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Reviewed, UniProtKB/Swiss-Prot Q8KCW2 (DLDH_CHLTE)

Last modified February 9, 2010. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes
Gene names
Name: lpd
Synonyms: lpd-1
Ordered Locus Names: CT1298
OrganismChlorobium tepidum [Complete proteome] [HAMAP]
Taxonomic identifier1097 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes By similarity.

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

Cytoplasm 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
   Biological processGlycolysis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

dihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Dihydrolipoyl dehydrogenase
PRO_0000068022

Regions

Nucleotide binding40 – 489FAD By similarity
Nucleotide binding186 – 1905NAD By similarity
Nucleotide binding275 – 2784NAD By similarity

Sites

Active site4501Proton acceptor By similarity
Binding site571FAD By similarity
Binding site1201FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2091NAD By similarity
Binding site3171FAD By similarity
Binding site3251FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond48 ↔ 53Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KCW2-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: CEEB79308FD4DC4E

FASTA46948,007
        10         20         30         40         50         60 
MQQADTLAAQ FDVAVIGSGP GGYEAAIHAA RYGLKTCIVE KAVLGGVCVN WGCIPTKALL 

        70         80         90        100        110        120 
RSAEVFDLAK NPETFGVNVG NVSFDLAQAV KRSRNVALKS SKGVAYLLKK AAVEVLAGEA 

       130        140        150        160        170        180 
VLTGGAGVMV TMPDGSVRML GAKNIIVATG STPRVIPGLE PDGKKIITSR EALILKEVPK 

       190        200        210        220        230        240 
SMIVVGGGAI GVEMAWFYAK AGSKVTIVEL MPRMLPAEEA EVSEALKRSF EKAGITVHCG 

       250        260        270        280        290        300 
AKLDNVAVSE SGVSAELVVE GSAPQTLNAS CLLVAVGVTG AIDGLGLDAV GVETERGFIR 

       310        320        330        340        350        360 
TDGQCRTSAP GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKSPEPLSEP LIPRCVYAQP 

       370        380        390        400        410        420 
SVASVGLTEE AAVNAGYQVA VGRSQFAASG KANAYGQLEG FVKLVFDAAT GKMLGGHLIG 

       430        440        450        460 
HDAVELIGEL GLACRYGVTA GGLVNTVHAH PTLSETVREA AFDALQSMG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006470 Genomic DNA. Translation: AAM72528.1.
RefSeqNP_662186.1.

3D structure databases

SMRQ8KCW2. Positions 10-468.
ModBaseSearch...

Genome annotation databases

GeneID1006658.
GenomeReviewsGene locus CT1298 in contig AE006470_GR.
KEGGcte:CT1298.
TIGRCT1298.

Phylogenomic databases

HOGENOMHBG515043.
OMAEMAWFYA.

Enzyme and pathway databases

BioCycCTEP194439:CT_1298-MONOMER.
BRENDA1.8.1.4. 189605.

Family and domain databases

InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHERPTHR22912:SF20. Lipoamide_DH. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLDH_CHLTE
AccessionPrimary (citable) accession number: Q8KCW2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2002
Last modified: February 9, 2010
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents