Reviewed, UniProtKB/Swiss-Prot O00087 (DLDH_SCHPO)

Names and origin

Protein names

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

Gene names

Name:	dld1
ORF Names:	SPAC1002.09c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	511 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 alpha-ketoacid dehydrogenase complexes By similarity. Malfunction of this protein blocks the progression of cell cycle from G1 to S phase.
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	Mitochondrion matrix 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
Cellular component	Mitochondrion
Domain	Redox-active center Transit peptide
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	2-oxoglutarate metabolic process Inferred by curator. Source: GeneDB_SPombe cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial oxoglutarate dehydrogenase complex Inferred by curator. Source: GeneDB_SPombe
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 – ?		Mitochondrion
	Chain	? – 511		Dihydrolipoyl dehydrogenase, mitochondrial		PRO_0000030300
Regions
	Nucleotide binding	75 – 84	10	FAD By similarity
	Nucleotide binding	187 – 189	3	FAD By similarity
	Nucleotide binding	224 – 231	8	NAD By similarity
	Nucleotide binding	363 – 366	4	FAD By similarity
Sites
	Active site	489	1	Proton acceptor By similarity
	Binding site	93	1	FAD By similarity
	Binding site	157	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	247	1	NAD By similarity
	Binding site	281	1	NAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	316	1	NAD; via amide nitrogen By similarity
	Binding site	357	1	FAD By similarity
Amino acid modifications
	Disulfide bond	84 ↔ 89		Redox-active By similarity
Experimental info
	Sequence conflict	210 – 216	7	ALSLSEV → GPYLYQRY in AAB97089. Ref.1
	Sequence conflict	277	1	T → R in AAB97089. Ref.1
	Sequence conflict	282	1	L → V in AAB97089. Ref.1
	Sequence conflict	424	1	P → G in AAB97089. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O00087-1 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: E68350146A93AD56	FASTA	511	54,731
	10 20 30 40 50 60 MLNSVIKRSA LCRFKFTCLQ VSECRPAQIE ISKRLYSAKA SGNGEYDLCV IGGGPGGYVA 70 80 90 100 110 120 AIRGAQLGLK TICVEKRGTL GGTCLNVGCI PSKALLNNSH IYHTVKHDTK RRGIDVSGVS 130 140 150 160 170 180 VNLSQMMKAK DDSVKSLTSG IEYLFKKNKV EYAKGTGSFI DPQTLSVKGI DGAADQTIKA 190 200 210 220 230 240 KNFIIATGSE VKPFPGVTID EKKIVSSTGA LSLSEVPKKM TVLGGGIIGL EMGSVWSRLG 250 260 270 280 290 300 AEVTVVEFLP AVGGPMDADI SKALSRIISK QGIKFKTSTK LLSAKVNGDS VEVEIENMKN 310 320 330 340 350 360 NKRETYQTDV LLVAIGRVPY TEGLGLDKLG ISMDKSNRVI MDSEYRTNIP HIRVIGDATL 370 380 390 400 410 420 GPMLAHKAED EGIAAVEYIA KGQGHVNYNC IPAVMYTHPE VAWVGITEQK AKESGIKYRI 430 440 450 460 470 480 GTFPFSANSR AKTNMDADGL VKVIVDAETD RLLGVHMIGP MAGELIGEAT LALEYGASAE 490 500 510 DVARVCHAHP TLSEATKEAM MAAWCGKSIH F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fission yeast dihydrolipoamide dehydrogenase gene is involved in G1/S cell cycle progression." Jang Y.-J., Chung K.-S., Park C., Yoo H.-S. Biochim. Biophys. Acta 1358:229-239(1997) [PubMed: 9366254] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ATCC 38366 / 972.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L40360 mRNA. Translation: AAB97089.1. CU329670 Genomic DNA. Translation: CAB65609.1.
PIR	T43405.
RefSeq	NP_593496.1.
3D structure databases
SMR	O00087. Positions 43-510.
ModBase	Search...
Protein-protein interaction databases
STRING	O00087.
Genome annotation databases
GeneID	2543269.
GenomeReviews	Gene locus dld1 in contig CU329670_GR.
KEGG	spo:SPAC1002.09c.
NMPDR	fig|4896.1.peg.3466.
Organism-specific databases
GeneDB_Spombe	SPAC1002.09c.
Phylogenomic databases
eggNOG	fuNOG07682.
HOGENOM	HBG515043.
OMA	FNRISHG.
OrthoDB	EOG900329.
PhylomeDB	O00087.
Enzyme and pathway databases
BRENDA	1.8.1.4. 653.
Gene expression databases
ArrayExpress	O00087.
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_SCHPO

Accession

Primary (citable) accession number: O00087
Secondary accession number(s): Q9US50

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 21, 2001
Last modified:	February 9, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)