DLDH_SCHPO
ID DLDH_SCHPO Reviewed; 511 AA.
AC O00087; Q9US50;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE Short=DLDH;
DE Flags: Precursor;
GN Name=dld1; ORFNames=SPAC1002.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9366254; DOI=10.1016/s0167-4889(97)00078-5;
RA Jang Y.-J., Chung K.-S., Park C., Yoo H.-S.;
RT "Fission yeast dihydrolipoamide dehydrogenase gene is involved in G1/S cell
RT cycle progression.";
RL Biochim. Biophys. Acta 1358:229-239(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid
CC dehydrogenase complexes (By similarity). Malfunction of this protein
CC blocks the progression of cell cycle from G1 to S phase. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; L40360; AAB97089.1; -; mRNA.
DR EMBL; CU329670; CAB65609.1; -; Genomic_DNA.
DR PIR; T43405; T43405.
DR RefSeq; NP_593496.1; NM_001018930.2.
DR AlphaFoldDB; O00087; -.
DR SMR; O00087; -.
DR BioGRID; 279697; 2.
DR STRING; 4896.SPAC1002.09c.1; -.
DR iPTMnet; O00087; -.
DR MaxQB; O00087; -.
DR PaxDb; O00087; -.
DR PRIDE; O00087; -.
DR EnsemblFungi; SPAC1002.09c.1; SPAC1002.09c.1:pep; SPAC1002.09c.
DR GeneID; 2543269; -.
DR KEGG; spo:SPAC1002.09c; -.
DR PomBase; SPAC1002.09c; dld1.
DR VEuPathDB; FungiDB:SPAC1002.09c; -.
DR eggNOG; KOG1335; Eukaryota.
DR HOGENOM; CLU_016755_0_1_1; -.
DR InParanoid; O00087; -.
DR OMA; DAKYGEW; -.
DR PhylomeDB; O00087; -.
DR Reactome; R-SPO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SPO-5362517; Signaling by Retinoic Acid.
DR Reactome; R-SPO-6783984; Glycine degradation.
DR Reactome; R-SPO-70268; Pyruvate metabolism.
DR Reactome; R-SPO-71064; Lysine catabolism.
DR Reactome; R-SPO-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:O00087; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005960; C:glycine cleavage complex; ISO:PomBase.
DR GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IC:PomBase.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; ISO:PomBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISO:PomBase.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISO:PomBase.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IC:PomBase.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; ISO:PomBase.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..511
FT /note="Dihydrolipoyl dehydrogenase, mitochondrial"
FT /id="PRO_0000030300"
FT ACT_SITE 489
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 75..84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 187..189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 224..231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 363..366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 84..89
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 210..216
FT /note="ALSLSEV -> GPYLYQRY (in Ref. 1; AAB97089)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="T -> R (in Ref. 1; AAB97089)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="L -> V (in Ref. 1; AAB97089)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="P -> G (in Ref. 1; AAB97089)"
FT /evidence="ECO:0000305"
SQ 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
