ID R9GPW4_9SPHI Unreviewed; 563 AA.
AC R9GPW4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=ADIARSV_3078 {ECO:0000313|EMBL:EOR93738.1};
OS Arcticibacter svalbardensis MN12-7.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR93738.1, ECO:0000313|Proteomes:UP000014174};
RN [1] {ECO:0000313|EMBL:EOR93738.1, ECO:0000313|Proteomes:UP000014174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MN12-7 {ECO:0000313|EMBL:EOR93738.1,
RC ECO:0000313|Proteomes:UP000014174};
RX PubMed=23846277;
RA Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA Kumar Pinnaka A.;
RT "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT Sample.";
RL Genome Announc. 1:E00484-13(2013).
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}.
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:EOR93738.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AQPN01000105; EOR93738.1; -; Genomic_DNA.
DR RefSeq; WP_016196308.1; NZ_AQPN01000105.1.
DR AlphaFoldDB; R9GPW4; -.
DR STRING; 1150600.ADIARSV_3078; -.
DR PATRIC; fig|1150600.3.peg.3047; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000014174; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; 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; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:EOR93738.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:EOR93738.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014174};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EOR93738.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 141..216
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 265..302
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 89..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 59428 MW; 177B360FEB291A46 CRC64;
MAEVVKMPKM SDTMTDGVIA KWHKKVGDKV STGDLIAEVE TDKATMDFES YQEGTLLYIG
AEEGSTVPID AVIAVLGAEG EDYKAALEAA GAGESKPEAA KEDVKQADST AETNDKPETV
TPDNDADQTE GEAVDPESVG ATIIRMPLLS DTMTEGVIAQ WNKKVGDVVK SDDNLADVET
DKATMEVTAY AEGILLYIGV EKGQAAKVND IIAIVGKEGT DVQALLRGGK PKAAPAAGTT
EAEKTEAPKE ETAPAGSSDA NARVKASPLA KKIAKDKGID LSQVKGSAEG GRIVKKDIES
YTPAAKAPDA PAPAAPAPAK EGKPAAPAPV IPVFVGEEKF TEKPVTQMRK TIGKRLSDSL
FTAPHFYVTM SIDMDSAITA RGKMNEFSPV KISFNDIVLK AVAAALKQHP NLNSSWRGDK
IRYNEHINIG VAVAVDEGLL VPVIRFADGK SLSHISAEVK DFAQKAKAKK LQPSDWEGST
FTISNLGMFG VDEFTAIINT PDACILAIGG IQQIPVVKNG AVVPGNVMKV TLSCDHRVVD
GAQGAAFLQT LKLLIEEPVR LLV
//
