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Database: UniProt
Entry: A0A0A5G6T0_9BACI
LinkDB: A0A0A5G6T0_9BACI
Original site: A0A0A5G6T0_9BACI 
ID   A0A0A5G6T0_9BACI        Unreviewed;       400 AA.
AC   A0A0A5G6T0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=N784_03190 {ECO:0000313|EMBL:KGX86873.1};
OS   Pontibacillus litoralis JSM 072002.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX86873.1, ECO:0000313|Proteomes:UP000030401};
RN   [1] {ECO:0000313|EMBL:KGX86873.1, ECO:0000313|Proteomes:UP000030401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX86873.1,
RC   ECO:0000313|Proteomes:UP000030401};
RA   Huang J., Wang G.;
RL   Submitted (AUG-2013) 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:KGX86873.1}.
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DR   EMBL; AVPG01000010; KGX86873.1; -; Genomic_DNA.
DR   RefSeq; WP_036833996.1; NZ_AVPG01000010.1.
DR   AlphaFoldDB; A0A0A5G6T0; -.
DR   STRING; 1385512.N784_03190; -.
DR   eggNOG; COG0508; Bacteria.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000030401; 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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030401};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KGX86873.1}.
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          111..148
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   400 AA;  44636 MW;  5AA96F78F5E2DB0D CRC64;
     MEVKLHDIGE GMTEAEIVHY FVQPGDAVVV DQPLVEVQTD KMTAELPAPA NGTIEDVLVK
     VGETIKVGTT VLSMITTSQP TSAVSEEKES TIEQQWQAKT FRIEKRKQPI LASPYTRKMA
     REQGVNIEEI KGTGPAGRIV DEDVYAYVQK EKESLLQENS PTQQVMKQEK EIHIIPFKGR
     RKQIAKKMKQ SLHTIAHCSH FEEVDVTNVL QWKEQSKQAG KNVSLTAYFV KAVSLALKDY
     PIFNATLNEE KEQIEVQTSH HIGLATNTEE GVIVPVLKHV EHKSLLTIQA EMRALTEKAL
     HHTLSREEIT GGSFTISNVG PLQGSIGATP IIHHPQTGIM AFHKTKKRPA VVEDEIVIRS
     MMNVSMTFDH RVADGATAVQ FTNRLVELIE HPNLLTLELV
//
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