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Database: UniProt
Entry: A4BYX9_9FLAO
LinkDB: A4BYX9_9FLAO
Original site: A4BYX9_9FLAO 
ID   A4BYX9_9FLAO            Unreviewed;       552 AA.
AC   A4BYX9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 81.
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=PI23P_07100 {ECO:0000313|EMBL:EAR12372.1};
OS   Polaribacter irgensii 23-P.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR12372.1, ECO:0000313|Proteomes:UP000003053};
RN   [1] {ECO:0000313|EMBL:EAR12372.1, ECO:0000313|Proteomes:UP000003053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=23-P {ECO:0000313|EMBL:EAR12372.1,
RC   ECO:0000313|Proteomes:UP000003053};
RA   Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:ARBA00000925};
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:EAR12372.1}.
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DR   EMBL; AAOG01000002; EAR12372.1; -; Genomic_DNA.
DR   RefSeq; WP_004570040.1; NZ_CH724148.1.
DR   AlphaFoldDB; A4BYX9; -.
DR   STRING; 313594.PI23P_07100; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_10; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000003053; Unassembled WGS sequence.
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; 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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:EAR12372.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003053};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          124..199
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          249..286
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          92..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   552 AA;  58899 MW;  2C598B27888AB1A9 CRC64;
     MATVINMPRL SDTMEEGVVA KWLKNVGDKI EEGDILAEIE TDKATMEFES FYEGTLLHIG
     IPEGGSSPVD VLLAVIGEEG EDISAIINRT ETDAQTEVPA ETEKEDAKEV TSSPESAGTI
     PEGVEIITMP RLSDTMTDGT VAAWLKKVGD VVAEGDILAE IETDKATMEF ECFYEGTILY
     IGVQEGETAP VDSLLTIIGP AGTDVTAIVA NGGASTSAEK TTEKPTDTVD TVKEEEEVPV
     IHNNNTRIFA SPLAKKIAAD KGINLAVVKG SGENGRIIKK DIENYTPAAA PIATPVKVQA
     PVVPVEEISQ PEPTEAPVMR FVAAGEEKSE EIKNSQMRKA IAKSLGASKF SAPDFSLNIE
     VHMDSAMESR KTINSIPNTK VSFNDMVVKA CAMALQKHPQ VNTSWTDNNT IYHSHIHVGV
     AVAVADGLLV PVVKHTNEMS LTQIGASVRD LAGKARNKKI SPAEMQGSTF TVSNLGMFGI
     ENFTSIINQP NSAILSVGAI VEKPVVKNGQ IVVGNTMKLT LTCDHRTVDG AVGAQFLQTL
     KTFIENPVTM LA
//
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