ID Q14PD7_SPICI Unreviewed; 427 AA.
AC Q14PD7;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:CAK98642.1};
GN ORFNames=GL982_02060 {ECO:0000313|EMBL:QIA72527.1}, SCITRI_00411
GN {ECO:0000313|EMBL:APE74316.1}, SPICI03_177
GN {ECO:0000313|EMBL:CAK98642.1};
OS Spiroplasma citri.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=2133 {ECO:0000313|EMBL:CAK98642.1};
RN [1] {ECO:0000313|EMBL:CAK98642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GII3-3X {ECO:0000313|EMBL:CAK98642.1};
RA Carle P., Saillard C., Carrere N., Carrere S., Duret S., Eveillard S.,
RA Gaurivaud P., Gourgues G., Gouzy J., Salar P., Verdin E., Breton M.,
RA Blanchard A., Laigret F., Bove J.M., Renaudin J., Foissac X.;
RT "Partial chromosome sequence of Spiroplasma citri reveals extensive viral
RT invasion and important gene decay.";
RL Appl. Environ. Microbiol. 76:3420-3426(2010).
RN [2] {ECO:0000313|EMBL:APE74316.1, ECO:0000313|Proteomes:UP000183717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R8-A2 {ECO:0000313|EMBL:APE74316.1,
RC ECO:0000313|Proteomes:UP000183717};
RA Davis R.E., Shao J., Gasparich G., Gaynor B., Donofrio N.;
RT "Complete Genome Sequence of Spiroplasma citri R8A2.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QIA72527.1, ECO:0000313|Proteomes:UP000464221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BLH-13 {ECO:0000313|EMBL:QIA72527.1,
RC ECO:0000313|Proteomes:UP000464221};
RA Yokomi R., Chen J., Rattner R., Selvaraj V., Maheshwari Y., Osman F.,
RA Vidalakis G.;
RT "Whole genome sequencing and comparative genomics analyses of six strains
RT of Spiroplasma citri.";
RL Submitted (JAN-2020) 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; CP013197; APE74316.1; -; Genomic_DNA.
DR EMBL; AM285304; CAK98642.1; -; Genomic_DNA.
DR EMBL; CP047428; QIA72527.1; -; Genomic_DNA.
DR RefSeq; WP_071937003.1; NZ_CP096807.1.
DR AlphaFoldDB; Q14PD7; -.
DR STRING; 2133.SCITRI_00411; -.
DR GeneID; 54238342; -.
DR KEGG; sck:SCITRI_00411; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000183717; Chromosome.
DR Proteomes; UP000464221; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:CAK98642.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:CAK98642.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:CAK98642.1}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 136..173
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 427 AA; 45840 MW; 7C6093077A2D2CB2 CRC64;
MVKFKFADIG EGLTEGKVAK IMIEVGDKIK DGVEMFAVET DKVNTEIYAP CDGIVSKINM
AVGDTIYVGD VVVEIDDGTA GDSPAPATSE QPTTVPVEEE KAAGVVGAVS ISNTVLAPRH
LPNNGSANVD SNKNVLSTPI VRKMAADLKI DLTKIQGSGQ NGKIMKADLV QGAKSTTTGP
TLSTMPINIP QINATGAVRR EAMSPIRKAI AKQMTLSKTV IAEATLMKNI DVTKLIEIRA
QLKGQAEQQG VKLTYMPFFM KACAIALKDF PILNAAYDQE QQEIIFKDYY NIGMATDTPT
GLMVPVVKGV DQLNIMQIAK MINDLATKTR ERKLKPDEMK DGTFTITNFG SAGIEFATPV
INFPEVAILG VGIIKKAPVI NKNNEIEISS ILPLSLTIDH RLIDGADGGR FLARVTELLE
SPALLLL
//
