SDF2B_DROWI
ID SDF2B_DROWI Reviewed; 156 AA.
AC B4N665;
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-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=GK18008;
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 -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
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DR EMBL; CH964154; EDW79854.1; -; Genomic_DNA.
DR RefSeq; XP_002068868.1; XM_002068832.2.
DR AlphaFoldDB; B4N665; -.
DR SMR; B4N665; -.
DR STRING; 7260.FBpp0247151; -.
DR EnsemblMetazoa; FBtr0248659; FBpp0247151; FBgn0220007.
DR GeneID; 6646210; -.
DR KEGG; dwi:6646210; -.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_103054_0_3_1; -.
DR InParanoid; B4N665; -.
DR OMA; HVKNHEK; -.
DR OrthoDB; 1492851at2759; -.
DR PhylomeDB; B4N665; -.
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; Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..156
FT /note="Succinate dehydrogenase assembly factor 2-B,
FT mitochondrial"
FT /id="PRO_0000383181"
SQ SEQUENCE 156 AA; 18255 MW; E9CEE7273BF1CC61 CRC64;
MLRQILSSAV AKSTRGLSFT VNRLASNLDK SEYTTPGEII DYDDPTHLPV PEYPLRPDEP
LETRKQRLLY QSRKRGMLEN DLLLSTFVAK YLRDFNADQT AQYDKLINGV SNDWDIFYWA
TETKATPAEY DNEIMQMLKQ HVKNEERVQR IRQPDL
