ID A0A1S2HPC2_9MICO Unreviewed; 518 AA.
AC A0A1S2HPC2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BIU96_13670 {ECO:0000313|EMBL:OII13346.1};
OS Curtobacterium sp. MCBA15_008.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1898736 {ECO:0000313|EMBL:OII13346.1, ECO:0000313|Proteomes:UP000180168};
RN [1] {ECO:0000313|EMBL:OII13346.1, ECO:0000313|Proteomes:UP000180168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBA15_008 {ECO:0000313|EMBL:OII13346.1,
RC ECO:0000313|Proteomes:UP000180168};
RA Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT "Evidence for ecological flexibility in the cosmopolitan genus
RT Curtobacterium.";
RL Submitted (SEP-2016) 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:OII13346.1}.
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DR EMBL; MJGN01000013; OII13346.1; -; Genomic_DNA.
DR RefSeq; WP_071291900.1; NZ_MJGN01000013.1.
DR AlphaFoldDB; A0A1S2HPC2; -.
DR STRING; 1898736.BIU96_13670; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000180168; 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; 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; 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; 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 Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:OII13346.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 217..254
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 63..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 52707 MW; 5055F8EF91F19416 CRC64;
MSESVNLPAL GESVTEGTVT RWLKNVGDRV EVDEPLLEVS TDKVDTEIPS PVAGVVEEIL
VPEDETVEVG TPLVKIGDGS GSGSSDGGSD QASDGSDQAS DESSNEAAAD AEAPEAEPST
EQESETPAPE PTEPEPAPAG QTQPAAPQAP AAPPAAAPVP QAAPVPPPAA APPAAVPAPA
AAPAPAAAPA PAASGSSAPS AAASVPNPSQ DASASGYVTP LVRKLANEQG VDLSTVTGSG
VGGRIRKEDV LAAAAAATAA PAAGGSAAAA PAGPFVAEVS PLRGTREKMT RLRKVVAERA
VQSMTSTAQL TSVVEVDVTK VAQFRDANKA EFLEKTGSKL SFMPFFALAA SEALKAHPKI
NSTVEGEEIV YPETENVSIA VDTERGLLTP VIKDAASLDL AKFAQSIADL AERTRNNQLK
PDELAGGTFT LTNTGSRGAL FDTPVVFLPQ SAILGTGIVT KRPAVVKVDG QEAIAIRSFV
YLALSYDHRI IDGADASRYL VAVKNRLEEG NFGPNLGY
//
