Reviewed, UniProtKB/Swiss-Prot Q54EW8 (DLDH_DICDI)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase
    Glycine cleavage system L protein

Gene names

Name:	lpd
Synonyms:	bkdD, dld, odhC, pdhD
ORF Names:	DDB_G0291648

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Cytoplasm Potential.
Miscellaneous	The active site is a redox-active disulfide bond By similarity.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
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 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 – 488	488	Dihydrolipoyl dehydrogenase		PRO_0000327450
Regions
	Nucleotide binding	52 – 61	10	FAD By similarity
	Nucleotide binding	163 – 165	3	FAD By similarity
	Nucleotide binding	200 – 207	8	NAD By similarity
	Nucleotide binding	341 – 344	4	FAD By similarity
Sites
	Active site	467	1	Proton acceptor By similarity
	Binding site	70	1	FAD By similarity
	Binding site	134	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	223	1	NAD By similarity
	Binding site	257	1	NAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	294	1	NAD; via amide nitrogen By similarity
	Binding site	335	1	FAD By similarity
Amino acid modifications
	Disulfide bond	61 ↔ 66		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54EW8-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: A7DD67E8F7707783	FASTA	488	51,794
	10 20 30 40 50 60 MLRINRISNL RTFGQRFFST EQQDVVVIGG GPGGYVAGIK AGQLGMKVTV VEKRGKLGGT 70 80 90 100 110 120 CLNVGCIPSK ALLNASHLYE EATTKMSKYG VKCSGVELDL GAMMQYKDKS VSGLTSGIEG 130 140 150 160 170 180 LFKKNKVKYD KGFGKITGPN TVEVTLNDGS VKTIETKNIV IATGSEVTSL PNVNIDEESI 190 200 210 220 230 240 ISSTGALALK SVPKKLIVIG GGVIGLELGS VWSRLGSETT VVEFTNRIAA GADGEVAKKF 250 260 270 280 290 300 QKSLEKQHMK FHLETKVTSV VKKSDGKVTV TVEQVGAGGF TGTLEADAVL VSVGRRPNTS 310 320 330 340 350 360 GLGLESVGIP TDKAGRVEVG DHFNTKVPSI FAIGDAIRGP MLAHKAEEEG IAIIEQIHNG 370 380 390 400 410 420 GGHVNYGAIP SIIYTHPEVA WVGKTEEELQ KEGIQYNIGR FPFVANSRAK TNDDVEGFVK 430 440 450 460 470 480 FLAAKDSDRV LGAHIMGTNA GELIGECVLA MEYGASCEDI ARTCHGHPTL SEAVKEAAMD AYDKPIHM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"A first glimpse into the pattern and scale of gene transfer in Apicomplexa." Huang J., Mullapudi N., Sicheritz-Ponten T., Kissinger J.C. Int. J. Parasitol. 34:265-274(2004) [PubMed: 15003488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-357.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000177 Genomic DNA. Translation: EAL61808.1. AY466389 Genomic DNA. Translation: AAS47709.1.
RefSeq	XP_635122.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q54EW8.
Genome annotation databases
GeneID	3386860.
GenomeReviews	Gene locus lpd in contig CM000155_GR.
KEGG	ddi:DDB_0216232.
Organism-specific databases
dictyBase	DDB_G0291648. lpd.
Phylogenomic databases
OMA	LAHGKDF.
Enzyme and pathway databases
BRENDA	1.8.1.4. 424.
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_DICDI

Accession

Primary (citable) accession number: Q54EW8
Secondary accession number(s): Q6S4V6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)