ID   C5CCR0_MICLC            Unreviewed;       496 AA.
AC   C5CCR0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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_1 {ECO:0000313|EMBL:SQG47691.1};
GN   OrderedLocusNames=Mlut_17790 {ECO:0000313|EMBL:ACS31262.1};
GN   ORFNames=NCTC2665_00455 {ECO:0000313|EMBL:SQG47691.1};
OS   Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS   NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Micrococcus.
OX   NCBI_TaxID=465515 {ECO:0000313|EMBL:ACS31262.1, ECO:0000313|Proteomes:UP000000738};
RN   [1] {ECO:0000313|EMBL:ACS31262.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NCTC 2665 {ECO:0000313|EMBL:ACS31262.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Lowry S., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Young M., Greenblatt C.;
RT   "Complete sequence of Micrococcus luteus NCTC 2665.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000000738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC   NCTC 2665 / VKM Ac-2230 {ECO:0000313|Proteomes:UP000000738};
RX   PubMed=19948807; DOI=10.1128/JB.01254-09;
RA   Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA   Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA   Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA   Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT   "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT   free-living actinobacterium.";
RL   J. Bacteriol. 192:841-860(2010).
RN   [3] {ECO:0000313|EMBL:SQG47691.1, ECO:0000313|Proteomes:UP000248985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC2665 {ECO:0000313|EMBL:SQG47691.1,
RC   ECO:0000313|Proteomes:UP000248985};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; CP001628; ACS31262.1; -; Genomic_DNA.
DR   EMBL; LS483396; SQG47691.1; -; Genomic_DNA.
DR   RefSeq; WP_012751052.1; NZ_WBMF01000035.1.
DR   AlphaFoldDB; C5CCR0; -.
DR   STRING; 465515.Mlut_17790; -.
DR   EnsemblBacteria; ACS31262; ACS31262; Mlut_17790.
DR   KEGG; mlu:Mlut_17790; -.
DR   PATRIC; fig|465515.4.peg.1718; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_11; -.
DR   Proteomes; UP000000738; Chromosome.
DR   Proteomes; UP000248985; Chromosome 1.
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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ACS31262.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:ACS31262.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000738};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SQG47691.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          189..226
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          118..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  50820 MW;  7B31BD0925FF92AF CRC64;
     MSNTFLLPDL GEGLTEADIV RWLVAEGDTV AVDQPMVEVE TAKALVEVPS PYAGTVLILH
     GAEGETMDVG SPLITIGEAG ESGEGSAPVA GTETLAVPPS TGAAAAEAAR PGALSYREEE
     MAGVQPKPDK ARGGDGDVAG SDDEASGAVL IGYGTSGHKA TSRSRPSKRG RGATRPTPAP
     TAEAGAPRVT SPIVRKLARE KGVDVAALTG TGPDGLITRA DVLTAAEGST PQAAPTPAPS
     AAAAPAAGAA AQPGAVDGRT GLAVVARTPI TGVRKVIADQ LSRSRREVPE VTAWLDVDVT
     ALLELRAALK AKDPENAPSL LGLIARFTLA GLRRYPVMNA RIEAGADGRD EIVEVDGVHL
     GLAVQTDRGL MVPSVEHAEK LSADELTAAI NDTVSRARAG RAAPAELTRG TFTLNNYGPL
     GTDGATPIIN VPEVGMLGIG RIIDRPWVVD GEIVVRKVTE MTVTFDHRVT DGATASAFLT
     FVADCLHDPT AALARF
//