPHKP LASNIGHESI 490 500 510 520 530 540 ANLDKVRNAR GSLKTSQIRL NMQRTMQKDV SVFRTQDTLD EGVRNITEVD KTFEDVHVSD 550 560 570 580 590 600 KSMIWNSDLV ETLELQNLLT CATQTAVSAS KRKESRGAHA REDYAKRDDV NWRKHTLSWQ 610 620 630 KGTSTPVKIK YRNVIAHTLD ENECAPVPPA VRSY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"Suppression of sdh1 mutations by the SDH1b gene of Saccharomyces cerevisiae." Colby G., Ishii Y., Tzagoloff A. Yeast 14:1001-1006(1998) [PubMed: 9730279] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49320 Genomic DNA. Translation: CAA89336.1.
PIR	S56817.
RefSeq	NP_012490.1.
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P10444.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4262N.
IntAct	P47052.
Proteomic databases
PeptideAtlas	P47052.
Genome annotation databases
Ensembl	YJL045W. Saccharomyces cerevisiae. [Contig view]
GeneID	853405.
GenomeReviews	Gene locus YJL045W in contig Y13136_GR.
KEGG	sce:YJL045W.
NMPDR	fig|4932.3.peg.3464.
Organism-specific databases
CYGD	YJL045w.
SGD	S000003581. YJL045W.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P47052.
Gene expression databases
ArrayExpress	P47052.
GermOnline	YJL045W. Saccharomyces cerevisiae.
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. IPR011281. Succ_DHase_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...
Other Resources
LinkHub	P47052.
NextBio	973903.

Entry information

Entry name

DHSX_YEAST

Accession

Primary (citable) accession number: P47052

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 25, 2008
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)