ID   G7T9Q1_XANOB            Unreviewed;       503 AA.
AC   G7T9Q1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=XOC_0489 {ECO:0000313|EMBL:AEQ94710.1};
OS   Xanthomonas oryzae pv. oryzicola (strain BLS256).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=383407 {ECO:0000313|EMBL:AEQ94710.1, ECO:0000313|Proteomes:UP000008851};
RN   [1] {ECO:0000313|EMBL:AEQ94710.1, ECO:0000313|Proteomes:UP000008851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BLS256 {ECO:0000313|EMBL:AEQ94710.1,
RC   ECO:0000313|Proteomes:UP000008851};
RX   PubMed=21784931; DOI=10.1128/JB.05262-11;
RA   Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA   Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA   Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA   Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA   Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA   Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA   Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA   Leach J.E., White F.F., Salzberg S.L.;
RT   "Two new complete genome sequences offer insight into host and tissue
RT   specificity of plant pathogenic Xanthomonas spp.";
RL   J. Bacteriol. 193:5450-5464(2011).
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; CP003057; AEQ94710.1; -; Genomic_DNA.
DR   RefSeq; WP_014501671.1; NC_017267.2.
DR   AlphaFoldDB; G7T9Q1; -.
DR   KEGG; xor:XOC_0489; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_6; -.
DR   Proteomes; UP000008851; Chromosome.
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: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.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AEQ94710.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AEQ94710.1}.
FT   DOMAIN          4..79
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          169..206
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          83..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  51921 MW;  808032089752855F CRC64;
     MSDNKNFHLP DLGEGLPDAT IVEWFVKEGD TVRLDDPLVS METAKAVVEV PSPFSGTVLK
     LAGAAGDVIV TGSVLAQFAL DASQPQRADG QDTGHSHGPV PTHSPTPSTG DSAAGPTARV
     VASDNGGESA DADAGDGSSD RDDAGTVVGA MQSSNAVQSE QAIAVGGVRA MPVVRALARK
     LRVDLAQVRA TGPDGTVTLA DVKQAAAADT ARPSPGAQGA PTSPARGSGG PVADSGRARG
     VADGGRDRPE PATVLPPAGE GARRPDEGST ARSPLSASGK PMRTQSPGTS VKGQPEQLKG
     VRRNMARVMA DAHTKVVPTT LNDDADLHAW HPGNDVTVRL VRGIVRACQA VPALNAWFDG
     DALSRTLHNQ IDIGIAVDTE EGLFVPALRN ADMLDAHGIH ESINRLRQQV ENRSIAASEL
     SGYTISLSNF GMFAGRYATP VVVPPCVAIV AAGRARYQLT PVMGGVETHK VMPLSLTFDH
     RAATGGEAAR FLRALLDDLA LAN
//