Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8LB02 (SDHB2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, mitochondrial

EC=1.3.5.1
Alternative name(s):
Iron-sulfur subunit of complex II
Short name=Ip
Gene names
Name:SDH2-2
Ordered Locus Names:At5g40650
ORF Names:MNF13.170, MNF13.21
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 + a quinone = fumarate + a quinol.

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; fumarate from succinate (eukaryal route): step 1/1.

Subunit structure

Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b composed of a large and a small subunit By similarity. Ref.6

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.7.

Tissue specificity

Ubiquitous. Preferentially expressed in flowers, inflorescences and root tips. Ref.1 Ref.6 Ref.8

Developmental stage

Expressed in floral meristems and sex organ primordia at early stages of development. Later expressed in anthers, particularly in the tapetum, pollen mother cells, and microspores. Ref.8

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitochondrial electron transport, succinate to ubiquinone

Inferred from sequence or structural similarity Ref.1. Source: TAIR

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial respiratory chain complex II

Inferred from direct assay PubMed 15604729. Source: TAIR

mitochondrion

Inferred from direct assay Ref.1Ref.7. Source: TAIR

succinate dehydrogenase complex

Inferred from sequence or structural similarity Ref.1. Source: TAIR

   Molecular_function2 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 sequence or structural similarity Ref.1. Source: TAIR

succinate dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: UniProtKB-EC

succinate dehydrogenase activity

Inferred from sequence or structural similarity Ref.1. Source: TAIR

zinc ion binding

Inferred from direct assay PubMed 20018591. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 280252Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, mitochondrial
PRO_0000247596

Regions

Domain51 – 140902Fe-2S ferredoxin-type
Domain183 – 213314Fe-4S ferredoxin-type

Sites

Metal binding1011Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1061Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1091Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1211Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1931Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1961Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1991Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2031Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2501Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2561Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2601Iron-sulfur 2 (4Fe-4S) By similarity
Binding site2081Ubiquinone; shared with DHSD By similarity

Experimental info

Sequence conflict141S → P in CAC19856. Ref.1
Sequence conflict141S → P in AAM65047. Ref.5
Sequence conflict311T → K in CAC19856. Ref.1
Sequence conflict311T → K in AAM65047. Ref.5
Sequence conflict1271S → F in CAC19856. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8LB02 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 1F505A8C7D68DACD

FASTA28031,141
        10         20         30         40         50         60 
MAFGLIGRVV GTKSSRLSTA ARLIPARWTS TGSEAQSKAS TGGGGASLKT FQIYRWNPDN 

        70         80         90        100        110        120 
PGKPELQDYK IDLKDCGPMV LDALIKIKNE MDPSLTFRRS CREGICGSCA MNIDGCNGLA 

       130        140        150        160        170        180 
CLTKIESGSK ETTITPLPHM FVIKDLVVDM TNFYNQYKSI EPWLKRKNPA SVPGKEILQS 

       190        200        210        220        230        240 
KKDRAKLDGM YECILCACCS TSCPSYWWNP ESYLGPAALL HANRWISDSR DEYTKERLEA 

       250        260        270        280 
IDDEFKLYRC HTILNCARAC PKGLNPGKQI THIKQLQKSG 

« Hide

References

« Hide 'large scale' references
[1]"Three different genes encode the iron-sulphur subunit of succinate dehydrogenase in Arabidopsis thaliana."
Figueroa P., Leon G., Elorza A., Holuigue L., Jordana X.
Plant Mol. Biol. 46:241-250(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The four subunits of mitochondrial respiratory complex II are encoded by multiple nuclear genes and targeted to mitochondria in Arabidopsis thaliana."
Figueroa P., Leon G., Elorza A., Holuigue L., Araya A., Jordana X.
Plant Mol. Biol. 50:725-734(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, TISSUE SPECIFICITY.
[7]"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Landsberg erecta.
[8]"Nuclear SDH2-1 and SDH2-2 genes, encoding the iron-sulfur subunit of mitochondrial complex II in Arabidopsis, have distinct cell-specific expression patterns and promoter activities."
Elorza A., Leon G., Gomez I., Mouras A., Holuigue L., Araya A., Jordana X.
Plant Physiol. 136:4072-4087(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ278911 mRNA. Translation: CAC19856.1.
AB009052 Genomic DNA. Translation: BAB08537.1.
CP002688 Genomic DNA. Translation: AED94578.1.
AY074299 mRNA. Translation: AAL66996.1.
AY123036 mRNA. Translation: AAM67569.1.
AY087504 mRNA. Translation: AAM65047.1.
RefSeqNP_198881.1. NM_123430.1.
UniGeneAt.20145.
At.67187.
At.7421.

3D structure databases

ProteinModelPortalQ8LB02.
SMRQ8LB02. Positions 46-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8LB02. 1 interaction.

Proteomic databases

PaxDbQ8LB02.
PRIDEQ8LB02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G40650.1; AT5G40650.1; AT5G40650.
GeneID834065.
KEGGath:AT5G40650.

Organism-specific databases

GeneFarm2169. 175.
TAIRAT5G40650.

Phylogenomic databases

eggNOGCOG0479.
HOGENOMHOG000160590.
InParanoidQ8LB02.
KOK00235.
OMAIMNCSRT.
PhylomeDBQ8LB02.

Enzyme and pathway databases

BioCycMetaCyc:AT5G40650-MONOMER.
UniPathwayUPA00223; UER01006.

Gene expression databases

GenevestigatorQ8LB02.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
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]
ProtoNetSearch...

Entry information

Entry nameSDHB2_ARATH
AccessionPrimary (citable) accession number: Q8LB02
Secondary accession number(s): Q9FM32, Q9G3L9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: May 14, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names