ID A0A136L2T2_9BACT Unreviewed; 407 AA.
AC A0A136L2T2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=UZ18_ATM001001508 {ECO:0000313|EMBL:KXK15856.1};
OS Armatimonadetes bacterium OLB18.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=1617424 {ECO:0000313|EMBL:KXK15856.1, ECO:0000313|Proteomes:UP000070351};
RN [1] {ECO:0000313|EMBL:KXK15856.1, ECO:0000313|Proteomes:UP000070351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB18 {ECO:0000313|EMBL:KXK15856.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:ARBA00043782};
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:KXK15856.1}.
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DR EMBL; JZQX01000140; KXK15856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136L2T2; -.
DR STRING; 1617424.UZ18_ATM001001508; -.
DR PATRIC; fig|1617424.3.peg.1607; -.
DR Proteomes; UP000070351; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 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 ECO:0000313|EMBL:KXK15856.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:KXK15856.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KXK15856.1}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 126..163
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 87..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 43176 MW; C10AC5267BBF9D81 CRC64;
MTEVIMPKMG DAMEEGVLVE WLAEDGQKVK SGQVIGTIQT DKATLELESP ASGVFGGVLV
KAGATVPVGI PIAAILAEGE KLPKNWGKDA LTSKEAPSPK EEAAPVQAHS SLAEAPAANA
STQRVKASPL AKKIAEELGV PIALVHGTGP GGRIVEQDVR AAASVATPAG TRLLATPSKE
DRVVSLNRIR KITADRTAQS KQQVPHFYVG VDVDVENLLD LKDQLDEEGV GKVSVNDFVI
RASALALRKM PGVNASFQGD SILEYGAVNI GLAVALEDGL TLPVLHNADS LPIRQIAERS
RELALKAREN RLTPDELSGS TFSISNMGML NVDDFSAIIN QPNAAILAVS TASRKVVPSD
TEEDAVEIRT LMRITGSFDH RVVDGAIGAR FMNVLRDYLQ NPIRLIV
//
