ID A0A1S9B329_9BACT Unreviewed; 467 AA.
AC A0A1S9B329;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=B0919_05180 {ECO:0000313|EMBL:OON70133.1};
OS Hymenobacter sp. CRA2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1955620 {ECO:0000313|EMBL:OON70133.1, ECO:0000313|Proteomes:UP000189843};
RN [1] {ECO:0000313|EMBL:OON70133.1, ECO:0000313|Proteomes:UP000189843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRA2 {ECO:0000313|EMBL:OON70133.1,
RC ECO:0000313|Proteomes:UP000189843};
RA Kabwe M.H., Vikram S., Govender N., Bezuidt O., Makhalanyane T.P.;
RT "Draft genome sequence of Hymenobacter sp. CRA2 isolated from the shrubland
RT biome in South Africa.";
RL Submitted (FEB-2017) 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:OON70133.1}.
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DR EMBL; MVBC01000002; OON70133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9B329; -.
DR STRING; 1955620.B0919_05180; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000189843; 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; 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; 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; PS00189; LIPOYL; 1.
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:UP000189843};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 134..174
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 184..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 49201 MW; A65366EC8E72635D CRC64;
MARVEMVMPK MGESIMEGTV LKWLKQVGDT IEQDESVLEV ATDKVDTEVP AIHAGVLQQI
LVEEGQVVAV GAPIAIVETD AAAASNGQAP AAAPAAAQET QEAEAAAAVP FVPNAAAAAN
AGGAQLGEAL PGRFYSPLVL NIAREEGISM ADLERVPGTG QGGRVTKKDI LDYVANRGQQ
AAPAAAPAAS APQAPAQPAA QAQPAAPAPA APAPVAQQAA APASKPAPSV SGNQELVEMD
RMRKMIAQRM VDSKRISPHV TSFVEADVTE IVNWRNKHKD AYKKREGENL TFTPIFVQAI
ARAIQDFPNI NVSVDGDYII KKRDINVGVA VALPSGNLIV PVIHGADQLN LNGLTKRVND
LANRARANKL KPEDLEGGTY TLSNVGSFGN VMGTPIIMQP QVAIMAVGAI KKKPAVIETP
QGDLIGVRHF MFLSHSYDHR VVDGSLGGMF VRRVADYLEQ FDPNTTI
//
