ID F7WZ70_9GAMM Unreviewed; 879 AA.
AC F7WZ70;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|PIRNR:PIRNR000156};
GN Name=aceE {ECO:0000313|EMBL:AEH39724.1};
GN ORFNames=BCTU_135 {ECO:0000313|EMBL:AEH39724.1};
OS Buchnera aphidicola (Cinara tujafilina).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=261317 {ECO:0000313|EMBL:AEH39724.1, ECO:0000313|Proteomes:UP000006811};
RN [1] {ECO:0000313|EMBL:AEH39724.1, ECO:0000313|Proteomes:UP000006811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cinara tujafilina {ECO:0000313|Proteomes:UP000006811};
RX PubMed=21571878; DOI=10.1128/AEM.00141-11;
RA Lamelas A., Gosalbes M.J., Moya A., Latorre A.;
RT "The genome of Buchnera aphidicola from the aphid Cinara tujafilina
RT provides new clues about the evolutionary history of metabolic losses in
RT bacterial endosymbionts.";
RL Appl. Environ. Microbiol. 77:4446-4454(2011).
CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|ARBA:ARBA00003157, ECO:0000256|PIRNR:PIRNR000156}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00043719,
CC ECO:0000256|PIRNR:PIRNR000156};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000156-1};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|PIRNR:PIRNR000156};
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DR EMBL; CP001817; AEH39724.1; -; Genomic_DNA.
DR AlphaFoldDB; F7WZ70; -.
DR STRING; 261317.BCTU_135; -.
DR KEGG; baj:BCTU_135; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_6; -.
DR Proteomes; UP000006811; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR035807; PDC_E1_N.
DR InterPro; IPR004660; PDH_E1.
DR InterPro; IPR041621; PDH_E1_M.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00759; aceE; 1.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR Pfam; PF17831; PDH_E1_M; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000156};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:AEH39724.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006811};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 1..26
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 879 AA; 100625 MW; F72300D044CEF07A CRC64;
MVTNISNDLD PLETNEWIEA IESVLKNDGK NEHFFLIKKI LEKINIDAIN INFKNYNFIN
SIHYTEEPRY PGNLKIEKNI RSVVCWNAIM IVLRASKKNL DLGGHISSFQ SFATVYEVCF
NHFFRASNKY DGGDLIYFQG HVSPGIYARA FLEDRLTETQ LDNFRQEICG FGLSSYPHPN
LMPDFWQFPT VSMGLSSVCA IYQARFLKYL HNRNLKNTTL QTVYAFLGDG EMDEPESKGA
VVLAAREQLD NLIFIINCNL QRLDGPVFGN GKIINELSSF FSGCGWHVIK VIWSSQWDTL
LDRDDQGFLK RLMNETVDGN YQTLKSKNGA YVRKHFFERY EETKKLVENF TDSELWALKR
GGHDPKKIYA AFHEAKKIKE KPVVILIHTV KGYGLGEVGE SKNISHQIKT IKDINVKYLY
DRFKLNAHKS VINNLSYIKF LPGSEEYHYI HQQRKKLYGY LPKRLKNFSN SFRIPTLNDF
KILLQKQSKP ISTTMIFIKI LNILLRFPGI QKKIVPIIAD EARTFGMEAL FQKIGIYNHL
GQLYTPSDKE KLLYYKEEKS GQILQEGINE LGACASWLAA ATAYSTNDFP MIPFYIYYSM
FGFQRVGDLL WACGDQNARG FLIGATSGRT TLNGEGLQHA DGHSHILSLT IPNCVSYDPA
YGYELSVIIQ DGLQRMYGNK QENIFYYITT VNENYLMPSM SNIMLEGICK GIYLLETFSG
KIGRVQLLGS GAILERIRKA ASILHAEYDI GSDVYSVTSF TELARNGQDC TRWNFLNPLQ
TKKIPYVSSI IKNYPTIAAT DYIKVFAEQI RAYIPSKIFH VLGTDGFGRS DSRKNLRNFF
EIDENYIISA AINALVDSNT IDQDILLKVF KNLIFFQIK
//
