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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

AN2332.2

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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).UniRule annotation

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster.UniRule annotation
  • [3Fe-4S] clusterUniRule annotationNote: Binds 1 [3Fe-4S] cluster.UniRule annotation
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster.UniRule annotation

Pathwayi

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

2Fe-2SUniRule annotation, 3Fe-4SUniRule annotation, 4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialUniRule annotation (EC:1.3.5.1UniRule annotation)
Gene namesi
ORF Names:AN2332.2Imported, ANIA_02332Imported
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)Imported
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VII

Subcellular locationi

  • Mitochondrion inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Matrix side UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membraneUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00009027.

Structurei

3D structure databases

ProteinModelPortaliQ5BAU8.
SMRiQ5BAU8. Positions 39-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.UniRule annotation
Contains 1 2Fe-2S ferredoxin-type domain.UniRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
KOiK00235.
OMAiHIDTIKK.
OrthoDBiEOG7X9GJ0.

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.
PF13183. Fer4_8. 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.

Q5BAU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLRTTSRL VASSRSLFRP ATFARSYATV ESAQEPAPQM KKFQVYRWNP
60 70 80 90 100
DKPSEKPKMQ TYELDLKKTG PMMLDALIRI KNEIDPTLTF RRSCREGICG
110 120 130 140 150
SCAMNIDGVN TLACLCRIPT DTTKESRIYP LPHTYVVKDL VPDLTQIYKQ
160 170 180 190 200
YKSIKPYLQR DTKTEDGLEN RQSPEDRKKL DGLYECILCF CCSTSCPSYW
210 220 230 240 250
WNSEEYLGPA ILLQSYRWLA DSRDQKTAER KHAIDNSMSV YRCHTILNCT
260 270
RTCPKGLNPA RAISEIKKML AAH
Length:273
Mass (Da):31,344
Last modified:April 26, 2005 - v1
Checksum:iA5A9411FBC532A7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN001307 Genomic DNA. Translation: CBF86624.1.
AACD01000038 Genomic DNA. Translation: EAA64443.1.
RefSeqiXP_659936.1. XM_654844.1.

Genome annotation databases

EnsemblFungiiCADANIAT00009027; CADANIAP00009027; CADANIAG00009027.
GeneIDi2875591.
KEGGiani:AN2332.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN001307 Genomic DNA. Translation: CBF86624.1.
AACD01000038 Genomic DNA. Translation: EAA64443.1.
RefSeqiXP_659936.1. XM_654844.1.

3D structure databases

ProteinModelPortaliQ5BAU8.
SMRiQ5BAU8. Positions 39-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00009027.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00009027; CADANIAP00009027; CADANIAG00009027.
GeneIDi2875591.
KEGGiani:AN2332.2.

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
KOiK00235.
OMAiHIDTIKK.
OrthoDBiEOG7X9GJ0.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

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.
PF13183. Fer4_8. 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. Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T., Blitshsteyn B.
    , Bloom T., Blye J., Boguslavskiy L., Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P., Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J., Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FGSC A4.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4Imported and FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139Imported.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139Imported.
  4. "The 2008 update of the Aspergillus nidulans genome annotation: A community effort."
    Russo Wortman J., Mabey Gilsenan J., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J.M., Durek P., Espeso E., Fekete E., Flipphi M., Garcia Estrada C.
    , Geysens S., Goldman G., de Groot P.W.J., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A.K.W., Kim J-M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., MacCabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Posci I., Punt P.J., Ram A.F.J., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van der Vondervoot P.J.I., de Vries R.P., Walton J., Xiang X., Xiong Y., Ping Zeng A., Brandt B.W., Cornell M.J., van den Hondel C.A.M.J.J., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-S13(2009)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FGSC A4Imported.

Entry informationi

Entry nameiQ5BAU8_EMENI
AccessioniPrimary (citable) accession number: Q5BAU8
Secondary accession number(s): C8VND1
Entry historyi
Integrated into UniProtKB/TrEMBL: April 26, 2005
Last sequence update: April 26, 2005
Last modified: May 27, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.