Reviewed, UniProtKB/Swiss-Prot P75393 (DLDH_MYCPN)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of pyruvate complex

Gene names

Name:	pdhD
Ordered Locus Names:	MPN_390
ORF Names:	MP448

Organism

Mycoplasma pneumoniae [Complete proteome] [HAMAP]

Taxonomic identifier

2104 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	457 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.
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 electron carrier activity 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 – 457	457	Dihydrolipoyl dehydrogenase		PRO_0000068032
Regions
	Nucleotide binding	32 – 40	9	FAD By similarity
	Nucleotide binding	178 – 182	5	NAD By similarity
	Nucleotide binding	262 – 265	4	NAD By similarity
Sites
	Active site	437	1	Proton acceptor By similarity
	Binding site	49	1	FAD By similarity
	Binding site	113	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	235	1	NAD; via amide nitrogen By similarity
	Binding site	303	1	FAD By similarity
	Binding site	311	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	40 ↔ 45		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P75393-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: EB044FD676F3F28E	FASTA	457	49,437
	10 20 30 40 50 60 MNYDLIIIGA GPAGYVAAEY AGKHKLKTLV VEKEYFGGVC LNVGCIPTKT LLKRAKIVDY 70 80 90 100 110 120 LRHAQDYGIS INGQVALNWN QLLEQKGKVV SKLVGGVKAI IASAKAETVM GEAKVLDPNT 130 140 150 160 170 180 VEVAGKTYTT KSIVVATGSR PRYLTLPGFA EARQNGFVID STQALSLEGV PRKLVVVGGG 190 200 210 220 230 240 VIGIEFAFLY ASLGSEVTIL QGVDRILEIF DTEVSDLVAK LLQTKNVKII TNAQVTRANN 250 260 270 280 290 300 NEVFYSQNGQ EGSVVGDRIL VSIGRIPNTE CLDGLNLQRD ERNRIVLNQD LQTSIPNIYI 310 320 330 340 350 360 VGDANAQLML AHFAYQQGRY AVNHILNKKQ VKPAQKLTCP SCIYTNPEVA SVGYTEMELK 370 380 390 400 410 420 KQGIPYVKTN LVLAHCGKAI ADNETNGFVK MMFDPQTGKI LGCCIIAATA SDMIAELALA 430 440 450 MGAGLTVFDI ANSISPHPTI NEMIADVCKK ALFDHFK

References

[1]

"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae." Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R. Nucleic Acids Res. 24:4420-4449(1996) [PubMed: 8948633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29342 / M129.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00089 Genomic DNA. Translation: AAB96096.1.
PIR	S73774.
RefSeq	NP_110078.1.
3D structure databases
HSSP	HSSP built from PDB template 1EBD based on UniProtKB P11959.
ModBase	Search...
Genome annotation databases
GeneID	877059.
GenomeReviews	Gene locus MPN_390 in contig U00089_GR.
KEGG	mpn:MPN390.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P75393.
OMA	FDIANSI.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-585. MPNE272634:MPN390-MON.
BRENDA	1.8.1.4. 39500.
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_MYCPN

Accession

Primary (citable) accession number: P75393

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	November 3, 2009
This is version 76 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)