ID   SDF2B_DROYA             Reviewed;         156 AA.
AC   B4NXN5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Succinate dehydrogenase assembly factor 2-B, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057};
DE            Short=SDH assembly factor 2-B {ECO:0000255|HAMAP-Rule:MF_03057};
DE            Short=SDHAF2-B {ECO:0000255|HAMAP-Rule:MF_03057};
DE   Flags: Precursor;
GN   ORFNames=GE21507;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
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   -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03057}.
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DR   EMBL; CM000157; EDW89660.1; -; Genomic_DNA.
DR   RefSeq; XP_002089948.1; XM_002089912.2.
DR   AlphaFoldDB; B4NXN5; -.
DR   SMR; B4NXN5; -.
DR   STRING; 7245.FBpp0266517; -.
DR   EnsemblMetazoa; FBtr0268025; FBpp0266517; FBgn0238764.
DR   GeneID; 6528916; -.
DR   KEGG; dya:Dyak_GE21507; -.
DR   eggNOG; KOG3326; Eukaryota.
DR   HOGENOM; CLU_103054_0_3_1; -.
DR   OMA; HVKNHEK; -.
DR   OrthoDB; 1492851at2759; -.
DR   PhylomeDB; B4NXN5; -.
DR   Proteomes; UP000002282; Chromosome 2L.
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; Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..156
FT                   /note="Succinate dehydrogenase assembly factor 2-B,
FT                   mitochondrial"
FT                   /id="PRO_0000383183"
SQ   SEQUENCE   156 AA;  18417 MW;  6B76A0A8F84A6FE2 CRC64;
     MLRQFIISTV GRRQPLLMIL QSRLASNLDK TEYTTPGEIV DYDDPPHLPV PEYPVRPDEP
     LETRKQRLLY QSRKRGMLEN DLLLSTFVAK YLKDFSAEQT AEYDQLINGV SNDWDIFYWA
     TDTKPTPPQF DTEIMRLLKE HVKNHEKVQR IRQPDL