Dihydrolipoyl dehydrogenase - Mycobacterium leprae (strain TN)

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Q50068 (DLDH_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dihydrolipoyl dehydrogenase
EC=1.8.1.4

Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of alpha-ketoacid dehydrogenase complexes

Gene names

Name:	lpd
Ordered Locus Names:	ML2387
ORF Names:	u1740l

Organism

Mycobacterium leprae (strain TN) [Complete proteome] [HAMAP]

Taxonomic identifier

272631 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium ›

Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the 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. Makes part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3), and of the BCKADH complex, consisting of multiple copies of BkdA/BkdB (E1), BkdC (E2) and Lpd (E3) 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 process	Glycolysis Tricarboxylic acid cycle
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dihydrolipoyl 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 467

467

Dihydrolipoyl dehydrogenase

PRO_0000068033

Regions

Nucleotide binding

33 – 41

FAD By similarity

Nucleotide binding

181 – 185

NAD By similarity

Nucleotide binding

269 – 272

NAD By similarity

Sites

Active site

446

Proton acceptor By similarity

Binding site

FAD By similarity

Binding site

113

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

204

NAD By similarity

Binding site

312

FAD By similarity

Binding site

320

FAD; via amide nitrogen By similarity

Amino acid modifications

Disulfide bond

41 ↔ 46

Redox-active By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q50068 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CA46B807119FC15A
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FASTA

467

50,077

        10         20         30         40         50         60 
MTHYDVVVLG AGPGGYVAAI RAAQLGLSTA VVEPKYWGGI CLNVGCIPSK VLLHNAELAH 

        70         80         90        100        110        120 
IFTKEAKTFG ISGDASFDYG IAYDRSRKVS EGRVAGVHFL MKKNKITEIH GYGRFTDANT 

       130        140        150        160        170        180 
LSVELSEGVP ETPLKVTFNN VIIATGSKTR LVPGTLLSTN VITYEEQILT RELPDSIVIV 

       190        200        210        220        230        240 
GAGAIGIEFG YVLKNYGVDV TIVEFLPRAM PNEDAEVSKE IEKQFKKMGI KILTGTKVES 

       250        260        270        280        290        300 
ISDNGSHVLV AVSKDGQFQE LKADKVLQAI GFAPNVDGYG LDKVGVALTA DKAVDIDDYM 

       310        320        330        340        350        360 
QTNVSHIYAI GDVTGKLQLA HVAEAQGVVA AEAIAGAETL ALSDYRMMPR ATFCQPNVAS 

       370        380        390        400        410        420 
FGLTEQQARD GGYDVVVAKF PFTANAKAHG MGDPSGFVKL VADAKYGELL GGHMIGHNVS 

       430        440        450        460 
ELLPELTLAQ KWDLTATELV RNVHTHPTLS EALQECFHGL IGHMINF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. Barrell B.G. Nature 409:1007-1011(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U15183 Genomic DNA. Translation: AAA63016.1. AL583925 Genomic DNA. Translation: CAC31903.1.
PIR	G87207.
RefSeq	NP_302544.1. NC_002677.1.
3D structure databases
ProteinModelPortal	Q50068.
SMR	Q50068. Positions 1-467.
ModBase	Search...
Protein-protein interaction databases
STRING	272631.ML2387.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC31903; CAC31903; CAC31903.
GeneID	908174.
KEGG	mle:ML2387.
PATRIC	18059357. VBIMycLep78757_4593.
Organism-specific databases
Leproma	ML2387.
CMR	Search...
Phylogenomic databases
eggNOG	COG1249.
HOGENOM	HOG000276708.
KO	K00382.
OMA	HNYGVKV.
ProtClustDB	PRK07818.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. 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]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 2 hits. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_MYCLE

Accession

Primary (citable) accession number: Q50068

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents