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Protein

Dihydrolipoyl dehydrogenase, mitochondrial

Gene

dld-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 sitei77 – 771FADBy similarity
Binding sitei229 – 2291NADBy similarity
Binding sitei264 – 2641NAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei299 – 2991NAD; via amide nitrogenBy similarity
Binding sitei340 – 3401FADBy similarity
Active sitei472 – 4721Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 6810FADBy similarity
Nucleotide bindingi169 – 1713FADBy similarity
Nucleotide bindingi206 – 2138NADBy similarity
Nucleotide bindingi346 – 3494FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

ReactomeiR-CEL-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-CEL-389661. Glyoxylate metabolism and glycine degradation.
R-CEL-5362517. Signaling by Retinoic Acid.
R-CEL-6783984. Glycine degradation.
R-CEL-70268. Pyruvate metabolism.
R-CEL-70895. Branched-chain amino acid catabolism.
R-CEL-71064. Lysine catabolism.
R-CEL-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
Gene namesi
Name:dld-1
ORF Names:LLC1.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiLLC1.3a; CE31971; WBGene00010794; dld-1.
LLC1.3b; CE44593; WBGene00010794; dld-1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 495Dihydrolipoyl dehydrogenase, mitochondrialPRO_0000421278
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 ↔ 73Redox-activeBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiO17953.
PaxDbiO17953.
PRIDEiO17953.

Interactioni

Protein-protein interaction databases

IntActiO17953. 1 interaction.
STRINGi6239.LLC1.3a.1.

Structurei

3D structure databases

ProteinModelPortaliO17953.
SMRiO17953. Positions 29-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG1335. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
InParanoidiO17953.
KOiK00382.
OMAiVYTQPEI.
OrthoDBiEOG77126S.
PhylomeDBiO17953.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform a (identifier: O17953-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSLSRTTQLP FAKRQFFQVL ARNYSNTQDA DLVVIGGGPG GYVAAIKAAQ
60 70 80 90 100
LGMKTVCVEK NATLGGTCLN VGCIPSKALL NNSHYLHMAQ HDFAARGIDC
110 120 130 140 150
TASLNLPKMM EAKSNSVKQL TGGIKQLFKA NKVGHVEGFA TIVGPNTVQA
160 170 180 190 200
KKNDGSVETI NARNILIASG SEVTPFPGIT IDEKQIVSST GALSLGQVPK
210 220 230 240 250
KMVVIGAGVI GLELGSVWQR LGAEVTAVEF LGHVGGMGID GEVSKNFQRS
260 270 280 290 300
LTKQGFKFLL NTKVMGASQN GSTITVEVEG AKDGKKQTLE CDTLLVSVGR
310 320 330 340 350
RPYTEGLGLS NVQIDLDNRG RVPVNERFQT KVPSIFAIGD VIEGPMLAHK
360 370 380 390 400
AEDEGILCVE GIAGGPVHID YNCVPSVVYT HPEVAWVGKA EEQLKQEGVA
410 420 430 440 450
YKIGKFPFVA NSRAKTNNDQ EGFVKVLADK QTDRMLGVHI IGPNAGEMIA
460 470 480 490
EATLAMEYGA SAEDVARVCH PHPTLSEAFR EANLAAYCGK AINNV
Length:495
Mass (Da):52,633
Last modified:March 1, 2003 - v2
Checksum:i77EB4A2FA935F0F6
GO
Isoform b (identifier: O17953-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-345: Missing.

Show »
Length:150
Mass (Da):16,136
Checksum:iFD2BED722A4FCA46
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 345345Missing in isoform b. CuratedVSP_045381Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z82277 Genomic DNA. Translation: CAB05249.2.
Z82277 Genomic DNA. Translation: CBK19462.1.
PIRiT23632.
RefSeqiNP_001255810.1. NM_001268881.1. [O17953-1]
NP_001255811.1. NM_001268882.1. [O17953-2]
UniGeneiCel.8993.

Genome annotation databases

EnsemblMetazoaiLLC1.3a; LLC1.3a; WBGene00010794. [O17953-1]
GeneIDi178387.
KEGGicel:CELE_LLC1.3.
UCSCiLLC1.3.1. c. elegans. [O17953-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z82277 Genomic DNA. Translation: CAB05249.2.
Z82277 Genomic DNA. Translation: CBK19462.1.
PIRiT23632.
RefSeqiNP_001255810.1. NM_001268881.1. [O17953-1]
NP_001255811.1. NM_001268882.1. [O17953-2]
UniGeneiCel.8993.

3D structure databases

ProteinModelPortaliO17953.
SMRiO17953. Positions 29-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO17953. 1 interaction.
STRINGi6239.LLC1.3a.1.

Proteomic databases

EPDiO17953.
PaxDbiO17953.
PRIDEiO17953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiLLC1.3a; LLC1.3a; WBGene00010794. [O17953-1]
GeneIDi178387.
KEGGicel:CELE_LLC1.3.
UCSCiLLC1.3.1. c. elegans. [O17953-1]

Organism-specific databases

CTDi178387.
WormBaseiLLC1.3a; CE31971; WBGene00010794; dld-1.
LLC1.3b; CE44593; WBGene00010794; dld-1.

Phylogenomic databases

eggNOGiKOG1335. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00550000074844.
HOGENOMiHOG000276708.
InParanoidiO17953.
KOiK00382.
OMAiVYTQPEI.
OrthoDBiEOG77126S.
PhylomeDBiO17953.

Enzyme and pathway databases

ReactomeiR-CEL-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-CEL-389661. Glyoxylate metabolism and glycine degradation.
R-CEL-5362517. Signaling by Retinoic Acid.
R-CEL-6783984. Glycine degradation.
R-CEL-70268. Pyruvate metabolism.
R-CEL-70895. Branched-chain amino acid catabolism.
R-CEL-71064. Lysine catabolism.
R-CEL-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi900918.
PROiO17953.

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

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: Bristol N2.

Entry informationi

Entry nameiDLDH_CAEEL
AccessioniPrimary (citable) accession number: O17953
Secondary accession number(s): D3YT81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 1, 2003
Last modified: March 16, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.