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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

SdhB

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi105 – 1051Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi108 – 1081Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi120 – 1201Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi195 – 1951Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi198 – 1981Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi201 – 2011Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi205 – 2051Iron-sulfur 3 (3Fe-4S)By similarity
Binding sitei210 – 2101Ubiquinone; shared with DHSDBy similarity
Metal bindingi252 – 2521Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi258 – 2581Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi262 – 2621Iron-sulfur 2 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. 3 iron, 4 sulfur cluster binding Source: UniProtKB
  3. 4 iron, 4 sulfur cluster binding Source: UniProtKB
  4. electron carrier activity Source: InterPro
  5. metal ion binding Source: UniProtKB-KW
  6. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC
  7. ubiquinone binding Source: UniProtKB

GO - Biological processi

  1. mitochondrial electron transport, succinate to ubiquinone Source: FlyBase
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_326398. Citric acid cycle (TCA cycle).
REACT_342103. Respiratory electron transport.
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SdhB
Synonyms:SDH
ORF Names:CG3283
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0014028. SdhB.

Subcellular locationi

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

GO - Cellular componenti

  1. microtubule associated complex Source: FlyBase
  2. mitochondrial inner membrane Source: UniProtKB
  3. mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone) Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 297Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010357
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

PaxDbiP21914.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiP21914.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi61486. 12 interactions.
DIPiDIP-20115N.
IntActiP21914. 3 interactions.
MINTiMINT-929605.
STRINGi7227.FBpp0085489.

Structurei

3D structure databases

ProteinModelPortaliP21914.
SMRiP21914. Positions 45-280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 140942Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini185 – 215314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0479.
GeneTreeiENSGT00390000013558.
InParanoidiP21914.
KOiK00235.
OMAiDMEPFFQ.
OrthoDBiEOG7H4DTN.
PhylomeDBiP21914.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLATEARQIL SRVGSLVARN QMRAISNGTA QLEQQAQPKE AQEPQIKKFE
60 70 80 90 100
IYRWNPDNAG EKPYMQTYEV DLRECGPMVL DALIKIKNEM DPTLTFRRSC
110 120 130 140 150
REGICGSCAM NIGGTNTLAC ISKIDINTSK SLKVYPLPHM YVVRDLVPDM
160 170 180 190 200
NNFYEQYRNI QPWLQRKNEA GEKKGKAQYL QSVEDRSKLD GLYECILCAC
210 220 230 240 250
CSTSCPSYWW NAEKYLGPAV LMQAYRWIID SRDENSAERL NKLKDPFSVY
260 270 280 290
RCHTIMNCTR TCPKGLNPGR AIAEIKKLLS GLASKPAPKL ETAALHK
Length:297
Mass (Da):33,741
Last modified:February 1, 1995 - v2
Checksum:i892380E8BAE08FFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27705 Genomic DNA. Translation: AAA61925.1.
AE013599 Genomic DNA. Translation: AAF57396.1.
AY118923 mRNA. Translation: AAM50783.1.
RefSeqiNP_477101.1. NM_057753.5.
UniGeneiDm.497.

Genome annotation databases

EnsemblMetazoaiFBtr0086156; FBpp0085489; FBgn0014028.
GeneIDi35590.
KEGGidme:Dmel_CG3283.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27705 Genomic DNA. Translation: AAA61925.1.
AE013599 Genomic DNA. Translation: AAF57396.1.
AY118923 mRNA. Translation: AAM50783.1.
RefSeqiNP_477101.1. NM_057753.5.
UniGeneiDm.497.

3D structure databases

ProteinModelPortaliP21914.
SMRiP21914. Positions 45-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61486. 12 interactions.
DIPiDIP-20115N.
IntActiP21914. 3 interactions.
MINTiMINT-929605.
STRINGi7227.FBpp0085489.

Proteomic databases

PaxDbiP21914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086156; FBpp0085489; FBgn0014028.
GeneIDi35590.
KEGGidme:Dmel_CG3283.

Organism-specific databases

CTDi6390.
FlyBaseiFBgn0014028. SdhB.

Phylogenomic databases

eggNOGiCOG0479.
GeneTreeiENSGT00390000013558.
InParanoidiP21914.
KOiK00235.
OMAiDMEPFFQ.
OrthoDBiEOG7H4DTN.
PhylomeDBiP21914.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.
ReactomeiREACT_326398. Citric acid cycle (TCA cycle).
REACT_342103. Respiratory electron transport.

Miscellaneous databases

GenomeRNAii35590.
NextBioi794181.
PROiP21914.

Gene expression databases

BgeeiP21914.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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.
    , 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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(1988) [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(1992)

Entry informationi

Entry nameiSDHB_DROME
AccessioniPrimary (citable) accession number: P21914
Secondary accession number(s): Q9V9A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1995
Last modified: April 1, 2015
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.