ID A0A1Y1RQT6_9MICC Unreviewed; 575 AA.
AC A0A1Y1RQT6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=A7979_02395 {ECO:0000313|EMBL:ORC18867.1};
OS Rothia nasimurium.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=85336 {ECO:0000313|EMBL:ORC18867.1, ECO:0000313|Proteomes:UP000192359};
RN [1] {ECO:0000313|EMBL:ORC18867.1, ECO:0000313|Proteomes:UP000192359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PT-32 {ECO:0000313|EMBL:ORC18867.1,
RC ECO:0000313|Proteomes:UP000192359};
RA Gaiser R.A., Van Baarlen P., Wells J.M.;
RT "Draft genome sequence of a porcine commensal Rothia nasimurium.";
RL Submitted (MAY-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:ORC18867.1}.
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DR EMBL; LXWF01000022; ORC18867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RQT6; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000192359; 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:UP000192359};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ORC18867.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..200
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 263..300
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 78..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 59846 MW; 045A65BAAF4DDC29 CRC64;
MSTTVELPAL GESVTEGTVT RWLVEVGETV EVDQPIVEVS TDKVDTEVPS PVAGVVEKIL
VEEDEDVEVG APLVVIGDGS GAGSSDDAPA AEAPEAEKKE EAPAAEEKKE EAPAAAPASS
GSASGTEVTL PALGESVTEG TITRWLKEVG EEVAVDEPLV EVSTDKVDTE VPSPVAGTLL
EIRIQEDEDA EVGQVLAIIG DASAAAPAAA EEKKEETSTP EEKEEAPAAE EEKAEEVAPV
SSTDEAAEAP AVELPSGDNG EAYVTPLVRK LAKQEGIDLS TLKGTGVGGR IRKQDVLAAA
ESKKGAAPVA AAPAAEAPAT AAPAKKEAPQ VAASSKRGTT EKAPRIRQTV AKRMVESLAV
SAQLTTVQEV DLTRLVALRN KAKAGFEARE GTKLTFLPFF TKAVTEALQQ FPQFNSSMSE
DYKEITYHGS ENIGLAVDTP KGLLVPVVKD AGDLNIAGIA KKINDVAKRA RDGQVGPEEL
SGSTFTISST GQSGGVFFTP IINQPNVAIL GIGSTNKRPA VIQDAEGNDV IAIRSLAYFA
LTYDHRVVDG ADAGRFLAFL KNRLEEAAFE AEVGL
//
