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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, mitochondrial

Gene

SDH2-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster.By similarity
  • [3Fe-4S] clusterBy similarityNote: Binds 1 [3Fe-4S] cluster.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Pathway: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes fumarate from succinate (eukaryal route).Curated
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate dehydrogenase [ubiquinone] flavoprotein subunit 1, mitochondrial (SDH1-1), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 3, mitochondrial (SDH2-3), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 1, mitochondrial (SDH2-1), Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial (SDH1-2), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, mitochondrial (SDH2-2)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes fumarate from succinate (eukaryal route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi106 – 1061Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi121 – 1211Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi193 – 1931Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi196 – 1961Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi199 – 1991Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi203 – 2031Iron-sulfur 3 (3Fe-4S)By similarity
Binding sitei208 – 2081Ubiquinone; shared with SdhD subunitBy similarity
Metal bindingi250 – 2501Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi256 – 2561Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi260 – 2601Iron-sulfur 2 (4Fe-4S)By similarity

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  • 3 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • electron carrier activity Source: TAIR
  • succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  • succinate dehydrogenase activity Source: TAIR
  • zinc ion binding Source: TAIR

GO - Biological processi

  • mitochondrial electron transport, succinate to ubiquinone Source: TAIR
  • tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:AT5G40650-MONOMER.
BRENDAi1.3.5.1. 399.
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SDH2-2
Ordered Locus Names:At5g40650
ORF Names:MNF13.170, MNF13.21
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G40650.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) Source: TAIR
  • mitochondrion Source: TAIR
  • respiratory chain complex II Source: UniProtKB
  • succinate dehydrogenase complex Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionSequence AnalysisAdd
BLAST
Chaini29 – 280252Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 2, mitochondrialPRO_0000247596Add
BLAST

Proteomic databases

PaxDbiQ8LB02.
PRIDEiQ8LB02.

Expressioni

Tissue specificityi

Ubiquitous. Preferentially expressed in flowers, inflorescences and root tips.2 Publications

Developmental stagei

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.1 Publication

Interactioni

Subunit structurei

Component of complex II composed of eight subunits in plants: four classical SDH subunits SDH1, SDH2, SDH3 and SDH4 (a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.), as well as four subunits unknown in mitochondria from bacteria and heterotrophic eukaryotes.1 Publication

Protein-protein interaction databases

IntActiQ8LB02. 1 interaction.
STRINGi3702.AT5G40650.1.

Structurei

3D structure databases

ProteinModelPortaliQ8LB02.
SMRiQ8LB02. Positions 46-279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 140902Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini183 – 213314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
InParanoidiQ8LB02.
KOiK00235.
OMAiIDSHERM.
PhylomeDBiQ8LB02.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8LB02-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFGLIGRVV GTKSSRLSTA ARLIPARWTS TGSEAQSKAS TGGGGASLKT
60 70 80 90 100
FQIYRWNPDN PGKPELQDYK IDLKDCGPMV LDALIKIKNE MDPSLTFRRS
110 120 130 140 150
CREGICGSCA MNIDGCNGLA CLTKIESGSK ETTITPLPHM FVIKDLVVDM
160 170 180 190 200
TNFYNQYKSI EPWLKRKNPA SVPGKEILQS KKDRAKLDGM YECILCACCS
210 220 230 240 250
TSCPSYWWNP ESYLGPAALL HANRWISDSR DEYTKERLEA IDDEFKLYRC
260 270 280
HTILNCARAC PKGLNPGKQI THIKQLQKSG
Length:280
Mass (Da):31,141
Last modified:July 25, 2006 - v2
Checksum:i1F505A8C7D68DACD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141S → P in CAC19856 (PubMed:11442063).Curated
Sequence conflicti14 – 141S → P in AAM65047 (Ref. 5) Curated
Sequence conflicti31 – 311T → K in CAC19856 (PubMed:11442063).Curated
Sequence conflicti31 – 311T → K in AAM65047 (Ref. 5) Curated
Sequence conflicti127 – 1271S → F in CAC19856 (PubMed:11442063).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_198881.1. NM_123430.1.
UniGeneiAt.20145.
At.67187.
At.7421.

Genome annotation databases

EnsemblPlantsiAT5G40650.1; AT5G40650.1; AT5G40650.
GeneIDi834065.
KEGGiath:AT5G40650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_198881.1. NM_123430.1.
UniGeneiAt.20145.
At.67187.
At.7421.

3D structure databases

ProteinModelPortaliQ8LB02.
SMRiQ8LB02. Positions 46-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8LB02. 1 interaction.
STRINGi3702.AT5G40650.1.

Proteomic databases

PaxDbiQ8LB02.
PRIDEiQ8LB02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G40650.1; AT5G40650.1; AT5G40650.
GeneIDi834065.
KEGGiath:AT5G40650.

Organism-specific databases

GeneFarmi2169. 175.
TAIRiAT5G40650.

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
InParanoidiQ8LB02.
KOiK00235.
OMAiIDSHERM.
PhylomeDBiQ8LB02.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.
BioCyciMetaCyc:AT5G40650-MONOMER.
BRENDAi1.3.5.1. 399.

Miscellaneous databases

PROiQ8LB02.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "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.
  7. "New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II."
    Eubel H., Jansch L., Braun H.P.
    Plant Physiol. 133:274-286(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes contain plant specific subunits."
    Millar A.H., Eubel H., Jansch L., Kruft V., Heazlewood J.L., Braun H.P.
    Plant Mol. Biol. 56:77-90(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
  9. "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.

Entry informationi

Entry nameiSDHB2_ARATH
AccessioniPrimary (citable) accession number: Q8LB02
Secondary accession number(s): Q9FM32, Q9G3L9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: June 24, 2015
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.