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Q09508 (DHSA_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=FP
Gene names
Name:sdha-1
ORF Names:C03G5.1/D2021.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length646 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 + 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.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.

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 – 3131Mitochondrion Potential
Chain32 – 646615Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
PRO_0000010339

Regions

Nucleotide binding49 – 546FAD By similarity
Nucleotide binding72 – 8716FAD By similarity
Nucleotide binding438 – 4392FAD By similarity

Sites

Active site3211Proton acceptor By similarity
Binding site2561FAD By similarity
Binding site2771Substrate By similarity
Binding site2891Substrate By similarity
Binding site3881Substrate By similarity
Binding site4221FAD By similarity
Binding site4331Substrate By similarity

Amino acid modifications

Modified residue801Tele-8alpha-FAD histidine By similarity

Experimental info

Sequence conflict641G → E in BAA21637. Ref.1
Sequence conflict2671N → S in BAA21637. Ref.1
Sequence conflict3031A → S in BAA21637. Ref.1
Sequence conflict3151A → S in BAA21637. Ref.1
Sequence conflict4631V → G in BAA21637. Ref.1
Sequence conflict483 – 4864HNKG → TTRE in BAA21637. Ref.1
Sequence conflict6401P → A in BAA21637. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q09508 [UniParc].

Last modified August 2, 2002. Version 3.
Checksum: CD7CF55A6D26E6D1

FASTA64670,398
        10         20         30         40         50         60 
MLRAASNGLR NTVAARSVSL SAANHSDAKR SDIAQYKVVD HAYDAVVVGA GGAGLRAAMG 

        70         80         90        100        110        120 
LAEGGLKTAV ITKLFPTRSH TVAAQGGINA ALGNMNPDNW RWHFYDTVKG SDWLGDQDAI 

       130        140        150        160        170        180 
HYMTREAERA VIELENYGMP FSRTTDGKIY QRAFGGQSND FGRGGQAHRT CCVADRTGHS 

       190        200        210        220        230        240 
LLHTLYGASL QYNCNYFVEY FALDLIMENG VCVGVIAMDL EDGTIHRFRS KNTVLATGGY 

       250        260        270        280        290        300 
GRAFFSCTSA HTCTGDGTAL TARAGINNSD MEFVQFHPTG IYGAGCLITE GSRGEGGYLV 

       310        320        330        340        350        360 
NSAGERFMER YAPNAKDLAS RDVVSRSMTV EIMEGRGVGP DKDHIYLQLH HLPAEQLQQR 

       370        380        390        400        410        420 
LPGISETAMI FAGVDVTKEP IPVIPTVHYN MGGVPTNYKG QVLNYTPKKG DEVVPGLYAA 

       430        440        450        460        470        480 
GECGAHSVHG ANRLGANSLL DLVIFGRACA IDILKNTSAG VGVPELPKNA GEASVANIDK 

       490        500        510        520        530        540 
LRHNKGDIST AELRLTMQKS MQNHAAVFRR GDILKEGVKV LSKLYKDQAH LNVADKGLVW 

       550        560        570        580        590        600 
NSDLIETLEL QNLLINATQT IVAAENREES RGAHARDDFP DRLDELDYSK PLEGQTKKEL 

       610        620        630        640 
KDHWRKHSII RSNIETGEVS LDYRPVIDTT LDKSETDWVP PKVRSY

« Hide

References

« Hide 'large scale' references
[1]"Sequence comparison between the flavoprotein subunit of the fumarate reductase (complex II) of the anaerobic parasitic nematode, Ascaris suum and the succinate dehydrogenase of the aerobic, free-living nematode, Caenorhabditis elegans."
Kuramochi T., Hirawake H., Kojima S., Takamiya S., Furushima R., Aoki T., Komuniecki R., Kita K.
Mol. Biochem. Parasitol. 68:177-187(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Bristol N2.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D30651 mRNA. Translation: BAA21637.1.
FO080313 Genomic DNA. Translation: CCD62793.1.
PIRT15398.
T41753.
RefSeqNP_509446.1. NM_077045.5.

3D structure databases

ProteinModelPortalQ09508.
SMRQ09508. Positions 34-646.
ModBaseSearch...

2D gel databases

World-2DPAGE0020:Q09508.

Proteomic databases

PaxDbQ09508.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC03G5.1.1; C03G5.1.1; C03G5.1.
C03G5.1.2; C03G5.1.2; C03G5.1.
GeneID181108.
KEGGcel:CELE_C03G5.1.
UCSCC03G5.1.2. c. elegans.

Organism-specific databases

CTD181108.
WormBaseC03G5.1; CE03917; WBGene00015391; sdha-1.

Phylogenomic databases

eggNOGCOG1053.
GeneTreeENSGT00390000010046.
HOGENOMHOG000160475.
InParanoidQ09508.
KOK00234.
OMALMANAIT.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
InterProIPR003953. 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]
PANTHERPTHR11632:SF5. PTHR11632:SF5. 1 hit.
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. Succ_DH_flav_C. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio912432.

Entry information

Entry nameDHSA_CAEEL
AccessionPrimary (citable) accession number: Q09508
Secondary accession number(s): Q17616, Q34089
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 2, 2002
Last modified: May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents