ID C6M314_NEISI Unreviewed; 250 AA.
AC C6M314;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=dihydrolipoyllysine-residue acetyltransferase {ECO:0000256|ARBA:ARBA00013114};
DE EC=2.3.1.12 {ECO:0000256|ARBA:ARBA00013114};
GN ORFNames=NEISICOT_00905 {ECO:0000313|EMBL:EET45278.1};
OS Neisseria sicca ATCC 29256.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=547045 {ECO:0000313|EMBL:EET45278.1, ECO:0000313|Proteomes:UP000005365};
RN [1] {ECO:0000313|EMBL:EET45278.1, ECO:0000313|Proteomes:UP000005365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29256 {ECO:0000313|EMBL:EET45278.1,
RC ECO:0000313|Proteomes:UP000005365};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
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:EET45278.1}.
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DR EMBL; ACKO02000004; EET45278.1; -; Genomic_DNA.
DR AlphaFoldDB; C6M314; -.
DR eggNOG; COG0508; Bacteria.
DR Proteomes; UP000005365; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
PE 4: Predicted;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Transferase {ECO:0000313|EMBL:EET45278.1}.
FT DOMAIN 3..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 110..184
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 250 AA; 25934 MW; C35FBAE3ED482B8F CRC64;
MSIVEIKVPD IGGHENVDII AVEVKAGDTI AVDDTLITLE TDKATMDVPA DAAGVVKEVK
VKVGDKISEG GVILTVETGA AAAEAAPAPV AEAQPAPAAA PAAAPAGGAT VQVAVPDIGG
HTDVDVIAVE VKVGDTVAED DTLITLETDK ATMDVPCTAA GVVKAVFLKV GDKVSEGTAI
YRSGKPPVLP PLPLLLKPLH RQQHPLRLLR LPPLRLLLPL LHLPQPKSTK PLSPKHTRVL
PHANWRANWA
//
