ID A0A1G1TEE9_9BACT Unreviewed; 594 AA.
AC A0A1G1TEE9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=BEN47_07600 {ECO:0000313|EMBL:OGX89254.1};
OS Hymenobacter lapidarius.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1908237 {ECO:0000313|EMBL:OGX89254.1, ECO:0000313|Proteomes:UP000176294};
RN [1] {ECO:0000313|EMBL:OGX89254.1, ECO:0000313|Proteomes:UP000176294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8643 {ECO:0000313|EMBL:OGX89254.1,
RC ECO:0000313|Proteomes:UP000176294};
RA Sedlacek I., Kralova S., Kyrova K., Maslanova I., Stankova E., Vrbovska V.,
RA Nemec M., Bartak M., Svec P., Busse H.-J., Pantucek R.;
RT "Hymenobacter coccineus sp. nov., Hymenobacter lapidarius sp. nov. and
RT Hymenobacter glacialis sp. nov., isolated from Antarctic soil.";
RL Submitted (AUG-2016) 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}.
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:OGX89254.1}.
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DR EMBL; MDZB01000033; OGX89254.1; -; Genomic_DNA.
DR RefSeq; WP_070724412.1; NZ_MDZB01000033.1.
DR AlphaFoldDB; A0A1G1TEE9; -.
DR STRING; 1908237.BEN47_07600; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000176294; 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|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:OGX89254.1};
KW Transferase {ECO:0000256|RuleBase:RU361137}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 146..221
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 288..325
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 91..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 61053 MW; 02EF34F972BA21C6 CRC64;
MAEIIKMPKM SDTMTEGTIA AWLKKVGDKV KSGDILAEVE TDKATMELEN YEDGVLLYIG
PKEQESVVVD GILAIVGKEG EDFSALLSGA QGGAEAPKAD APKPEAAPAP AAAPAAEAPK
EAPAATPAPT PAAPAPVAAP ANGKKATVVR MPKMSDTMTE GTIAAWLKNV GDKVKSGDIL
AEVETDKATM ELENYEDGTL LYTGPKAGEA VAVDGILAII GEEGADIQAL LGEPSGDAAP
VPEAAATEAP APAEAPKAAD APKVAEDAPA TAATPVAATP AAPGGRIFAS PLAKSIAKEK
GINLAQVVGS GDNGRIVQRD VENFYPGAAA PAPQAAPAAA PAAPAPAAAP QATAPAAQPA
ASVAAPASDT YTDTPVSQMR KVIAKRLSES LFTAPHFYLT MEINMDKAIE ARVKLNELSP
IKLSFNDLVL KSAAVALRQH PAINSSWMGD KIRQNKVINI GVAVAVDEGL LVPVIRNADQ
KGLSQIATEV KELAGRAKTK KLQPAEWEGS TFTISNLGMF GIDEFTAIIN TPDACILAVG
GIKQTPIVKD GQIVVGNIMK VTLSCDHRVV DGATGAAFLQ TLKGLLEDPM RMLI
//
