Reviewed, UniProtKB/Swiss-Prot P43784 (DLDH_HAEIN)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes

Gene names

Name:	lpdA
Ordered Locus Names:	HI1231

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 478	477	Dihydrolipoyl dehydrogenase		PRO_0000068030
Regions
	Nucleotide binding	36 – 45	10	FAD By similarity
	Nucleotide binding	183 – 187	5	NAD By similarity
	Nucleotide binding	270 – 273	4	NAD By similarity
Sites
	Active site	445	1	Proton acceptor By similarity
	Binding site	54	1	FAD By similarity
	Binding site	117	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	206	1	NAD By similarity
	Binding site	239	1	NAD; via amide nitrogen By similarity
	Binding site	313	1	FAD By similarity
	Binding site	321	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	45 ↔ 50		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43784-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E2554EE977AF749C	FASTA	478	51,154
	10 20 30 40 50 60 MSKEIKTQVV VLGAGPAGYS AAFRCADLGL ETVIVERYST LGGVCLNVGC IPSKALLHVA 70 80 90 100 110 120 KVIEEAKHAN KNGIYFSEPR IELDEVRAGK EAVVAKLTGG LAGMAKARKV TVVEGLATFT 130 140 150 160 170 180 DSHTLVARDR DGNPTTVKFD NAIIAAGSRP VQLPFIPHED PRIWDSTDAL KLKEVPKKLL 190 200 210 220 230 240 IMGGGIIGLE MGTVYNALGS EVEVVEMFDQ VIPAADKDVV GIYTKQVEKK FKLMLETKVT 250 260 270 280 290 300 AVEAKDDGIY VSMEGKACND TKRYDAVLVA IGRVPNGKLI DAGKAGVEVD DRGFIHVDKQ 310 320 330 340 350 360 MRTNVPHIYA IGDIVGQPML AHKGVHEGHV AAEVIAGQKH YFDPKVIPSI AYTEPEVAWV 370 380 390 400 410 420 GKTEKECKQE GLNYEVAKFP WAASGRAIAS ECSEGMTKLI FDKDTHRVLG GAIVGSNGGE 430 440 450 460 470 LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNAK AKEKIISI

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC22884.1.
PIR	H64111.
RefSeq	NP_439387.1.
3D structure databases
HSSP	HSSP built from PDB template 1OJT based on UniProtKB Q51225.
ModBase	Search...
Genome annotation databases
GeneID	950173.
GenomeReviews	Gene locus HI1231 in contig L42023_GR.
KEGG	hin:HI1231.
NMPDR	fig|71421.1.peg.1177.
TIGR	HI1231.
Phylogenomic databases
HOGENOM	P43784.
OMA	P43784. PFIPEDP.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1231-MON.
BRENDA	1.8.1.4. 109.
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_HAEIN

Accession

Primary (citable) accession number: P43784

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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