ODPX_SCHPO
ID ODPX_SCHPO Reviewed; 456 AA.
AC O94709; P78909;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable pyruvate dehydrogenase protein X component, mitochondrial;
DE AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex;
DE Flags: Precursor;
GN ORFNames=SPCC1259.09c;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-456.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
CC -!- FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to
CC the dihydrolipoamide transacetylase (E2) core of the pyruvate
CC dehydrogenase complexes of eukaryotes. This specific binding is
CC essential for a functional PDH complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13921.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329672; CAA22547.1; -; Genomic_DNA.
DR EMBL; D89260; BAA13921.1; ALT_SEQ; mRNA.
DR PIR; T40898; T40898.
DR RefSeq; NP_588065.1; NM_001023057.2.
DR AlphaFoldDB; O94709; -.
DR BioGRID; 275653; 11.
DR STRING; 4896.SPCC1259.09c.1; -.
DR MaxQB; O94709; -.
DR PaxDb; O94709; -.
DR PRIDE; O94709; -.
DR EnsemblFungi; SPCC1259.09c.1; SPCC1259.09c.1:pep; SPCC1259.09c.
DR GeneID; 2539081; -.
DR KEGG; spo:SPCC1259.09c; -.
DR PomBase; SPCC1259.09c; -.
DR VEuPathDB; FungiDB:SPCC1259.09c; -.
DR eggNOG; KOG0557; Eukaryota.
DR HOGENOM; CLU_035825_2_1_1; -.
DR InParanoid; O94709; -.
DR OMA; CMPALSP; -.
DR PhylomeDB; O94709; -.
DR PRO; PR:O94709; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:PomBase.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; PTHR23151; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 2: Evidence at transcript level;
KW Lipoyl; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..456
FT /note="Probable pyruvate dehydrogenase protein X component,
FT mitochondrial"
FT /id="PRO_0000020486"
FT DOMAIN 35..110
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 168..206
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 123..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 175
FT /note="Y -> N (in Ref. 2; BAA13921)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="H -> D (in Ref. 2; BAA13921)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="I -> M (in Ref. 2; BAA13921)"
FT /evidence="ECO:0000305"
FT CONFLICT 345..347
FT /note="KNN -> NNK (in Ref. 2; BAA13921)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="I -> F (in Ref. 2; BAA13921)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="S -> R (in Ref. 2; BAA13921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 50884 MW; 40C1AD24240E1116 CRC64;
MLKHYIHQCV KASSCKHSLS VKQRYFHCSA LNGVASMFRM PALSPTMEEG NITKWHFKEG
DSFKSGDILL EVETDKATMD VEVQDNGILA KVLIEKGSNI PVGKNIAIVA DAEDNLKDLE
LPKDEASSEE QSFSSSKEEV KPIVQDRETK SNVEHKSTSQ ANDAVNKSFL PSVSYLIHQY
KIENPWSIPA TGPHGRLLKG DVLAHVGKID KGVPSSLQKF VRNLEVLDFS GVEPKKPSYT
EDSVPVRKST MIETLKTVPM KDEYITFERS ISLEKLKSLL AKRKEKDAFG IDEVVSAMIG
DALSISELSK VEPNSIESAY DLLLGAPIVK LKSSVSNFQP KLFPKNNNTK DLHKYIRDSM
IGLPSNLSDY VKLNFSSVTK SSSNNVEFLD DVYDMLLGSN SDSIDSRINR HEEPSTTEDL
TLTLSIKDNI SKSRAIKFVD CLKSNFENPE FVLSRW
