SDHF3_EMENI
ID SDHF3_EMENI Reviewed; 135 AA.
AC Q5BBH7; C8VLY2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Succinate dehydrogenase assembly factor 3, mitochondrial {ECO:0000250|UniProtKB:Q04401};
DE Short=SDH assembly factor 3 {ECO:0000250|UniProtKB:Q04401};
DE Short=SDHAF3 {ECO:0000250|UniProtKB:Q04401};
DE Flags: Precursor;
GN ORFNames=AN2103;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Plays an essential role in the assembly of succinate
CC dehydrogenase (SDH), an enzyme complex (also referred to as respiratory
CC complex II) that is a component of both the tricarboxylic acid (TCA)
CC cycle and the mitochondrial electron transport chain, and which couples
CC the oxidation of succinate to fumarate with the reduction of ubiquinone
CC (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur
CC protein subunit of the SDH catalytic dimer, protecting it from the
CC deleterious effects of oxidants. May act together with SDHAF1.
CC {ECO:0000250|UniProtKB:Q04401, ECO:0000250|UniProtKB:Q8SZ16}.
CC -!- SUBUNIT: Interacts with the iron-sulfur protein subunit within the SDH
CC catalytic dimer. {ECO:0000250|UniProtKB:Q04401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q04401}.
CC -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily.
CC {ECO:0000305}.
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DR EMBL; AACD01000032; EAA64935.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF86184.1; -; Genomic_DNA.
DR RefSeq; XP_659707.1; XM_654615.1.
DR AlphaFoldDB; Q5BBH7; -.
DR SMR; Q5BBH7; -.
DR STRING; 162425.CADANIAP00008776; -.
DR EnsemblFungi; CBF86184; CBF86184; ANIA_02103.
DR EnsemblFungi; EAA64935; EAA64935; AN2103.2.
DR GeneID; 2874949; -.
DR KEGG; ani:AN2103.2; -.
DR VEuPathDB; FungiDB:AN2103; -.
DR eggNOG; KOG4100; Eukaryota.
DR HOGENOM; CLU_102310_1_0_1; -.
DR InParanoid; Q5BBH7; -.
DR OMA; LTEWQMY; -.
DR OrthoDB; 1613308at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central.
DR InterPro; IPR008381; SDHAF3/Sdh7.
DR PANTHER; PTHR13137; PTHR13137; 1.
PE 3: Inferred from homology;
KW Chaperone; Gluconeogenesis; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..135
FT /note="Succinate dehydrogenase assembly factor 3,
FT mitochondrial"
FT /id="PRO_0000042746"
SQ SEQUENCE 135 AA; 15403 MW; 3B080FADBB6A946C CRC64;
MRIFTRLLYA APSNMGSAAS LSEALALLPP IPLYRRILRV HRKKLDPEMR ILGDSYVKSE
FRAHRGTENP LHIIGFLTEW QLYAQKLEGD SWIGEKLDQG KLDKMSDQQL GQLYELMQTI
QNKDGKGEGE GESEK
