ID   Q7U8E9_PARMW            Unreviewed;       441 AA.
AC   Q7U8E9;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=SYNW0671 {ECO:0000313|EMBL:CAE07186.1};
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588 {ECO:0000313|EMBL:CAE07186.1, ECO:0000313|Proteomes:UP000001422};
RN   [1] {ECO:0000313|EMBL:CAE07186.1, ECO:0000313|Proteomes:UP000001422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102 {ECO:0000313|EMBL:CAE07186.1,
RC   ECO:0000313|Proteomes:UP000001422};
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F., Land M., Hauser L., Chain P.,
RA   Lamerdin J., Regala W., Allen E.A., McCarren J., Paulsen I., Dufresne A.,
RA   Partensky F., Webb E., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC         + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00043782};
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}.
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DR   EMBL; BX569690; CAE07186.1; -; Genomic_DNA.
DR   RefSeq; WP_011127538.1; NC_005070.1.
DR   AlphaFoldDB; Q7U8E9; -.
DR   STRING; 84588.SYNW0671; -.
DR   KEGG; syw:SYNW0671; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_3; -.
DR   Proteomes; UP000001422; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; IPR045257; E2/Pdx1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF75; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 5 OF PYRUVATE DEHYDROGENASE COMPLEX, CHLOROPLASTIC; 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:CAE07186.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:CAE07186.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001422};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CAE07186.1}.
FT   DOMAIN          3..81
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          142..179
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          95..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..124
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  45168 MW;  45234FB7686FDBC5 CRC64;
     MATHDIFMPA LSSTMTEGKI VEWLKQPGDK VGRGESVLVV ESDKADMDVE SFQDGYLAAV
     LMPAGSTAPV GETIGLIVET EAEIADAQAK ATSAAPAASA PAPTPAPAAV QAPAPTPAPT
     QAPAAPAPVA ASAAPVANGR VVASPRAKKL ASQMGVDLST VRGSGPHGRI QAEDVEQAGG
     QPISVPRVAE GTAAAVAASA APSAAAPSAP AGNSFGRPGD TVAFNTLQGA VNRNMEASLA
     VPCFRVGYTI TTDKLDAFSK LVKPKGVTMT ALLAKAVAVT LARHPQVNAA TTAAGMTYPA
     EVNVAIAVAM EDGGLITPVL RNADRTDLYE MSRQWKDLVK RSRSKQLQPE EYSTGTFTLS
     NLGMFGVDRF DAILPPGTGA ILAVAASRPT VVAGKDGSIA VKRQMQVNLT ADHRVIYGAD
     GAAFLKDLAE LIEHRPESLA L
//