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Database: UniProt
Entry: A0A254VHM4_9BURK
LinkDB: A0A254VHM4_9BURK
Original site: A0A254VHM4_9BURK 
ID   A0A254VHM4_9BURK        Unreviewed;       537 AA.
AC   A0A254VHM4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 7.
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=aceF {ECO:0000313|EMBL:OWY38288.1};
GN   ORFNames=CEK28_13550 {ECO:0000313|EMBL:OWY38288.1};
OS   Xenophilus sp. AP218F.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Xenophilus.
OX   NCBI_TaxID=2014876 {ECO:0000313|EMBL:OWY38288.1, ECO:0000313|Proteomes:UP000197405};
RN   [1] {ECO:0000313|EMBL:OWY38288.1, ECO:0000313|Proteomes:UP000197405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP218F {ECO:0000313|EMBL:OWY38288.1,
RC   ECO:0000313|Proteomes:UP000197405};
RA   Lebert B.M., Sanford S., Reisinger L., Forsman A.M., Savage A.E.;
RT   "A novel Xenophilus sp. bacterium isolated from a southern leopard
RT   frog (Rana sphenocephala) in Florida, USA.";
RL   Submitted (JUN-2017) 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   -!- 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:OWY38288.1}.
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DR   EMBL; NJIE01000024; OWY38288.1; -; Genomic_DNA.
DR   Proteomes; UP000197405; 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:UP000197405};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197405};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:OWY38288.1}.
FT   DOMAIN        4     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      111    185       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      235    272       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   537 AA;  55276 MW;  707C559CCF33BEF4 CRC64;
     MSNLIELKVP DIGGHSNVDI IEVFIAPGQT VSVDDSLITL ETDKATMEVP AEAAGVVKEV
     KAVVGGKISE GDVIAIIEVG AAASAPAPAA AVPAPAPAVA APAAAPAASG RSEIRVPDIG
     GHNGVDVIEV AVKVGDDIAI DDSLITLETD KATMEVPASA AGRVVEVKVK VGDKVSEGDL
     IVVVEGAAVA AAPVAAAQAP APAAPAPVAA APAAAPVAAQ AASVAIDEAA FSKAHAGPSV
     RRLARELGVD LGKVKGNGRK GRITEDDVKA FVKGVLQNPA GLAQAAAPAG SGVGLDLLPW
     PKVDFAKFGP IETKPLSRIQ KISGANLSRN WVMIPHVTFN DECDITELED FRKTVGKEWE
     KSGLKISPLA FIIKAAAEAL KAFPTFNSSL DGDNLVLKQY YHIGFAADTP NGLVVPVIKD
     ADKKGLRQIA QELTDLSKLA REGKLKPTDM QGATFTISSL GGIGGTSFTP IVNAPEVAIL
     GVCKSQIKPV WNGKEFAPRL MCPLSLSFDH RVIDGAAAAR FTVHLGKLLS DVRRLIL
//
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