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Database: UniProt
Entry: A0A0N0D9P2_9RHOB
LinkDB: A0A0N0D9P2_9RHOB
Original site: A0A0N0D9P2_9RHOB 
ID   A0A0N0D9P2_9RHOB        Unreviewed;       437 AA.
AC   A0A0N0D9P2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   05-JUN-2019, entry version 15.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   Name=pdhC {ECO:0000313|EMBL:KPA22804.1};
GN   ORFNames=shim_10920 {ECO:0000313|EMBL:KPA22804.1};
OS   Shimia sp. SK013.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae.
OX   NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA22804.1, ECO:0000313|Proteomes:UP000037951};
RN   [1] {ECO:0000313|EMBL:KPA22804.1, ECO:0000313|Proteomes:UP000037951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK013 {ECO:0000313|EMBL:KPA22804.1,
RC   ECO:0000313|Proteomes:UP000037951};
RA   Voget S., Kanukollu S., Daniel R., Engelen B.;
RT   "Genome Sequence of Shimia sp. SK013.";
RL   Submitted (MAR-2015) 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 1 lipoyl cofactor covalently.
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:KPA22804.1}.
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DR   EMBL; LAJH01000009; KPA22804.1; -; Genomic_DNA.
DR   RefSeq; WP_054001552.1; NZ_LAJH01000009.1.
DR   EnsemblBacteria; KPA22804; KPA22804; shim_10920.
DR   PATRIC; fig|1389006.3.peg.1119; -.
DR   OrthoDB; 1626282at2; -.
DR   Proteomes; UP000037951; Unassembled WGS sequence.
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   ECO:0000313|EMBL:KPA22804.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037951};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:KPA22804.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037951};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:KPA22804.1}.
FT   DOMAIN        2     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      132    169       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       86    126       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0N0D9P2}.
SQ   SEQUENCE   437 AA;  45237 MW;  D4CAA0D004EDD59A CRC64;
     MPTEILMPAL SPTMEEGTLA KWLVKEGDEI SSGDLIAEIE TDKATMEFEA VDEGVIGKIL
     VAEGSEGVAV NSPIAVLLTD GETADDIGAT PTTAPQAAPA ADSGKEAAPA GGSDAPAPAP
     SAPMSADGAR IFASPLARRI AADKGIDLAL VTGSGPRGRI VKADVEGTTA SSPAVQMKPV
     PSGAASAQAA ALASGPATDT VLRMYEDRET EEVALDGMRK TIAARLTEAK QSIPHFYLRR
     DIQLDALLSF RAQLNGQLEK RGVKLSVNDF IIKACALALQ QVPESNAVWA NDRILRLKPS
     DVAVAVAIEG GLFTPVIRDS DAKSLSTLSA EMKDLAARAR DRKLAPHEYQ GGSFAISNLG
     MFGIDNFDAV INPPHGAILA VGAGAKKPVV GEGGQIEVAT VMSVTLSVDH RVIDGALGAQ
     LLQAIVDNLE NPMAMLA
//
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