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Database: UniProt
Entry: S5M0U0_9MOLU
LinkDB: S5M0U0_9MOLU
Original site: S5M0U0_9MOLU 
ID   S5M0U0_9MOLU            Unreviewed;       447 AA.
AC   S5M0U0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:AGR41622.1};
GN   ORFNames=STAIW_v1c10390 {ECO:0000313|EMBL:AGR41622.1};
OS   Spiroplasma taiwanense CT-1.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=1276220 {ECO:0000313|EMBL:AGR41622.1, ECO:0000313|Proteomes:UP000014984};
RN   [1] {ECO:0000313|EMBL:AGR41622.1, ECO:0000313|Proteomes:UP000014984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT-1 {ECO:0000313|EMBL:AGR41622.1};
RX   PubMed=23873917; DOI=10.1093/gbe/evt108;
RA   Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT   "Comparison of metabolic capacities and inference of gene content evolution
RT   in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL   Genome Biol. Evol. 5:1512-1523(2013).
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; CP005074; AGR41622.1; -; Genomic_DNA.
DR   RefSeq; WP_020834761.1; NC_021846.1.
DR   AlphaFoldDB; S5M0U0; -.
DR   STRING; 1276220.STAIW_v1c10390; -.
DR   KEGG; stai:STAIW_v1c10390; -.
DR   PATRIC; fig|1276220.3.peg.1056; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_14; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000014984; 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: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; 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   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:AGR41622.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014984};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AGR41622.1}.
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          143..180
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          79..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  47756 MW;  4612CBBFD7FEEBCA CRC64;
     MFKVKFADIG EGLTEGTVTE VLVKVGDSVK MGDSLFNVET DKVTSDIYAP VDGKIAKILI
     SAKQEIKVGD VVIEIDDGKG EATAEPEKKS SSNVQPVEEN ASVVGATPVS NDLISRDTNR
     NVATKQTISN QASIIDNSHV DVKASPLARK IAAVMGVDLS KVTPTGPNGR ILANDIQSFA
     ANPAKSAPVA FVGGASAKQQ IDYSNPLISV PEINEPLTFE SKPWNPIRKA TVKAMTTAHE
     KVAGFTGLRN LDVTELVNIR KQLKAFADSQ RVKLTYLAFI IKACANALKD MPNLNVRIDE
     ENKATKFAQQ INIGMACDTP DGLMVPVIKG ADKLSVLQIA VKINDLAMKA RSKKLASNEM
     SGATFTVTNF GAVGLDYATP IVNFPESAIL GVGTITRAPG VINDKIEIRD FMPFSITADH
     KVIDGADAGR FLTKVAYYLQ NPATLLV
//
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