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Database: UniProt
Entry: A9NHS5_ACHLI
LinkDB: A9NHS5_ACHLI
Original site: A9NHS5_ACHLI 
ID   A9NHS5_ACHLI            Unreviewed;       544 AA.
AC   A9NHS5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=pdhC {ECO:0000313|EMBL:ABX81905.1};
GN   OrderedLocusNames=ACL_1310 {ECO:0000313|EMBL:ABX81905.1};
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81905.1, ECO:0000313|Proteomes:UP000008558};
RN   [1] {ECO:0000313|EMBL:ABX81905.1, ECO:0000313|Proteomes:UP000008558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-8A {ECO:0000313|EMBL:ABX81905.1,
RC   ECO:0000313|Proteomes:UP000008558};
RX   PubMed=21784942; DOI=10.1128/JB.05059-11;
RA   Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA   Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA   Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA   Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA   Ladygina V.G., Govorun V.M.;
RT   "Complete genome and proteome of Acholeplasma laidlawii.";
RL   J. Bacteriol. 193:4943-4953(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; CP000896; ABX81905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9NHS5; -.
DR   STRING; 441768.ACL_1310; -.
DR   KEGG; acl:ACL_1310; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_14; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000008558; Chromosome.
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; 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: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; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABX81905.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008558};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ABX81905.1}.
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          113..188
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          242..279
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   544 AA;  57260 MW;  81EE9B269CFF7484 CRC64;
     MYEFKFADIG EGIHEGTVLQ WNFKVGDKVK EGETLVIVET DKVNAELPSP VDGTIVSLGA
     KEGEEIHVGQ IIVTIDDGTG TPAAAPAPAQ VSAPTPAPAA APQVAAPAAS GDIYDFKFAD
     IGEGIHEGTI LQWNFKVGDK VKEGETLVVV ETDKVNAELP SPVDGTILKL GKAEGEVIHV
     GETVVLIGQN GATLEQAQAP KAEAPVSEPK KGAGVVGEIE VSDDIIGGSE EVHVVATTGK
     VLASPVARKL ASDLGVDIAT IKGSGEQGRV MKDDVQNSKA PAKAQAPVQQ TQAPAQAAAS
     VAPSFAAAGK PQGDVEVVKI TRLRKAVSNA MTRSKSIIPE TVLMDEINVD ALVNFRNEAK
     GLAESKGIKL TYMAFIAKAV LIALKEFPMF NASFNHDTDE VYIKKFINLG MAVDTPDGLI
     VPNIKNADRL SVFELASQVR SLADDTIARK ISMDQQTGGT FTITNFGSAG IAFGTPVINY
     PELAILGIGK IDRKPWVVGN EIKIAHTLPL SLAVDHRIID GADGGRFLMR VKELLTNPTL
     LLLS
//
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