ID I3Z6G2_BELBD Unreviewed; 550 AA.
AC I3Z6G2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN OrderedLocusNames=Belba_2265 {ECO:0000313|EMBL:AFL84830.1};
OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL84830.1, ECO:0000313|Proteomes:UP000006050};
RN [1] {ECO:0000313|Proteomes:UP000006050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC {ECO:0000313|Proteomes:UP000006050};
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Belliella baltica DSM 15883.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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:ARBA00043782,
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}.
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DR EMBL; CP003281; AFL84830.1; -; Genomic_DNA.
DR AlphaFoldDB; I3Z6G2; -.
DR STRING; 866536.Belba_2265; -.
DR KEGG; bbd:Belba_2265; -.
DR PATRIC; fig|866536.3.peg.2327; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_2_10; -.
DR Proteomes; UP000006050; Chromosome.
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|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:AFL84830.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006050};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:AFL84830.1}.
FT DOMAIN 1..68
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 126..201
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 264..301
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 59055 MW; 685EF92BC4056278 CRC64;
MSDTMEEGVI AAWLKKVGDE VKPGDILAEV ETDKATMELE SYEEGVLLHI GVEEKDAVPV
NGVIAIIGEK GENIDNLLKE ANSGDAPAKS ESKSDKEDVK EEKPEKAAEP KESAKTESID
TSGINANLIT MPKMSDTMTE GVIASWLKKV GDEIKAGDII AEVETDKATM ELESYDDGIL
LHIGVEAGEA VEIDGVIAVI GEKGADYETL IKAHQSKGGS TEEAQSEVKK EEKAPEKAEE
KKEEKPAPKE SSSASSTTDG GRVKASPLAK KLASDKGVDI SLVKGSGEGG RIVKRDIESF
DPASVKAPAA KASEGSTSVP ALGQESFKEE KVSQMRKVIA KRLAESKFNA PHFYLTMEIN
MDKAIEARKS MNEIAPVKIS FNDMVIKAAA AALRQHPKVN SSWLGDKIRY NDHIHIGMAV
AVEEGLLVPV IRFADNKSLS QISNEAKSLG GKAKNKELQP KDWEGNTFTI SNLGMFGIDE
FTAIINPPDA CIMAVGGIKE TVIVKDGQMV IGNLMKVTLS CDHRVVDGAV GSAFLQTFKN
LLEDPVRILI
//
