ID A0A0Q8Q2E2_9SPHN Unreviewed; 433 AA.
AC A0A0Q8Q2E2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ASE00_18815 {ECO:0000313|EMBL:KRB79763.1};
OS Sphingomonas sp. Root710.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB79763.1, ECO:0000313|Proteomes:UP000051854};
RN [1] {ECO:0000313|EMBL:KRB79763.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB79763.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB79763.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB79763.1,
RC ECO:0000313|Proteomes:UP000051854};
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:KRB79763.1}.
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DR EMBL; LMIB01000017; KRB79763.1; -; Genomic_DNA.
DR RefSeq; WP_056383498.1; NZ_LMIB01000017.1.
DR AlphaFoldDB; A0A0Q8Q2E2; -.
DR STRING; 1736594.ASE00_18815; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000051854; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000051854};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KRB79763.1}.
FT DOMAIN 3..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 123..160
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 433 AA; 45484 MW; C52DB376A08859B6 CRC64;
MGYIDILVPA EQEGTKAIVR SWLKRVGERV EENDPLVELE TDKVTQEVPA PATGIIEEII
LQSDAEAEPG ALLGRLRIGA AVDGAEAPAA AGDAGAAPGE VALAPAPASL PAAGGGTNAM
AQALSPSVRR AVRTHNIDPA TITGTGRAGR ITRADVDKAV AARAEPSVPV ATVVAVPAPQ
PASRPDAPAP TGGVRSIPHD RMRLAIAQNM LNSVTVAPHV TAMFECDFSA IMAHRRKHKD
AFAKDGANLT FTAYFIAACV AAMKAAPAIN SRWYDDRLDI FDDVNIGIGT ALGDKGLVVP
VVGQCQELSL LGIAKRLTDM VERARANKLT PADMRGGTFT ISNHGVSGSL FATPIIISQP
QSAILGIGKT EKRVVVREID GVDTIQIRPL AYVSLTIDHR VVDGHQTNGW LSRFVEVIET
WPVDGSHAFC ALS
//