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Database: UniProt
Entry: A0A095YD35_9MICC
LinkDB: A0A095YD35_9MICC
Original site: A0A095YD35_9MICC 
ID   A0A095YD35_9MICC        Unreviewed;       480 AA.
AC   A0A095YD35;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-JUN-2023, entry version 31.
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=HMPREF2128_06665 {ECO:0000313|EMBL:KGF20158.1};
OS   Pseudoglutamicibacter albus DNF00011.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudoglutamicibacter.
OX   NCBI_TaxID=1401063 {ECO:0000313|EMBL:KGF20158.1, ECO:0000313|Proteomes:UP000053528};
RN   [1] {ECO:0000313|EMBL:KGF20158.1, ECO:0000313|Proteomes:UP000053528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00011 {ECO:0000313|EMBL:KGF20158.1,
RC   ECO:0000313|Proteomes:UP000053528};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) 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:KGF20158.1}.
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DR   EMBL; JRNH01000021; KGF20158.1; -; Genomic_DNA.
DR   RefSeq; WP_035756390.1; NZ_JRNH01000021.1.
DR   AlphaFoldDB; A0A095YD35; -.
DR   Proteomes; UP000053528; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000053528};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          169..206
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          76..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  50047 MW;  FF97A5767D7D209E CRC64;
     MTTFNLPDVG EGLTEADIVE WKVAVGDEVA LNQPFVEIET AKSLVELPCP FEGTVTRLHA
     DVGEVVEVGQ PLIDIARPGE ETTDDAGDGS VSAAGSGAGK DGAVGEAAAG PGPLVGSGPV
     ADKATLRSRR RRAPQHAGER RAGERGVEYG GPAARAQRSL PGSVGVPALA KPPVRKLARD
     LGVDLRDVPA TGPRGEVTRE DLASFADKRL GTYRSSAPAA SSEVPRGAVA ASFGAGMHNG
     VSAEPPAGEV TVVPVRGVRK ATAEAMVRSA FSAPHVSLFV DVDATRTMEF VRRLKASRDF
     EGVKVTPLLV VAKAVMWAAQ RNPEINSTWV ETESGAEIHQ KGYINLGIAA STDRGLIVPN
     IKNADELSLK ELAIALNDLA LNARDGKTQP ADMRDGTISI TNVGTLGIDT GTPIINPPEA
     GIVAFGTVRE RPWVVDGAVV PRYVTTVGGS FDHRIVDGDK CAVFLADIAA ILEEPALLLD
//
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