Reviewed, UniProtKB/Swiss-Prot Q9PJI3 (DLDH_CHLMU)

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:	TC_0846

Organism

Chlamydia muridarum [Complete proteome] [HAMAP]

Taxonomic identifier

83560 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia

Protein attributes

Sequence length	465 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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tRNA processing Inferred from electronic annotation. Source: InterPro
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
	Chain	1 – 465	465	Dihydrolipoyl dehydrogenase		PRO_0000068024
Regions
	Nucleotide binding	34 – 42	9	FAD By similarity
	Nucleotide binding	180 – 184	5	NAD By similarity
	Nucleotide binding	264 – 267	4	NAD By similarity
Sites
	Active site	439	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	203	1	NAD By similarity
	Binding site	237	1	NAD; via amide nitrogen By similarity
	Binding site	307	1	FAD By similarity
	Binding site	315	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	42 ↔ 47		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PJI3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1F395C7550DD5818	FASTA	465	49,562
	10 20 30 40 50 60 MNEAFDCVVI GAGPGGYVAA ITAAQAGLKT ALIEEREAGG TCLNRGCIPS KALLASAEIV 70 80 90 100 110 120 AQIRHADQFG IHINGFSIDY PAMVQRKDTV VRSIRDGLNG LIRSNKITVF SGRGSLISST 130 140 150 160 170 180 EVKILGETPS VIKAQSIILA TGSEPRAFPG VPFSQQSPRI LCSTGVLNLK EIPQKMAIIG 190 200 210 220 230 240 GGVIGCEFAS LFHTLGSEVS VIEASQQILA LNNPDISKTM FDKFTRHGIR FMLGASVSSI 250 260 270 280 290 300 EDMGDRVRLT INGNIEEYDY VLVSIGRRLN TENIGLDKAG VICDERGVIP TDSTMRTNVP 310 320 330 340 350 360 NIYAIGDITG KWQLAHVASH QGIVAARNIA GHKDEIDYSA VPSVIFTFPE VASVGLSPTS 370 380 390 400 410 420 AQQQGIPVKV TKFPFRAIGK AVAMGESDGF AAIISHETSQ QILGAYVIGP HASSLISEIT 430 440 450 460 LAIRNELTLP CIYETIHAHP TLAEVWAESA LLAVDTPLHM PPTRK

References

[1]

"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: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002160 Genomic DNA. Translation: AAF39644.1.
PIR	B81658.
RefSeq	NP_297219.1.
3D structure databases
SMR	Q9PJI3. Positions 4-453.
ModBase	Search...
Genome annotation databases
GeneID	1246214.
GenomeReviews	Gene locus TC_0846 in contig AE002160_GR.
KEGG	cmu:TC0846.
TIGR	TC_0846.
Phylogenomic databases
HOGENOM	HBG515043.
OMA	EITIIEV.
PhylomeDB	Q9PJI3.
Enzyme and pathway databases
BioCyc	CMUR243161:TC_0846-MONOMER.
BRENDA	1.8.1.4. 256349.
Family and domain databases
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR002218. GIDA-rel. IPR000815. Hg_reductase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PANTHER	PTHR22912:SF20. Lipoamide_DH. 1 hit.
Pfam	PF01134. GIDA. 2 hits. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_CHLMU

Accession

Primary (citable) accession number: Q9PJI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 74 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)