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Database: UniProt
Entry: C5CCM6_MICLC
LinkDB: C5CCM6_MICLC
Original site: C5CCM6_MICLC 
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
//
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