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

O82663 (SDHA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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] flavoprotein subunit 1, mitochondrial

EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit 1 of complex II
Short name=FP
Gene names
Name:SDH1-1
Ordered Locus Names:At5g66760
ORF Names:MSN2.16
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Flavoprotein (FP) 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

FAD 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: a flavoprotein (FP), an iron-sulfur protein (IP), 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 and inflorescences. Ref.6

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion Potential
Chain33 – 634602Succinate dehydrogenase [ubiquinone] flavoprotein subunit 1, mitochondrial
PRO_0000158659

Regions

Nucleotide binding56 – 616FAD By similarity
Nucleotide binding79 – 9416FAD By similarity
Nucleotide binding446 – 4472FAD By similarity

Sites

Active site3291Proton acceptor By similarity
Binding site2641FAD By similarity
Binding site2851Substrate By similarity
Binding site2971Substrate By similarity
Binding site3961Substrate By similarity
Binding site4301FAD By similarity
Binding site4411Substrate By similarity

Amino acid modifications

Modified residue871Tele-8alpha-FAD histidine By similarity

Sequences

Sequence LengthMass (Da)Tools
O82663 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: AECE471C7AD43B84

FASTA63469,656
        10         20         30         40         50         60 
MWRCVSRGFR APASKTSSLF DGVSGSRFSR FFSTGSTDTR SSYTIVDHTY DAVVVGAGGA 

        70         80         90        100        110        120 
GLRAAIGLSE HGFNTACITK LFPTRSHTVA AQGGINAALG NMSEDDWRWH MYDTVKGSDW 

       130        140        150        160        170        180 
LGDQDAIQYM CREAPKAVIE LENYGLPFSR TEEGKIYQRA FGGQSLDFGK GGQAYRCACA 

       190        200        210        220        230        240 
ADRTGHALLH TLYGQAMKHN TQFFVEYFAL DLLMASDGSC QGVIALNMED GTLHRFRSSQ 

       250        260        270        280        290        300 
TILATGGYGR AYFSATSAHT CTGDGNAMVA RAGLPLQDLE FVQFHPTGIY GAGCLITEGS 

       310        320        330        340        350        360 
RGEGGILRNS EGERFMERYA PTAKDLASRD VVSRSMTMEI REGRGVGPHK DHIYLHLNHL 

       370        380        390        400        410        420 
PPEVLKERLP GISETAAIFA GVDVTKEPIP VLPTVHYNMG GIPTNYHGEV VTIKGDDPDA 

       430        440        450        460        470        480 
VIPGLMAAGE AACASVHGAN RLGANSLLDI VVFGRACANR VAEISKPGEK QKPLEKDAGE 

       490        500        510        520        530        540 
KTIAWLDRLR NSNGSLPTST IRLNMQRIMQ NNAAVFRTQE TLEEGCQLID KAWESFGDVQ 

       550        560        570        580        590        600 
VKDRSMIWNS DLIETLELEN LLINASITMH SAEARKESRG AHAREDFTKR EDGEWMKHTL 

       610        620        630 
GYWEDEKVRL DYRPVHMDTL DDEIDTFPPK ARVY 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of succinyl-CoA-ligase from Arabidopsis thaliana."
Machuy N., Klein M., Mueller-Roeber B.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. C24.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
DNA Res. 7:31-63(2000) [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]"Proteomic approach to identify novel mitochondrial proteins in Arabidopsis."
Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.
Plant Physiol. 127:1694-1710(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 160-170.
Tissue: Leaf and Stem.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001809 mRNA. Translation: CAA05025.1.
AB018119 Genomic DNA. Translation: BAA97282.1.
CP002688 Genomic DNA. Translation: AED98260.1.
AF367341 mRNA. Translation: AAK32928.1.
AY045674 mRNA. Translation: AAK74032.1.
AF436833 mRNA. Translation: AAL32015.1.
AY124812 mRNA. Translation: AAM70521.1.
PIRT51815.
RefSeqNP_201477.1. NM_126074.2.
UniGeneAt.22655.
At.67108.

3D structure databases

ProteinModelPortalO82663.
SMRO82663. Positions 41-634.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO82663. 6 interactions.
MINTMINT-8063231.
STRING3702.AT5G66760.1-P.

Proteomic databases

PaxDbO82663.
PRIDEO82663.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G66760.1; AT5G66760.1; AT5G66760.
GeneID836809.
KEGGath:AT5G66760.

Organism-specific databases

GeneFarm2175. 174.
TAIRAT5G66760.

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000160475.
InParanoidO82663.
KOK00234.
OMAHGQVIIK.
PhylomeDBO82663.
ProtClustDBPLN00128.

Enzyme and pathway databases

BioCycARA:AT5G66760-MONOMER.
MetaCyc:AT5G66760-MONOMER.
UniPathwayUPA00223; UER01006.

Gene expression databases

GenevestigatorO82663.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROO82663.

Entry information

Entry nameSDHA1_ARATH
AccessionPrimary (citable) accession number: O82663
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 128 of the entry and version 1 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