ID G4FPI2_9SYNE Unreviewed; 438 AA.
AC G4FPI2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=Syn8016DRAFT_2586 {ECO:0000313|EMBL:EHA60204.1};
OS Synechococcus sp. WH 8016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=166318 {ECO:0000313|EMBL:EHA60204.1, ECO:0000313|Proteomes:UP000002752};
RN [1] {ECO:0000313|EMBL:EHA60204.1, ECO:0000313|Proteomes:UP000002752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8016 {ECO:0000313|Proteomes:UP000002752};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Palenik B., Woyke T.J.;
RT "The draft genome of Synechococcus sp. WH 8016.";
RL Submitted (SEP-2011) 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:EHA60204.1}.
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DR EMBL; AGIK01000005; EHA60204.1; -; Genomic_DNA.
DR AlphaFoldDB; G4FPI2; -.
DR STRING; 166318.Syn8016DRAFT_2586; -.
DR PATRIC; fig|166318.3.peg.2746; -.
DR eggNOG; COG0508; Bacteria.
DR Proteomes; UP000002752; 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; 1.
DR Gene3D; 2.40.50.100; -; 1.
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:SF75; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT 5 OF PYRUVATE DEHYDROGENASE COMPLEX, CHLOROPLASTIC; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
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; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:EHA60204.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EHA60204.1}.
FT DOMAIN 1..74
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 140..177
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 44597 MW; D8897989B5BB411C CRC64;
MPALSSTMTE GKIVEWLKQP GDKVARGESV LVVESDKADM DVESFQEGYL AAVLMPAGST
APVGETIGLI VETEAEIADA KAKAPTAAPS ASPASAPTAP AAAAPPAPAP PAAPVAPAPV
AAPAPISAPV AAPASNGRLI VSPRARKLAS QMGVDLAGLR GTGPNGRIQA EDVEKAAGRP
VTPPRVGEGT SAAVVAGATG AASPSAPAGN SFGAPGDTVA FNTLQAAVNR NMEASLAVPC
FRVGYTITTD KLDAFYKQVK PKGVTMTALL AKAVAVTLAR HPQVNAATTA SGMSYPAEVN
VAVAVAMEDG GLITPVLRNA DRTDLYELSR QWGDLVKRSR SKQLQPEEYS TGTFTLSNLG
MFGVDRFDAI LPPGTGAILA VAASRPTVVA GKDGSIAVKR QMQVNLTADH RVIYGADGAA
FLKDLAELID TRPESLAL
//