ID C5WD32_9ENTR Unreviewed; 519 AA.
AC C5WD32;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:BAH83238.1};
GN ORFNames=ICMP_385 {ECO:0000313|EMBL:BAH83238.1};
OS Candidatus Ishikawaella capsulata Mpkobe.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Ishikawaella.
OX NCBI_TaxID=476281 {ECO:0000313|EMBL:BAH83238.1, ECO:0000313|Proteomes:UP000061704};
RN [1] {ECO:0000313|EMBL:BAH83238.1, ECO:0000313|Proteomes:UP000061704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mpkobe {ECO:0000313|EMBL:BAH83238.1,
RC ECO:0000313|Proteomes:UP000061704};
RX PubMed=21737395;
RA Nikoh N., Hosokawa T., Ohshima K., Hattori M., Fukatsu T.;
RT "Reductive evolution of bacterial genome in insect gut environment.";
RL Genome Biol. Evol. 3:702-714(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}.
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DR EMBL; AP010872; BAH83238.1; -; Genomic_DNA.
DR AlphaFoldDB; C5WD32; -.
DR STRING; 476281.ICMP_385; -.
DR KEGG; icp:ICMP_385; -.
DR HOGENOM; CLU_016733_10_0_6; -.
DR Proteomes; UP000061704; Chromosome.
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; 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; 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; 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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000061704};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BAH83238.1}.
FT DOMAIN 8..81
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 106..179
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 218..255
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 519 AA; 57604 MW; 3F7A31514EA9391F CRC64;
MRGNVLMSIE IKLPDIGSDT VEVTDILVNV GEFVETDHPL ITVEGDKASM EIPAPFAGII
KEINVSIGDK LNTGSNIMIF DKPDKSEYLI KDHIKDIKEK NTAVHHKDIV LPDIGNNEME
ITEIKVKIGD NVSVEQTLII IEGDKASIEI PAPFSGKVIM INVAVGDKVK TGLIIMVFEV
VETENNKISK PLEKTLDSNS DLPIKNNNCY FPEYSYVHAT PVIRRLAREF GIDLSNIIGT
GRKGRILKED LKSYINKLSL IDTNSVKTAS SSSLPSVTQL NIDFSKFGEV EEIELSRIKK
ISGANLSKSW STIPHVTHFD KYDITDLEGF RQKLILELKN NVDIKITPLV FIMKAVAYAL
KRIPHFNSSL SYDCQKLILK KYINIGVAVD TTKGLVVPVF KNVYEKGIIK LSEELIEMSK
KARSGKLMIN DMQGGCFTIS SLGKLGTTAF TPIINTPEVA ILGISKSHVE PVWNGKKFIP
RLMLPISLSF DHRVIEGADA ARFIAMVGNI LTDIRRLIM
//
