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Database: UniProt
Entry: Q7MDL3_VIBVY
LinkDB: Q7MDL3_VIBVY
Original site: Q7MDL3_VIBVY 
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
//
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