[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Wirsel S.G.R., Voegele R.T., Baenninger R., Hahn M., Mendgen K.W.; "Prelude to transformation: characterization of the beta-tubulin and succinate dehydrogenase genes from the rust fungus Uromyces fabae."; Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.

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).
COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
COFACTOR: Binds 1 4Fe-4S cluster (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 succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.

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

AJ575686; CAE02642.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q70KF8; 51-282.

ModBase

Q70KF8.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051538;	Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
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: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

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 of domain structure.

Gene3D

G3DSA:3.10.20.30; Ferredoxin_fold; 1.
G3DSA:1.10.1060.10; Fum_reductase_C; 1.

TIGRFAMs

TIGR00384; dhsB; 1.

PROSITE

PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS00198; 4FE4S_FER_1; 1.
PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

Q70KF8.

UniRef

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

Keywords

2Fe-2S; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide; Transport; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Mitochondrion.`
`CHAIN`	`? 283`		`Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial.`	`PRO_0000010351`
`DOMAIN`	`66 145`	`80`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`186 216`	`31`	`4Fe-4S ferredoxin-type.`
`METAL`	`105 105`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`110 110`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`113 113`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`125 125`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`196 196`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`199 199`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`202 202`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`206 206`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`253 253`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`259 259`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`263 263`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`BINDING`	`211 211`		`Ubiquinone; shared with DHSD (By similarity).`

Sequence information

Length: 283 AA [This is the length of the unprocessed precursor]

Molecular weight: 32104 Da [This is the MW of the unprocessed precursor]

CRC64: 058945BABE06185F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MINIPNSIRP FIRSANRTPC YLRSISSSSS SSFATPAEEH AGKQPSSAVP VKEFSIYRWN 

        70         80         90        100        110        120 
PDEPSKKPTL QTYSIDLKKC GPMVLDALIK IKNELDPTLT FRRSCREGIC GSCAMNIDGV 

       130        140        150        160        170        180 
NTLACLKRIN KETSAPVKIY PLPHMYIIKD LVPDMTHFYK QYKSIEPFLK NDNPPAQGEF 

       190        200        210        220        230        240 
LQSPEDRKKL DGMYECILCA CCSTSCPSYW WNQDEYLGPA VLMQAYRWMA DSRDSYGEDR 

       250        260        270        280 
KEKLQNTLSL YRCHTIFNCT KTCPKGLNPA KAISHIKREM ASA

Q70KF8 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