ODPA_RICPR
ID ODPA_RICPR Reviewed; 326 AA.
AC Q9ZDR4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE EC=1.2.4.1;
GN Name=pdhA; OrderedLocusNames=RP261;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; 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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
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DR EMBL; AJ235271; CAA14723.1; -; Genomic_DNA.
DR PIR; A71681; A71681.
DR RefSeq; NP_220646.1; NC_000963.1.
DR RefSeq; WP_004596096.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDR4; -.
DR SMR; Q9ZDR4; -.
DR STRING; 272947.RP261; -.
DR PRIDE; Q9ZDR4; -.
DR EnsemblBacteria; CAA14723; CAA14723; CAA14723.
DR GeneID; 57569389; -.
DR KEGG; rpr:RP261; -.
DR PATRIC; fig|272947.5.peg.268; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_0_5; -.
DR OMA; FGMPGVT; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR InterPro; IPR029061; THDP-binding.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE 3: Inferred from homology;
KW Glycolysis; Oxidoreductase; Pyruvate; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..326
FT /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT /id="PRO_0000162204"
SQ SEQUENCE 326 AA; 36824 MW; BC9A6F66044B213A CRC64;
MDIKPEKYKP IKEEYIKSFK DMLLLRRFEE KCGQLYGMGK IGGFCHLYIG QEAVISAVAM
IKKKGDSTIT SYRDHAHIIL AGTEPKYVLA ELMGRATGCS KGKGGSMHLF DIPNKFYGGH
GIVGAQVPIG TGLAFAEKYN GTNNICFTFL GDGAVNQGQV YEAFNMASLW GLPIVYIIEN
NEYSMGTSVA RSTFMCDLYK KGESFGIRGF QLDGMDFEEM YNGTKQVAEY VRENSFPVIL
EVKTYRYRGH SMSDPAKYRS KEEVEKYKER DTLVRIREII LDNKYATEAD LKAIEQSVRE
IIKVAVEFSE NSPLPAEDEL YTEIYV