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Database: UniProt
Entry: H0E659_9ACTN
LinkDB: H0E659_9ACTN
Original site: H0E659_9ACTN 
ID   H0E659_9ACTN            Unreviewed;       422 AA.
AC   H0E659;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   03-MAY-2023, entry version 48.
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=PAI11_23090 {ECO:0000313|EMBL:EHN10828.1};
OS   Patulibacter medicamentivorans.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Patulibacteraceae; Patulibacter.
OX   NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN10828.1, ECO:0000313|Proteomes:UP000005143};
RN   [1] {ECO:0000313|EMBL:EHN10828.1, ECO:0000313|Proteomes:UP000005143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I11 {ECO:0000313|EMBL:EHN10828.1,
RC   ECO:0000313|Proteomes:UP000005143};
RX   PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA   Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA   Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT   "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT   strain I11.";
RL   Biodegradation 24:615-630(2013).
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   -!- 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:EHN10828.1}.
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DR   EMBL; AGUD01000200; EHN10828.1; -; Genomic_DNA.
DR   RefSeq; WP_007575091.1; NZ_AGUD01000200.1.
DR   AlphaFoldDB; H0E659; -.
DR   PATRIC; fig|1097667.3.peg.2290; -.
DR   Proteomes; UP000005143; Unassembled WGS sequence.
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; 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; 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; 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:EHN10828.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EHN10828.1}.
FT   DOMAIN          1..71
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          132..169
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          80..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  42426 MW;  C090BE0C62DA4D20 CRC64;
     MPQLGLEVTE GVVVELFVLP GATVTKDLPL LELETDKAST EVVAPRDGVL RAWSVGVGDA
     VPVGDVLALI ADTADEPLEA ESSAVDTAAA EAGVPPGADD ARAAGVGAAV SGASGSGSPG
     AGDAPDGAPR RRVAPVARRA AAALGVSLAA VEGTGPRGRV TLDDVRRAAA AESAPATSAG
     PLAAPAPGAA SGTAEELPIS AIRRAIARRM RASQLIPQYQ LQRDIDASHL LAQKAAQAEG
     RNAAARIGVN DLLVQALAET VRRHPELAVT WVDGDDGPRM IRSGADGVGL AVASDKGLVV
     PVIRDPQTAG LAAIAEQRQR LVAAARGGTL GLDEMAGAAI TLSNLGGFGV DRFTAMLNPG
     ESAIVAVGRT VERVVPRRRG TAVVPVLAVT VSFDHRVIDG AVGAAALGTL AALLEGDLAW
     RP
//
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