Q04933 (DLDH_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Dihydrolipoyl dehydrogenase EC=1.8.1.4 Alternative name(s): Dihydrolipoamide dehydrogenase
Organism	Trypanosoma brucei brucei
Taxonomic identifier	5702 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma › Trypanozoon › Trypanosoma brucei

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

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.
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
Domain	Redox-active center
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
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: InterPro
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 – 479	479	Dihydrolipoyl dehydrogenase		PRO_0000068008
Regions
	Nucleotide binding	41 – 50	10	FAD By similarity
	Nucleotide binding	153 – 155	3	FAD By similarity
	Nucleotide binding	190 – 197	8	NAD By similarity
	Nucleotide binding	332 – 335	4	FAD By similarity
Sites
	Active site	458	1	Proton acceptor By similarity
	Binding site	59	1	FAD By similarity
	Binding site	124	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	213	1	NAD By similarity
	Binding site	247	1	NAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	284	1	NAD; via amide nitrogen By similarity
	Binding site	325	1	FAD By similarity
Amino acid modifications
	Disulfide bond	50 ↔ 55		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q04933 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: ABE40113CDFAF830	FASTA	479	50,220
	10 20 30 40 50 60 MFRRCFPIFN PYDVVVVGGG PGGYVAAIKA AQLGLKTACV EKRGALGGTC LNVGCIPSKA 70 80 90 100 110 120 LLHATHMYHD AHANFERYGL MGGAGVTMDV AKMQQQKEKS VNGLTSGVEY LLKKNKVTYY 130 140 150 160 170 180 KGEAGFVTPN TLNVKGIDGK DEAIEAKNTI IATGSEPTAL PFLPFDEKVV LSSTGALALQ 190 200 210 220 230 240 QVPKKMVVIG GGVIGLELGS VWARLGSDVT VVEFAPRCAP TLDSDVTDAL VGALKRNGED 250 260 270 280 290 300 EVPMTGIEGV NGTNNGSIAL TLEVEQAGGQ AETLHCDALL VSVGRRPYTA GLGLEKNNVS 310 320 330 340 350 360 LNERGFVKIG SHFETNVAGV YAIGDVVDKG PMLAHKAEDE GVACAEILAG RPGHVNYDVI 370 380 390 400 410 420 PGVIYTMPEV ASVGKTEEEL KKAGVAYKVG KFPFNANSRA KAVATEDGFV KVLTDKATDR 430 440 450 460 470 ILGVHIVCSA AGELIAGALL AMEYGASSED VGRTCHAHPT MSEAVKEACM ACFAKTINF

References

[1]	"Cloning, sequencing, and expression of Trypanosoma brucei dihydrolipoamide dehydrogenase." Else A.J., Hough D.W., Danson M.J. Eur. J. Biochem. 212:423-429(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X70646 Genomic DNA. Translation: CAA49991.1.
PIR	S30057.
3D structure databases
ProteinModelPortal	Q04933.
SMR	Q04933. Positions 10-479.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
EuPathDB	TriTrypDB:Tb11.01.8470. TriTrypDB:Tb427tmp.01.8470.
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]
PANTHER	PTHR22912:SF20. PTHR22912:SF20. 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.
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_TRYBB

Accession

Primary (citable) accession number: Q04933

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 3, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)