ID E0NH30_PEDAC Unreviewed; 540 AA.
AC E0NH30;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:EFL95490.1};
GN ORFNames=HMPREF0623_1227 {ECO:0000313|EMBL:EFL95490.1};
OS Pediococcus acidilactici DSM 20284.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=862514 {ECO:0000313|EMBL:EFL95490.1, ECO:0000313|Proteomes:UP000004470};
RN [1] {ECO:0000313|EMBL:EFL95490.1, ECO:0000313|Proteomes:UP000004470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20284 {ECO:0000313|EMBL:EFL95490.1,
RC ECO:0000313|Proteomes:UP000004470};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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:EFL95490.1}.
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DR EMBL; AEEG01000004; EFL95490.1; -; Genomic_DNA.
DR RefSeq; WP_004166341.1; NZ_GL397067.1.
DR AlphaFoldDB; E0NH30; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_9; -.
DR Proteomes; UP000004470; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
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:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:EFL95490.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004470};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EFL95490.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 110..185
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 231..268
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 74..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 56665 MW; 8DB00FD1E1396472 CRC64;
MTEIFKMPDI GEGMAEGEIA NWLVKVGDDV KADDAVAEVQ NDKLLQEILS PYSGKVTKLF
VDAGTVVKVG EPLIEFDGDG TGGGDDSKDN AADAAPAADK GSDNAPSGDA EIFNMPDIGE
GMAEGEIANW LVKVGDEVKE DDPVAEVQND KLMQEILSPY SGKVTKLFVD AGTVVKVGEP
LIEFNGDGSG AGSGNAAPAA SAAPAKENAA PANNDEPTKV GTAVASNGQV LAMPSVREYA
RKHDIDLMQV PATGRHGHIT MADVKNFSGG GTAPSAPKAA ESAAPSPSAA PAAEAPKPAP
AKPASVKAGR VPLSPIRKAI SRNLTQRVQT VPHVTIMDEV EVSKLMELRD QFKEQTKAKG
YKLTYMPFVA KALAAAARKY PELSATIDDE TQEIVYYEET NVGFAVDTDQ GLFVPNVKNT
ASKSIMQVAQ EIDDLAIRGR DGKLKPAELQ GGTVTISNIG SESGSGFFTP ITNPGESSIL
GIGRIRKTPI VNEDGELAVG NTLKLSLSFD HRLIDGALAQ KIMNELKALL GNPAYMLMEV
//
