ID Q7MDL3_VIBVY Unreviewed; 381 AA.
AC Q7MDL3;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 123.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN OrderedLocusNames=VVA1023 {ECO:0000313|EMBL:BAC97049.1};
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC97049.1, ECO:0000313|Proteomes:UP000002675};
RN [1] {ECO:0000313|EMBL:BAC97049.1, ECO:0000313|Proteomes:UP000002675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016 {ECO:0000313|EMBL:BAC97049.1,
RC ECO:0000313|Proteomes:UP000002675};
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA Tsai S.F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; BA000038; BAC97049.1; -; Genomic_DNA.
DR RefSeq; WP_011152307.1; NC_005140.1.
DR AlphaFoldDB; Q7MDL3; -.
DR STRING; 672.VV93_v1c39660; -.
DR KEGG; vvy:VVA1023; -.
DR PATRIC; fig|196600.6.peg.4192; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OMA; RAMAQNM; -.
DR Proteomes; UP000002675; Chromosome II.
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:SF12; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BAC97049.1}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 381 AA; 41340 MW; 5776EF6367CF4B53 CRC64;
MKTFILPDLG EGLAESEIIK WHVSVGDKVE VDQVILTVET AKATVDVPAP WAGTIITRHG
NEGDVVNIGA LLLEIEDGDV ATNSDKKVQK REDAATVVGH VSNQMHQVKV DDFWIGGNQN
HTTEKRVTAL PSARLLAQKL GVNLEMVSGT GPSGLIMDHD VYDEAGKQRP GTEVLKGARR
TMMTTMTESH LQVAAVTITE EALLEHWSSQ EDITVRLVQA VVYACQQEPA LNAWFDADTV
TRCVHHTVNI GVAVDSAHGL YVPVMRHADE FSPDDIRSWI NQTVSGIRER KIGREQLQHA
TITLSNFGAI AGIYATPVVS PPQVAIVGAG RIIEKVVLRE GKAVAVKAMP LSITFDHRAC
TGGEAARFTK ALAEHLRKPS V
//