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UniProtKB/Swiss-Prot entry Q8LBZ7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHSB1_ARATH
Primary accession number Q8LBZ7
Secondary accession numbers Q9G3M0 Q9LTZ2
Integrated into Swiss-Prot on July 25, 2006
Sequence was last modified on July 25, 2006 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 46)
Name and origin of the protein
Protein name Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 1, mitochondrial [Precursor]
Synonyms EC 1.3.5.1
Iron-sulfur subunit of complex II
Ip
Gene name
Name: SDH2-1
OrderedLocusNames: At3g27380
ORFNames: K1G2.9
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
DOI=10.1023/A:1010612506070; PubMed=11442063 [NCBI, ExPASy, EBI, Israel, Japan]
Figueroa P., Leon G., Elorza A., Holuigue L., Jordana X.;
"Three different genes encode the iron-sulphur subunit of succinate dehydrogenase in Arabidopsis thaliana.";
Plant Mol. Biol. 46:241-250(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/7.2.131; PubMed=10819329 [NCBI, ExPASy, EBI, Israel, Japan]
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones.";
DNA Res. 7:131-135(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W., Redman J.C., Wu H.C., Utterback T., Town C.D.;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
SUBUNIT, AND TISSUE SPECIFICITY.
DOI=10.1023/A:1019926301981; PubMed=12374303 [NCBI, ExPASy, EBI, Israel, Japan]
Figueroa P., Leon G., Elorza A., Holuigue L., Araya A., Jordana X.;
"The four subunits of mitochondrial respiratory complex II are encoded by multiple nuclear genes and targeted to mitochondria in Arabidopsis thaliana.";
Plant Mol. Biol. 50:725-734(2002).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[8]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
DOI=10.1104/pp.104.049528; PubMed=15563621 [NCBI, ExPASy, EBI, Israel, Japan]
Elorza A., Leon G., Gomez I., Mouras A., Holuigue L., Araya A., Jordana X.;
"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.";
Plant Physiol. 136:4072-4087(2004).
Comments
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
AJ278910; CAC19855.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB024028; BAA95713.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY035013; AAK59518.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY063053; AAL34227.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY924777; AAX23852.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086901; AAM63946.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001118718.1; -.
NP_189374.1; -.
UniGene At.72257
3D structure databases
HSSP P07014; 1NEK. [HSSP ENTRY / PDB]
ModBase Q8LBZ7.
Organism-specific databases
GeneFarm 2168; 175.
TAIR At3g27380; -.
Gene expression databases
GermOnline AT3G27380; Arabidopsis thaliana.
Ontologies
GO
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.
Pfam PF00111; Fer2; 1.
Pfam graphical view of domain structure.
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).
ProtoNet Q8LBZ7.
Genome annotation databases
GeneID 822359; -.
GenomeReviews BA000014_GR; AT3G27380.
KEGG ath:AT3G27380; -.
NMPDR fig|3702.1.peg.15028; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; 3Fe-4S; 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide; Transport; Tricarboxylic acid cycle.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    28  28     Mitochondrion (Potential). 
CHAIN   29   279  251     Succinate dehydrogenase [ubiquinone] iron-sulfur subunit 1, mitochondrial. PRO_0000247595
DOMAIN   52   141  90     2Fe-2S ferredoxin-type. 
DOMAIN   184   214  31     4Fe-4S ferredoxin-type. 
METAL   102   102        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   107   107        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   110   110        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   122   122        Iron-sulfur 1 (2Fe-2S) (By similarity). 
METAL   194   194        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   197   197        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   200   200        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   204   204        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   251   251        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   257   257        Iron-sulfur 3 (3Fe-4S) (By similarity). 
METAL   261   261        Iron-sulfur 2 (4Fe-4S) (By similarity). 
BINDING   209   209        Ubiquinone; shared with DHSD (By similarity). 
CONFLICT   20    20        A -> V (in Ref. 1 and 4). 
CONFLICT   26    26        A -> V (in Ref. 1 and 4). 
CONFLICT   200   200        C -> F (in Ref. 4; AAM63946). 
Sequence information
Length: 279 AA [This is the length of the unprocessed precursor] Molecular weight: 31171 Da [This is the MW of the unprocessed precursor] CRC64: ADA885EC59A3EA36 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASGLIGRLV GTKPSKLATA ARLIPARWTS TGAEAETKAS SGGGRGSNLK TFQIYRWNPD 

        70         80         90        100        110        120 
NPGKPELQNY QIDLKDCGPM VLDALIKIKN EMDPSLTFRR SCREGICGSC AMNIDGCNGL 

       130        140        150        160        170        180 
ACLTKIQDEA SETTITPLPH MFVIKDLVVD MTNFYNQYKS IEPWLKRKTP ASVPAKEILQ 

       190        200        210        220        230        240 
SKKDRAKLDG MYECILCACC STSCPSYWWN PESYLGPAAL LHANRWISDS RDEYTKERLE 

       250        260        270 
AIDDEFKLYR CHTILNCARA CPKGLNPGKQ ITHIKQLQR 

Q8LBZ7 in FASTA format

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