ID   A5CV90_CLAM3            Unreviewed;       466 AA.
AC   A5CV90;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-OCT-2025, entry version 98.
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=CMM_2942 {ECO:0000313|EMBL:CAN03029.1};
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN03029.1, ECO:0000313|Proteomes:UP000001564};
RN   [1] {ECO:0000313|EMBL:CAN03029.1, ECO:0000313|Proteomes:UP000001564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN03029.1,
RC   ECO:0000313|Proteomes:UP000001564};
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M.,
RA   Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C.,
RA   Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN03029.1; -; Genomic_DNA.
DR   RefSeq; WP_012039629.1; NC_009480.1.
DR   AlphaFoldDB; A5CV90; -.
DR   KEGG; cmi:CMM_2942; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_11; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000001564; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:TreeGrafter.
DR   GO; GO:0031405; F:lipoic acid binding; IEA:TreeGrafter.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   FunFam; 3.30.559.10:FF:000007; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; 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; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR050743; 2-oxoacid_DH_E2_comp.
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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001564};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          184..221
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          138..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..177
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  49215 MW;  2C1AC239FC5E8CC1 CRC64;
     MADSEFTLPD VGEGLIDAEI VSWRVQPGDR VALNQVIVEI ETAKSLVELP SPFEGTVSGL
     LVQEGQTVEV GTPIIAIAQG SPSLSAPAET PAQMALPGET VIEDDTAIEN REPAPAPAAE
     ETSGAVLVGY GTVGKVASRR RRPELGDAAP AARRPASPSA PAGAPAARAP RPASVPAASA
     VPIIAKPPIR KLAKDLEVDL AQVEATGLVG EITREDVIRT AQQASVFKNI ETPEWPDARE
     DRIPVKGVRK VIAAAMVQSA FQAPHVSLFV DVDATRTMEF VKRLKASTDF AGVKVSPLLI
     MAKAMIWAVR RNPTVNSSWT DQEIIVRHYV NLGVAAATPR GLVVPNVKEA QAMSLLELAR
     ALEQLTLTAR DGKTSPADMS QGTITITNIG VFGMDTGTPI LNPGEVAIVA LGTIKQKPWV
     VDGEVRPRFV TTIGASFDHR VVDGDVASRF LADVASIIEE PALLLE
//