ID C5CCM6_MICLC Unreviewed; 609 AA.
AC C5CCM6;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 13-SEP-2023, entry version 83.
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=dlaT {ECO:0000313|EMBL:SQG47257.1};
GN OrderedLocusNames=Mlut_13330 {ECO:0000313|EMBL:ACS30838.1};
GN ORFNames=NCTC2665_00010 {ECO:0000313|EMBL:SQG47257.1};
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:ACS30838.1, ECO:0000313|Proteomes:UP000000738};
RN [1] {ECO:0000313|EMBL:ACS30838.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC 2665 {ECO:0000313|EMBL:ACS30838.1};
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:SQG47257.1, ECO:0000313|Proteomes:UP000248985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC2665 {ECO:0000313|EMBL:SQG47257.1,
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; ACS30838.1; -; Genomic_DNA.
DR EMBL; LS483396; SQG47257.1; -; Genomic_DNA.
DR RefSeq; WP_010078528.1; NZ_WBMF01000136.1.
DR AlphaFoldDB; C5CCM6; -.
DR STRING; 465515.Mlut_13330; -.
DR EnsemblBacteria; ACS30838; ACS30838; Mlut_13330.
DR KEGG; mlu:Mlut_13330; -.
DR PATRIC; fig|465515.4.peg.1275; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_11; -.
DR OMA; MKVPSPG; -.
DR Proteomes; UP000000738; Chromosome.
DR Proteomes; UP000248985; Chromosome 1.
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; IPR014276; 2-oxoglutarate_DH_E2.
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 NCBIfam; TIGR02927; SucB_Actino; 1.
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:SQG47257.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000000738};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SQG47257.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 133..208
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 293..330
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 72..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 63371 MW; 77259635E6AFEDD1 CRC64;
MSETVNLPAL GESVTEGTVT RWLKAVGDEV AVDEPLVEVS TDKVDTEIPS PVAGVLEEIL
VEEDDTVEVG APLATIGGGS ADTSEDDAAA EEPAVEEAQQ DDVQQEPAGE PAPEERASTD
QGSNEAPSAG GDASEVTLPA LGESVTEGTV TRWLKSVGDE VEVDEPLLEV STDKVDTEIP
SPVAGTLLEI RAEEDDTVEV GAVLALVGSG SAGGGSAPSE GSSGQDEASA EEIEDKATEA
EAPEETEEAA EAAGVEKSEK TPEASPSEEA SRRESAQGET AEAPSATEPG QGYVTPLVRR
LAHQNNVDLS TVRGTGVGGR IRKQDVLAAA LASQAAADGS EAPAEQSSEA AAPSSAASAP
ATSSSVDPSV RGEVEKAPRI RQVIAQRMRE SLDLSAQLTQ VHEVDLTRIV KLRNKAKASF
QQQAGVNLTY LPFITKAVAE ALKQHPKLNA SLSKDNKEIT YHASEDIAIA VDTEKGLLVP
VIKDAGSLNL TGLAQKIADV AERTRTNKIS PDELSGGTFS ITNIGSVGAL FDTPIINQPQ
VAILGTGAIV KRPMVVTDAD GNDSIAIRHM MYLSLTYDHR LVDGADAGRF LMTVRQRLEG
GEFANELGL
//