ID   B1WU36_CROS5            Unreviewed;       433 AA.
AC   B1WU36;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   Name=pdhC {ECO:0000313|EMBL:ACB52098.1};
GN   OrderedLocusNames=cce_2750 {ECO:0000313|EMBL:ACB52098.1};
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB52098.1, ECO:0000313|Proteomes:UP000001203};
RN   [1] {ECO:0000313|EMBL:ACB52098.1, ECO:0000313|Proteomes:UP000001203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68 {ECO:0000313|Proteomes:UP000001203};
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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; CP000806; ACB52098.1; -; Genomic_DNA.
DR   RefSeq; WP_009544565.1; NC_010546.1.
DR   AlphaFoldDB; B1WU36; -.
DR   STRING; 43989.cce_2750; -.
DR   KEGG; cyt:cce_2750; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_3; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000001203; Chromosome circular.
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   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:ACB52098.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001203};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          136..173
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          84..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..203
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  45762 MW;  885D70401B199952 CRC64;
     MIHDIFMPAL SSTMTEGKIV SWVKSPGDKV SKGETVVVVE SDKADMDVES FYDGYLATIL
     VEAGQEAPVG DAIALIAETE EEIAQAKAKG SSGLSTPPPE SPPKKEEKQP SQAPATTATA
     TATAPSSTNG KSNRIVASPR AKKLAKQLGI SLNSVEGSGP YGRIVAEDIE KAAGKTPTPP
     SIPTQTTQPP KPTQTPTVAP ATPTPAPVTA GETVPLNTLQ KAVVQNMVAT LQVPTFHVGY
     TITTDELDKL YKKLKPKGVT MTALLAKAVA VTLEKHPLVN ANYSEQGIRY PQSINIAIAV
     AMPDGGLITP VLQNADKVDI YSLSRTWKDL VDRARAKQLQ PEEYNSGTFT LSNLGMFGVD
     RFDAILPPGQ GSILAIGASS PQVVATPDGL LGVKRQMAVN ITCDHRIIYG SHAAAFLQEF
     ANLLETDVQS LTM
//