Q9Z773 (DLDH_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyl dehydrogenase
EC=1.8.1.4

Alternative name(s):
Dihydrolipoamide dehydrogenase
E3 component of 2-oxoglutarate dehydrogenase complex

Gene names

Name:	lpdA
Ordered Locus Names:	CPn_0833, CP_1037, CpB0862

Organism

Chlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]

Taxonomic identifier

83558 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chlamydiae/Verrucomicrobia group › Chlamydiae › Chlamydiia › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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.
Cofactor	Binds 1 FAD per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
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
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding 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 – 461	461	Dihydrolipoyl dehydrogenase		PRO_0000068025
Regions
	Nucleotide binding	34 – 42	9	FAD By similarity
	Nucleotide binding	177 – 181	5	NAD By similarity
	Nucleotide binding	261 – 264	4	NAD By similarity
Sites
	Active site	436	1	Proton acceptor By similarity
	Binding site	51	1	FAD By similarity
	Binding site	114	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	200	1	NAD By similarity
	Binding site	304	1	FAD By similarity
	Binding site	312	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	42 ↔ 47		Redox-active By similarity
Experimental info
	Sequence conflict	64	1	K → T in AAP98791. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9Z773 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: CADD4483E758FFAD	FASTA	461	49,167
	10 20 30 40 50 60 MTQEFDCVVI GAGPSGYVAA ITAAQSKLRT ALIEEDQAGG TCLNRGCIPS KALIAGANVV 70 80 90 100 110 120 SHIKHAEQFG IHVDGYTIDY PAMAKRKNTV VQGIRQGLEG LIRSNKITVL KGTGSLVSST 130 140 150 160 170 180 EVKVIGQDTT IIKANHIILA TGSEPRPFPG VPFSSRILSS TGILELEVLP KKLAIIGGGV 190 200 210 220 230 240 IGCEFASLFH TLGVEITVIE ALDHILAVNN KEVSQTVTNK FTKQGIRILT KASISAIEES 250 260 270 280 290 300 QNQVRITVND QVEEFDYVLV AIGRQFNTAS IGLDNAGVIR DDRGVIPVDE TMRTNVPNIY 310 320 330 340 350 360 AIGDITGKWL LAHVASHQGV IAAKNISGHH EVMDYSAIPS VIFTHPEIAM VGLSLQEAEQ 370 380 390 400 410 420 QNLPAKLTKF PFKAIGKAVA LGASDGFAAI VSHEITQQIL GAYVIGPHAS SLIGEMTLAI 430 440 450 460 RNELTLPCIY ETVHAHPTLS EVWAEGALLA TNHPLHFPPK S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomes of Chlamydia pneumoniae and C. trachomatis." Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S. Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CWL029.
[2]	"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AR39.
[3]	"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA." Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T. Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J138.
[4]	"Genomic sequence comparison of two unrelated isolates of Chlamydia pneumoniae from Japan and U.S." Shirai M. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: J138.
[5]	"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis." Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TW-183.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001363 Genomic DNA. Translation: AAD18970.1. AE002161 Genomic DNA. Translation: AAF38812.1. BA000008 Genomic DNA. Translation: BAA99041.1. AB035943 Genomic DNA. Translation: BAA88651.1. AE009440 Genomic DNA. Translation: AAP98791.1.
PIR	C72031. G86594.
RefSeq	NP_225028.1. NC_000922.1. NP_300890.1. NC_002491.1. NP_445574.1. NC_002179.2. NP_877134.1. NC_005043.1.
3D structure databases
ProteinModelPortal	Q9Z773.
ModBase	Search...
Protein-protein interaction databases
STRING	115713.CPn0833.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD18970; AAD18970; CPn_0833. AAF38812; AAF38812; CP_1037. AAP98791; AAP98791; CpB0862. BAA99041; BAA99041; BAA99041.
GeneID	1467541. 895532. 919599. 963515.
KEGG	cpa:CP1037. cpj:CPj0833. cpn:CPn0833. cpt:CpB0862.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1249.
HOGENOM	HOG000276708.
KO	K00382.
OMA	LLATNHP.
ProtClustDB	PRK06327.
Enzyme and pathway databases
BioCyc	CPNE115711:GI7B-1035-MONOMER. CPNE115713:GHEY-836-MONOMER. CPNE138677:GH8N-823-MONOMER. CPNE182082:GH4N-859-MONOMER.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_CHLPN

Accession

Primary (citable) accession number: Q9Z773
Secondary accession number(s): Q9JQE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program