ID H3NHS0_9LACT Unreviewed; 571 AA.
AC H3NHS0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=HMPREF9708_00348 {ECO:0000313|EMBL:EHR37719.1};
OS Facklamia languida CCUG 37842.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR37719.1, ECO:0000313|Proteomes:UP000006190};
RN [1] {ECO:0000313|EMBL:EHR37719.1, ECO:0000313|Proteomes:UP000006190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR37719.1,
RC ECO:0000313|Proteomes:UP000006190};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia languida CCUG 37842.";
RL Submitted (JAN-2012) 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:EHR37719.1}.
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DR EMBL; AGEG01000003; EHR37719.1; -; Genomic_DNA.
DR RefSeq; WP_006308291.1; NZ_JH601133.1.
DR AlphaFoldDB; H3NHS0; -.
DR STRING; 883113.HMPREF9708_00348; -.
DR PATRIC; fig|883113.3.peg.352; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_9; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000006190; Unassembled WGS sequence.
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; 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; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000006190};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EHR37719.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 113..188
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 251..288
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 76..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 60847 MW; 83E5D19919ED72DC CRC64;
MAFQFKLPAL GEGIMEGEIV SWAVKEGDTI EEDQTLVEVQ NDKSVEELPS PVAGTITKIL
VQEGTVAHLG EPLVEIDAPG HEDNSEEAAP AQAEEAEAAP AASQPAASGS TAYFQFKLPA
LGEGIMEGEI VSWAVNEGDT IEEDNTIVEV QNDKSVEELP SPVSGVVKKI HVPAGQIAQL
GDVLVEIDSP DHNGQAGDAE AAQAHANAYD DAAAPAEEVP ADPRGESQKQ DTSIEVSQGL
SDEEAKNRRV LAMPSVRKLA RDKGFDITRI PGSGKNGRIT REDVENFNPA ANAGQSAAQQ
PAAPAGQEQA QAAGVEQSAA PASQPAAPAK PFTSSQAERE ERVAMSGTRT AIAQAMVNSK
HTAPHVTLYD EVEVSKLWAH RKKYKEVAAE QDVKLTFLPY VVKALIAAAK KYPVINASID
DVSNEIVYKN YYNIGIATDT DRGLYVPNIK NANTKNMFQI AQEIVDLSSK AHDGSLQMSE
MSEGTITISN IGSAGGKWFS PIINHPEVAI LGFGSIVQQP IVNEEGELAV GRVCKLSLSF
DHRIVDGATA QRALNEVKRF LADPELLLME G
//