ID A0A1J6WYZ1_9BACI Unreviewed; 440 AA.
AC A0A1J6WYZ1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BHE18_08740 {ECO:0000313|EMBL:OIU71121.1};
OS Rossellomorea aquimaris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189382 {ECO:0000313|EMBL:OIU71121.1, ECO:0000313|Proteomes:UP000182062};
RN [1] {ECO:0000313|EMBL:OIU71121.1, ECO:0000313|Proteomes:UP000182062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAMM {ECO:0000313|EMBL:OIU71121.1,
RC ECO:0000313|Proteomes:UP000182062};
RA Waghmode S.R., Suryavanshi M.V.;
RT "Bacillus aquimaris SAMM genome sequence reveals colonization and
RT biosurfactant production capacities.";
RL Submitted (SEP-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:OIU71121.1}.
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DR EMBL; MINN01000085; OIU71121.1; -; Genomic_DNA.
DR RefSeq; WP_071618512.1; NZ_MINN01000085.1.
DR AlphaFoldDB; A0A1J6WYZ1; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000182062; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000182062};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 119..156
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 79..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 47648 MW; 4573F2C039C3C6E8 CRC64;
MGIEKMKMPQ LGESVTEGTI SKWLVSPGDT VNKYDPIAEV QTDKVNAEVP SSFTGTIKEL
IAEEGDTLEV GEIICSIEVE GAGSEPSEEA PKEEKKETSG EKTPSASNAP KKEDGNKARY
SPAVLKLSQE HDIDLNQVEG TGNGGRITRK DLKKIIESGN IPKAGDAPAA QQPETAPAPQ
QAPAKDEAQP GAAQKQAAPA PNVPVMPGDI EIPVTGVRKA IASNMVRSKH EAPHAWTMME
VDVTNLVEYR NSLKTEFKQR EGFNLTFFAF FVKAVSQALK EFPQINSMWA GDKIIQKKDV
NISIAVATDD ALFVPVIKNA DEKTIKGIAR EITDLAGKVR SGKLKSEDMQ GGTFTVNNTG
SFGSVQSMGI INYPQAAILQ VESIVKRPVV MNNGMIAVRD MVNLCMSLDH RVLDGLVCGR
FLQRIKEILE NTSKENTSVY
//
