Q8KCW2 (DLDH_CHLTE) 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 pyruvate and 2-oxoglutarate dehydrogenases complexes

Gene names

Name:	lpd
Synonyms:	lpd-1
Ordered Locus Names:	CT1298

Organism

Chlorobium tepidum

Taxonomic identifier

1097 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
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 Potential.
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 Reference 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 – 469	469	Dihydrolipoyl dehydrogenase		PRO_0000068022
Regions
	Nucleotide binding	40 – 48	9	FAD By similarity
	Nucleotide binding	186 – 190	5	NAD By similarity
	Nucleotide binding	275 – 278	4	NAD By similarity
Sites
	Active site	450	1	Proton acceptor By similarity
	Binding site	57	1	FAD By similarity
	Binding site	120	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	209	1	NAD By similarity
	Binding site	317	1	FAD By similarity
	Binding site	325	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Disulfide bond	48 ↔ 53		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8KCW2 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: CEEB79308FD4DC4E	FASTA	469	48,007
	10 20 30 40 50 60 MQQADTLAAQ FDVAVIGSGP GGYEAAIHAA RYGLKTCIVE KAVLGGVCVN WGCIPTKALL 70 80 90 100 110 120 RSAEVFDLAK NPETFGVNVG NVSFDLAQAV KRSRNVALKS SKGVAYLLKK AAVEVLAGEA 130 140 150 160 170 180 VLTGGAGVMV TMPDGSVRML GAKNIIVATG STPRVIPGLE PDGKKIITSR EALILKEVPK 190 200 210 220 230 240 SMIVVGGGAI GVEMAWFYAK AGSKVTIVEL MPRMLPAEEA EVSEALKRSF EKAGITVHCG 250 260 270 280 290 300 AKLDNVAVSE SGVSAELVVE GSAPQTLNAS CLLVAVGVTG AIDGLGLDAV GVETERGFIR 310 320 330 340 350 360 TDGQCRTSAP GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKSPEPLSEP LIPRCVYAQP 370 380 390 400 410 420 SVASVGLTEE AAVNAGYQVA VGRSQFAASG KANAYGQLEG FVKLVFDAAT GKMLGGHLIG 430 440 450 460 HDAVELIGEL GLACRYGVTA GGLVNTVHAH PTLSETVREA AFDALQSMG

References

[1]

"The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. , Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed: 12093901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006470 Genomic DNA. Translation: AAM72528.1.
RefSeq	NP_662186.1. NC_002932.3.
3D structure databases
ProteinModelPortal	Q8KCW2.
ModBase	Search...
Proteomic databases
PRIDE	Q8KCW2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1006658.
GenomeReviews	Gene locus CT1298 in contig AE006470_GR.
KEGG	cte:CT1298.
PATRIC	21400551. VBIChlTep116050_1183.
TIGR	CT1298.
Phylogenomic databases
HOGENOM	HBG515043.
OMA	EMAWFYA.
ProtClustDB	CLSK637692.
Enzyme and pathway databases
BioCyc	CTEP194439:CT_1298-MONOMER.
Family and domain databases
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]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KO	K00382.
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_CHLTE

Accession

Primary (citable) accession number: Q8KCW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program