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
//