ID A0A031JXU2_9SPHN Unreviewed; 478 AA.
AC A0A031JXU2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=BES08_24665 {ECO:0000313|EMBL:AOR79934.1}, BV97_02853
GN {ECO:0000313|EMBL:EZP81192.1};
OS Novosphingobium resinovorum.
OG Plasmid pSA1 {ECO:0000313|EMBL:AOR79934.1,
OG ECO:0000313|Proteomes:UP000094626}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=158500 {ECO:0000313|EMBL:EZP81192.1, ECO:0000313|Proteomes:UP000024329};
RN [1] {ECO:0000313|EMBL:EZP81192.1, ECO:0000313|Proteomes:UP000024329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KF1 {ECO:0000313|EMBL:EZP81192.1,
RC ECO:0000313|Proteomes:UP000024329};
RA Gan H.M., Gan H.Y., Chew T.H., Savka M.A.;
RT "Whole genome sequence of Novosphingobium resinovorum KF1.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOR79934.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1 {ECO:0000313|EMBL:AOR79934.1};
RC PLASMID=pSA1 {ECO:0000313|EMBL:AOR79934.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000094626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1 {ECO:0000313|Proteomes:UP000094626};
RX PubMed=27851894; DOI=10.1016/j.jbiotec.2016.11.013;
RA Hegedus B., Kos P.B., Balint B., Maroti G., Gan H.M., Perei K., Rakhely G.;
RT "Complete genome sequence of Novosphingobium resinovorum SA1, a versatile
RT xenobiotic-degrading bacterium capable of utilizing sulfanilic acid.";
RL J. Biotechnol. 241:76-80(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00043782};
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; CP017076; AOR79934.1; -; Genomic_DNA.
DR EMBL; JFYZ01000013; EZP81192.1; -; Genomic_DNA.
DR RefSeq; WP_036526580.1; NZ_JFYZ01000013.1.
DR AlphaFoldDB; A0A031JXU2; -.
DR KEGG; nre:BES08_24665; -.
DR PATRIC; fig|158500.4.peg.2920; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000024329; Unassembled WGS sequence.
DR Proteomes; UP000094626; Plasmid pSA1.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; 2.
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; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 2.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Plasmid {ECO:0000313|EMBL:AOR79934.1};
KW Pyruvate {ECO:0000313|EMBL:EZP81192.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EZP81192.1}.
FT DOMAIN 4..79
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 135..172
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT DOMAIN 193..230
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 100..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 49575 MW; 938EE41B0301C623 CRC64;
MAKLTPFTMP KWGIEMAEGT IADWMVAENA PFERGAVLTL VETDKITNEI EADKDGRFVR
ILAEAGQTYP VGALLAVLSD GGEASAAEID AVIAAFRPSE SGFGPDGDDA SGPAPAAPAV
EPEKPAAPPV PEGLAISPAA LAEAQRLGVD LATVTGTGRG RRIFAQDVHQ AARPEAKPQL
VGVFAATPDS PVLSTPVARR LGALHGLDLA TIKGSGARGK VRRDDVLAIV QQAAPTPAPA
SAAPAPVAAA PAPRPASGNV DVMPMSSMRR TIARRLTEAK QQIPHFYVRR RVRADRLLAL
RASLGPDKPS VNDFIVKACA LALMEIPAVN VQVHGNDIHR FGSADVAVAV ATDKGLVTPI
VFGADDLSVA AIGAVMKGLA QRARSGKLKP EEFTGGSFSL SNLGGFGVEQ FDAIINPPQG
AILAVGTARP EPIDDDGAIR IVPVLHLSLS CDHRAIDGAD GGRFMAALAN LIEQPHLL
//
