Reviewed, UniProtKB/Swiss-Prot Q6FWS8 (DHSB_CANGA)

Names and origin

Protein names

Recommended name:
    Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
    EC=1.3.5.1
Alternative name(s):
    Iron-sulfur subunit of complex II
      Short name=Ip

Gene names

Name:	SDH2
Ordered Locus Names:	CAGL0C03223g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Iron-sulfur protein (IP) 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	Binds 1 2Fe-2S cluster By similarity. Binds 1 3Fe-4S cluster By similarity. Binds 1 4Fe-4S cluster By similarity.
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 sideBy similarity.
Sequence similarities	Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
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	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – ?		Mitochondrion
	Chain	? – 253		Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial		PRO_0000010348
Regions
	Domain	23 – 114	92	2Fe-2S ferredoxin-type
	Domain	156 – 186	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	74	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	79	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	82	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	94	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	166	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	169	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	172	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	176	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	223	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	229	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	233	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Binding site	181	1	Ubiquinone; shared with DHSD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FWS8-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 2557E1940B402EA3	FASTA	253	29,054
	10 20 30 40 50 60 MFMLRVSRRG LATATSVPRL KTFKIYRWNP DKPTEKPHLQ EYKVDLEDCG PMVLDALLKI 70 80 90 100 110 120 KNEQDATLTF RRSCREGICG SCAMNIGGAN TLACLCKIDQ DESKTTKIYP LPHMFIVKDL 130 140 150 160 170 180 VPDLTGFYQQ YKSIQPYLQR TDYPADGKEV LQSIDDRKKL DGLYECILCA CCSTSCPSYW 190 200 210 220 230 240 WNQEEYLGPA VLMQAYRWLI DSRDQATKAR RTMLQNSMSL YRCHTIMNCT RTCPKGLNPG 250 RSIAEIKKQL AFD

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380949 Genomic DNA. Translation: CAG58222.1.
RefSeq	XP_445316.1.
3D structure databases
SMR	Q6FWS8. Positions 19-251.
ModBase	Search...
Genome annotation databases
GeneID	2886893.
KEGG	cgr:CAGL0C03223g.
Phylogenomic databases
HOGENOM	Q6FWS8.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001450. 4Fe4S_Fe_S_bd. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR004489. Succ_DHase/fum_Rdtase_Fe-S. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00384. dhsB. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHSB_CANGA

Accession

Primary (citable) accession number: Q6FWS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 19, 2004
Last modified:	November 25, 2008
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)