Reviewed, UniProtKB/Swiss-Prot Q60HG3 (DLDH_MACFA)

Names and origin

Protein names

Recommended name:
    Dihydrolipoyl dehydrogenase, mitochondrial
    EC=1.8.1.4
Alternative name(s):
    Dihydrolipoamide dehydrogenase

Gene names

Name:	DLD
ORF Names:	QflA-16416, QtsA-11266

Organism

Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey)

Taxonomic identifier

9541 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Lipoamide dehydrogenase is a component of the glycine cleavage system as well as 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. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds By similarity.
Subcellular location	Mitochondrion matrix 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
Cellular component	Mitochondrion
Domain	Redox-active center Transit peptide
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond
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	mitochondrial matrix 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
	Transit peptide	1 – 35	35	Mitochondrion By similarity
	Chain	36 – 509	474	Dihydrolipoyl dehydrogenase, mitochondrial		PRO_0000030296
Regions
	Nucleotide binding	71 – 80	10	FAD By similarity
	Nucleotide binding	183 – 185	3	FAD By similarity
	Nucleotide binding	220 – 227	8	NAD By similarity
	Nucleotide binding	361 – 364	4	FAD By similarity
Sites
	Active site	487	1	Proton acceptor By similarity
	Binding site	89	1	FAD By similarity
	Binding site	154	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	243	1	NAD By similarity
	Binding site	278	1	NAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	314	1	NAD; via amide nitrogen By similarity
	Binding site	355	1	FAD By similarity
Amino acid modifications
	Modified residue	127	1	N6-acetyllysine By similarity
	Modified residue	143	1	N6-acetyllysine By similarity
	Modified residue	267	1	N6-acetyllysine By similarity
	Modified residue	320	1	N6-acetyllysine By similarity
	Modified residue	410	1	N6-acetyllysine By similarity
	Modified residue	417	1	N6-acetyllysine By similarity
	Modified residue	420	1	N6-acetyllysine By similarity
	Disulfide bond	80 ↔ 85		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q60HG3-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 85DE7AF9EEE18FA2	FASTA	509	54,221
	10 20 30 40 50 60 MQSWSRVYCS LAKRGHFNRI SHGLQGLSAV PLRTYADQLI DADVTVIGSG PGGYVAAIKA 70 80 90 100 110 120 AQLGFKTVCV EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL 130 140 150 160 170 180 DKMMEQKSTA VKALTGGIAH LFKQNKVIHV NGYGKITGKN QVTATKVDGG TQVVDTKNIL 190 200 210 220 230 240 IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT 250 260 270 280 290 300 AVEFLGHVGG IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK 310 320 330 340 350 360 AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP 370 380 390 400 410 420 MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK 430 440 450 460 470 480 FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI 490 500 ARVCHAHPTL SEAFREANLA ASFGKSINF

References

[1]	"Isolation and characterization of cDNA for macaque neurological disease genes." Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Frontal cortex.
[2]	"DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications." International consortium for macaque cDNA sequencing and analysis Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB125164 mRNA. Translation: BAD51952.1. AB168328 mRNA. Translation: BAE00452.1.
3D structure databases
SMR	Q60HG3. Positions 40-509.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q60HG3.
Enzyme and pathway databases
BRENDA	1.8.1.4. 3438.
Family and domain databases
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. 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.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DLDH_MACFA

Accession

Primary (citable) accession number: Q60HG3
Secondary accession number(s): Q4R8W9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	November 23, 2004
Last modified:	February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)