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Database: UniProt
Entry: A0A090WA80_9FLAO
LinkDB: A0A090WA80_9FLAO
Original site: A0A090WA80_9FLAO 
ID   A0A090WA80_9FLAO        Unreviewed;       538 AA.
AC   A0A090WA80;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   ORFNames=JCM19302_2316 {ECO:0000313|EMBL:GAL73093.1}, JCM19538_1595
GN   {ECO:0000313|EMBL:GAL89692.1};
OS   Jejuia pallidilutea.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Jejuia.
OX   NCBI_TaxID=504487 {ECO:0000313|EMBL:GAL73093.1, ECO:0000313|Proteomes:UP000029646};
RN   [1] {ECO:0000313|Proteomes:UP000029646, ECO:0000313|Proteomes:UP000030184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19302 {ECO:0000313|EMBL:GAL73093.1}, JCM 19538
RC   {ECO:0000313|EMBL:GAL89692.1, ECO:0000313|Proteomes:UP000030184}, and
RC   JCM19302 {ECO:0000313|Proteomes:UP000029646};
RA   Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA   Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA   Sawabe T., Sawabe T.;
RT   "Draft Genome Sequence of Marine Flavobacterium Jejuia pallidilutea Strain
RT   11shimoA1 and Pigmentation Mutants.";
RL   Genome Announc. 2:e01236-14(2014).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
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         ECO:0000256|RuleBase:RU361137};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 2 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
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:RU361137}.
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:GAL73093.1}.
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DR   EMBL; BBNS01000039; GAL73093.1; -; Genomic_DNA.
DR   EMBL; BBNY01000020; GAL89692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090WA80; -.
DR   Proteomes; UP000029646; Unassembled WGS sequence.
DR   Proteomes; UP000030184; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
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; IPR006257; LAT1.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01349; PDHac_trf_mito; 1.
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:RU361137};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW   Pyruvate {ECO:0000313|EMBL:GAL73093.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361137}.
FT   DOMAIN          1..64
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          122..197
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          259..296
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          72..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   538 AA;  57458 MW;  FD5A7CAFF149279C CRC64;
     MEEGTVATWL KKVGDKIEEG DILAEIETDK ATMEFESFNE GTLLHIGVQE GETTKVDELL
     AIIGDEGEDI SDLLNGGGNA SAEDSNAEDA KAEASDEVES NKDETTETEE ASNASADLPE
     GVIVVTMPRL SDTMEEGTVA TWLKKVGDSV EEGDILAEIE TDKATMEFES FQSGTLLEIG
     LKEGESAKVD ELLAIIGPAG TDVSGVAANF SASSAPAAKK EEAPKQETKK EAPKTATAST
     ETKTKAPAPT PVTENGRLYV SPLAKKLAEE KGINLTKVQG SGENGRIIKR DIENYEPAAG
     AAAVGKFVPS GQEDFEDIPN SQMRKAIAKS LTKSKFSAPH YYLAVEFNMD NAMAFRAQFN
     SIPDTKISFN DIVVKACALA LKQHPQVNSQ WFDDKMRLNN HVHIGVAVAV PDGLVVPVVR
     FANEQSLPQI GAEVKALAGK ARNKKLTPDE MSGSTFTVSN LGMFGIDYFT SIINQPNSAI
     LSVGAIVQKP VVKNGEIVVG NTMKLTLACD HRTVDGATGA EFLQTLRGYI ENPVTMLV
//
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