[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s002940050036; PubMed=8821668 [NCBI, ExPASy, EBI, Israel, Japan] Viehmann S., Richard O., Boyen C., Zetsche K.; "Genes for two subunits of succinate dehydrogenase form a cluster on the mitochondrial genome of Rhodophyta."; Curr. Genet. 29:199-201(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Apices; DOI=10.1006/jmbi.1995.0392; PubMed=7616569 [NCBI, ExPASy, EBI, Israel, Japan] Leblanc C., Boyen C., Richard O., Bonnard G., Grienenberger J.-M., Kloareg B.; "Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus crispus (Gigartinales). Gene content and genome organization."; J. Mol. Biol. 250:484-495(1995).

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

Z47547; CAA87611.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S59114; S59114.

RefSeq

NP_062488.1; -.

3D structure databases

HSSP

P07014; 1NEK. [HSSP ENTRY / PDB]

ModBase

P48932.

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).

BLOCKS

P48932.

Genome annotation databases

GeneID

809396; -.

Other

ProtoNet

P48932.

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; Transport; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 250`	`250`	`Succinate dehydrogenase [ubiquinone] iron-sulfur subunit.`	`PRO_0000158694`
`DOMAIN`	`30 110`	`81`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`153 183`	`31`	`4Fe-4S ferredoxin-type.`
`METAL`	`73 73`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`78 78`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`81 81`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`93 93`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`163 163`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`166 166`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`169 169`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`173 173`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`220 220`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`226 226`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`230 230`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`BINDING`	`178 178`		`Ubiquinone; shared with DHSD (By similarity).`

Sequence information

Length: 250 AA [This is the length of the unprocessed precursor]

Molecular weight: 28887 Da [This is the MW of the unprocessed precursor]

CRC64: 09511AE52A4CA149 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIIKNLNQKI ITIDNSSPYQ KFIRIYRWNP NLNLNPWFSI FPISTNNCGP MILDALIQIK 

        70         80         90        100        110        120 
NIQDSSLTFR RSCREGICGS CSMNIDGTNS LACLRSLNTK SNFITIYPLP HTYIIKDLVP 

       130        140        150        160        170        180 
DLSNFYAQYK LIKPWLINKI GFSLKENLQS KIDRLELDGL YECILCACCS ASCPSYWWNQ 

       190        200        210        220        230        240 
DKYLGPAILL QAYRWIVDSR DNSTENRLNF LNNKMRLFRC HTIMNCSKTC PKSLNPGKAI 

       250 
ASIKYRIINN

P48932 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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