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Database: UniProt
Entry: F6FSB8_ISOV2
LinkDB: F6FSB8_ISOV2
Original site: F6FSB8_ISOV2 
ID   F6FSB8_ISOV2            Unreviewed;       492 AA.
AC   F6FSB8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=Isova_0255 {ECO:0000313|EMBL:AEG43059.1};
OS   Isoptericola variabilis (strain 225).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN   [1] {ECO:0000313|EMBL:AEG43059.1, ECO:0000313|Proteomes:UP000009236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Isoptericola variabilis 225.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002810; AEG43059.1; -; Genomic_DNA.
DR   RefSeq; WP_013837454.1; NC_015588.1.
DR   AlphaFoldDB; F6FSB8; -.
DR   STRING; 743718.Isova_0255; -.
DR   KEGG; iva:Isova_0255; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_0_11; -.
DR   OMA; TIKQKPW; -.
DR   Proteomes; UP000009236; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AEG43059.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009236};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AEG43059.1}.
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          195..232
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          78..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  51463 MW;  E7D092703504FA2B CRC64;
     MSTQRFPLPD VGEGLTEAEI VEWRVAEGDT VTVNQVVVEI ETAKSLVELP SPWAGTVTAL
     LAEEGTTVAV GTPIIEIATG SSPAPASPEL SGSGGGMDQP EPDNSAEKGS GSVLVGYGTG
     EGAAGRRRRR RATATPAPTP APTPAPTPAP ELSGADRGIP RREPDSSQDA GGPAIAKAMA
     SVPVSEGATS GTRVLAKPPV RKLAKDLGID LGSVHPTGPG GIVTREDVVA RAEASKPQTL
     ATYPDDDQPW LSTGTVSPDG RQTRVPVKSV RKRTAEAMVA SAFTAPHVTV FHTVDVTRTM
     RLVERLKADR DFADVRVTPL LIAAKAVLLA VRRHPEINAS WDDAAQEIVY KHYVNLGIAA
     ATPRGLVVPN IKDAHALDLL GLARAIQDLT STARAGRTTP AAMSDGTFTI TNVGVFGIDT
     GTPILNPGEA GILAFGAIRE QPWVHKGKVK PRWVTQLALS FDHRLVDGAL GARFLSDVAR
     VLEDPARGLV WG
//
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