GenomeNet

Database: UniProt
Entry: F7S3K4_9PROT
LinkDB: F7S3K4_9PROT
Original site: F7S3K4_9PROT 
ID   F7S3K4_9PROT            Unreviewed;        90 AA.
AC   F7S3K4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Pyruvate dehydrogenase subunit beta {ECO:0000313|EMBL:EGO96289.1};
DE            EC=2.3.1.12 {ECO:0000313|EMBL:EGO96289.1};
DE   Flags: Fragment;
GN   ORFNames=APM_0905 {ECO:0000313|EMBL:EGO96289.1};
OS   Acidiphilium sp. PM.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=1043206 {ECO:0000313|EMBL:EGO96289.1, ECO:0000313|Proteomes:UP000004823};
RN   [1] {ECO:0000313|EMBL:EGO96289.1, ECO:0000313|Proteomes:UP000004823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM {ECO:0000313|EMBL:EGO96289.1,
RC   ECO:0000313|Proteomes:UP000004823};
RX   PubMed=21914891; DOI=10.1128/JB.05386-11;
RA   San Martin-Uriz P., Gomez M.J., Arcas A., Bargiela R., Amils R.;
RT   "Draft Genome Sequence of the Electricigen Acidiphilium sp. Strain PM (DSM
RT   24941).";
RL   J. Bacteriol. 193:5585-5586(2011).
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   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGO96289.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFPR01000088; EGO96289.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7S3K4; -.
DR   HOGENOM; CLU_016733_7_6_5; -.
DR   Proteomes; UP000004823; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR045257; E2/Pdx1.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 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|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:EGO96289.1}; Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Pyruvate {ECO:0000313|EMBL:EGO96289.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGO96289.1}.
FT   DOMAIN          2..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   NON_TER         90
FT                   /evidence="ECO:0000313|EMBL:EGO96289.1"
SQ   SEQUENCE   90 AA;  9475 MW;  859ED7594661894D CRC64;
     MTTDVLMPAL SPTMTEGKLA KWLKKVGDRV KAGDVLAEIE TDKATMEVEA VDEGELLRIL
     VDEGTENVAV NTPIAVLGAH GEKAESPSAA
//
DBGET integrated database retrieval system