Reviewed, UniProtKB/Swiss-Prot Q9I1L9 (DLDH1_PSEAE)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    LPD-Val
    E3 component of branched-chain alpha-keto acid dehydrogenase complex

Gene names

Name:	lpdV
Ordered Locus Names:	PA2250

Organism

Pseudomonas aeruginosa [Complete proteome] [HAMAP]

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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) By similarity.
Catalytic activity	Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. UniProtKB P18925
Cofactor	Binds 1 FAD per subunit By similarity. UniProtKB P18925
Subunit structure	Homodimer By similarity. UniProtKB P18925
Subcellular location	Cytoplasm By similarity. UniProtKB P18925
Miscellaneous	The active site is a redox-active disulfide bond By similarity. UniProtKB P18925
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 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 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 – 464	464	Dihydrolipoyl dehydrogenase		PRO_0000068036
Regions
	Nucleotide binding	36 – 44	9	FAD By similarity UniProtKB P18925
	Nucleotide binding	184 – 188	5	NAD By similarity
	Nucleotide binding	269 – 272	4	NAD By similarity
Sites
	Active site	443	1	Proton acceptor By similarity UniProtKB P18925
	Binding site	53	1	FAD By similarity
	Binding site	119	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	207	1	NAD By similarity
	Binding site	311	1	FAD By similarity
	Binding site	319	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	44 ↔ 49		Redox-active By similarity UniProtKB P18925

Sequences

	Sequence		Length	Mass (Da)
	Q9I1L9-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 52604A0708418434	FASTA	464	48,589
	10 20 30 40 50 60 MSQILKTSLL IVGGGPGGYV AAIRAGQLGI PTVLVEGAAL GGTCLNVGCI PSKALIHAAE 70 80 90 100 110 120 EYLKARHYAS RSALGIQVQA PSIDIARTVE WKDAIVDRLT SGVAALLKKH GVDVVQGWAR 130 140 150 160 170 180 ILDGKSVAVE LAGGGSQRIE CEHLLLAAGS QSVELPILPL GGKVISSTEA LAPGSLPKRL 190 200 210 220 230 240 VVVGGGYIGL ELGTAYRKLG VEVAVVEAQP RILPGYDEEL TKPVAQALRR LGVELYLGHS 250 260 270 280 290 300 LLGPSENGVR VRDGAGEERE IAADQVLVAV GRKPRSEGWN LESLGLDMNG RAVKVDDQCR 310 320 330 340 350 360 TSMRNVWAIG DLAGEPMLAH RAMAQGEMVA ELIAGKRRQF APVAIPAVCF TDPEVVVAGL 370 380 390 400 410 420 SPEQAKDAGL DCLVASFPFA ANGRAMTLEA NEGFVRVVAR RDNHLVVGWQ AVGKAVSELS 430 440 450 460 TAFAQSLEMG ARLEDIAGTI HAHPTLGEAV QEAALRALGH ALHI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]	"Biofouling in water treatment systems: effect of membrane properties on biofilm formation." Liddor M. Thesis (2005), Ben-Gurion University, Israel Cited for: PROTEIN SEQUENCE OF 7-24; 54-64; 72-87; 99-108; 164-178; 199-211; 253-272; 305-336; 385-396 AND 415-456. Strain: ATCC 33467 / type 1 smooth.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE004091 Genomic DNA. Translation: AAG05638.1.
PIR	F83365.
RefSeq	NP_250940.1.
3D structure databases
HSSP	HSSP built from PDB template 1LVL based on UniProtKB P09063.
SMR	Q9I1L9. Positions 3-464.
ModBase	Search...
Genome annotation databases
GeneID	878470.
GenomeReviews	Gene locus PA2250 in contig AE004091_GR.
KEGG	pae:PA2250.
NMPDR	fig|208964.1.peg.2250.
Organism-specific databases
PseudoCAP	PA2250.
CMR	Search...
Phylogenomic databases
HOGENOM	Q9I1L9.
OMA	PIISSTE.
Enzyme and pathway databases
BioCyc	PAER208964:PA2250-MON.
BRENDA	1.8.1.4. 354.
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

DLDH1_PSEAE

Accession

Primary (citable) accession number: Q9I1L9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	March 1, 2001
Last modified:	November 3, 2009
This is version 54 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)