ID H6Q4Z5_WIGGL Unreviewed; 497 AA.
AC H6Q4Z5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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:AFA41278.1};
GN Synonyms=aceE2 {ECO:0000313|EMBL:AFA41278.1};
GN ORFNames=WIGMOR_0448 {ECO:0000313|EMBL:AFA41278.1};
OS Wigglesworthia glossinidia endosymbiont of Glossina morsitans morsitans
OS (Yale colony).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=1142511 {ECO:0000313|EMBL:AFA41278.1, ECO:0000313|Proteomes:UP000009061};
RN [1] {ECO:0000313|EMBL:AFA41278.1, ECO:0000313|Proteomes:UP000009061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WGM {ECO:0000313|EMBL:AFA41278.1};
RX PubMed=22334516;
RA Rio R.V., Symula R.E., Wang J., Lohs C., Wu Y.N., Snyder A.K.,
RA Bjornson R.D., Oshima K., Biehl B.S., Perna N.T., Hattori M., Aksoy S.;
RT "Insight into the transmission biology and species-specific functional
RT capabilities of tsetse (Diptera: glossinidae) obligate symbiont
RT wigglesworthia.";
RL MBio 3:E00240-11(2012).
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; CP003315; AFA41278.1; -; Genomic_DNA.
DR RefSeq; WP_014354217.1; NC_016893.1.
DR AlphaFoldDB; H6Q4Z5; -.
DR STRING; 1142511.WIGMOR_0448; -.
DR KEGG; wgl:WIGMOR_0448; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_6; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000009061; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
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; 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; 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|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:AFA41278.1};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..75
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 201..238
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 497 AA; 56173 MW; 5D30AE9ED472E208 CRC64;
MNTVVKIPDI GIEDAEVTEI LVKIEDKIKK EQALITVEGD KASMQIPSPI SGILKKIMVK
IGDKVSTNQE IMFFEKTDKN DKFIAKKMLK KVEKKLLDSK HEEFKKIYAS ELGILNRAEI
IRVSIHEENN IKINSPILII QDCKGTRKIL STISGIVKNV QIKAGDHVDP DTLLYDIYVS
KIFEKKPKNL LKTIIQNNQI YASPLIRRIA LKYNINLSHI HGSGRKGRIL PTDLEKYINI
YENNQLSQNT KNVQSFSEDS QYEVYGKIEI QELTKIKKVS GKNLSKNWKN IPHVTQFDQA
DIHELEIFRK NQNIILQKKN KIKITILSFV IKAVIATLKE YPQFNSSLSQ DQKKIFLKKY
FNIGIAVNTE QGLMVPIIFN ADSKGILEIS QEISNIAKKA RSGILSNKDM KGGCFTISNL
GGIGGKEFTP IINAPEVAIL GISQASIQAI WNGDTFVPKL MLPLSLSYDH RVIDGVEGAK
FINFFKNLIS DIRLLIL
//