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UniProtKB/Swiss-Prot entry O00087


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DLDH_SCHPO
Primary accession number O00087
Secondary accession number Q9US50
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on February 21, 2001 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 82)
Name and origin of the protein
Protein name Dihydrolipoyl dehydrogenase, mitochondrial [Precursor]
Synonyms EC 1.8.1.4
Dihydrolipoamide dehydrogenase
DLDH
Gene name
Name: dld1
ORFNames: SPAC1002.09c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1016/S0167-4889(97)00078-5; PubMed=9366254 [NCBI, ExPASy, EBI, Israel, Japan]
Jang Y.-J., Chung K.-S., Park C., Yoo H.-S.;
"Fission yeast dihydrolipoamide dehydrogenase gene is involved in G1/S cell cycle progression.";
Biochim. Biophys. Acta 1358:229-239(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L40360; AAB97089.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAB65609.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T43405; T43405.
RefSeq NP_593496.1; -.
3D structure databases
HSSP P09624; 1JEH. [HSSP ENTRY / PDB]
ModBase O00087.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-001178-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC1002.09c; -.
Gene expression databases
ArrayExpress O00087; -.
Ontologies
GO
GO:0009353; Cellular component: mitochondrial oxoglutarate dehydrogenase complex (inferred by curator from GeneDB_SPombe).
GO:0004148; Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006103; Biological process: 2-oxoglutarate metabolic process (inferred by curator from GeneDB_SPombe).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR006258; Lipoamide_DHase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
PANTHER PTHR22912:SF20; Lipoamide_DH; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01350; lipoamide_DH; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
Genome annotation databases
GeneID 2543269; -.
KEGG spo:SPAC1002.09c; -.
NMPDR fig|4896.1.peg.3466; -.
Other
ProtoNet O00087.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Mitochondrion. 
CHAIN   ?   511        Dihydrolipoyl dehydrogenase, mitochondrial. PRO_0000030300
NP_BIND   75    84  10     FAD (By similarity). 
NP_BIND   187   189  3     FAD (By similarity). 
NP_BIND   224   231  8     NAD (By similarity). 
NP_BIND   363   366  4     FAD (By similarity). 
ACT_SITE   489   489        Proton acceptor (By similarity). 
BINDING   93    93        FAD (By similarity). 
BINDING   157   157        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   247   247        NAD (By similarity). 
BINDING   281   281        NAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   316   316        NAD; via amide nitrogen (By similarity). 
BINDING   357   357        FAD (By similarity). 
DISULFID   84    89        Redox-active (By similarity). 
CONFLICT   210   216        ALSLSEV -> GPYLYQRY (in Ref. 1; AAB97089). 
CONFLICT   277   277        T -> R (in Ref. 1; AAB97089). 
CONFLICT   282   282        L -> V (in Ref. 1; AAB97089). 
CONFLICT   424   424        P -> G (in Ref. 1; AAB97089). 
Sequence information
Length: 511 AA [This is the length of the unprocessed precursor] Molecular weight: 54731 Da [This is the MW of the unprocessed precursor] CRC64: E68350146A93AD56 [This is a checksum on the sequence]
        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 

O00087 in FASTA format

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