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Database: UniProt
Entry: Q2JME8_SYNJB
LinkDB: Q2JME8_SYNJB
Original site: Q2JME8_SYNJB 
ID   Q2JME8_SYNJB            Unreviewed;       424 AA.
AC   Q2JME8;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 106.
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=CYB_1116 {ECO:0000313|EMBL:ABD02093.1};
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD02093.1, ECO:0000313|Proteomes:UP000001938};
RN   [1] {ECO:0000313|EMBL:ABD02093.1, ECO:0000313|Proteomes:UP000001938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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:ARBA00000925};
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; CP000240; ABD02093.1; -; Genomic_DNA.
DR   RefSeq; WP_011432746.1; NC_007776.1.
DR   AlphaFoldDB; Q2JME8; -.
DR   STRING; 321332.CYB_1116; -.
DR   KEGG; cyb:CYB_1116; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_3; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000001938; Chromosome.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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:ABD02093.1};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001938};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ABD02093.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          139..176
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          94..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  44362 MW;  96A0110A43F99524 CRC64;
     MIHELSMPAL SSTMETGKIV TWLKNPGDRV EKGENILVVE SDKADMDVES FHSGILASIL
     VPAGESAPVG APIALIAESE AEVAQAQEKA KALAAGVTPA APPSADRASA AQPTSPAPAA
     TPTSTLPNGS DGAGSQRIVA SPRAKKLAES LGIDLRTVRG SGPNGRIIAE DVERAAALSA
     PAVAAPSAPA PAPPTPVAVP LGETVPLSTL QAAVVRNMNA SLGVPVFHVG YTITTDSLDH
     LYQQVKPKGV TLTALLVKAV AMTLEKHPLL NASYTEGGIH YKSDINIAVA VAMEDGGLIT
     PVLKQANRLD LYEISRRWKD LVERARRKQL QPEEYNSGTF TLSNLGMFGV DRFDAILPPN
     QGSILAIGAS RPTVVATPEK AIAIRSQMQV NLTCDHRVIY GAHAAAFLQD LAQLIEHKVG
     SLTL
//
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