ID A0A0E3U3T8_9ENTR Unreviewed; 426 AA.
AC A0A0E3U3T8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:AKC59736.1};
GN ORFNames=BTURN675_147 {ECO:0000313|EMBL:AKC59736.1};
OS Blochmannia endosymbiont of Polyrhachis (Hedomyrma) turneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=1505596 {ECO:0000313|EMBL:AKC59736.1, ECO:0000313|Proteomes:UP000033094};
RN [1] {ECO:0000313|EMBL:AKC59736.1, ECO:0000313|Proteomes:UP000033094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=675 {ECO:0000313|EMBL:AKC59736.1,
RC ECO:0000313|Proteomes:UP000033094};
RX PubMed=25861561;
RA Williams L.E., Wernegreen J.J.;
RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene loss
RT among Blochmannia spanning the origin of the ant tribe Camponotini.";
RL PeerJ 3:E881-E881(2015).
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; CP010048; AKC59736.1; -; Genomic_DNA.
DR RefSeq; WP_046288683.1; NZ_CP010048.1.
DR AlphaFoldDB; A0A0E3U3T8; -.
DR STRING; 1505596.BTURN675_147; -.
DR KEGG; bed:BTURN675_147; -.
DR PATRIC; fig|1505596.4.peg.151; -.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000033094; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:AKC59736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033094};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AKC59736.1}.
FT DOMAIN 2..75
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 120..157
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 426 AA; 48080 MW; 6FFA5119CA53C6A2 CRC64;
MTIKVYIPNI GNDKLEVTDI MVKIEDTVLT DQPLAILEGD KTSIEVPSPS SGIVKSIMIN
IGDKVNTGSL IMLIENTEIT KKTTIPIKNN QNNTPINQNN TTIIHHHDQT IIHDNKNHIH
ATPLIRHMAR IFGINLKHIH GTGRKGRILR EDIQNYIKNN IQNINKKTIN QHTQSKTFNN
IAPWPRINFD EFGPTEKIKL KHIQKTSGAN LHRNWIMLPH VTQFDEVDIT ELEKFRKEKN
EEAEKEKLNF KITPIIFIMK AVALTLKKLP RFNSSLSENN HTLILKKYIN IGIAVNTHYG
LIVPVIKDVN KKNIITLTKE LSNILQKTSN NNQLVASDMQ GGCFTISSLG KTGGTAFTPI
VNVPEVAILG VSRASIKPIW NGKKFSPRLM LPLSLSYDHR VINGVDGAQF MNIINKLLSD
IRNLIM
//
