ID T5KEJ4_9MICO Unreviewed; 579 AA.
AC T5KEJ4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=L687_03880 {ECO:0000313|EMBL:EQM74605.1};
OS Microbacterium maritypicum MF109.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1333857 {ECO:0000313|EMBL:EQM74605.1, ECO:0000313|Proteomes:UP000016033};
RN [1] {ECO:0000313|EMBL:EQM74605.1, ECO:0000313|Proteomes:UP000016033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF109 {ECO:0000313|EMBL:EQM74605.1,
RC ECO:0000313|Proteomes:UP000016033};
RX PubMed=24092793;
RA Chauhan A., Green S., Pathak A., Thomas J., Venkatramanan R.;
RT "Whole-genome sequences of five oyster-associated bacteria show potential
RT for crude oil hydrocarbon degradation.";
RL Genome Announc. 1:e00802-e00813(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQM74605.1}.
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DR EMBL; ATAO01000206; EQM74605.1; -; Genomic_DNA.
DR RefSeq; WP_021200697.1; NZ_ATAO01000206.1.
DR AlphaFoldDB; T5KEJ4; -.
DR PATRIC; fig|1333857.3.peg.2758; -.
DR Proteomes; UP000016033; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000016033};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EQM74605.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 138..213
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 284..321
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 87..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 58170 MW; 9A932D783CB3FD95 CRC64;
MSTSVVLPAL GESVTEGTVT RWLKQVGDTV QADEGLLEIS TDKVDTEIPS PVSGVIEEIL
VAEDETVEVG ALLARIGDGS AAAPAADAPA AAAPAAEEAP AEASPAAEET PAAEAPTPAA
EAPAPAAESA PAAPAGDATD IVLPELGESV TEGTVTRWLK QVGDTIAVDE ALLEISTDKV
DTEIPSPVAG VLQEIVAGED ETVAVGAVLA RVGSGAAPAS EAPAAPAPAA APAPAAAPAA
AAPAPAAASA PAAAPAPAAA PAPAPAAAQP ASKLALPTES DNLYVTPLVR RLASQQGVDL
ASVTGTGVGG RIRKEDVLKA AETAKSAPAA AAAAPAPLEV SPLRGTTQPM SRLRKVLAKR
AVESMQQTAQ LTTVVEVDVT ALADYRDSVK ASFLEKTGDK LSFLPFFALA TAEALQAFPI
VNATVDGENI VYPASENVSI AVDTERGLLT PVLRDAASKN IAQIAHEIAD LAARTRDNKL
KPDELAGGTF TLTNTGSRGA LFDTPVVFLP QSAILGTGTV VKRPGLVKVG GTDAIAVRSY
VYLALSYDHR IIDGADAARF LGAVKARLES AQFAAQLGA
//
