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Database: UniProt
Entry: H0GMM0_SACCK
LinkDB: H0GMM0_SACCK
Original site: H0GMM0_SACCK 
ID   H0GMM0_SACCK            Unreviewed;       437 AA.
AC   H0GMM0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   05-JUN-2019, entry version 36.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   ORFNames=VIN7_4175 {ECO:0000313|EMBL:EHN04866.1};
OS   Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS   (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN04866.1, ECO:0000313|Proteomes:UP000009009};
RN   [1] {ECO:0000313|EMBL:EHN04866.1, ECO:0000313|Proteomes:UP000009009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN7 {ECO:0000313|EMBL:EHN04866.1,
RC   ECO:0000313|Proteomes:UP000009009};
RX   PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "The genome sequence of the wine yeast VIN7 reveals an allotriploid
RT   hybrid genome with Saccharomyces cerevisiae and Saccharomyces
RT   kudriavzevii origins.";
RL   FEMS Yeast Res. 12:88-96(2012).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA =
CC         (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHN04866.1}.
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DR   EMBL; AGVY01000045; EHN04866.1; -; Genomic_DNA.
DR   EnsemblFungi; EHN04866; EHN04866; VIN7_4175.
DR   PhylomeDB; H0GMM0; -.
DR   Proteomes; UP000009009; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009009};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137};
KW   Transferase {ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN        1     65       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      130    167       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       75    125       Disordered. {ECO:0000256|MobiDB-lite:
FT                                H0GMM0}.
FT   REGION      169    206       Disordered. {ECO:0000256|MobiDB-lite:
FT                                H0GMM0}.
FT   COMPBIAS     97    116       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                H0GMM0}.
SQ   SEQUENCE   437 AA;  46784 MW;  5E83C2E5AF0BD017 CRC64;
     MTQGNLAAWT KKEGDQLSPG EVIAEIETDK AQMDFEFQED GYLAKILVPE GTKDIPVNKP
     IAVYVEDKAD VPAFKDFKLE DSGSDSKTST KAQPAEPQAE KKQEAPAEET KTSAPEAKKS
     DVAAPQGRIF ASPLAKTIAL EKGISLKDVH GTGPRGRITK ADIESYLEKS SKQSSQTSGA
     AAATPAAATS XTTAGSAPSP SSTASYEDVP ISTMRSIIGE RLLQSTQGIP SYIVSSKISV
     SKLLKLRQSL NATANDKYKL SINDLLVKAI TVAAKRVPDA NAYWLPNENV IRKFKNVDVS
     VAVATPTGLL TPIVKNCEAK GLSQISNEIK ELVKRARINK LAPEEFQGGT ICISNMGMNN
     AVNMFTSIIN PPQSTILAIA TVERVAVEDA AAENGFSFDN QVTITGTFDH RTIDGAKGAE
     FMKELKTVIE NPLEMLL
//
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