ID D1A1L0_THECD Unreviewed; 523 AA.
AC D1A1L0;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=Tcur_0330 {ECO:0000313|EMBL:ACY95932.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY95932.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY95932.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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; CP001738; ACY95932.1; -; Genomic_DNA.
DR RefSeq; WP_012850716.1; NC_013510.1.
DR AlphaFoldDB; D1A1L0; -.
DR STRING; 471852.Tcur_0330; -.
DR KEGG; tcu:Tcur_0330; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_11; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000001918; 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; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; PS00189; LIPOYL; 1.
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:UP000001918};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 152..189
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 54743 MW; 4277A76281E9C2C8 CRC64;
MPEIKTFKLP DVGEGLTEAE IVRWHVHPGD RVEVNQVIVE IETAKAVVEL PCPYEGTVAE
LLVEEGRTVE VGTPIISVSV PAGEAGESAP PPAPDGAAEP GPRQDPETGP SEPARQPVLV
GYGVRPGATR RRPRKRPAAI RHARPAPAPH ALAKPPVRKL ARDLGVDLST VTGTGPHGTI
TREDVRQAAE RAATSPAPPA VERPGFAEVP QAPVHEGRGP AEMPQEAGGV PGGEAVRGLT
EMPGGVLPGR QGRGPAEMPG GLAEVSAPGE ARAVQEGAAG PAVPSAGGRE ERVPVRGVRK
STAAAMVGSA FTAPQVTEFL QVDVTETMET VRRLRELPEF AELKVTPLLL VAKALLTAVR
RHPMINSSWA DGGEAGDEIV VRHYVNLGIA TATSRGLLVP NVKDADRLTL PELAAALGRL
VEEARAGRAR PADLTGGTIT ITNIGVFGVD AGTPILTPGE AAILAFGQIR DMPWVHQGEL
AVRKVTTLAL TFDHRIVDGE LGSAVLRDIG AMLENPLRLL AWS
//
