ID A0A2T0XUG3_9MICO Unreviewed; 492 AA.
AC A0A2T0XUG3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=BCE75_1023 {ECO:0000313|EMBL:PRZ09296.1}, BCE75_12029
GN {ECO:0000313|EMBL:PRZ02502.1};
OS Isoptericola sp. CG 20/1183.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=1881052 {ECO:0000313|EMBL:PRZ02502.1, ECO:0000313|Proteomes:UP000239858};
RN [1] {ECO:0000313|EMBL:PRZ02502.1, ECO:0000313|Proteomes:UP000239858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG 20 {ECO:0000313|EMBL:PRZ02502.1,
RC ECO:0000313|Proteomes:UP000239858};
RA Rubin E.;
RT "Comparative analysis of microorganisms from saline springs in Andes
RT Mountain Range, Colombia.";
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:PRZ02502.1}.
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DR EMBL; PVTW01000020; PRZ02502.1; -; Genomic_DNA.
DR EMBL; PVTW01000002; PRZ09296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0XUG3; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000239858; 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; 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 Pyruvate {ECO:0000313|EMBL:PRZ02502.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239858};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:PRZ02502.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 195..232
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 51080 MW; 304CB5E8C99F4720 CRC64;
MSTQRFPLPD VGEGLTEAEI VEWKVAVGDT VAVNDVIVEI ETAKSLVELP SPFAGTVVAL
LAEEGTTVDV GTPIIEVGSA DASASEPAPS GAPASPGDSS GGSTNGEGSG SVLVGYGTGD
AAAGSRRRRR RAEEPAAPAT AASKPAPAPA PAPAPSSAPE RTPGIAKPMM SVPAAVDGAG
AASSGTTPAG RIRVLAKPPV RKLAKDLGVD LASVQPTGPG GIVTREDVVA RADAAEPRTL
ATYPDDDQPW LASGSVTNDG RQTRVPVKSV RKRTAEVMVA SAFTAPHVTV FRTVDVTRTM
KLVEKLKADR DFADVRVTPL LIAAKAALLA IKRHPEINAS WDDEAREIVY KHYVNLGIAA
ATPRGLVVPN VKDAHRHELL PLARALAELT ATARAGRTSP ADMSDGTFTI TNVGVFGIDT
GTPILNPGEA GILAFGAIRQ QPWVHKGKVK PRWVTQLALS FDHRLVDGEL GSRFLSDVAR
VLEDPAHGLV WG
//
