ID   A0K281_ARTS2            Unreviewed;       527 AA.
AC   A0K281;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Arth_4026 {ECO:0000313|EMBL:ABK05401.1};
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK05401.1, ECO:0000313|Proteomes:UP000000754};
RN   [1] {ECO:0000313|Proteomes:UP000000754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754};
RX   PubMed=24501649; DOI=10.4056/sigs.4438185;
RA   Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA   Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT   "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL   Stand. Genomic Sci. 9:106-116(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}.
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DR   EMBL; CP000454; ABK05401.1; -; Genomic_DNA.
DR   RefSeq; WP_011693849.1; NC_008541.1.
DR   AlphaFoldDB; A0K281; -.
DR   STRING; 290399.Arth_4026; -.
DR   KEGG; art:Arth_4026; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_11; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000000754; Chromosome.
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   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000754};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          232..269
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          118..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  54583 MW;  8FE81945800D8BBC CRC64;
     MTVNKFNLPD VGEGLTEAEI VSWNVKPGDS VAINDILCEI ETAKSLVELP SPFAGTVTEL
     LVPVGVTVDV GTPIISVSDA VSGDPTPADA PVPVAPAAAA QTPAAPTANA PMYGKLFEDH
     DEQDSGTPGA QAVPASGKAV GPLVGSGPKA DAVKRRPRKA SPSAAVLPAP AAATSPVVEP
     APLAEPVETQ GIWINAGAAS ASGTPDTAGV PEEASGRPTL GGTISGLVNR VLAKPPVRKI
     ARDLGIDLAD VVATGARGEV TREDLVSYQA QRDAEVDKAD TFWGKSGRPQ DQRIERIPVK
     GVRKATAKAM VESAFAAPHV SIFVDVDASR TMEFVKRLKV SRDFEGIKVS PLLILAKAVI
     WAAARNPSVN ATWVDSADGS DTAEIHVKHF MNLGIAAATP RGLMVPNIKN AQDLSLKELA
     LALNDLATTA RAGKTRPAEM QGGTLTVTNI GALGIDTGTP IINPGEVAIV AFGTIKQKPW
     VLDGEVIPRW ITTLGGSFDH RVVDGDLSAR FMADVAAILE EPALLLD
//