ID J4UZN4_9GAMM Unreviewed; 429 AA.
AC J4UZN4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=aceF {ECO:0000313|EMBL:EJP71852.1};
GN ORFNames=NT01SARS_0334 {ECO:0000313|EMBL:EJP71852.1};
OS SAR86 cluster bacterium SAR86A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX NCBI_TaxID=1123866 {ECO:0000313|EMBL:EJP71852.1, ECO:0000313|Proteomes:UP000010305};
RN [1] {ECO:0000313|EMBL:EJP71852.1, ECO:0000313|Proteomes:UP000010305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT lineage.";
RL ISME J. 6:1186-1199(2012).
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 -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; JH611156; EJP71852.1; -; Genomic_DNA.
DR AlphaFoldDB; J4UZN4; -.
DR STRING; 1123866.NT01SARS_0334; -.
DR HOGENOM; CLU_016733_10_0_6; -.
DR Proteomes; UP000010305; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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; 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; 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:RU003423};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:EJP71852.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010305};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EJP71852.1}.
FT DOMAIN 4..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 137..174
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 429 AA; 47946 MW; B046E3C31517D064 CRC64;
MSNVKTINLP DYGDFDEVEV IEICVESGQE VDSEEPILIL ETDKAAMEIP SSVNGIVNKV
ILNVGDKVKV GMPFLEIEVQ ENKEVDKTNI DTKEEVSVDE KTFMDDPPSA VDDAANVMSK
QESNVINLNN HKSKNIHSGP ATRKLAREFG INLSLVAGSG PKGRILKEDL HQYVKNILSS
PQEQTFKSTQ PDIDFSEWGN TKEVDLTKFQ KTSLDNLHSS WVNIPHVTQH EEINISKLMK
IREKLCKKYK VKISPLAFIL KGLSVSLKEY EMMNSSLSKD LNTIIFKDFI NIGVAVDTEY
GLIVPNIKNI DSKNISNIAS EVKELADLAK KRRLKNEHLQ GASFTVSSLS GVGGKFFTPI
INPPEVGILG LSRTFDSLKL DKLKLETVKM LPVSLSYDHR VINGVYAIQF INHLSEVLND
IKFLEDSFK
//
