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Database: UniProt
Entry: A0A059KQG0_9BURK
LinkDB: A0A059KQG0_9BURK
Original site: A0A059KQG0_9BURK 
ID   A0A059KQG0_9BURK        Unreviewed;       562 AA.
AC   A0A059KQG0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   08-MAY-2019, entry version 31.
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=X805_07760 {ECO:0000313|EMBL:KDB53590.1};
OS   Sphaerotilus natans subsp. natans DSM 6575.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilus.
OX   NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB53590.1, ECO:0000313|Proteomes:UP000026714};
RN   [1] {ECO:0000313|EMBL:KDB53590.1, ECO:0000313|Proteomes:UP000026714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB53590.1,
RC   ECO:0000313|Proteomes:UP000026714};
RX   PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA   Park S., Kim D.H., Lee J.H., Hur H.G.;
RT   "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide
RT   minerals formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL   FEMS Microbiol. Ecol. 90:68-77(2014).
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   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {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:KDB53590.1}.
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DR   EMBL; AZRA01000021; KDB53590.1; -; Genomic_DNA.
DR   RefSeq; WP_037478409.1; NZ_AZRA01000021.1.
DR   STRING; 1286631.X805_07760; -.
DR   EnsemblBacteria; KDB53590; KDB53590; X805_07760.
DR   PATRIC; fig|1286631.3.peg.765; -.
DR   OrthoDB; 1626282at2; -.
DR   Proteomes; UP000026714; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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; IPR006256; AcTrfase_Pyrv_DH_cplx.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178:SF2; PTHR43178:SF2; 3.
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; TIGR01348; PDHac_trf_long; 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:UP000026714};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:KDB53590.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026714};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:KDB53590.1}.
FT   DOMAIN        3     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      120    194       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      252    289       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   562 AA;  57572 MW;  495E4A110AEBC946 CRC64;
     MALIEVKVPD IGDFKEVTII EVLVKAGDTI KAEQSLITVE SDKASMEIPS SHAGVIKELK
     VALGDKVAEG SLVLLLEVAG AAAAPAPVAA APAPAPVAAP APAPVAAAPA APAAVAAAGP
     IEVVVPDIGD FDAVAVIELL VKVGDTVKAE QSLITVESDK ASMEIPSSHA GVIKELKVKL
     GDKVSKGSLV AILEGAAGAV AAPAPAAVAP AAAPVAAPAA APAPAAAAPA AAAPVAAVPA
     HDPTAPALNL PHASPSMRKF ARELGVPLAE VKGSGPKGRI TEADIQGFVK GVMAGAVQTA
     AQKAAAPAPA AAAAAGGAFP GLLPWPKVDF AKFGPIERKD LSRIKKISGA NLHRNWVVIP
     HVTNHDDADI TELEAFRVQT NKENEKSGVK VTMLAFMIKA AVAALKKFPE FNSSLDGDQL
     VLKNYFHIGF AADTPNGLVV PVIKDCDKKG IFQISQEMGE LAKKARDGKL GPADMSGACF
     TISSLGGIGG RYFTPIINAP EVAIMGVCKS QIEPKWDGKQ FQPRLMLPLS LSWDHRVIDG
     AAAARFNVYF ASLLADFRRI VL
//
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