Reviewed, UniProtKB/Swiss-Prot O18480 (DLDH_MANSE)

Names and origin

Protein names	Recommended name:     Dihydrolipoyl dehydrogenase     EC=1.8.1.4 Alternative name(s):     Dihydrolipoamide dehydrogenase     E3
Organism	Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifier	7130 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Sphingidae › Sphinginae › Sphingini › Manduca

Protein attributes

Sequence length	497 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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 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
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 497	497	Dihydrolipoyl dehydrogenase		PRO_0000068007
Regions
	Nucleotide binding	60 – 69	10	FAD By similarity
	Nucleotide binding	170 – 172	3	FAD By similarity
	Nucleotide binding	207 – 214	8	NAD By similarity
	Nucleotide binding	349 – 352	4	FAD By similarity
Sites
	Active site	475	1	Proton acceptor By similarity
	Binding site	78	1	FAD By similarity
	Binding site	142	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	230	1	NAD By similarity
	Binding site	264	1	NAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	302	1	NAD; via amide nitrogen By similarity
	Binding site	343	1	FAD By similarity
Amino acid modifications
	Disulfide bond	69 ↔ 74		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	O18480-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 1689E564E165137A	FASTA	497	53,083
	10 20 30 40 50 60 MGYKFLKLAS ASFRNGGVRI VSRQYSTTHD ADLVVIGAGP GGYVAAIKAA QLGMKVVSVE 70 80 90 100 110 120 KEPSLGGTCL NVGCIPSKAL LHNTHLYHMA KHDFKHRGIE TGEVKFNFKA MMDYKVNAVK 130 140 150 160 170 180 ALTGGIAMLF QKNKVKLVRG AGTIVAPNKV EVKGEKGVET VNTKNILIAT GSEVTPFPGV 190 200 210 220 230 240 TFDEKQIITS TGALSLESVP KKMLVIGAGV IGLELGSVYQ RLGADVTAIE FLGSIGGIGI 250 260 270 280 290 300 DMEVSKDYRI LAKQGMKFKL ETKVLGVKKE GSTVKVEDVS IEGAKGGNKE TMDCDVVLIS 310 320 330 340 350 360 IGRRPYTKDL GLDKVGIALD DRGRVPVNNK FQTTVPGIYA IGDVIHGPML AHKAEDEGIV 370 380 390 400 410 420 CVEGIKGMPV HFNYDAIPSV IYTSPEVGWV RKTEEDLKKE GKAYKVRKFP FLANSRAKTN 430 440 450 460 470 480 GEPDGFVKVL SDKATDVILG THIIGPGGGE LINEAVLAQE YGAAAEDVAR VCHAHPTCAE 490 ALREANLAAY CGKPINF

References

[1]	"Primary structure of an invertebrate dihydrolipoamide dehydrogenase with phylogenetic relationship to vertebrate and bacterial disulfide oxidoreductases." Pullikuth A.K., Gill S.S. Gene 200:163-172(1997) [PubMed: 9373151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF008586 mRNA. Translation: AAB88282.1.
3D structure databases
HSSP	HSSP built from PDB template 1DXL based on UniProtKB P31023.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.4. 15145.
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_MANSE

Accession

Primary (citable) accession number: O18480

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)