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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

dld1

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

Functioni

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.By similarity

Catalytic activityi

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

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931FADBy similarity
Binding sitei157 – 1571FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei247 – 2471NADBy similarity
Binding sitei281 – 2811NAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei316 – 3161NAD; via amide nitrogenBy similarity
Binding sitei357 – 3571FADBy similarity
Active sitei489 – 4891Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi75 – 8410FADBy similarity
Nucleotide bindingi187 – 1893FADBy similarity
Nucleotide bindingi224 – 2318NADBy similarity
Nucleotide bindingi363 – 3664FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

ReactomeiR-SPO-389661. Glyoxylate metabolism and glycine degradation.
R-SPO-6783984. Glycine degradation.
R-SPO-70268. Pyruvate metabolism.
R-SPO-71064. Lysine catabolism.
R-SPO-71403. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial (EC:1.8.1.4)
Alternative name(s):
Dihydrolipoamide dehydrogenase
Short name:
DLDH
Gene namesi
Name:dld1
ORF Names:SPAC1002.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1002.09c.
PomBaseiSPAC1002.09c. dld1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 511Dihydrolipoyl dehydrogenase, mitochondrialPRO_0000030300
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi84 ↔ 89Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiO00087.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-4666396.

Structurei

3D structure databases

ProteinModelPortaliO00087.
SMRiO00087. Positions 43-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

HOGENOMiHOG000276708.
InParanoidiO00087.
KOiK00382.
OMAiVYTQPEI.
OrthoDBiEOG7K0ZNC.
PhylomeDBiO00087.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O00087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNSVIKRSA LCRFKFTCLQ VSECRPAQIE ISKRLYSAKA SGNGEYDLCV
60 70 80 90 100
IGGGPGGYVA AIRGAQLGLK TICVEKRGTL GGTCLNVGCI PSKALLNNSH
110 120 130 140 150
IYHTVKHDTK RRGIDVSGVS VNLSQMMKAK DDSVKSLTSG IEYLFKKNKV
160 170 180 190 200
EYAKGTGSFI DPQTLSVKGI DGAADQTIKA KNFIIATGSE VKPFPGVTID
210 220 230 240 250
EKKIVSSTGA LSLSEVPKKM TVLGGGIIGL EMGSVWSRLG AEVTVVEFLP
260 270 280 290 300
AVGGPMDADI SKALSRIISK QGIKFKTSTK LLSAKVNGDS VEVEIENMKN
310 320 330 340 350
NKRETYQTDV LLVAIGRVPY TEGLGLDKLG ISMDKSNRVI MDSEYRTNIP
360 370 380 390 400
HIRVIGDATL GPMLAHKAED EGIAAVEYIA KGQGHVNYNC IPAVMYTHPE
410 420 430 440 450
VAWVGITEQK AKESGIKYRI GTFPFSANSR AKTNMDADGL VKVIVDAETD
460 470 480 490 500
RLLGVHMIGP MAGELIGEAT LALEYGASAE DVARVCHAHP TLSEATKEAM
510
MAAWCGKSIH F
Length:511
Mass (Da):54,731
Last modified:February 21, 2001 - v2
Checksum:iE68350146A93AD56
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2167ALSLSEV → GPYLYQRY in AAB97089 (PubMed:9366254).Curated
Sequence conflicti277 – 2771T → R in AAB97089 (PubMed:9366254).Curated
Sequence conflicti282 – 2821L → V in AAB97089 (PubMed:9366254).Curated
Sequence conflicti424 – 4241P → G in AAB97089 (PubMed:9366254).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40360 mRNA. Translation: AAB97089.1.
CU329670 Genomic DNA. Translation: CAB65609.1.
PIRiT43405.
RefSeqiNP_593496.1. NM_001018930.2.

Genome annotation databases

EnsemblFungiiSPAC1002.09c.1; SPAC1002.09c.1:pep; SPAC1002.09c.
GeneIDi2543269.
KEGGispo:SPAC1002.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40360 mRNA. Translation: AAB97089.1.
CU329670 Genomic DNA. Translation: CAB65609.1.
PIRiT43405.
RefSeqiNP_593496.1. NM_001018930.2.

3D structure databases

ProteinModelPortaliO00087.
SMRiO00087. Positions 43-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4666396.

Proteomic databases

MaxQBiO00087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1002.09c.1; SPAC1002.09c.1:pep; SPAC1002.09c.
GeneIDi2543269.
KEGGispo:SPAC1002.09c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1002.09c.
PomBaseiSPAC1002.09c. dld1.

Phylogenomic databases

HOGENOMiHOG000276708.
InParanoidiO00087.
KOiK00382.
OMAiVYTQPEI.
OrthoDBiEOG7K0ZNC.
PhylomeDBiO00087.

Enzyme and pathway databases

ReactomeiR-SPO-389661. Glyoxylate metabolism and glycine degradation.
R-SPO-6783984. Glycine degradation.
R-SPO-70268. Pyruvate metabolism.
R-SPO-71064. Lysine catabolism.
R-SPO-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

PROiO00087.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01350. lipoamide_DH. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiDLDH_SCHPO
AccessioniPrimary (citable) accession number: O00087
Secondary accession number(s): Q9US50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 21, 2001
Last modified: June 8, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.

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.