O00087 (DLDH_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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 (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

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 Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred by curator. Source: PomBase G1/S transition of mitotic cell cycle Inferred from mutant phenotype Ref.1. Source: PomBase L-serine biosynthetic process Inferred from sequence orthology. Source: PomBase acetyl-CoA biosynthetic process from pyruvate Inferred from sequence orthology. Source: PomBase cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycine decarboxylation via glycine cleavage system Inferred from sequence orthology. Source: PomBase isoleucine catabolic process Inferred from sequence orthology. Source: PomBase leucine catabolic process Inferred from sequence orthology. Source: PomBase valine catabolic process Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	glycine cleavage complex Inferred from sequence orthology. Source: PomBase mitochondrial nucleoid Inferred from sequence or structural similarity. Source: PomBase mitochondrial oxoglutarate dehydrogenase complex Inferred by curator. Source: PomBase mitochondrial pyruvate dehydrogenase complex Inferred from sequence or structural similarity. Source: PomBase
Molecular_function	dihydrolipoyl dehydrogenase activity Inferred from sequence or structural similarity. Source: PomBase disulfide oxidoreductase activity Inferred from sequence model. Source: PomBase flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro pyruvate dehydrogenase (acetyl-transferring) activity Inferred from sequence orthology. Source: PomBase
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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 972 / ATCC 24843.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L40360 mRNA. Translation: AAB97089.1. CU329670 Genomic DNA. Translation: CAB65609.1.
PIR	T43405.
RefSeq	NP_593496.1. NM_001018930.2.
3D structure databases
ProteinModelPortal	O00087.
SMR	O00087. Positions 43-510.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4666396.
STRING	4896.SPAC1002.09c-1.
Proteomic databases
PaxDb	O00087.
PRIDE	O00087.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC1002.09c.1; SPAC1002.09c.1:pep; SPAC1002.09c.
GeneID	2543269.
KEGG	spo:SPAC1002.09c.
Organism-specific databases
PomBase	SPAC1002.09c.
Phylogenomic databases
eggNOG	COG1249.
HOGENOM	HOG000276708.
KO	K00382.
OMA	GFEKQMS.
OrthoDB	EOG43FM59.
Family and domain databases
Gene3D	3.30.390.30. 1 hit.
InterPro	IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006258. Lipoamide_DH. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view]
PANTHER	PTHR22912:SF20. PTHR22912:SF20. 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.
SUPFAM	SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMs	TIGR01350. lipoamide_DH. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20804290.

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:	May 29, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program