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P21914 (SDHB_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. 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] iron-sulfur subunit, mitochondrial

EC=1.3.5.1
Alternative name(s):
Iron-sulfur subunit of complex II
Short name=Ip
Gene names
Name:SdhB
Synonyms:SDH
ORF Names:CG3283
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Iron-sulfur protein (IP) 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

Binds 1 2Fe-2S cluster By similarity.

Binds 1 3Fe-4S cluster By similarity.

Binds 1 4Fe-4S cluster 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.

Tissue specificity

Most abundant in the adult thorax and low in abdominal tissues. Ref.1

Developmental stage

Expressed throughout development; pupae have very low levels of expression, in contrast to larvae. Ref.1

Sequence similarities

Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
   Biological processElectron transport
Transport
Tricarboxylic acid cycle
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   Ligand2Fe-2S
3Fe-4S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmitochondrial electron transport, succinate to ubiquinone

Inferred from direct assay PubMed 17056719. Source: FlyBase

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmicrotubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

mitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial respiratory chain complex II

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

3 iron, 4 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

4 iron, 4 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

electron carrier activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

succinate dehydrogenase (ubiquinone) activity

Inferred from electronic annotation. Source: UniProtKB-EC

ubiquinone binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 297Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010357

Regions

Domain47 – 140942Fe-2S ferredoxin-type
Domain185 – 215314Fe-4S ferredoxin-type

Sites

Metal binding1001Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1051Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1081Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1201Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1951Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1981Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2011Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2051Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2521Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2581Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2621Iron-sulfur 2 (4Fe-4S) By similarity
Binding site2101Ubiquinone; shared with DHSD By similarity

Sequences

Sequence LengthMass (Da)Tools
P21914 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 892380E8BAE08FFF

FASTA29733,741
        10         20         30         40         50         60 
MLATEARQIL SRVGSLVARN QMRAISNGTA QLEQQAQPKE AQEPQIKKFE IYRWNPDNAG 

        70         80         90        100        110        120 
EKPYMQTYEV DLRECGPMVL DALIKIKNEM DPTLTFRRSC REGICGSCAM NIGGTNTLAC 

       130        140        150        160        170        180 
ISKIDINTSK SLKVYPLPHM YVVRDLVPDM NNFYEQYRNI QPWLQRKNEA GEKKGKAQYL 

       190        200        210        220        230        240 
QSVEDRSKLD GLYECILCAC CSTSCPSYWW NAEKYLGPAV LMQAYRWIID SRDENSAERL 

       250        260        270        280        290 
NKLKDPFSVY RCHTIMNCTR TCPKGLNPGR AIAEIKKLLS GLASKPAPKL ETAALHK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the gene encoding the iron-sulfur protein subunit of succinate dehydrogenase from Drosophila melanogaster."
Au H.C., Scheffler I.E.
Gene 149:261-265(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species."
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 113-258.
[6]Erratum
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L27705 Genomic DNA. Translation: AAA61925.1.
AE013599 Genomic DNA. Translation: AAF57396.1.
AY118923 mRNA. Translation: AAM50783.1.
RefSeqNP_477101.1. NM_057753.5.
UniGeneDm.497.

3D structure databases

ProteinModelPortalP21914.
SMRP21914. Positions 45-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61486. 12 interactions.
DIPDIP-20115N.
IntActP21914. 3 interactions.
MINTMINT-929605.
STRING7227.FBpp0085489.

Proteomic databases

PaxDbP21914.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0086156; FBpp0085489; FBgn0014028.
GeneID35590.
KEGGdme:Dmel_CG3283.

Organism-specific databases

CTD6390.
FlyBaseFBgn0014028. SdhB.

Phylogenomic databases

eggNOGCOG0479.
GeneTreeENSGT00390000013558.
InParanoidP21914.
KOK00235.
OMAEGVWRCR.
OrthoDBEOG7H4DTN.
PhylomeDBP21914.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Gene expression databases

BgeeP21914.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi35590.
NextBio794181.
PROP21914.

Entry information

Entry nameSDHB_DROME
AccessionPrimary (citable) accession number: P21914
Secondary accession number(s): Q9V9A0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase