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Q9PJI3 (DLDH_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrolipoyl dehydrogenase

EC=1.8.1.4
Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of 2-oxoglutarate dehydrogenase complex
Gene names
Name:lpdA
Ordered Locus Names:TC_0846
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity.

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

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

tRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydrolipoyl dehydrogenase activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Dihydrolipoyl dehydrogenase
PRO_0000068024

Regions

Nucleotide binding34 – 429FAD By similarity
Nucleotide binding180 – 1845NAD By similarity
Nucleotide binding264 – 2674NAD By similarity

Sites

Active site4391Proton acceptor By similarity
Binding site511FAD By similarity
Binding site1141FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2031NAD By similarity
Binding site2371NAD; via amide nitrogen By similarity
Binding site3071FAD By similarity
Binding site3151FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond42 ↔ 47Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PJI3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1F395C7550DD5818

FASTA46549,562
        10         20         30         40         50         60 
MNEAFDCVVI GAGPGGYVAA ITAAQAGLKT ALIEEREAGG TCLNRGCIPS KALLASAEIV 

        70         80         90        100        110        120 
AQIRHADQFG IHINGFSIDY PAMVQRKDTV VRSIRDGLNG LIRSNKITVF SGRGSLISST 

       130        140        150        160        170        180 
EVKILGETPS VIKAQSIILA TGSEPRAFPG VPFSQQSPRI LCSTGVLNLK EIPQKMAIIG 

       190        200        210        220        230        240 
GGVIGCEFAS LFHTLGSEVS VIEASQQILA LNNPDISKTM FDKFTRHGIR FMLGASVSSI 

       250        260        270        280        290        300 
EDMGDRVRLT INGNIEEYDY VLVSIGRRLN TENIGLDKAG VICDERGVIP TDSTMRTNVP 

       310        320        330        340        350        360 
NIYAIGDITG KWQLAHVASH QGIVAARNIA GHKDEIDYSA VPSVIFTFPE VASVGLSPTS 

       370        380        390        400        410        420 
AQQQGIPVKV TKFPFRAIGK AVAMGESDGF AAIISHETSQ QILGAYVIGP HASSLISEIT 

       430        440        450        460 
LAIRNELTLP CIYETIHAHP TLAEVWAESA LLAVDTPLHM PPTRK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39644.1.
PIRB81658.
RefSeqNP_297219.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PJI3.
ModBaseSearch...

Protein-protein interaction databases

STRING243161.TC0846.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39644; AAF39644; TC_0846.
GeneID1246214.
KEGGcmu:TC0846.
PATRIC20373206. VBIChlMur19118_0907.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1249.
KOK00382.
OMAVANSRAK.
ProtClustDBPRK06327.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-836-MONOMER.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR002218. GIDA-rel.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
[Graphical view]
PfamPF01134. GIDA. 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...

Entry information

Entry nameDLDH_CHLMU
AccessionPrimary (citable) accession number: Q9PJI3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families