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Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (DLDH)

 DLDH_SCHPO              Reviewed;         511 AA.
O00087; Q9US50;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
25-OCT-2017, entry version 157.
RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
Short=DLDH;
Flags: Precursor;
Name=dld1; ORFNames=SPAC1002.09c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=972 / ATCC 24843;
PubMed=9366254; DOI=10.1016/S0167-4889(97)00078-5;
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=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
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).
-!- 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. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L40360; AAB97089.1; -; mRNA.
EMBL; CU329670; CAB65609.1; -; Genomic_DNA.
PIR; T43405; T43405.
RefSeq; NP_593496.1; NM_001018930.2.
ProteinModelPortal; O00087; -.
SMR; O00087; -.
MINT; MINT-4666396; -.
STRING; 4896.SPAC1002.09c.1; -.
iPTMnet; O00087; -.
MaxQB; O00087; -.
PRIDE; O00087; -.
EnsemblFungi; SPAC1002.09c.1; SPAC1002.09c.1:pep; SPAC1002.09c.
GeneID; 2543269; -.
KEGG; spo:SPAC1002.09c; -.
EuPathDB; FungiDB:SPAC1002.09c; -.
PomBase; SPAC1002.09c; dld1.
HOGENOM; HOG000276708; -.
InParanoid; O00087; -.
KO; K00382; -.
OMA; TMSEAVM; -.
OrthoDB; EOG092C1XBY; -.
PhylomeDB; O00087; -.
Reactome; R-SPO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-SPO-5362517; Signaling by Retinoic Acid.
Reactome; R-SPO-6783984; Glycine degradation.
Reactome; R-SPO-70268; Pyruvate metabolism.
Reactome; R-SPO-71064; Lysine catabolism.
Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
PRO; PR:O00087; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005960; C:glycine cleavage complex; ISO:PomBase.
GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IC:PomBase.
GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISS:PomBase.
GO; GO:0005739; C:mitochondrion; IDA:PomBase.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; ISS:PomBase.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISO:PomBase.
GO; GO:0006103; P:2-oxoglutarate metabolic process; IC:PomBase.
GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISO:PomBase.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; ISO:PomBase.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; FAD; Flavoprotein; Mitochondrion;
NAD; Oxidoreductase; Redox-active center; Reference proteome;
Transit peptide.
TRANSIT 1 ? Mitochondrion.
CHAIN ? 511 Dihydrolipoyl dehydrogenase,
mitochondrial.
/FTId=PRO_0000030300.
NP_BIND 75 84 FAD. {ECO:0000250}.
NP_BIND 187 189 FAD. {ECO:0000250}.
NP_BIND 224 231 NAD. {ECO:0000250}.
NP_BIND 363 366 FAD. {ECO:0000250}.
ACT_SITE 489 489 Proton acceptor. {ECO:0000250}.
BINDING 93 93 FAD. {ECO:0000250}.
BINDING 157 157 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 247 247 NAD. {ECO:0000250}.
BINDING 281 281 NAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 316 316 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 357 357 FAD. {ECO:0000250}.
DISULFID 84 89 Redox-active. {ECO:0000250}.
CONFLICT 210 216 ALSLSEV -> GPYLYQRY (in Ref. 1;
AAB97089). {ECO:0000305}.
CONFLICT 277 277 T -> R (in Ref. 1; AAB97089).
{ECO:0000305}.
CONFLICT 282 282 L -> V (in Ref. 1; AAB97089).
{ECO:0000305}.
CONFLICT 424 424 P -> G (in Ref. 1; AAB97089).
{ECO:0000305}.
SEQUENCE 511 AA; 54731 MW; E68350146A93AD56 CRC64;
MLNSVIKRSA LCRFKFTCLQ VSECRPAQIE ISKRLYSAKA SGNGEYDLCV IGGGPGGYVA
AIRGAQLGLK TICVEKRGTL GGTCLNVGCI PSKALLNNSH IYHTVKHDTK RRGIDVSGVS
VNLSQMMKAK DDSVKSLTSG IEYLFKKNKV EYAKGTGSFI DPQTLSVKGI DGAADQTIKA
KNFIIATGSE VKPFPGVTID EKKIVSSTGA LSLSEVPKKM TVLGGGIIGL EMGSVWSRLG
AEVTVVEFLP AVGGPMDADI SKALSRIISK QGIKFKTSTK LLSAKVNGDS VEVEIENMKN
NKRETYQTDV LLVAIGRVPY TEGLGLDKLG ISMDKSNRVI MDSEYRTNIP HIRVIGDATL
GPMLAHKAED EGIAAVEYIA KGQGHVNYNC IPAVMYTHPE VAWVGITEQK AKESGIKYRI
GTFPFSANSR AKTNMDADGL VKVIVDAETD RLLGVHMIGP MAGELIGEAT LALEYGASAE
DVARVCHAHP TLSEATKEAM MAAWCGKSIH F


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