ID   F5Y7S9_LEAAZ            Unreviewed;       470 AA.
AC   F5Y7S9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=TREAZ_3439 {ECO:0000313|EMBL:AEF81923.1};
OS   Leadbettera azotonutricia (strain ATCC BAA-888 / DSM 13862 / ZAS-9)
OS   (Treponema azotonutricium).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Breznakiellaceae;
OC   Leadbettera.
OX   NCBI_TaxID=545695 {ECO:0000313|EMBL:AEF81923.1, ECO:0000313|Proteomes:UP000009222};
RN   [1] {ECO:0000313|Proteomes:UP000009222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9
RC   {ECO:0000313|Proteomes:UP000009222};
RA   Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA   Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA   Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA   Paulsen I.T.;
RT   "Complete sequence of Treponema azotonutricium strain ZAS-9.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEF81923.1, ECO:0000313|Proteomes:UP000009222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9
RC   {ECO:0000313|Proteomes:UP000009222};
RX   PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA   Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT   "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT   spirochete species in co-culture.";
RL   ISME J. 5:1133-1142(2011).
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}.
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DR   EMBL; CP001841; AEF81923.1; -; Genomic_DNA.
DR   RefSeq; WP_015712133.1; NC_015577.1.
DR   AlphaFoldDB; F5Y7S9; -.
DR   STRING; 545695.TREAZ_3439; -.
DR   KEGG; taz:TREAZ_3439; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_12; -.
DR   InParanoid; F5Y7S9; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000009222; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016746; F:acyltransferase activity; 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:SF1; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 3 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:AEF81923.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009222};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AEF81923.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          134..171
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   470 AA;  47866 MW;  589E6067A6823D25 CRC64;
     MAHVLIMPRQ GNTVESCIIG EWKVKEGDTV QADTPVCVVE TDKATFEVPS GASGTVLKIF
     HSQGDDVPVL QPIMVVGNPG ENWEAAVPGG ASAASAAQAA PAAASGATSA ALAVSVPAVE
     AVQAPAPQTE GHLAASPRAK KLADAEAVDI RTLGGSGPGG RIIEVDVAAA LAARPPLTEA
     AKDELRKRIA VGLPAGTAGQ GTGIGGRFTL GDLASGGAGS GAVVGTSPPA ASSAAPAPGG
     FTDIPIKGIR KVIADQMMNS HTNTAAFTLN TSASVVNLQK LRARFKASDP ELGLSKITLN
     DLVLFAASRV LPLYTYMNAH RLDGVVRAYN DVQLGVAVST PRGLMVPVMR NADKLSLVQI
     SQKARELAEA CRSGSISPDD LHGSTFTVTN LGNTGIESFS PVINIPEVAI MGVCGISPKA
     AETSPGVYEI LPHLGLSLTI DHAVVDGAPA AEFLKAFAGA IRDIDIWVAK
//