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O00087 (DLDH_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase, mitochondrial

EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
Short name=DLDH
Gene names
Name:dld1
ORF Names:SPAC1002.09c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes By similarity. Malfunction of this protein blocks the progression of cell cycle from G1 to S phase.

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix Potential.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainRedox-active center
Transit peptide
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred by curator. Source: PomBase

G1/S transition of mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: PomBase

L-serine biosynthetic process

Inferred from sequence orthology. Source: PomBase

acetyl-CoA biosynthetic process from pyruvate

Inferred from sequence orthology. Source: PomBase

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycine decarboxylation via glycine cleavage system

Inferred from sequence orthology. Source: PomBase

isoleucine catabolic process

Inferred from sequence orthology. Source: PomBase

leucine catabolic process

Inferred from sequence orthology. Source: PomBase

valine catabolic process

Inferred from sequence or structural similarity. Source: PomBase

   Cellular_componentglycine cleavage complex

Inferred from sequence orthology. Source: PomBase

mitochondrial nucleoid

Inferred from sequence or structural similarity. Source: PomBase

mitochondrial oxoglutarate dehydrogenase complex

Inferred by curator. Source: PomBase

mitochondrial pyruvate dehydrogenase complex

Inferred from sequence or structural similarity. Source: PomBase

   Molecular_functiondihydrolipoyl dehydrogenase activity

Inferred from sequence or structural similarity. Source: PomBase

disulfide oxidoreductase activity

Inferred from sequence model. Source: PomBase

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

pyruvate dehydrogenase (acetyl-transferring) activity

Inferred from sequence orthology. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 511Dihydrolipoyl dehydrogenase, mitochondrialPRO_0000030300

Regions

Nucleotide binding75 – 8410FAD By similarity
Nucleotide binding187 – 1893FAD By similarity
Nucleotide binding224 – 2318NAD By similarity
Nucleotide binding363 – 3664FAD By similarity

Sites

Active site4891Proton acceptor By similarity
Binding site931FAD By similarity
Binding site1571FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2471NAD By similarity
Binding site2811NAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3161NAD; via amide nitrogen By similarity
Binding site3571FAD By similarity

Amino acid modifications

Disulfide bond84 ↔ 89Redox-active By similarity

Experimental info

Sequence conflict210 – 2167ALSLSEV → GPYLYQRY in AAB97089. Ref.1
Sequence conflict2771T → R in AAB97089. Ref.1
Sequence conflict2821L → V in AAB97089. Ref.1
Sequence conflict4241P → G in AAB97089. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O00087 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: E68350146A93AD56

FASTA51154,731
        10         20         30         40         50         60 
MLNSVIKRSA LCRFKFTCLQ VSECRPAQIE ISKRLYSAKA SGNGEYDLCV IGGGPGGYVA 

        70         80         90        100        110        120 
AIRGAQLGLK TICVEKRGTL GGTCLNVGCI PSKALLNNSH IYHTVKHDTK RRGIDVSGVS 

       130        140        150        160        170        180 
VNLSQMMKAK DDSVKSLTSG IEYLFKKNKV EYAKGTGSFI DPQTLSVKGI DGAADQTIKA 

       190        200        210        220        230        240 
KNFIIATGSE VKPFPGVTID EKKIVSSTGA LSLSEVPKKM TVLGGGIIGL EMGSVWSRLG 

       250        260        270        280        290        300 
AEVTVVEFLP AVGGPMDADI SKALSRIISK QGIKFKTSTK LLSAKVNGDS VEVEIENMKN 

       310        320        330        340        350        360 
NKRETYQTDV LLVAIGRVPY TEGLGLDKLG ISMDKSNRVI MDSEYRTNIP HIRVIGDATL 

       370        380        390        400        410        420 
GPMLAHKAED EGIAAVEYIA KGQGHVNYNC IPAVMYTHPE VAWVGITEQK AKESGIKYRI 

       430        440        450        460        470        480 
GTFPFSANSR AKTNMDADGL VKVIVDAETD RLLGVHMIGP MAGELIGEAT LALEYGASAE 

       490        500        510 
DVARVCHAHP TLSEATKEAM MAAWCGKSIH F 

« Hide

References

« Hide 'large scale' references
[1]"Fission yeast dihydrolipoamide dehydrogenase gene is involved in G1/S cell cycle progression."
Jang Y.-J., Chung K.-S., Park C., Yoo H.-S.
Biochim. Biophys. Acta 1358:229-239(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L40360 mRNA. Translation: AAB97089.1.
CU329670 Genomic DNA. Translation: CAB65609.1.
PIRT43405.
RefSeqNP_593496.1. NM_001018930.2.

3D structure databases

ProteinModelPortalO00087.
SMRO00087. Positions 43-510.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4666396.
STRING4896.SPAC1002.09c-1.

Proteomic databases

PaxDbO00087.
PRIDEO00087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC1002.09c.1; SPAC1002.09c.1:pep; SPAC1002.09c.
GeneID2543269.
KEGGspo:SPAC1002.09c.

Organism-specific databases

PomBaseSPAC1002.09c.

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHOG000276708.
KOK00382.
OMAGFEKQMS.
OrthoDBEOG43FM59.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PANTHERPTHR22912:SF20. PTHR22912:SF20. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804290.

Entry information

Entry nameDLDH_SCHPO
AccessionPrimary (citable) accession number: O00087
Secondary accession number(s): Q9US50
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 21, 2001
Last modified: May 29, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families