SDF2B_DROMO
ID SDF2B_DROMO Reviewed; 157 AA.
AC B4KPG8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=GI20928;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933808; EDW10164.1; -; Genomic_DNA.
DR RefSeq; XP_002006229.1; XM_002006193.2.
DR AlphaFoldDB; B4KPG8; -.
DR SMR; B4KPG8; -.
DR STRING; 7230.FBpp0170145; -.
DR EnsemblMetazoa; FBtr0171653; FBpp0170145; FBgn0143662.
DR GeneID; 6580383; -.
DR KEGG; dmo:Dmoj_GI20928; -.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_103054_0_3_1; -.
DR InParanoid; B4KPG8; -.
DR OMA; YGKPQNP; -.
DR OrthoDB; 1492851at2759; -.
DR PhylomeDB; B4KPG8; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0055070; P:copper ion homeostasis; IEA:EnsemblMetazoa.
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..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03057"
FT CHAIN 23..157
FT /note="Succinate dehydrogenase assembly factor 2-B,
FT mitochondrial"
FT /id="PRO_0000383170"
SQ SEQUENCE 157 AA; 18743 MW; 276474399660F2CB CRC64;
MLSQWFRGRH LVVRSALFSR RRVSSESTST KDDVIVDFED PDLPLPEYPK RPDEPLETRK
QRLMYQSRKR GMLENDLLLS TFAHKYLKDF NAEQTALYDD LINGVSNDWD IYYWATGVKQ
TPKEYDTEIM KLLKLHVDNA ERVTRFRQPE LTYYLKC
