Reviewed, UniProtKB/Swiss-Prot Q8CIZ7 (DLDH_CRIGR)

Names and origin

Protein names

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

Gene names

Name:

DLD

Organism

Cricetulus griseus (Chinese hamster)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

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_0000260226
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
	Disulfide bond	80 ↔ 85		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8CIZ7-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: FADBCF01E42576AB	FASTA	509	54,131
	10 20 30 40 50 60 MQSWSRVYCS LAKRGHFNRI SHGLQGVSSV PLRTYADQPI DADVTVIGSG PGGYVAAIKA 70 80 90 100 110 120 AQLGFKTVCI EKNDTLGGTC LNVGCIPSKA LLNNSHYYHL AHGRDFASRG IELSEVRLNL 130 140 150 160 170 180 EKMMEQKSSA VKALIGGIAH LFKQNKVVHV NGFGKITGKN QVTATKADGS SQVIGTKNIL 190 200 210 220 230 240 IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKLVVIG AGVIGVELGS VWQRLGADVT 250 260 270 280 290 300 AVEFLGHVGG IGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKRSDGKID VSVEAASGGK 310 320 330 340 350 360 AEVITCDVLL VCIGRRPFTQ 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 ASFGKPINF

References

[1]	"2D gel analysis of the proteomic adaptation of a mammalian cell line to oxidative stress reveals changes in the expression of metabolically relevant enzymes." Keightley J.A., Shang L., Kinter M. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF539836 mRNA. Translation: AAN15202.1.
3D structure databases
HSSP	HSSP built from PDB template 1DXL based on UniProtKB P31023.
SMR	Q8CIZ7. Positions 37-509.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q8CIZ7.
Enzyme and pathway databases
BRENDA	1.8.1.4. 18.
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_CRIGR

Accession

Primary (citable) accession number: Q8CIZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)