Reviewed, UniProtKB/Swiss-Prot P0A0E7 (DLDH_STAAW)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of pyruvate complex
    Membrane-bound ribosome protein complex 50 kDa subunit

Gene names

Name:	pdhD
Ordered Locus Names:	MW0979

Organism

Staphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]

Taxonomic identifier

196620 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	468 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. Membrane; Peripheral membrane protein.
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 Membrane
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 membrane 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 – 468	468	Dihydrolipoyl dehydrogenase		PRO_0000068049
Regions
	Nucleotide binding	39 – 47	9	FAD By similarity
	Nucleotide binding	183 – 187	5	NAD By similarity
	Nucleotide binding	271 – 274	4	NAD By similarity
Sites
	Active site	446	1	Proton acceptor By similarity
	Binding site	56	1	FAD By similarity
	Binding site	119	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	206	1	NAD By similarity
	Binding site	314	1	FAD By similarity
	Binding site	322	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	47 ↔ 52		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A0E7-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: 7B061FE2C39ED2D9	FASTA	468	49,451
	10 20 30 40 50 60 MVVGDFPIET DTIVIGAGPG GYVAAIRAAQ LGQKVTIVEK GNLGGVCLNV GCIPSKALLH 70 80 90 100 110 120 ASHRFVEAQH SENLGVIAES VSLNFQKVQE FKSSVVNKLT GGVEGLLKGN KVNIVKGEAY 130 140 150 160 170 180 FVDNNSLRVM DEKSAQTYNF KNAIIATGSR PIEIPNFKFG KRVIDSTGAL NLQEVPGKLV 190 200 210 220 230 240 VVGGGYIGSE LGTAFANFGS EVTILEGAKD ILGGFEKQMT QPVKKGMKEK GVEIVTEAMA 250 260 270 280 290 300 KSAEETDNGV KVTYEAKGEE KTIEADYVLV TVGRRPNTDE LGLEELGVKF ADRGLLEVDK 310 320 330 340 350 360 QSRTSISNIY AIGDIVPGLP LAHKASYEAK VAAEAIDGQA AEVDYIGMPA VCFTEPELAT 370 380 390 400 410 420 VGYSEAQAKE EGLAIKASKF PYAANGRALS LDDTNGFVKL ITLKEDDTLI GAQVVGTGAS 430 440 450 460 DIISELGLAI EAGMNAEDIA LTIHAHPTLG EMTMEAAEKA IGYPIHTM

References

[1]

"Genome and virulence determinants of high virulence community-acquired MRSA." Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K. Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000033 Genomic DNA. Translation: BAB94844.1.
RefSeq	NP_645796.1.
3D structure databases
HSSP	HSSP built from PDB template 1EBD based on UniProtKB P11959.
SMR	P0A0E7. Positions 8-461.
ModBase	Search...
Genome annotation databases
GeneID	1003091.
GenomeReviews	Gene locus MW0979 in contig BA000033_GR.
KEGG	sam:MW0979.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A0E7.
OMA	P0A0E7. PFIPEDP.
Enzyme and pathway databases
BioCyc	SAUR196620:MW0979-MON.
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_STAAW

Accession

Primary (citable) accession number: P0A0E7
Secondary accession number(s): Q59822

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	June 16, 2009
This is version 35 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)