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Protein

Probable pyruvate dehydrogenase protein X component, mitochondrial

Gene

SPCC1259.09c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Probable pyruvate dehydrogenase protein X component, mitochondrial
Alternative name(s):
Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
Gene namesi
ORF Names:SPCC1259.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1259.09c.
PomBaseiSPCC1259.09c.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial pyruvate dehydrogenase complex Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 456Probable pyruvate dehydrogenase protein X component, mitochondrialPRO_0000020486
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761N6-lipoyllysinePROSITE-ProRule annotationBy similarity

Proteomic databases

MaxQBiO94709.

Interactioni

Protein-protein interaction databases

BioGridi275653. 7 interactions.
MINTiMINT-4686401.

Structurei

3D structure databases

ProteinModelPortaliO94709.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 11076Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

InParanoidiO94709.
OrthoDBiEOG092C3YQ0.
PhylomeDBiO94709.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O94709-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKHYIHQCV KASSCKHSLS VKQRYFHCSA LNGVASMFRM PALSPTMEEG
60 70 80 90 100
NITKWHFKEG DSFKSGDILL EVETDKATMD VEVQDNGILA KVLIEKGSNI
110 120 130 140 150
PVGKNIAIVA DAEDNLKDLE LPKDEASSEE QSFSSSKEEV KPIVQDRETK
160 170 180 190 200
SNVEHKSTSQ ANDAVNKSFL PSVSYLIHQY KIENPWSIPA TGPHGRLLKG
210 220 230 240 250
DVLAHVGKID KGVPSSLQKF VRNLEVLDFS GVEPKKPSYT EDSVPVRKST
260 270 280 290 300
MIETLKTVPM KDEYITFERS ISLEKLKSLL AKRKEKDAFG IDEVVSAMIG
310 320 330 340 350
DALSISELSK VEPNSIESAY DLLLGAPIVK LKSSVSNFQP KLFPKNNNTK
360 370 380 390 400
DLHKYIRDSM IGLPSNLSDY VKLNFSSVTK SSSNNVEFLD DVYDMLLGSN
410 420 430 440 450
SDSIDSRINR HEEPSTTEDL TLTLSIKDNI SKSRAIKFVD CLKSNFENPE

FVLSRW
Length:456
Mass (Da):50,884
Last modified:May 1, 1999 - v1
Checksum:i40C1AD24240E1116
GO

Sequence cautioni

The sequence BAA13921 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751Y → N in BAA13921 (PubMed:9501991).Curated
Sequence conflicti178 – 1781H → D in BAA13921 (PubMed:9501991).Curated
Sequence conflicti299 – 2991I → M in BAA13921 (PubMed:9501991).Curated
Sequence conflicti345 – 3473KNN → NNK in BAA13921 (PubMed:9501991).Curated
Sequence conflicti356 – 3561I → F in BAA13921 (PubMed:9501991).Curated
Sequence conflicti368 – 3681S → R in BAA13921 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA22547.1.
D89260 mRNA. Translation: BAA13921.1. Sequence problems.
PIRiT40898.
RefSeqiNP_588065.1. NM_001023057.2.

Genome annotation databases

EnsemblFungiiSPCC1259.09c.1; SPCC1259.09c.1:pep; SPCC1259.09c.
GeneIDi2539081.
KEGGispo:SPCC1259.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA22547.1.
D89260 mRNA. Translation: BAA13921.1. Sequence problems.
PIRiT40898.
RefSeqiNP_588065.1. NM_001023057.2.

3D structure databases

ProteinModelPortaliO94709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275653. 7 interactions.
MINTiMINT-4686401.

Proteomic databases

MaxQBiO94709.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1259.09c.1; SPCC1259.09c.1:pep; SPCC1259.09c.
GeneIDi2539081.
KEGGispo:SPCC1259.09c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1259.09c.
PomBaseiSPCC1259.09c.

Phylogenomic databases

InParanoidiO94709.
OrthoDBiEOG092C3YQ0.
PhylomeDBiO94709.

Miscellaneous databases

PROiO94709.

Family and domain databases

Gene3Di4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODPX_SCHPO
AccessioniPrimary (citable) accession number: O94709
Secondary accession number(s): P78909
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.