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

Q9ZPX5 (SDHA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 101. 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 2, mitochondrial

EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit 2 of complex II
Short name=FP
Gene names
Name:SDH1-2
Ordered Locus Names:At2g18450
ORF Names:T30D6.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length632 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.5

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.6.

Tissue specificity

Expressed at a low level. Ref.5

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 – 2929Mitochondrion Potential
Chain30 – 632603Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial
PRO_0000247592

Regions

Nucleotide binding54 – 596FAD By similarity
Nucleotide binding77 – 9216FAD By similarity
Nucleotide binding444 – 4452FAD By similarity

Sites

Active site3271Proton acceptor By similarity
Binding site2621FAD By similarity
Binding site2831Substrate By similarity
Binding site2951Substrate By similarity
Binding site3941Substrate By similarity
Binding site4281FAD By similarity
Binding site4391Substrate By similarity

Amino acid modifications

Modified residue851Tele-8alpha-FAD histidine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZPX5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DEC34651679CEF88

FASTA63269,363
        10         20         30         40         50         60 
MWRCLRVASS SRRSESNGAF ITSQLSRFFS APPSAGDKSS YTIVDHTYDA VVVGAGGAGL 

        70         80         90        100        110        120 
RAAIGLSEHG FNTACITKLF PTRSHTVAAQ GGINAALGNM SVDDWRWHMY DTVKGSDWLG 

       130        140        150        160        170        180 
DQDAIQYMCR EAPKAVIELE NYGLPFSRTE DGKIYQRAFG GQSLEFGIGG QAYRCACAAD 

       190        200        210        220        230        240 
RTGHALLHTL YGQAMKHNTQ FFVEYFALDL IMNSDGTCQG VIALNMEDGT LHRFHAGSTI 

       250        260        270        280        290        300 
LATGGYGRAY FSATSAHTCT GDGNAMVARA GLPLQDLEFV QFHPTGIYGA GCLITEGARG 

       310        320        330        340        350        360 
EGGILRNSEG EKFMDRYAPT ARDLASRDVV SRSMTMEIRQ GRGAGPMKDY LYLYLNHLPP 

       370        380        390        400        410        420 
EVLKERLPGI SETAAIFAGV DVTREPIPVL PTVHYNMGGI PTNYHGEVIT LRGDDPDAVV 

       430        440        450        460        470        480 
PGLMAAGEAA CASVHGANRL GANSLLDIVV FGRACANRVA EIQKPGEKLK PLEKDAGEKS 

       490        500        510        520        530        540 
IEWLDRIRNS NGSLPTSKIR LNMQRVMQNN AAVFRTQETL EEGCDLIDKT WDSFGDVKVT 

       550        560        570        580        590        600 
DRSMIWNSDL IETMELENLL VNACITMHSA EARKESRGAH AREDFTKRDD ANWMKHTLGY 

       610        620        630 
WEEGNVKLEY RPVHMKTLDD EVDTFPPKPR VY 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC006439 Genomic DNA. Translation: AAD15493.1.
CP002685 Genomic DNA. Translation: AEC06769.1.
AK119142 mRNA. Translation: BAC43712.1.
BT005938 mRNA. Translation: AAO64873.1.
PIRD84564.
RefSeqNP_179435.1. NM_127401.2.
UniGeneAt.39995.

3D structure databases

ProteinModelPortalQ9ZPX5.
SMRQ9ZPX5. Positions 39-632.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G18450.1-P.

Proteomic databases

PRIDEQ9ZPX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G18450.1; AT2G18450.1; AT2G18450.
GeneID816359.
KEGGath:AT2G18450.

Organism-specific databases

GeneFarm2186. 174.
TAIRAT2G18450.

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000160475.
InParanoidQ9ZPX5.
KOK00234.
OMAETIRWAE.
PhylomeDBQ9ZPX5.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Gene expression databases

GenevestigatorQ9ZPX5.

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...

Entry information

Entry nameSDHA2_ARATH
AccessionPrimary (citable) accession number: Q9ZPX5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 101 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