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SDHF3_ASPFU
ID   SDHF3_ASPFU             Reviewed;         129 AA.
AC   Q4WHK3;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=AFUA_2G05090;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL87602.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000008; EAL87602.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_749640.2; XM_744547.2.
DR   AlphaFoldDB; Q4WHK3; -.
DR   SMR; Q4WHK3; -.
DR   STRING; 746128.CADAFUBP00002160; -.
DR   GeneID; 3507104; -.
DR   KEGG; afm:AFUA_2G05090; -.
DR   eggNOG; KOG4100; Eukaryota.
DR   HOGENOM; CLU_102310_1_0_1; -.
DR   InParanoid; Q4WHK3; -.
DR   OrthoDB; 1613308at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..129
FT                   /note="Succinate dehydrogenase assembly factor 3,
FT                   mitochondrial"
FT                   /id="PRO_0000042741"
SQ   SEQUENCE   129 AA;  14976 MW;  A7F2C7747E354B50 CRC64;
     MRLFHRLLMA TPSTMGSKSS LSEALALLPP LQLYRRILRV HRRKLDPEMR ILGDSYVKSE
     FRAHRNVENP LHIIGFLTEW QLYAQKLEGD AWVGEKLDKS KLDKMSDQQI GQLYELMQAI
     KNPEGEGKE
 
 
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