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Q5BAU8

- Q5BAU8_EMENI

UniProt

Q5BAU8 - Q5BAU8_EMENI

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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: 2 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:
  • Note: Binds 1 2Fe-2S cluster.UniRule annotation
  • Note: Binds 1 3Fe-4S cluster.UniRule annotation
  • Note: Binds 1 4Fe-4S cluster.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: InterPro
  2. electron carrier activity Source: InterPro
  3. oxidoreductase activity Source: InterPro

GO - Biological processi

  1. tricarboxylic acid cycle Source: InterPro
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: Chromosome VII

Subcellular locationi

Mitochondrion inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Matrix side UniRule 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.
OMAiIMNCSRT.
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 .
RefSeqi XP_659936.1. XM_654844.1.

3D structure databases

ProteinModelPortali Q5BAU8.
SMRi Q5BAU8. Positions 39-273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00009027.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00009027 ; CADANIAP00009027 ; CADANIAG00009027 .
GeneIDi 2875591.
KEGGi ani:AN2332.2.

Phylogenomic databases

eggNOGi COG0479.
HOGENOMi HOG000160590.
KOi K00235.
OMAi IMNCSRT.
OrthoDBi EOG7X9GJ0.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01006 .

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 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 ]
Pfami PF13085. Fer2_3. 1 hit.
PF13183. Fer4_8. 1 hit.
[Graphical view ]
SUPFAMi SSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR00384. dhsB. 1 hit.
PROSITEi PS00197. 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 ]
ProtoNeti Search...

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: November 26, 2014
This is version 82 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