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Reviewed, UniProtKB/Swiss-Prot O42772 (DHSB_MYCGR)

Last modified September 2, 2008. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMycosphaerella graminicola (Septoria tritici)
Taxonomic identifier54734 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCapnodialesMycosphaerellaceaeMycosphaerella

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 processElectron transport
Transport
Tricarboxylic acid cycle
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   Ligand2Fe-2S
3Fe-4S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionOxidoreductase

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 297Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Regions

Domain78 – 157802Fe-2S ferredoxin-type
Domain199 – 229314Fe-4S ferredoxin-type

Sites

Metal binding1171Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1221Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1251Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1371Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding2091Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2121Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2151Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2191Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2661Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2721Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2761Iron-sulfur 2 (4Fe-4S) By similarity
Binding site2241Ubiquinone; shared with DHSD By similarity

Sequences

Sequence LengthMass (Da)Tools
O42772-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: A50010A24F48F6D4

FASTA29733,667
        10         20         30         40         50         60 
MALRLATRRF APIAFRRGMA TTIEHTKEPI SATAEALSAS RPPIKETKTS TVKEPQMDAD 

        70         80         90        100        110        120 
AKTKTFHIYR WNPDQPTDKP RMQSYTLDLN KTGPMMLDAL IRIKNEVDPT LTFRRSCREG 

       130        140        150        160        170        180 
ICGSCAMNID GVNTLACLCR IPTDTAKETR IYPLPHTYVV KDLVPDMTQF YKQYKSIKPY 

       190        200        210        220        230        240 
LQRDTAPPDG KENRQSVADR KKLDGLYECI LCACCSTSCP SYWWNSEEYL GPAVLLQSYR 

       250        260        270        280        290 
WINDSRDEKT AQRKDALNNS MSLYRCHTIL NCSRTCPKGL NPALAIAEIK KSMAFTG 

« Hide

References

[1]"A single amino-acid substitution in the iron-sulphur protein subunit of succinate dehydrogenase determines resistance to carboxin in Mycosphaerella graminicola."
Skinner W., Bailey A.M., Renwick A., Keon J.P.R., Gurr S.J., Hargreaves J.A.
Curr. Genet. 34:393-398(1998) [PubMed: 9871122] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AF042062 Genomic DNA. Translation: AAB97419.1.

3D structure databases

HSSPHSSP built from PDB template 1NEK based on UniProtKB P07014.
SMRO42772. Positions 61-294.
ModBaseSearch...

Family and domain databases

InterProIPR006058. 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]
Gene3DG3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
PfamPF00111. Fer2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 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]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameDHSB_MYCGR
AccessionPrimary (citable) accession number: O42772
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: September 2, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents