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Database: UniProt
Entry: A0A091CP27_FUKDA
LinkDB: A0A091CP27_FUKDA
Original site: A0A091CP27_FUKDA 
ID   A0A091CP27_FUKDA        Unreviewed;       653 AA.
AC   A0A091CP27;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   05-JUN-2019, entry version 24.
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=H920_17902 {ECO:0000313|EMBL:KFO20739.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Bathyergidae; Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO20739.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO20739.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO20739.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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 2 lipoyl cofactors 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}.
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DR   EMBL; KN124601; KFO20739.1; -; Genomic_DNA.
DR   RefSeq; XP_010609006.1; XM_010610704.2.
DR   STRING; 885580.XP_010609006.1; -.
DR   GeneID; 104852878; -.
DR   CTD; 1737; -.
DR   OrthoDB; 747232at2759; -.
DR   Proteomes; UP000028990; 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; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028990};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137};
KW   Pyruvate {ECO:0000313|EMBL:KFO20739.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:KFO20739.1}.
FT   DOMAIN       92    168       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      222    298       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      362    399       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION      186    217       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A091CP27}.
SQ   SEQUENCE   653 AA;  69420 MW;  60C35557601B573D CRC64;
     MWRVCARRAQ RAAPGTGLRA RWTALREGPG APCVSLRAGR APARSNSTTI PGYGGVRALC
     GWSTSSGATP RNRLLQQLLG SPGRRCYSLP PHQKVPLPSL SPTMQAGTIA RWEKKEGEKI
     NEGDLIAEVE TDKATVGFES VEECYMAKIL VAEGTRDVPV GAIICITVGK PEDIEAFKNY
     TLDSTAAPTP QAAPAPTVAP TTAASTPVPS SAQAPGSSYP THMQVLLPAL SPTMTMGTVQ
     RWEKKVGEKL SEGDLLAEIE TDKATIGFEV QEEGYLAKIL VPEGTRDVPL GTPLCIIVEK
     EADIAAFADY RPTEVTDLKP QAPPPTQPLV ATVPPTPQPV TPMPSGTPAA LATPVGPRGR
     VFVSPLAKKL AAEKGIDLTQ VKGTGPDGRI IKKDIDSFVP TKAAPAPAVA VPPPSPGMAP
     VPTGVFTDIP ISNIRRVIAQ RLMQSKQTIP HYYLSIDVNM GEVLLVRKEL NKMLEGKSKI
     SVNDFIIKAS ALACLKVPEA NSSWLDTVIR QNHVVDVSVA VSTPAGLITP IVFNAHIKGL
     ESIANDVVSL AAKAREGKLQ PHEFQGGTFT ISNLGMFGIK NFSAIINPPQ ACILAIGASE
     DKLVPADNEK GFDVVSMMSV TLSCDHRVVD GAVGAQWLAE FRKYLEKPIT MLL
//
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