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Database: UniProt
Entry: B1VAP9_PHYAS
LinkDB: B1VAP9_PHYAS
Original site: B1VAP9_PHYAS 
ID   B1VAP9_PHYAS            Unreviewed;       407 AA.
AC   B1VAP9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   Name=pdhC {ECO:0000313|EMBL:CAM12022.1};
GN   OrderedLocusNames=PA0688 {ECO:0000313|EMBL:CAM12022.1};
OS   Phytoplasma australiense.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma; 16SrXII (Stolbur group).
OX   NCBI_TaxID=59748 {ECO:0000313|EMBL:CAM12022.1, ECO:0000313|Proteomes:UP000008323};
RN   [1] {ECO:0000313|EMBL:CAM12022.1, ECO:0000313|Proteomes:UP000008323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18359806; DOI=10.1128/JB.01301-07;
RA   Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT   "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT   (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT   and AY-WB.";
RL   J. Bacteriol. 190:3979-3991(2008).
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; AM422018; CAM12022.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1VAP9; -.
DR   STRING; 59748.PA0688; -.
DR   KEGG; pal:PA0688; -.
DR   eggNOG; COG0508; Bacteria.
DR   OMA; TPIFMEA; -.
DR   Proteomes; UP000008323; 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:CAM12022.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:CAM12022.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008323};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CAM12022.1}.
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          116..153
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          79..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   407 AA;  44979 MW;  30502DF407025264 CRC64;
     MFEFKFADVG EGIHEGTITR WFFKKGDSVK KDDVLVKIET DKLDVELTSP ATGTIIKMTH
     KEGDVINVGE TLVLIKEPGD SEIEVKTEKT PSSHTSSKEE KTPSFQPKSN DNQKILATPL
     VRSLAKELGV DLTKVKGTGF GGKILKADIL SNQKQTQTPS PLMTQSSQLT SMDSVAQTEV
     VKISRLRKAI AQKMVLSKSN IPETNLMDEV NITALVNLRK QLKEEAEKQG IKLTFMAFIM
     KAVAIALKEF PLFNASYDEP KEEIIFKKFI NLGIAVDTKD GLIVPNVKNA YPLSLLELAK
     NLQEVVKATI ERKVQLEQLQ NSTFTITNFG SLDISYGTPV INYPEVAILG VGKISKKPIV
     ENNQIVVADM LPLSLAIDHR IIDGADGGRF LKRIKELLKS PTLLFLS
//
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