SDF2A_DROWI
ID SDF2A_DROWI Reviewed; 157 AA.
AC B4MRE7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Succinate dehydrogenase assembly factor 2-A, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDH assembly factor 2-A {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDHAF2-A {ECO:0000255|HAMAP-Rule:MF_03057};
GN ORFNames=GK15773;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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}.
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DR EMBL; CH963850; EDW74686.1; -; Genomic_DNA.
DR RefSeq; XP_002063700.1; XM_002063664.2.
DR AlphaFoldDB; B4MRE7; -.
DR SMR; B4MRE7; -.
DR STRING; 7260.FBpp0244916; -.
DR EnsemblMetazoa; FBtr0246424; FBpp0244916; FBgn0217776.
DR GeneID; 6641050; -.
DR KEGG; dwi:6641050; -.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_103054_0_3_1; -.
DR InParanoid; B4MRE7; -.
DR OMA; RPMIAPH; -.
DR OrthoDB; 1492851at2759; -.
DR PhylomeDB; B4MRE7; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:UniProtKB.
DR GO; GO:0018293; P:protein-FAD linkage; ISS:UniProtKB.
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..157
FT /note="Succinate dehydrogenase assembly factor 2-A,
FT mitochondrial"
FT /id="PRO_0000383180"
SQ SEQUENCE 157 AA; 18457 MW; CDF2DEF297030F27 CRC64;
MLRQLNLTRE ISRWIFMPWQ RGAAGTASAE PPALPINDVI VDYDGPDLPL PEYPQRPNEP
LEIRKQRLVY QSRKRGMLEN DLLLSTFAAK YLKNFNEEQT AIYDQLINGV SNDWDIYYWA
TDVKTTPAEY NTEIMQLLKE HVKNTERVQR FRQPDLT