ID A0A1T0A2U6_9GAMM Unreviewed; 648 AA.
AC A0A1T0A2U6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=aceF {ECO:0000313|EMBL:STZ14660.1};
GN ORFNames=B0181_05210 {ECO:0000313|EMBL:OOR90053.1}, NCTC10293_02257
GN {ECO:0000313|EMBL:STZ14660.1};
OS Moraxella caviae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=34060 {ECO:0000313|EMBL:OOR90053.1, ECO:0000313|Proteomes:UP000190435};
RN [1] {ECO:0000313|EMBL:OOR90053.1, ECO:0000313|Proteomes:UP000190435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 355 {ECO:0000313|EMBL:OOR90053.1,
RC ECO:0000313|Proteomes:UP000190435};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Moore E.;
RT "Draft genome sequence of Moraxella caviae CCUG 355 type strain.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:STZ14660.1, ECO:0000313|Proteomes:UP000255279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10293 {ECO:0000313|EMBL:STZ14660.1,
RC ECO:0000313|Proteomes:UP000255279};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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 -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
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:RU003423}.
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DR EMBL; MUXU01000034; OOR90053.1; -; Genomic_DNA.
DR EMBL; UGQE01000004; STZ14660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0A2U6; -.
DR STRING; 34060.B0181_05210; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000190435; Unassembled WGS sequence.
DR Proteomes; UP000255279; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 3.
DR Gene3D; 2.40.50.100; -; 3.
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; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 3.
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; 3.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR PROSITE; PS00189; LIPOYL; 3.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:STZ14660.1}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:OOR90053.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190435};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:OOR90053.1}.
FT DOMAIN 1..73
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 104..183
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 220..293
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 346..383
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 189..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 66928 MW; 0F3209D5FE03E00C CRC64;
MEIKAPDLGV DSAEVAEILV KVGDTVSEND NIVLVESDKA SVEIPAGASG VVSAILVNVG
DQVSEGSALI SIDSAAPAAA PAQEEVKPAE TAAPVAQEAS PAPAVAAGAS QTHALPDLGV
DSATVAEIMV NVGDTVEKDQ PLLLVESDKA SVEVPAPVAG KVEKLLVNAG DSVANGQDFI
VIAGDESAAP APAAPQSAPQ AQAETQPQAQ AAAPAQAGGS QTYNLPDLGV DSAEVAEVMV
NVGDEVTEGQ SLLLVESDKA SVEVPAPATG KVEKVLLKAG DSVANGQAFI VIASASAAPA
PQAAPKAETP ASPAPAAQPA AKPSAPAPAT AKLPEAEVNK RAKDAHAGPA VRKLARELGV
DISRVTGTAA HGRILKEDLF GYVKSVMTNI DKPAAAPIAA AARSGLPPLP DMSNKEIWGE
IEVQDLTRLQ KVSIPQLNLN TYLPQVTQFD LADITDTENL RGELKGEFKA QGIGLTILAF
IVKAVAYALT QHPKFNSHLS DDNTQIIVRK SVNMGIAVAT EEGLIVPVIR NAQDKGIKQL
AIEIGELAKK ARDKKLAAKD LQGASFTISS QGNMGGTYFT PLVNHPQVAI LGISESTFQP
RWNGKEFEPC LMLPLSLSYD HRVINGADAA VFTRYIAKLL ADPRKILL
//
