Reviewed, UniProtKB/Swiss-Prot P31052 (DLDH2_PSEPU)

Names and origin

Protein names

Recommended name:
    Dihydrolipoamide dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    LPD-GLC
    E3 component of 2-oxoglutarate dehydrogenase complex
    Glycine oxidation system L-factor

Gene names

Name:

lpdG

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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). Also acts in the glycine cleavage system.
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.
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	Direct protein sequencing
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
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 478	477	Dihydrolipoamide dehydrogenase		PRO_0000068039
Regions
	Nucleotide binding	34 – 49	16	FAD By similarity
	Nucleotide binding	188 – 192	5	NAD By similarity
	Nucleotide binding	276 – 279	4	NAD By similarity
Sites
	Active site	451	1	Proton acceptor By similarity
	Binding site	58	1	FAD By similarity
	Binding site	122	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	211	1	NAD By similarity
	Binding site	245	1	NAD; via amide nitrogen By similarity
	Binding site	319	1	FAD By similarity
	Binding site	327	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	49 ↔ 54		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P31052-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 2B7979445DC60812	FASTA	478	49,896
	10 20 30 40 50 60 MTQKFDVVVI GAGPGGYVAA IKAAQLGLKT ACIEKYTDAE GKLALGGTCL NVGCIPSKAL 70 80 90 100 110 120 LDSSWKYKEA KESFNVHGIS TGEVKMDVAA MVGRKAGIVK NLTGGVATLF KANGVTSIQG 130 140 150 160 170 180 HGKLLAGKKV EVTKADGTTE VIEAENVILA SGSRPIDIPP APVDQNVIVD STGALEFQAV 190 200 210 220 230 240 PKRLGVIGAG VIGLELGSVW ARLGAEVTVL EALDTFLMAA DTAVSKEAQK TLTKQGLDIK 250 260 270 280 290 300 LGARVTGSKV NGNEVEVTYT NAEGEQKITF DKLIVAVGRR PVTTDLLAAD SGVTIDERGY 310 320 330 340 350 360 IFVDDYCATS VPGVYAIGDV VRGMMLAHKA SEEGIMVVER IKGHKAQMNY DLIPSVIYTH 370 380 390 400 410 420 PEIAWVGKTE QALKAEGVEV NVGTFPFAAS GRAMAANDTG GFVKVIADAK TDRVLGVHVI 430 440 450 460 470 GPSAAELVQQ GAIAMEFGTS AEDLGMMVFS HPTLSEALHE AALAVNGGAI HVANRKKR

References

[1]	"Cloning and sequence analysis of the LPD-glc structural gene of Pseudomonas putida." Palmer J.A., Hatter K., Sokatch J.R. J. Bacteriol. 173:3109-3116(1991) [PubMed: 1902462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G2.
[2]	Sokatch J.R. Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Isolation of a third lipoamide dehydrogenase from Pseudomonas putida." Burns G., Sykes P.J., Hatter K., Sokatch J.R. J. Bacteriol. 171:665-668(1989) [PubMed: 2914869] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M80189 Genomic DNA. Translation: AAA96437.1.
PIR	A39406.
3D structure databases
HSSP	HSSP built from PDB template 1LPF based on UniProtKB P14218.
SMR	P31052. Positions 2-473.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 403.
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

DLDH2_PSEPU

Accession

Primary (citable) accession number: P31052

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 78 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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