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Entry: A0A2G8T851_9BURK
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ID   A0A2G8T851_9BURK        Unreviewed;       466 AA.
AC   A0A2G8T851;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
DE   Flags: Fragment;
GN   Name=aceF {ECO:0000313|EMBL:PIL42237.1};
GN   ORFNames=CR105_25200 {ECO:0000313|EMBL:PIL42237.1};
OS   Massilia eurypsychrophila.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1485217 {ECO:0000313|EMBL:PIL42237.1, ECO:0000313|Proteomes:UP000230390};
RN   [1] {ECO:0000313|EMBL:PIL42237.1, ECO:0000313|Proteomes:UP000230390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 30074 {ECO:0000313|EMBL:PIL42237.1,
RC   ECO:0000313|Proteomes:UP000230390};
RA   Wang H.;
RT   "Massilia psychrophilum sp. nov., a novel purple-pigmented bacterium
RT   isolated from Tianshan glacier, Xinjiang Municipality, China.";
RL   Submitted (OCT-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). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00000925,
CC         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   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|ARBA:ARBA00011484,
CC       ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIL42237.1}.
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DR   EMBL; PDOC01000031; PIL42237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8T851; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000230390; 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   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 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   NCBIfam; TIGR01348; PDHac_trf_long; 1.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230390};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:PIL42237.1}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..466
FT                   /note="Acetyltransferase component of pyruvate
FT                   dehydrogenase complex"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013715154"
FT   DOMAIN          33..107
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          159..196
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PIL42237.1"
SQ   SEQUENCE   466 AA;  47082 MW;  A43AAA5BC16F11E6 CRC64;
     APAPAAAAAA AAAAAAAAAA PAAAPAAAGA TSTVEVKVPD IGDFKEVEVI DLMVKPGDTI
     KVDQSLITVE SDKASMEIPS SHAGVVKEMK VKVGDKVAMG SIVLVIESAG AGAPAAAAPA
     AAPAPAAAAP APAAAPAAAT AAPAPAASSA AQVDASKAHA SPSIRKFARE LGVNLGLVGG
     SGPKGRITQE DVQKFVKGVL AESASPSAKP AVGGGTGVGL DLLPWPSLDF SKFGPTELLP
     LSRIKKISGP NLHRNWVMIP HVTTFDEADV TDLEQFRVDS NAALAKQKSA VKLTMLAFVI
     KASVAALKKF PQFNASLSGD GASLILKQYY NIGFAADTPN GLMVPVVKDA DKKTVSQIAT
     EMGELSAQAR DGKLSPANMQ GATFTISSLG GIGGTGFTPI INAPELAILG LSKSAMKPVW
     DGKAFQPRLM LPLSLSYDHR VIDGAGAARF AAYLAEVLAD LRKTLL
//
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