GenomeNet

Database: UniProt
Entry: K9SF65_9CYAN
LinkDB: K9SF65_9CYAN
Original site: K9SF65_9CYAN 
ID   K9SF65_9CYAN            Unreviewed;       441 AA.
AC   K9SF65;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=Pse7367_0465 {ECO:0000313|EMBL:AFY68775.1};
OS   Pseudanabaena sp. PCC 7367.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC   Pseudanabaenaceae; Pseudanabaena.
OX   NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY68775.1, ECO:0000313|Proteomes:UP000010386};
RN   [1] {ECO:0000313|EMBL:AFY68775.1, ECO:0000313|Proteomes:UP000010386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY68775.1,
RC   ECO:0000313|Proteomes:UP000010386};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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; CP003592; AFY68775.1; -; Genomic_DNA.
DR   RefSeq; WP_015163749.1; NC_019701.1.
DR   AlphaFoldDB; K9SF65; -.
DR   STRING; 82654.Pse7367_0465; -.
DR   KEGG; pseu:Pse7367_0465; -.
DR   PATRIC; fig|82654.3.peg.534; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_3; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000010386; 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   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010386};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          143..180
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          88..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  45738 MW;  2EFD0C0690E637F4 CRC64;
     MIHEIFMPAL SSTMTEGKIT SWVKSLGDKV EKGETVVIVE SDKADMDVET FYEGYLGAIA
     VPEGEVAPVG AAIAYVAETE AEIEAAKQKA AQSTTAPSAA PAATNNASSA SSTSNNASAS
     SPEAATTTTT IAAPARKKGD RIIASPRAKK LAKANNLDLG VINGTGPNGR ITAADVEARL
     KPSTPSASAP ALPAQPASAI VATTPPAIVA VPTPAPATAT VQPLSTFQNA VIRNMNWSLA
     VPTYHVAYSI TTTALDALYK QIKPKGVTMT ALLAKAVAIT LQKHPLLNAS YSDQGIAYKS
     DINVAVAVAM DDGGLITPVL PKADQIDIYS LSRHWKELVG KARAKQLQPD EYSTGTFTIS
     NLGMFGVDSF DAILPPGTGA ILAIGGSKPQ PVITADGAIA IRSQMKVNIT CDHRVIYGAH
     AAQFLQDLAK LIETNAQSLV L
//
DBGET integrated database retrieval system