SDHF2_ASHGO
ID SDHF2_ASHGO Reviewed; 160 AA.
AC Q756Q4;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Succinate dehydrogenase assembly factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDH assembly factor 2 {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDHAF2 {ECO:0000255|HAMAP-Rule:MF_03057};
GN OrderedLocusNames=AER200C; ORFNames=AGOS_AER200C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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. Required for flavinylation (covalent
CC attachment of FAD) of the flavoprotein subunit of the SDH catalytic
CC dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC -!- SUBUNIT: Interacts with the flavoprotein subunit within the SDH
CC catalytic dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
CC -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016818; AAS52881.1; -; Genomic_DNA.
DR RefSeq; NP_985057.1; NM_210411.1.
DR AlphaFoldDB; Q756Q4; -.
DR SMR; Q756Q4; -.
DR STRING; 33169.AAS52881; -.
DR EnsemblFungi; AAS52881; AAS52881; AGOS_AER200C.
DR GeneID; 4621267; -.
DR KEGG; ago:AGOS_AER200C; -.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_103054_0_1_1; -.
DR InParanoid; Q756Q4; -.
DR OMA; YGKPQNP; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:UniProtKB.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR GO; GO:0017013; P:protein flavinylation; IEA:EnsemblFungi.
DR GO; GO:0018293; P:protein-FAD linkage; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 1.10.150.250; -; 1.
DR HAMAP; MF_03057; SDHAF2; 1.
DR InterPro; IPR005631; SDH.
DR InterPro; IPR036714; SDH_sf.
DR InterPro; IPR028882; SDHAF2.
DR Pfam; PF03937; Sdh5; 1.
DR SUPFAM; SSF109910; SSF109910; 1.
PE 3: Inferred from homology;
KW Chaperone; Mitochondrion; Reference proteome.
FT CHAIN 1..160
FT /note="Succinate dehydrogenase assembly factor 2,
FT mitochondrial"
FT /id="PRO_0000383186"
SQ SEQUENCE 160 AA; 18662 MW; F377773D8C1DDBD3 CRC64;
MLRFSFSHAF AGSYGLAPAR ATRFYPRILP FAARAYSADK QGDDVILRVK VAPIKRNNET
LEQQRARLVY QSRKRGILET DLLLSGFAAK YLKHMTAEEL NEYDELLNEL DWDIYYWATK
NSDASPLPEK WQHSKILRKL QAYSENKDKQ ILKMPDLSEF
