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Database: UniProt
Entry: A0A0Q8Q2E2_9SPHN
LinkDB: A0A0Q8Q2E2_9SPHN
Original site: A0A0Q8Q2E2_9SPHN 
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
//
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