ID Q9A8Z0_CAUVC Unreviewed; 784 AA.
AC Q9A8Z0;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 124.
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 OrderedLocusNames=CC_1205 {ECO:0000313|EMBL:AAK23188.1};
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650 {ECO:0000313|EMBL:AAK23188.1, ECO:0000313|Proteomes:UP000001816};
RN [1] {ECO:0000313|EMBL:AAK23188.1, ECO:0000313|Proteomes:UP000001816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15 {ECO:0000313|Proteomes:UP000001816};
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R., Ohta N., Maddock J.R., Potocka I.,
RA Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T.,
RA Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J.,
RA Craven M.B., Khouri H., Shetty J., Berry K., Utterback T., Tran K.,
RA Wolf A., Vamathevan J., Ermolaeva M., White O., Salzberg S.L., Venter J.C.,
RA Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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}.
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DR EMBL; AE005673; AAK23188.1; -; Genomic_DNA.
DR PIR; H87398; H87398.
DR RefSeq; NP_420020.1; NC_002696.2.
DR RefSeq; WP_010919088.1; NC_002696.2.
DR AlphaFoldDB; Q9A8Z0; -.
DR SMR; Q9A8Z0; -.
DR STRING; 190650.CC_1205; -.
DR EnsemblBacteria; AAK23188; AAK23188; CC_1205.
DR KEGG; ccr:CC_1205; -.
DR PATRIC; fig|190650.5.peg.1229; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_020309_0_0_5; -.
DR BioCyc; CAULO:CC1205-MONOMER; -.
DR Proteomes; UP000001816; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000001816};
KW Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 420..625
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 784 AA; 84994 MW; E3FB821AB826A348 CRC64;
MPDGALTAKR QEIALLRRLE ERILWLAAWT IHNANHLRES RDGLKVGGHQ ASSASLTTIM
TALYMKALRP QDRVAVKPHA SPVFHAIQHL FGRQSLDNLK RFRALGGAQS YPSRTKDVDD
VDFSTGSVGL GVAMTAFASL TQDYLAARGA VKPEKMGRMI SLLGDAELDE GNIYEALIEA
CKHDIRNTWW IVDYNRQSLD ATTQDRMFTR YGEIFEAAGW AVETLKWSRR QREAFARPGG
DKLQAWIETA PNDLFSALTY QGGAAWRERL TADLADSPEA LALIAAYKDV DLAELMTELG
GHCLETLLEA FEKASQDDRP RFFIAYTVKG LRLPFQGHKD NHAGLMTPAQ IAELRARLGV
VEGEEWDPLS GLSAAERTAI KGLVARAPFA AEVERNHLAP QIPTPSASEL LAAVAGGGDQ
STQAAFGKVM FEIAARKDEF AGRVVTTSPD VTVSTNLGGF VNRRGVFQRR AHDDVFKRRR
IPSAQVWSKA ETGQHVELGI AENNLFIALA ALGLTAPLFG ERLFPVGTLY DPFIARGLDA
LNYACYQDAR FLLVATPSGL TLAPEGGAHQ SINAPVIGMA QPGLDTYEPA FADETAVLMA
HAFERIQAKD GASTYLRLST RAIPQPDRTG EAWRQGVIDG GYWLRAPARG ARLAIAYSGA
LAPEALAAFE ALAEDMPEAG LLAVTSADLL HRDWTASGRA RWTGEGARTS TIETLLAPLA
QGAGLVTLTD GAPLALSWLG SVRGQRVRAL GLETFGQSGD LPDLYAKYRL DADAVLDACA
DLLA
//
