Reviewed, UniProtKB/Swiss-Prot P66005 (DLDH_MYCBO)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of alpha keto acid dehydrogenase complexes

Gene names

Name:	lpd
Ordered Locus Names:	Mb0471

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 process	Glycolysis
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 464	464	Dihydrolipoyl dehydrogenase		PRO_0000068035
Regions
	Nucleotide binding	33 – 41	9	FAD By similarity
	Nucleotide binding	178 – 182	5	NAD By similarity
	Nucleotide binding	266 – 269	4	NAD By similarity
Sites
	Active site	443	1	Proton acceptor By similarity
	Binding site	50	1	FAD By similarity
	Binding site	113	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	201	1	NAD By similarity
	Binding site	309	1	FAD By similarity
	Binding site	317	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	41 ↔ 46		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P66005-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: DD93D95DC6F76B22	FASTA	464	49,239
	10 20 30 40 50 60 MTHYDVVVLG AGPGGYVAAI RAAQLGLSTA IVEPKYWGGV CLNVGCIPSK ALLRNAELVH 70 80 90 100 110 120 IFTKDAKAFG ISGEVTFDYG IAYDRSRKVA EGRVAGVHFL MKKNKITEIH GYGTFADANT 130 140 150 160 170 180 LLVDLNDGGT ESVTFDNAII ATGSSTRLVP GTSLSANVVT YEEQILSREL PKSIIIAGAG 190 200 210 220 230 240 AIGMEFGYVL KNYGVDVTIV EFLPRALPNE DADVSKEIEK QFKKLGVTIL TATKVESIAD 250 260 270 280 290 300 GGSQVTVTVT KDGVAQELKA EKVLQAIGFA PNVEGYGLDK AGVALTDRKA IGVDDYMRTN 310 320 330 340 350 360 VGHIYAIGDV NGLLQLAHVA EAQGVVAAET IAGAETLTLG DHRMLPRATF CQPNVASFGL 370 380 390 400 410 420 TEQQARNEGY DVVVAKFPFT ANAKAHGVGD PSGFVKLVAD AKHGELLGGH LVGHDVAELL 430 440 450 460 PELTLAQRWD LTASELARNV HTHPTMSEAL QECFHGLVGH MINF

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX248335 Genomic DNA. Translation: CAD93334.1.
RefSeq	NP_854134.1.
3D structure databases
HSSP	HSSP built from PDB template 1EBD based on UniProtKB P11959.
SMR	P66005. Positions 1-464.
ModBase	Search...
Genome annotation databases
GeneID	1091506.
GenomeReviews	Gene locus Mb0471 in contig BX248333_GR.
KEGG	mbo:Mb0471.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P66005.
OMA	P66005. FAPRVEG.
Enzyme and pathway databases
BRENDA	1.8.1.4. 3091.
Family and domain databases
InterPro	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]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHER	PTHR22912:SF20. Lipoamide_DH. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_MYCBO

Accession

Primary (citable) accession number: P66005
Secondary accession number(s): O53747

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)