ID A0A2T0SKW9_9PSEU Unreviewed; 594 AA.
AC A0A2T0SKW9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CLV43_11887 {ECO:0000313|EMBL:PRY34061.1};
OS Umezawaea tangerina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Umezawaea.
OX NCBI_TaxID=84725 {ECO:0000313|EMBL:PRY34061.1, ECO:0000313|Proteomes:UP000239494};
RN [1] {ECO:0000313|EMBL:PRY34061.1, ECO:0000313|Proteomes:UP000239494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44720 {ECO:0000313|EMBL:PRY34061.1,
RC ECO:0000313|Proteomes:UP000239494};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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}.
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:PRY34061.1}.
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DR EMBL; PVTF01000018; PRY34061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0SKW9; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000239494; 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:UP000239494};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 129..204
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 77..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 61826 MW; 9843B31F7768B3C4 CRC64;
MAFSVQMPAL GESVTEGTVT RWLKQEGDRV EVDEPLLEVS TDKVDTEIPS PAAGVLQKIV
AQEDETVEVG AELAVIGDGA GGGESAPAAP AEEAQPEPEQ APEPEAEAPK QEEAPKQEAP
APSGGSGEGT PVVMPALGES VTEGTVTRWL KQVGDSIEVD EPLLEVSTDK VDTEIPSPVA
GTVLEITAAE DSTVEVGGRL AVIGSGSPAQ SSAPAPAPTP EAPKQEAPKQ EAPKQEAPQQ
KAPQQEAPKQ QEAPKQEAPK AAPAPAAPAQ QSAPAEESSN GTPYVTPLVR KLASENGIDL
NSLTGTGVGG RIRKQDVLAA VEAKKAPAPA PAAPAPAAAA PARAAAPAAA DTSGLRGSTQ
KLPRLRQIVA QRTRESLQMS AQLTQVFEVD VTKIARLRNR AKAAFEQREG VKLTFLPFFA
KATVEALKQH PKLNASIDEE AKQVTYYGAE HLGIAVDTER GLLNAVIHNA GDLNLAGLAH
NIADLAARTR ANKVTPDELS GGTFSLTNLG SNGALFDTPI IQQPQVGILG VGVVKKRPVV
ITDENGDDNI AIRSMAYLAL TYDHRLVDGA DAGRFLTTIK NRLEEGAFEA DLGL
//
