ID F0KHB8_ACICP Unreviewed; 662 AA.
AC F0KHB8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
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:ADY83379.1};
GN OrderedLocusNames=BDGL_002793 {ECO:0000313|EMBL:ADY83379.1};
OS Acinetobacter calcoaceticus (strain PHEA-2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY83379.1, ECO:0000313|Proteomes:UP000007477};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PHEA-2;
RA Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT environmental adaptation.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADY83379.1, ECO:0000313|Proteomes:UP000007477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY83379.1,
RC ECO:0000313|Proteomes:UP000007477};
RX PubMed=21441526; DOI=10.1128/JB.00261-11;
RA Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA Yuan M., Zhou Z., Elmerich C., Lin M.;
RT "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT industry wastewater.";
RL J. Bacteriol. 193:2672-2673(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002177; ADY83379.1; -; Genomic_DNA.
DR RefSeq; WP_014207930.1; NC_016603.1.
DR RefSeq; YP_004997061.1; NC_016603.1.
DR AlphaFoldDB; F0KHB8; -.
DR STRING; 871585.BDGL_002793; -.
DR GeneID; 11637440; -.
DR KEGG; acc:BDGL_002793; -.
DR PATRIC; fig|871585.3.peg.2792; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OMA; HPCIMAP; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000007477; Chromosome.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:ADY83379.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007477};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..73
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 119..192
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 232..305
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 364..401
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 80..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 68643 MW; 5BA051C5818AFC25 CRC64;
MQIKTPDIGV DKAVVAEILV KVGDSIAEND SLVLLESDKA SVEVPSTSAG VVKSILIKEG
DSVAEGTVLL ELEAEGAAPV AQAEEAPKAA PAAEQTAAPA AAQQPSTAAQ PATATTSQVV
EVQVPDIGVE KALVGEILVK VGEQIDVEQS IVVVESDKAT VEVPSSVAGT VESIQVKEGD
TVKEGVVLIK VKTTSASSAP AEAPASTTAA PAAAPAPAQQ ETVASTATQS GPVDINVPDL
GVDKAVVAEI LVQVGDKVDV DQSLVVVESD KATVEVPSTV AGVVKAIHLQ AGQQVSQGVL
LATIEAEGQA PAAAPAAKAE SAPAQQAAAP KAAAPAPTQA VSAPASSGND KLTKEQEAEN
AKVYAGPAVR KLARELGVVL SQVKTSGEHG RVVKEDIFAY VKTRLTAPQA APVASAAPAV
SGLPKLPDFT AFGGVEEKVL TRLQQVSIPQ LSLNNFIPQV TQFDLADITE LEDWRNELKG
NFKKEGVSLT IMAFIIKAVA YLLKEEREFA GHLSDDGKSV LLRNEIHMGI AVATPDGLTV
PVLRNPDQKS IKQIAVELGM LGQKARDKKL TPKDLQGANF TISSLGAIGG TAFTPLVNWP
QVAILGISPA TMQPVWNGKD FDPRLMLPLS LSYDHRVING ADAARFTNKL TKLLKDIRTL
LI
//