SDHF3_USTMA
ID SDHF3_USTMA Reviewed; 173 AA.
AC Q4PCI7; A0A0D1C864;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 76.
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=UMAG_10065;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003144; KIS69642.1; -; Genomic_DNA.
DR RefSeq; XP_011388792.1; XM_011390490.1.
DR AlphaFoldDB; Q4PCI7; -.
DR SMR; Q4PCI7; -.
DR STRING; 5270.UM02176P0; -.
DR EnsemblFungi; KIS69642; KIS69642; UMAG_10065.
DR GeneID; 23566139; -.
DR KEGG; uma:UMAG_10065; -.
DR VEuPathDB; FungiDB:UMAG_10065; -.
DR eggNOG; KOG4100; Eukaryota.
DR InParanoid; Q4PCI7; -.
DR OrthoDB; 1613308at2759; -.
DR Proteomes; UP000000561; Chromosome 5.
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..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 60..173
FT /note="Succinate dehydrogenase assembly factor 3,
FT mitochondrial"
FT /id="PRO_0000042752"
FT REGION 149..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 173 AA; 19742 MW; EFD62CC0F001EE56 CRC64;
MFRPSTSLAL RSTLRQLASA SNQPIPPGSE INAVKRTVAT ILPPIRLYRR IIRAHRRLDP
DMRAVGDNYV KDEFRRHKNI DNPLQIIGFL SSWKMYLDQL EVQQGQPGGF RGQRLDPQLL
EKMSDEQIYQ IHELMTATQE AYSDKAQAFP PEKQRELAEK AAADAGLSVK KDE