ID W0ZBK3_9MICO Unreviewed; 602 AA.
AC W0ZBK3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:CDK00747.1};
GN ORFNames=MIC448_320051 {ECO:0000313|EMBL:CDK00747.1};
OS Microbacterium sp. C448.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDK00747.1, ECO:0000313|Proteomes:UP000028883};
RN [1] {ECO:0000313|EMBL:CDK00747.1, ECO:0000313|Proteomes:UP000028883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C448 {ECO:0000313|EMBL:CDK00747.1,
RC ECO:0000313|Proteomes:UP000028883};
RX PubMed=24526651; DOI=10.1128/genomeA.01113-13;
RA Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.;
RT "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading
RT Microbacterium sp. Strain C448.";
RL Genome Announc. Announc.2:e01113-e01113(2014).
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:CDK00747.1}.
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DR EMBL; CBVQ010000195; CDK00747.1; -; Genomic_DNA.
DR RefSeq; WP_036295784.1; NZ_HG779612.1.
DR AlphaFoldDB; W0ZBK3; -.
DR STRING; 1177594.MIC448_320051; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_11; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000028883; 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 ECO:0000313|EMBL:CDK00747.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:CDK00747.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028883};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CDK00747.1}.
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 306..343
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 75..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 602 AA; 61186 MW; 9253C7A01457BF0D CRC64;
MSTSVVLPAL GESVTEGTVT RWLKQVGDEV KADEGLLEIS TDKVDTEIPS PVSGILEEIL
VQEDETVEVG GLLAKIGDGS GQPSDDAAPE ASAPAEAQAP AEDKVVEAPA EPELVAEAEP
AGNASAEPAA VGASSGSSTS VVLPELGESV TEGTVTRWLK NVGDDVAVDE PLLEISTDKV
DTEIPSPVAG VLQEIVAAED ETIAVGAVLA KIGSGAPAAA SEPAPAPAAE PVTEPEAPST
EKPVEADVPA SETPEQAPAP EPAPAAAAPA PAASAPAASA PAPSAPAPSA PAAPAAPSDS
SDDRTYVTPL VRRLAQQQGV DLASVTGTGV GGRIRKEDVL KAAESASAAP AAPAAEKAPA
LEVSPLRGTT QKMSRLRKVL AERAVASMQA TAQLTTVVEV DVTRLAGFRD SVKVDFQKKT
SDKLSFLPFF ALAAAEALRA FPIVNATVDG DTIVYPASEN LSIAVDTERG LLTPVLRDAA
SKNIAEIAHE IADLAARTRD NKLKPDELGG GTFTLTNTGS RGALFDTPVV FLPQSAILGT
GIVVKRPGVV KVDGVEAIGV RSVVYLALSY DHRIIDGADA ARFLGAVKAR LEAAEFAADL
GI
//
