Succinate dehydrogenase [ubiquinone] flavoprotein subunit 1, mitochondrial precursor

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O82663 (DHSA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	634 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 + ubiquinone = fumarate + ubiquinol.
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.
Tissue specificity	Ubiquitous. Preferentially expressed in flowers and inflorescences. Ref.6
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial electron transport, succinate to ubiquinone Traceable author statement Ref.6. Source: TAIR tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cell wall Inferred from direct assay PubMed 16287169. Source: TAIR mitochondrial respiratory chain complex II Inferred from direct assay PubMed 15604729. Source: TAIR
Molecular_function	ATP binding Inferred from direct assay PubMed 17137349. Source: TAIR cobalt ion binding Inferred from direct assay PubMed 20018591. Source: TAIR disulfide oxidoreductase activity Inferred from electronic annotation. Source: EnsemblPlants/Gramene flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC succinate dehydrogenase activity Traceable author statement Ref.6. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 32

Mitochondrion Potential

Chain

33 – 634

602

Succinate dehydrogenase [ubiquinone] flavoprotein subunit 1, mitochondrial

PRO_0000158659

Regions

Nucleotide binding

56 – 61

FAD By similarity

Nucleotide binding

79 – 94

FAD By similarity

Nucleotide binding

446 – 447

FAD By similarity

Sites

Active site

329

Proton acceptor By similarity

Binding site

264

FAD By similarity

Binding site

285

Substrate By similarity

Binding site

297

Substrate By similarity

Binding site

396

Substrate By similarity

Binding site

430

FAD By similarity

Binding site

441

Substrate By similarity

Amino acid modifications

Modified residue

Tele-8alpha-FAD histidine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O82663 [UniParc].

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

634

69,656

        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' referencesShow '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. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], 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.
IPI	IPI00533552.
PIR	T51815.
RefSeq	NP_201477.1. NM_126074.2.
UniGene	At.22655. At.67108.
3D structure databases
ProteinModelPortal	O82663.
SMR	O82663. Positions 41-634.
ModBase	Search...
Protein-protein interaction databases
IntAct	O82663. 5 interactions.
STRING	3702.AT5G66760.1-P.
Proteomic databases
PaxDb	O82663.
PRIDE	O82663.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G66760.1; AT5G66760.1; AT5G66760.
GeneID	836809.
KEGG	ath:AT5G66760.
Organism-specific databases
GeneFarm	2175. 174.
TAIR	At5g66760.
Phylogenomic databases
eggNOG	COG1053.
HOGENOM	HOG000160475.
InParanoid	O82663.
KO	K00234.
OMA	CFTADAT.
PhylomeDB	O82663.
ProtClustDB	PLN00128.
Enzyme and pathway databases
BioCyc	ARA:AT5G66760-MONOMER. MetaCyc:AT5G66760-MONOMER.
UniPathway	UPA00223; UER01006.
Gene expression databases
Genevestigator	O82663.
GermOnline	AT5G66760. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.20.58.100. 1 hit.
InterPro	IPR003953. FAD_bind_dom. IPR003952. FRD_SDH_FAD_BS. IPR015939. Fum_Rdtase/Succ_DH_flav-like_C. IPR011281. Succ_DH_flav_su_fwd. IPR014006. Succ_Dhase_FrdA_Gneg. [Graphical view]
PANTHER	PTHR11632:SF5. PTHR11632:SF5. 1 hit.
Pfam	PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF46977. Succ_DH_flav_C. 1 hit.
TIGRFAMs	TIGR01816. sdhA_forward. 1 hit. TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITE	PS00504. FRD_SDH_FAD_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHSA1_ARATH

Accession

Primary (citable) accession number: O82663

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents