ID F7XXL8_MOREP Unreviewed; 889 AA.
AC F7XXL8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=MEPCIT_194 {ECO:0000313|EMBL:AEI74844.1};
OS Moranella endobia (strain PCIT).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Moranella.
OX NCBI_TaxID=903503 {ECO:0000313|EMBL:AEI74844.1, ECO:0000313|Proteomes:UP000000504};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCIT;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested three-way symbiosis of
RT mealybugs.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEI74844.1, ECO:0000313|Proteomes:UP000000504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCIT {ECO:0000313|EMBL:AEI74844.1,
RC ECO:0000313|Proteomes:UP000000504};
RX PubMed=21835622; DOI=10.1016/j.cub.2011.06.051;
RA McCutcheon J.P., von Dohlen C.D.;
RT "An interdependent metabolic patchwork in the nested symbiosis of
RT mealybugs.";
RL Curr. Biol. 21:1366-1372(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; CP002243; AEI74844.1; -; Genomic_DNA.
DR RefSeq; WP_013975595.1; NC_015735.1.
DR AlphaFoldDB; F7XXL8; -.
DR STRING; 903503.MEPCIT_194; -.
DR KEGG; men:MEPCIT_194; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_6; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000000504; 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; 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.
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:AEI74844.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000504};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 85..297
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 490..702
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 889 AA; 99987 MW; CA62DB3DBE0D6530 CRC64;
MSTSLYNDVD PIETHDWLQA IESVIRTDGI ERAQFLIDQL LDKANKCGVR SIACAANERN
YINTIPVEDE PEYPGNIKLE RRIRSAIRWN AIMIVLRASK KNLDLGGHMA SFQSAATIYE
VCFNHLFRAR NNKDGGDLVY FQGHISPGVY ARAFLEGRIT EVQMNNFRQE VHGKGLSSYP
HPKLMPNFWQ FPTVSMGLGP ISAIYQAKFL KYLDHRLLKD TSNQTVYAFL GDGEMDEPES
TGAITIATRE KLDNLVFIIN CNLQRLDGPV TGNGKIINEL AGVFGGAGWE VIKVVWGSRW
DELLRKDTSG KLMQLMNETV DGDYQTFKSK NGAYVRKHFF GKYPETAALV KDMRDDEIWA
LNRGGHDPKK IYAALQKAQK ITGKPVVILA HTIKGYGMGL TAEGMNIAHQ VKKINIEGLR
YFRDRFNLSF ITDEKIESLP YITFDAGSEE HTYLHKQRQV LHGYLPSRLS EFTNQLELPK
LEDFAPLLEE QNKEISTTIA FVRVLSTMLK QKSIKDRLVP IVADEARTFG MEGLFRQIGI
YSPNGQQYTP QDREQVAYYR EDAKGQILQE GINELGAAAS WLAAATSYST NNLVMIPFYI
YYSIFGFQRI GDLCWAAGDQ QARGFLIGGT SGRTTLNGEG LQHEDGHSHI QSLTIPNCIS
YDPAYAYEVA VIIQDGLNRM YGDKPENIYY YITTMNENYT MPAMPKGAAD GIRKGIYKLE
TLVGSKGKVQ LMGSGAILRH VRKAAQILSK EYDISSDIYS VTSFTELARD GQDCERWNML
NPTKTPRIPY VATVLNNAPA VASTDYMKLF AEQIRNFIPA KEFRTLGTDG FGRSDSRDNL
RHHFEVDASY VVVAALGELA KRGDISDDIV AQAINKFKIY ANKVNPRLA
//
