Reviewed, UniProtKB/Swiss-Prot O84561 (DLDH_CHLTR)

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:	CT_557

Organism

Chlamydia trachomatis [Complete proteome] [HAMAP]

Taxonomic identifier

813 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia

Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
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 – 465	465	Dihydrolipoyl dehydrogenase		PRO_0000068026
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)
	O84561-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 56449CCD2AB61477	FASTA	465	49,491
	10 20 30 40 50 60 MNEAFDCVVI GAGPGGYVAA ITAAQAGLKT ALIEKREAGG TCLNRGCIPS KALLAGAEVV 70 80 90 100 110 120 TQIRHADQFG IHVEGFSINY PAMVQRKDSV VRSIRDGLNG LIRSNKITVF SGRGSLISST 130 140 150 160 170 180 EVKILGENPS VIKAHSIILA TGSEPRAFPG IPFSAESPRI LCSTGVLNLK EIPQKMAIIG 190 200 210 220 230 240 GGVIGCEFAS LFHTLGSEVS VIEASSQILA LNNPDISKTM FDKFTRQGLR FVLEASVSNI 250 260 270 280 290 300 EDIGDRVRLT INGNVEEYDY VLVSIGRRLN TENIGLDKAG VICDERGVIP TDATMRTNVP 310 320 330 340 350 360 NIYAIGDITG KWQLAHVASH QGIIAARNIA GHKEEIDYSA VPSVIFTFPE VASVGLSPTA 370 380 390 400 410 420 AQQQKIPVKV TKFPFRAIGK AVAMGEADGF AAIISHETTQ QILGAYVIGP HASSLISEIT 430 440 450 460 LAVRNELTLP CIYETIHAHP TLAEVWAESA LLAVDTPLHM PPAKK

References

[1]

"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed: 9784136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE001273 Genomic DNA. Translation: AAC68159.1.
PIR	E71500.
RefSeq	NP_220072.1.
3D structure databases
HSSP	HSSP built from PDB template 1EBD based on UniProtKB P11959.
ModBase	Search...
2-D gel databases
PHCI-2DPAGE	O84561.
Genome annotation databases
GeneID	884341.
GenomeReviews	Gene locus CT_557 in contig AE001273_GR.
KEGG	ctr:CT557.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O84561.
OMA	IEVDACL.
Enzyme and pathway databases
BioCyc	CTRA315277:CT557-MON.
BRENDA	1.8.1.4. 108.
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_CHLTR

Accession

Primary (citable) accession number: O84561

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
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)