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Protein

Succinate dehydrogenase assembly factor 2, mitochondrial

Gene

SDH5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SDH1 of the SDH catalytic dimer. It is unclear whether it participates in the chemistry of FAD attachment (enzymatic function) or acts as a chaperone that maintains SDH1 in a conformation that is susceptible to autocatalytic FAD attachment (PubMed:19628817). Does not bind FAD or FADH2 in vitro (PubMed:23062074). Involved in sporulation (PubMed:12432101). Required for the full activation of the early meiotic inducer IME1 (PubMed:12586695).UniRule annotation4 Publications

GO - Biological processi

  • mitochondrial electron transport, succinate to ubiquinone Source: UniProtKB
  • mitochondrial respiratory chain complex II assembly Source: SGD
  • protein-FAD linkage Source: UniProtKB
  • tricarboxylic acid cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciYEAST:G3O-33476-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase assembly factor 2, mitochondrial1 PublicationUniRule annotation
Short name:
SDH assembly factor 2UniRule annotation
Short name:
SDHAF21 PublicationUniRule annotation
Gene namesi
Name:SDH51 PublicationUniRule annotation
Synonyms:EMI51 Publication
Ordered Locus Names:YOL071WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL071W.
SGDiS000005432. SDH5.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Respiratory deficient phenotype: viable on glucose medium, but is inviable on non-fermentable carbon sources such as glycerol. Cells lack SDH activity due to a complete loss of FAD cofactor attachment of SDH1.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681R → E: Loss of covalent FAD in SDH1. 1 Publication
Mutagenesisi71 – 711Y → D: Loss of covalent FAD in SDH1. 1 Publication
Mutagenesisi98 – 992EE → KK: No effect. 1 Publication
Mutagenesisi113 – 1131W → A: Loss of covalent FAD in SDH1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535Mitochondrion1 PublicationAdd
BLAST
Chaini36 – 162127Succinate dehydrogenase assembly factor 2, mitochondrialPRO_0000007814Add
BLAST

Proteomic databases

MaxQBiQ08230.

Interactioni

Subunit structurei

Interacts with SDH1 within the SDH catalytic dimer.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi34330. 27 interactions.
DIPiDIP-61727N.
MINTiMINT-4501860.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi62 – 7312Combined sources
Helixi79 – 9517Combined sources
Helixi98 – 10811Combined sources
Helixi112 – 1198Combined sources
Turni123 – 1253Combined sources
Helixi130 – 1334Combined sources
Helixi136 – 14712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LM4NMR-A55-152[»]
ProteinModelPortaliQ08230.
SMRiQ08230. Positions 55-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SDHAF2 family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000001149.
HOGENOMiHOG000230636.
InParanoidiQ08230.
KOiK18168.
OMAiYWATENY.
OrthoDBiEOG7MPRSB.

Family and domain databases

Gene3Di1.10.150.250. 1 hit.
HAMAPiMF_03057. SDHAF2.
InterProiIPR005631. SDH.
IPR028882. SDHAF2.
[Graphical view]
PfamiPF03937. Sdh5. 1 hit.
[Graphical view]
SUPFAMiSSF109910. SSF109910. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHNMFPALTK TLSLQGYKII NSQTGSAAWS CGRRWFSSDK DDHDDVVTRI
60 70 80 90 100
KIAPIKRTNE PLDKKRARLI YQSRKRGILE TDLLLSGFAA KYLKKMNEEE
110 120 130 140 150
LEEYDSLLNE LDWDIYYWAT KNFKTSPLPD KWANSKLLKQ LQEFSENKEK
160
EILSMPDLSK YQ
Length:162
Mass (Da):19,042
Last modified:November 1, 1996 - v1
Checksum:i8CDF8E943D46A12D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74813 Genomic DNA. Translation: CAA99081.1.
BK006948 Genomic DNA. Translation: DAA10712.1.
PIRiS66764.
RefSeqiNP_014570.1. NM_001183326.1.

Genome annotation databases

EnsemblFungiiYOL071W; YOL071W; YOL071W.
GeneIDi854083.
KEGGisce:YOL071W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74813 Genomic DNA. Translation: CAA99081.1.
BK006948 Genomic DNA. Translation: DAA10712.1.
PIRiS66764.
RefSeqiNP_014570.1. NM_001183326.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LM4NMR-A55-152[»]
ProteinModelPortaliQ08230.
SMRiQ08230. Positions 55-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34330. 27 interactions.
DIPiDIP-61727N.
MINTiMINT-4501860.

Proteomic databases

MaxQBiQ08230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL071W; YOL071W; YOL071W.
GeneIDi854083.
KEGGisce:YOL071W.

Organism-specific databases

EuPathDBiFungiDB:YOL071W.
SGDiS000005432. SDH5.

Phylogenomic databases

GeneTreeiENSGT00390000001149.
HOGENOMiHOG000230636.
InParanoidiQ08230.
KOiK18168.
OMAiYWATENY.
OrthoDBiEOG7MPRSB.

Enzyme and pathway databases

BioCyciYEAST:G3O-33476-MONOMER.

Miscellaneous databases

PROiQ08230.

Family and domain databases

Gene3Di1.10.150.250. 1 hit.
HAMAPiMF_03057. SDHAF2.
InterProiIPR005631. SDH.
IPR028882. SDHAF2.
[Graphical view]
PfamiPF03937. Sdh5. 1 hit.
[Graphical view]
SUPFAMiSSF109910. SSF109910. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Parallel phenotypic analysis of sporulation and postgermination growth in Saccharomyces cerevisiae."
    Deutschbauer A.M., Williams R.M., Chu A.M., Davis R.W.
    Proc. Natl. Acad. Sci. U.S.A. 99:15530-15535(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae."
    Enyenihi A.H., Saunders W.S.
    Genetics 163:47-54(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  8. "Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability."
    Vogtle F.N., Wortelkamp S., Zahedi R.P., Becker D., Leidhold C., Gevaert K., Kellermann J., Voos W., Sickmann A., Pfanner N., Meisinger C.
    Cell 139:428-439(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF MATURE N-TERMINUS, MASS SPECTROMETRY.
  9. Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH SDH1.
  10. "Solution NMR structure of yeast succinate dehydrogenase flavinylation factor Sdh5 reveals a putative Sdh1 binding site."
    Eletsky A., Jeong M.Y., Kim H., Lee H.W., Xiao R., Pagliarini D.J., Prestegard J.H., Winge D.R., Montelione G.T., Szyperski T.
    Biochemistry 51:8475-8477(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-54, FUNCTION, MUTAGENESIS OF ARG-68; TYR-71; 98-GLU-GLU-99 AND TRP-113.

Entry informationi

Entry nameiSDHF2_YEAST
AccessioniPrimary (citable) accession number: Q08230
Secondary accession number(s): D6W1Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1080 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.