ID A0A0D7E456_RHOPL Unreviewed; 798 AA.
AC A0A0D7E456;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN ORFNames=OO17_26030 {ECO:0000313|EMBL:KIZ35190.1};
OS Rhodopseudomonas palustris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ35190.1, ECO:0000313|Proteomes:UP000032515};
RN [1] {ECO:0000313|EMBL:KIZ35190.1, ECO:0000313|Proteomes:UP000032515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL398 {ECO:0000313|EMBL:KIZ35190.1,
RC ECO:0000313|Proteomes:UP000032515};
RA Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT isolated from estuarine surface water.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000156-1};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|PIRNR:PIRNR000156};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIZ35190.1}.
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DR EMBL; JXXE01000639; KIZ35190.1; -; Genomic_DNA.
DR RefSeq; WP_044417376.1; NZ_JXXE01000639.1.
DR AlphaFoldDB; A0A0D7E456; -.
DR PATRIC; fig|1076.23.peg.1665; -.
DR OrthoDB; 9773339at2; -.
DR Proteomes; UP000032515; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF4; 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 SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
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|PIRNR:PIRNR000156};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 409..626
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 798 AA; 87363 MW; 5D3B729E9CB4A15E CRC64;
MPKAPNRLEL LSALSRKVLW LSSWTIHHAN HIRPNADGLK VGGHQASSAS LVTIMSALYF
SVLRPQDRVA VKPHASAVFH AIQYLFGRQS RARLENFRGF KGAQSYPSRT KDVDDVDFST
GSVGLGVAQT LFSSLVQDYV TAHGWMKDRP EGRMIALVGD AEMDEGNIFE ALLEGWKHGL
RNTWWVVDYN RQSLDAVVRE GLWEKFESMF RNFGWDVVIV KYGRLMQAAF AEPGGAALRN
WIDTCPNQMY AALCFQGGAA FRKRLNDEIG DQGEVSRLID ARSDDELLAL MSNLGGHDMA
SMVEAFEAID HDRPVCFIAY TIKGVGLPFQ GHKDNHAGLM TPTQMETLRA AQNIRPGHEW
DRFEGLEQDE ATLQAFLDAA PINRGGDRKL TAPVIEVPSQ LSFKPAAEMS TQQGFGLILN
ELARGDSDLA ARIVTASPDV TVSTNLGAWV NRRGLFARAE KADLFRSEKI PTTFNWDFSP
KGQHLELGIA EMNLFILMSA LGLSHAINGE RLLPIATLYD PFIQRGLDAL NYACYQDARF
MVVATPSGIT LAPEGGAHQS IATPLIGIAQ DGLAAFEPGF VDELAVIMRW GFAHMQREAS
EGGDARSGMR AGGSVYLRLS TRSIAQPQRV MTPQLQQAIT DGGYWLRPPG PNCELVIAYT
GALAPEAIEA VGLLGDSRRD VGLLAITSAD RLHAGWTAAR RLRRERRGAH QPSHIEQLLA
PLPRDCGIVT VLDGHPATLG WIGAVCGHRM EALGVEHFGQ TGSIGDLYRH YGLDANAIID
AAEGLVRGAP VLHRKMAV
//
