ID A0A0Q5PKB0_9SPHN Unreviewed; 450 AA.
AC A0A0Q5PKB0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ASG07_01015 {ECO:0000313|EMBL:KQR87528.1};
OS Sphingomonas sp. Leaf343.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736345 {ECO:0000313|EMBL:KQR87528.1, ECO:0000313|Proteomes:UP000051323};
RN [1] {ECO:0000313|EMBL:KQR87528.1, ECO:0000313|Proteomes:UP000051323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR87528.1,
RC ECO:0000313|Proteomes:UP000051323};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR87528.1, ECO:0000313|Proteomes:UP000051323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf343 {ECO:0000313|EMBL:KQR87528.1,
RC ECO:0000313|Proteomes:UP000051323};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
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:KQR87528.1}.
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DR EMBL; LMPG01000001; KQR87528.1; -; Genomic_DNA.
DR RefSeq; WP_055840968.1; NZ_LMPG01000001.1.
DR AlphaFoldDB; A0A0Q5PKB0; -.
DR STRING; 1736345.ASG07_01015; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000051323; Unassembled WGS sequence.
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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000051323};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 163..198
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 101..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 48307 MW; D4CBCBA2B2E9789B CRC64;
MARFTFRLPD IGEGIAEAEI VAWHVRVGER VEEDQNIADM MTDKATVEME SPVSGVVVEL
AGEVGDQVAI GAALVVIETD VDASAEEAPA LGPVDVELKA APASREQEEV AEQYEAENPG
VEEVVASPAP APMTADPARS GDQGGSARPT PHAPRSERAE AVLASPAVRA RAKDLGVDLS
QVKSESDRIR HSDLDAFLRY GSDQGYAAPG ASRARPDEAI RVIGMRRKIA ENMAAAKRNI
PHFTYVDEID VTELERVRAD LNDNRGNRPK LTLLPLMIVA MCRTLPEFPM LNARYDDEAG
VVTRHGRVHV GMAAQTDAGL TVPVIRDAQD RNVWQLATEI GRLADAARAG KLKPDELGGG
TITVTSLGPL GGIATTPVIN RPEVAIIGPN KIVERPVFRP NGRGGDDIVR AKLMNLSISC
DHRVVDGWDA ASYVQALKKM LETPVLLFAD
//
